Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P06214
|
HEM2_RAT
|
MHHQSVLHSGYFHPLLRAWQTTPSTVSATNLIYPIFVTDVPDDVQPIASLPGVARYGVNQLEEMLRPLVEAGLRCVLIFGVPSRVPKDEQGSAADSEDSPTIEAVRLLRKTFPTLLVACDVCLCPYTSHGHCGLLSENGAFLAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKAALLKHGLGNRVSVMSYSAKFASCFYGPFRDAAQSSPAFGDRRCYQLPPGARGLALRAVARDIQEGADILMVKPGLPYLDMVQEVKDKHPELPLAVYQVSGEFAMLWHGAKAGAFDLRTAVLESMTAFRRAGADIIITYFAPQLLKWLKEE
|
4.2.1.24
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 8 zinc ions per octamer. Requires four zinc ions per octamer for full catalytic activity. Can bind up to 2 zinc ions per subunit. {ECO:0000250};
|
cellular response to interleukin-4 [GO:0071353]; cellular response to lead ion [GO:0071284]; heme A biosynthetic process [GO:0006784]; heme B biosynthetic process [GO:0006785]; heme biosynthetic process [GO:0006783]; heme O biosynthetic process [GO:0048034]; negative regulation of proteasomal protein catabolic process [GO:1901799]; protein homooligomerization [GO:0051260]; protoporphyrinogen IX biosynthetic process [GO:0006782]; response to activity [GO:0014823]; response to aluminum ion [GO:0010044]; response to amino acid [GO:0043200]; response to arsenic-containing substance [GO:0046685]; response to cadmium ion [GO:0046686]; response to cobalt ion [GO:0032025]; response to ethanol [GO:0045471]; response to fatty acid [GO:0070542]; response to glucocorticoid [GO:0051384]; response to herbicide [GO:0009635]; response to hormone [GO:0009725]; response to hypoxia [GO:0001666]; response to inorganic substance [GO:0010035]; response to ionizing radiation [GO:0010212]; response to iron ion [GO:0010039]; response to lead ion [GO:0010288]; response to lipopolysaccharide [GO:0032496]; response to mercury ion [GO:0046689]; response to metal ion [GO:0010038]; response to methylmercury [GO:0051597]; response to nutrient [GO:0007584]; response to nutrient levels [GO:0031667]; response to organic cyclic compound [GO:0014070]; response to organic substance [GO:0010033]; response to oxidative stress [GO:0006979]; response to platinum ion [GO:0070541]; response to selenium ion [GO:0010269]; response to toxic substance [GO:0009636]; response to vitamin [GO:0033273]; response to vitamin B1 [GO:0010266]; response to vitamin E [GO:0033197]; response to xenobiotic stimulus [GO:0009410]; response to zinc ion [GO:0010043]
|
cytosol [GO:0005829]; extracellular space [GO:0005615]
|
identical protein binding [GO:0042802]; porphobilinogen synthase activity [GO:0004655]; proteasome core complex binding [GO:1904854]; zinc ion binding [GO:0008270]
|
PF00490;
|
3.20.20.70;
|
ALAD family
| null | null |
CATALYTIC ACTIVITY: Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24;
| null |
PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
| null | null |
FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
P06229
|
FEN_BPT5
|
MSKSWGKFIEEEEAEMASRRNLMIVDGTNLGFRFKHNNSKKPFASSYVSTIQSLAKSYSARTTIVLGDKGKSVFRLEHLPEYKGNRDEKYAQRTEEEKALDEQFFEYLKDAFELCKTTFPTFTIRGVEADDMAAYIVKLIGHLYDHVWLISTDGDWDTLLTDKVSRFSFTTRREYHLRDMYEHHNVDDVEQFISLKAIMGDLGDNIRGVEGIGAKRGYNIIREFGNVLDIIDQLPLPGKQKYIQNLNASEELLFRNLILVDLPTYCVDAIAAVGQDVLDKFTKDILEIAEQ
|
3.1.11.-; 3.1.11.3
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:12606565, ECO:0000269|PubMed:15077103, ECO:0000269|PubMed:27273516}; Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:27273516}; Note=Binds divalent metal cations, probably Mg(2+). In vitro low metal concentrations selectively stimulate the endonuclease reaction. Endonuclease activity is suggested to require only the first cation, whereas exonuclease activity is suggested to require binding of both. High pH favors the exonuclease activity whereas low pH favors the endonuclease activity. Metal ions enhance substrate binding. {ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:12606565, ECO:0000269|PubMed:15077103, ECO:0000269|PubMed:27273516};
|
DNA replication, Okazaki fragment processing [GO:0033567]; late viral transcription [GO:0019086]; viral DNA genome replication [GO:0039693]
|
viral replication complex [GO:0019034]
|
5'-3' DNA exonuclease activity [GO:0035312]; 5'-3' exonuclease activity [GO:0008409]; 5'-flap endonuclease activity [GO:0017108]; DNA binding [GO:0003677]; DNA exonuclease activity [GO:0004529]; double-stranded DNA 5'-3' DNA exonuclease activity [GO:0051908]; double-stranded DNA endonuclease activity [GO:1990238]; metal ion binding [GO:0046872]
|
PF01367;PF02739;
|
1.10.150.20;3.40.50.1010;
| null | null | null |
CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.3; Evidence={ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:10364212, ECO:0000269|PubMed:17559871, ECO:0000269|PubMed:2211703, ECO:0000269|PubMed:27273516, ECO:0000269|PubMed:9380501, ECO:0000269|PubMed:9874768, ECO:0000269|PubMed:9889266};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.3 for the exonuclease activity, 5.5 for endonuclease activity. High pH favors the exonuclease activity whereas low pH favors the endonuclease activity. {ECO:0000269|PubMed:10364212, ECO:0000269|PubMed:9874768};
| null |
FUNCTION: Catalyzes both the 5'-exonucleolytic and structure-specific endonucleolytic hydrolysis of DNA branched nucleic acid molecules and probably plays a role in viral genome replication (PubMed:10364212, PubMed:15077103, PubMed:9874768). Active on flap (branched duplex DNA containing a free single-stranded 5'-end), 5'overhangs and pseudo-Y structures (PubMed:10364212, PubMed:15077103, PubMed:9874768). The substrates require a free, single-stranded 5' end, with endonucleolytic hydrolysis occurring at the junction of double- and single-stranded DNA (PubMed:9874768). This function may be used for example to trim such branched molecules generated by Okazaki fragments synthesis during replication. {ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:10364212, ECO:0000269|PubMed:15077103, ECO:0000269|PubMed:9874768}.
|
Escherichia phage T5 (Enterobacteria phage T5)
|
P06238
|
A2MG_RAT
|
MGKHRLRSLALLPLLLRLLLLLLPTDASAPQKPIYMVMVPSLLHAGTPEKACFLFSHLNETVAVRVSLESVRGNQSLFTDLVVDKDLFHCTSFTVPQSSSDEVMFFTVQVKGATHEFRRRSTVLVKKKESLVFAQTDKPIYKPGQTVRFRVVSLDESFHPLNELIPLLYIQDPKNNRIAQWQNFNLEGGLKQLSFPLSSEPTQGSYKVVIRTESGRTVEHPFSVEEFVLPKFEVRVTVPETITILEEEMNVSVCGIYTYGKPVPGRVTVNICRKYSNPSNCFGEESVAFCEKLSQQLDGRGCFSQLVKTKSFQLKRQEYEMQLDVHAKIQEEGTGVEETGKGLTKITRTITKLSFVNVDSHFRQGIPFVGQVLLVDGRGTPIPYETIFIGADEANLYINTTTDKHGLARFSINTDDIMGTSLTVRAKYKDSNACYGFRWLTEENVEAWHTAYAVFSPSRSFLHLESLPDKLRCDQTLEVQAHYILNGEAMQELKELVFYYLMMAKGGIVRAGTHVLPLKQGQMRGHFSILISMETDLAPVARLVLYAILPNGEVVGDTAKYEIENCLANKVDLVFRPNSGLPATRALLSVMASPQSLCGLRAVDQSVLLMKPETELSASLIYDLLPVKDLTGFPQGADQREEDTNGCVKQNDTYINGILYSPVQNTNEEDMYGFLKDMGLKVFTNSNIRKPKVCERLRDNKGIPAAYHLVSQSHMDAFLESSESPTETRRSYFPETWIWDLVVVDSAGVAEVEVTVPDTITEWKAGAFCLSNDTGLGLSPVVQFQAFQPFFVELTMPYSVIRGEAFTLKATVLNYLPTCIRVAVQLEASPDFLAAPEEKEQRSHCICMNQRHTASWAVIPKSLGNVNFTVSAEALNSKELCGNEVPVVPEQGKKDTIIKSLLVEPEGLENEVTFNSLLCPMGAEVSELIALKLPSDVVEESARASVTVLGDILGSAMQNTQDLLKMPYGCGEQNMVLFAPNIYVLDYLNETQQLTQEIKTKAIAYLNTGYQRQLNYKHRDGSYSTFGDKPGRNHANTWLTAFVLKSFAQARKYIFIDEVHITQALLWLSQQQKDNGCFRSSGSLLNNAMKGGVEDEVTLSAYITIALLEMSLPVTHPVVRNALFCLDTAWKSARGGAGGSHVYTKALLAYAFALAGNQDTKKEILKSLDEEAVKEEDSVHWTRPQKPSVSVALWYQPQAPSAEVEMTAYVLLAYLTTEPAPTQEDLTAAMLIVKWLTKQQNSHGGFSSTQDTVVALHALSKYGSATFTRAKKAAQVTIHSSGTFSTKFQVNNNNQLLLQRVTLPTVPGDYTVKVTGEGCVYLQTSLKYSVLPREEEFPFTVVVQTLPGTCEDPKAHTSFQISLNISYTGSRSESNMAIADVKMVSGFIPLKPTVKMLERSVHVSRTEVSNNHVLIYLDKVSNQTVNLSFTVQQDIPIRDLKPAVVKVYDYYEKDEFAVAKYSAPCSTDYGNA
| null | null |
acute inflammatory response to antigenic stimulus [GO:0002438]; acute-phase response [GO:0006953]; embryonic liver development [GO:1990402]; luteinization [GO:0001553]; negative regulation of complement activation, lectin pathway [GO:0001869]; response to carbon dioxide [GO:0010037]; response to glucocorticoid [GO:0051384]; response to nutrient [GO:0007584]; response to prostaglandin E [GO:0034695]; stem cell differentiation [GO:0048863]
|
extracellular space [GO:0005615]
|
brain-derived neurotrophic factor binding [GO:0048403]; calcium-dependent protein binding [GO:0048306]; endopeptidase inhibitor activity [GO:0004866]; enzyme binding [GO:0019899]; growth factor binding [GO:0019838]; identical protein binding [GO:0042802]; interleukin-1 binding [GO:0019966]; interleukin-8 binding [GO:0019959]; nerve growth factor binding [GO:0048406]; protease binding [GO:0002020]; serine-type endopeptidase inhibitor activity [GO:0004867]; signaling receptor binding [GO:0005102]; tumor necrosis factor binding [GO:0043120]
|
PF00207;PF07703;PF07677;PF01835;PF17791;PF17789;PF07678;
|
1.50.10.20;2.20.130.20;2.60.120.1540;2.60.40.1930;2.60.40.1940;2.60.40.690;2.60.40.10;
|
Protease inhibitor I39 (alpha-2-macroglobulin) family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase.
|
Rattus norvegicus (Rat)
|
P06239
|
LCK_HUMAN
|
MGCGCSSHPEDDWMENIDVCENCHYPIVPLDGKGTLLIRNGSEVRDPLVTYEGSNPPASPLQDNLVIALHSYEPSHDGDLGFEKGEQLRILEQSGEWWKAQSLTTGQEGFIPFNFVAKANSLEPEPWFFKNLSRKDAERQLLAPGNTHGSFLIRESESTAGSFSLSVRDFDQNQGEVVKHYKIRNLDNGGFYISPRITFPGLHELVRHYTNASDGLCTRLSRPCQTQKPQKPWWEDEWEVPRETLKLVERLGAGQFGEVWMGYYNGHTKVAVKSLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEPIYIITEYMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMVRPDNCPEELYQLMRLCWKERPEDRPTFDYLRSVLEDFFTATEGQYQPQP
|
2.7.10.2
| null |
activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; B cell receptor signaling pathway [GO:0050853]; Fc-gamma receptor signaling pathway [GO:0038094]; hemopoiesis [GO:0030097]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; intracellular zinc ion homeostasis [GO:0006882]; leukocyte migration [GO:0050900]; peptidyl-tyrosine autophosphorylation [GO:0038083]; peptidyl-tyrosine phosphorylation [GO:0018108]; platelet activation [GO:0030168]; positive regulation of heterotypic cell-cell adhesion [GO:0034116]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of leukocyte cell-cell adhesion [GO:1903039]; positive regulation of T cell activation [GO:0050870]; positive regulation of T cell receptor signaling pathway [GO:0050862]; protein phosphorylation [GO:0006468]; regulation of lymphocyte activation [GO:0051249]; release of sequestered calcium ion into cytosol [GO:0051209]; response to xenobiotic stimulus [GO:0009410]; T cell costimulation [GO:0031295]; T cell differentiation [GO:0030217]; T cell receptor signaling pathway [GO:0050852]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; immunological synapse [GO:0001772]; membrane raft [GO:0045121]; pericentriolar material [GO:0000242]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; ATPase binding [GO:0051117]; CD4 receptor binding [GO:0042609]; CD8 receptor binding [GO:0042610]; identical protein binding [GO:0042802]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphatidylinositol 3-kinase binding [GO:0043548]; phospholipase activator activity [GO:0016004]; phospholipase binding [GO:0043274]; phosphotyrosine residue binding [GO:0001784]; protein kinase binding [GO:0019901]; protein phosphatase binding [GO:0019903]; protein serine/threonine phosphatase activity [GO:0004722]; protein tyrosine kinase activity [GO:0004713]; SH2 domain binding [GO:0042169]; signaling receptor binding [GO:0005102]; T cell receptor binding [GO:0042608]
|
PF07714;PF00017;PF00018;
|
3.30.505.10;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, SRC subfamily
|
PTM: Autophosphorylated on Tyr-394, increasing enzymatic activity, this site is dephosphorylated by PTN22. Phosphorylated on Tyr-505 by CSK, decreasing activity. Dephosphorylated by PTPRC/CD45. Dephosphorylation at Tyr-394 by PTPN2 negatively regulates T-cell receptor signaling. {ECO:0000269|PubMed:1639064, ECO:0000269|PubMed:22080863, ECO:0000269|PubMed:8139546, ECO:0000269|PubMed:8631775}.; PTM: Myristoylation is required prior to palmitoylation. {ECO:0000250}.; PTM: Palmitoylation regulates association with the plasma membrane and could be mediated by ZDHHC2. {ECO:0000269|PubMed:22034844}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:22034844}; Lipid-anchor {ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:22034844}; Cytoplasmic side {ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:22034844}. Cytoplasm, cytosol {ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:22034844}. Note=Present in lipid rafts in an inactive form. {ECO:0000269|PubMed:12218089}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: Non-receptor tyrosine-protein kinase that plays an essential role in the selection and maturation of developing T-cells in the thymus and in the function of mature T-cells. Plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways. Constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, thereby recruiting the associated LCK protein to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosine residues within the immunoreceptor tyrosine-based activation motifs (ITAM) of the cytoplasmic tails of the TCR-gamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. Once stimulated, the TCR recruits the tyrosine kinase ZAP70, that becomes phosphorylated and activated by LCK. Following this, a large number of signaling molecules are recruited, ultimately leading to lymphokine production. LCK also contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, which leads to hyperphosphorylation and activation of LCK. Also plays a role in the IL2 receptor-linked signaling pathway that controls the T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR. Phosphorylates other substrates including RUNX3, PTK2B/PYK2, the microtubule-associated protein MAPT, RHOH or TYROBP. Interacts with FYB2 (PubMed:27335501). {ECO:0000269|PubMed:16339550, ECO:0000269|PubMed:16709819, ECO:0000269|PubMed:20028775, ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:20851766, ECO:0000269|PubMed:21269457, ECO:0000269|PubMed:22080863, ECO:0000269|PubMed:27335501}.
|
Homo sapiens (Human)
|
P06240
|
LCK_MOUSE
|
MGCVCSSNPEDDWMENIDVCENCHYPIVPLDSKISLPIRNGSEVRDPLVTYEGSLPPASPLQDNLVIALHSYEPSHDGDLGFEKGEQLRILEQSGEWWKAQSLTTGQEGFIPFNFVAKANSLEPEPWFFKNLSRKDAERQLLAPGNTHGSFLIRESESTAGSFSLSVRDFDQNQGEVVKHYKIRNLDNGGFYISPRITFPGLHDLVRHYTNASDGLCTKLSRPCQTQKPQKPWWEDEWEVPRETLKLVERLGAGQFGEVWMGYYNGHTKVAVKSLKQGSMSPDAFLAEANLMKQLQHPRLVRLYAVVTQEPIYIITEYMENGSLVDFLKTPSGIKLNVNKLLDMAAQIAEGMAFIEEQNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMVRPDNCPEELYHLMMLCWKERPEDRPTFDYLRSVLDDFFTATEGQYQPQP
|
2.7.10.2
| null |
activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; B cell receptor signaling pathway [GO:0050853]; cell surface receptor signaling pathway [GO:0007166]; gamma-delta T cell differentiation [GO:0042492]; innate immune response [GO:0045087]; intracellular zinc ion homeostasis [GO:0006882]; phosphorylation [GO:0016310]; positive regulation of gamma-delta T cell differentiation [GO:0045588]; positive regulation of gene expression [GO:0010628]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of T cell activation [GO:0050870]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; positive regulation of uterine smooth muscle contraction [GO:0070474]; regulation of regulatory T cell differentiation [GO:0045589]; regulation of T cell receptor signaling pathway [GO:0050856]; release of sequestered calcium ion into cytosol [GO:0051209]; response to hydrogen peroxide [GO:0042542]; response to mechanical stimulus [GO:0009612]; response to metal ion [GO:0010038]; response to xenobiotic stimulus [GO:0009410]; T cell differentiation [GO:0030217]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
cell-cell junction [GO:0005911]; cytosol [GO:0005829]; endocytic vesicle [GO:0030139]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; glutamatergic synapse [GO:0098978]; immunological synapse [GO:0001772]; membrane raft [GO:0045121]; pericentriolar material [GO:0000242]; postsynaptic specialization, intracellular component [GO:0099091]
|
antigen binding [GO:0003823]; ATP binding [GO:0005524]; CD4 receptor binding [GO:0042609]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein antigen binding [GO:1990405]; protein phosphatase binding [GO:0019903]; protein serine/threonine phosphatase activity [GO:0004722]; protein tyrosine kinase activity [GO:0004713]; protein-containing complex binding [GO:0044877]; SH2 domain binding [GO:0042169]; signaling receptor binding [GO:0005102]
|
PF07714;PF00017;PF00018;
|
3.30.505.10;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, SRC subfamily
|
PTM: Autophosphorylated on Tyr-394, increasing enzymatic activity, this site is dephosphorylated by PTN22. Phosphorylated on Tyr-505 by CSK, decreasing activity. Dephosphorylated by PTPRC/CD45. Dephosphorylation at Tyr-394 by PTPN2 negatively regulates T-cells differentiation (By similarity). {ECO:0000250}.; PTM: Myristoylation is required prior to palmitoylation. {ECO:0000269|PubMed:7980442, ECO:0000269|PubMed:8413237}.; PTM: Palmitoylation regulates association with the plasma membrane and could be mediated by ZDHHC2. {ECO:0000250|UniProtKB:P06239}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12218089}; Lipid-anchor {ECO:0000269|PubMed:12218089}; Cytoplasmic side {ECO:0000269|PubMed:12218089}. Cytoplasm, cytosol {ECO:0000269|PubMed:12218089}. Note=Present in lipid rafts in an inactive form. {ECO:0000250|UniProtKB:P06239}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: Non-receptor tyrosine-protein kinase that plays an essential role in the selection and maturation of developing T-cells in the thymus and in the function of mature T-cells. Plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways. Constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, thereby recruiting the associated LCK protein to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosine residues within the immunoreceptor tyrosine-based activation motifs (ITAM) of the cytoplasmic tails of the TCR-gamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. Once stimulated, the TCR recruits the tyrosine kinase ZAP70, that becomes phosphorylated and activated by LCK. Following this, a large number of signaling molecules are recruited, ultimately leading to lymphokine production. LCK also contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, which leads to hyperphosphorylation and activation of LCK. Also plays a role in the IL2 receptor-linked signaling pathway that controls the T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR. Phosphorylates other substrates including RUNX3, PTK2B/PYK2, the microtubule-associated protein MAPT, RHOH or TYROBP (By similarity). Interacts with UNC119; this interaction plays a crucial role in activation of LCK (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
P06241
|
FYN_HUMAN
|
MGCVQCKDKEATKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHAAGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQSFLEDYFTATEPQYQPGENL
|
2.7.10.2
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
|
activated T cell proliferation [GO:0050798]; adaptive immune response [GO:0002250]; axon guidance [GO:0007411]; calcium ion transport [GO:0006816]; cell differentiation [GO:0030154]; cellular response to amyloid-beta [GO:1904646]; cellular response to glycine [GO:1905430]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to L-glutamate [GO:1905232]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; cellular response to transforming growth factor beta stimulus [GO:0071560]; dendrite morphogenesis [GO:0048813]; dendritic spine maintenance [GO:0097062]; detection of mechanical stimulus involved in sensory perception of pain [GO:0050966]; ephrin receptor signaling pathway [GO:0048013]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; feeding behavior [GO:0007631]; forebrain development [GO:0030900]; G protein-coupled glutamate receptor signaling pathway [GO:0007216]; gene expression [GO:0010467]; heart process [GO:0003015]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; learning [GO:0007612]; leukocyte migration [GO:0050900]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of dendritic spine maintenance [GO:1902951]; negative regulation of gene expression [GO:0010629]; negative regulation of hydrogen peroxide biosynthetic process [GO:0010730]; negative regulation of inflammatory response to antigenic stimulus [GO:0002862]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of protein ubiquitination [GO:0031397]; neuron migration [GO:0001764]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of cysteine-type endopeptidase activity [GO:2001056]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein localization to membrane [GO:1905477]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; protein catabolic process [GO:0030163]; protein phosphorylation [GO:0006468]; protein ubiquitination [GO:0016567]; regulation of calcium ion import across plasma membrane [GO:1905664]; regulation of cell shape [GO:0008360]; regulation of glutamate receptor signaling pathway [GO:1900449]; regulation of peptidyl-tyrosine phosphorylation [GO:0050730]; response to amyloid-beta [GO:1904645]; response to ethanol [GO:0045471]; response to singlet oxygen [GO:0000304]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; T cell costimulation [GO:0031295]; T cell receptor signaling pathway [GO:0050852]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]
|
actin filament [GO:0005884]; cell body [GO:0044297]; cytosol [GO:0005829]; dendrite [GO:0030425]; endosome [GO:0005768]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; glial cell projection [GO:0097386]; membrane raft [GO:0045121]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear endoplasmic reticulum [GO:0097038]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; Schaffer collateral - CA1 synapse [GO:0098685]
|
alpha-tubulin binding [GO:0043014]; ATP binding [GO:0005524]; disordered domain specific binding [GO:0097718]; enzyme binding [GO:0019899]; ephrin receptor binding [GO:0046875]; growth factor receptor binding [GO:0070851]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phospholipase activator activity [GO:0016004]; phospholipase binding [GO:0043274]; protein tyrosine kinase activity [GO:0004713]; scaffold protein binding [GO:0097110]; signaling receptor binding [GO:0005102]; tau protein binding [GO:0048156]; tau-protein kinase activity [GO:0050321]; transmembrane transporter binding [GO:0044325]; type 5 metabotropic glutamate receptor binding [GO:0031802]
|
PF07714;PF00017;PF00018;
|
3.30.505.10;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, SRC subfamily
|
PTM: Autophosphorylated at Tyr-420 (By similarity). Phosphorylation on the C-terminal tail at Tyr-531 by CSK maintains the enzyme in an inactive state (PubMed:1699196). PTPRC/CD45 dephosphorylates Tyr-531 leading to activation (PubMed:1533589). Ultraviolet B (UVB) strongly increase phosphorylation at Thr-12 and kinase activity, and promotes translocation from the cytoplasm to the nucleus (PubMed:15537652). Dephosphorylation at Tyr-420 by PTPN2 negatively regulates T-cell receptor signaling (PubMed:22080863). Phosphorylated at tyrosine residues, which can be enhanced by NTN1 (By similarity). {ECO:0000250|UniProtKB:P39688, ECO:0000269|PubMed:10196263, ECO:0000269|PubMed:1533589, ECO:0000269|PubMed:15537652, ECO:0000269|PubMed:1699196, ECO:0000269|PubMed:22080863}.; PTM: Palmitoylated. Palmitoylation at Cys-3 and Cys-6, probably by ZDHHC21, regulates subcellular location. {ECO:0000250|UniProtKB:P39688}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15537652, ECO:0000269|PubMed:8206991}. Nucleus {ECO:0000269|PubMed:15537652}. Cell membrane {ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:8206991}. Perikaryon {ECO:0000250|UniProtKB:Q62844}. Note=Present and active in lipid rafts (PubMed:12218089). Palmitoylation is crucial for proper trafficking (PubMed:8206991). {ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:8206991}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL1 and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1. In mast cells, phosphorylates CLNK after activation of immunoglobulin epsilon receptor signaling (By similarity). {ECO:0000250|UniProtKB:P39688, ECO:0000269|PubMed:11005864, ECO:0000269|PubMed:11162638, ECO:0000269|PubMed:11536198, ECO:0000269|PubMed:12788081, ECO:0000269|PubMed:14707117, ECO:0000269|PubMed:14761972, ECO:0000269|PubMed:15536091, ECO:0000269|PubMed:15557120, ECO:0000269|PubMed:16387660, ECO:0000269|PubMed:16841086, ECO:0000269|PubMed:17194753, ECO:0000269|PubMed:18056706, ECO:0000269|PubMed:18258597, ECO:0000269|PubMed:19179337, ECO:0000269|PubMed:19652227, ECO:0000269|PubMed:20028775, ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:22080863, ECO:0000269|PubMed:7568038, ECO:0000269|PubMed:7822789}.
|
Homo sapiens (Human)
|
P06242
|
KIN28_YEAST
|
MKVNMEYTKEKKVGEGTYAVVYLGCQHSTGRKIAIKEIKTSEFKDGLDMSAIREVKYLQEMQHPNVIELIDIFMAYDNLNLVLEFLPTDLEVVIKDKSILFTPADIKAWMLMTLRGVYHCHRNFILHRDLKPNNLLFSPDGQIKVADFGLARAIPAPHEILTSNVVTRWYRAPELLFGAKHYTSAIDIWSVGVIFAELMLRIPYLPGQNDVDQMEVTFRALGTPTDRDWPEVSSFMTYNKLQIYPPPSRDELRKRFIAASEYALDFMCGMLTMNPQKRWTAVQCLESDYFKELPPPSDPSSIKIRN
|
2.7.11.23
| null |
7-methylguanosine mRNA capping [GO:0006370]; cell cycle [GO:0007049]; cell division [GO:0051301]; cellular response to nitrogen starvation [GO:0006995]; nucleotide-excision repair [GO:0006289]; positive regulation of Atg1/ULK1 kinase complex assembly [GO:1905866]; positive regulation of autophagy [GO:0010508]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; protein phosphorylation [GO:0006468]; recruitment of 3'-end processing factors to RNA polymerase II holoenzyme complex [GO:0034402]; recruitment of mRNA capping enzyme to RNA polymerase II holoenzyme complex [GO:0036031]; transcription by RNA polymerase I [GO:0006360]; transcription by RNA polymerase II [GO:0006366]; transcription initiation at RNA polymerase II promoter [GO:0006367]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; transcription factor TFIIH holo complex [GO:0005675]; transcription factor TFIIK complex [GO:0070985]
|
ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein kinase activity [GO:0004672]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily
|
PTM: Phosphorylation of Thr-162 regulates the affinity of interaction between CCL1, KIN28 and TFB3. Thr-162 phosphorylation does not vary through the cell cycle and is necessary for full kinase activity. {ECO:0000269|PubMed:10373527, ECO:0000269|PubMed:11839796, ECO:0000269|PubMed:9774652}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
|
CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23;
| null | null | null | null |
FUNCTION: Catalytic component of the TFIIK complex (KIN28-CCL1 dimer) which is the protein kinase component of transcription factor IIH (TFIIH) and phosphorylates the C-terminal domain of RNA polymerase II during transition from transcription to elongation after preinitiation complex (PIC) formation, thereby positively regulating transcription. TFIIH (or factor B) is essential for both basal and activated transcription, and is involved in nucleotide excision repair (NER) of damaged DNA. TFIIH has DNA-dependent ATPase activity and is essential for polymerase II transcription in vitro. Essential for cell proliferation. {ECO:0000269|PubMed:10594013}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06243
|
CDC7_YEAST
|
MTSKTKNIDDIPPEIKEEMIQLYHDLPGIENEYKLIDKIGEGTFSSVYKAKDITGKITKKFASHFWNYGSNYVALKKIYVTSSPQRIYNELNLLYIMTGSSRVAPLCDAKRVRDQVIAVLPYYPHEEFRTFYRDLPIKGIKKYIWELLRALKFVHSKGIIHRDIKPTNFLFNLELGRGVLVDFGLAEAQMDYKSMISSQNDYDNYANTNHDGGYSMRNHEQFCPCIMRNQYSPNSHNQTPPMVTIQNGKVVHLNNVNGVDLTKGYPKNETRRIKRANRAGTRGFRAPEVLMKCGAQSTKIDIWSVGVILLSLLGRRFPMFQSLDDADSLLELCTIFGWKELRKCAALHGLGFEASGLIWDKPNGYSNGLKEFVYDLLNKECTIGTFPEYSVAFETFGFLQQELHDRMSIEPQLPDPKTNMDAVDAYELKKYQEEIWSDHYWCFQVLEQCFEMDPQKRSSAEDLLKTPFFNELNENTYLLDGESTDEDDVVSSSEADLLDKDVLLISE
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
cell division [GO:0051301]; DNA replication initiation [GO:0006270]; double-strand break repair via break-induced replication [GO:0000727]; mitotic DNA damage checkpoint signaling [GO:0044773]; mitotic DNA replication checkpoint signaling [GO:0033314]; mitotic DNA replication preinitiation complex assembly [GO:1902977]; negative regulation of exit from mitosis [GO:0001100]; phosphorylation [GO:0016310]; positive regulation of kinetochore assembly [GO:1905561]; positive regulation of meiosis I [GO:0060903]; positive regulation of meiotic DNA double-strand break formation [GO:1903343]; positive regulation of meiotic DNA double-strand break formation involved in reciprocal meiotic recombination [GO:1905263]; positive regulation of spindle attachment to meiosis I kinetochore [GO:1904968]; premeiotic DNA replication [GO:0006279]; protein-containing complex localization [GO:0031503]; signal transduction [GO:0007165]
|
centrosome [GO:0005813]; chromatin [GO:0000785]; chromosome, centromeric region [GO:0000775]; Dbf4-dependent protein kinase complex [GO:0031431]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, CDC7 subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase. Needed for the initiation of DNA synthesis during mitosis as well as for synaptonemal complex formation and commitment to recombination during meiosis. Required for HTA1-HTB1 locus transcription repression. {ECO:0000269|PubMed:1865880}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06244
|
KAPA_YEAST
|
MSTEEQNGGGQKSLDDRQGEESQKGETSERETTATESGNESKSVEKEGGETQEKPKQPHVTYYNEEQYKQFIAQARVTSGKYSLQDFQILRTLGTGSFGRVHLIRSRHNGRYYAMKVLKKEIVVRLKQVEHTNDERLMLSIVTHPFIIRMWGTFQDAQQIFMIMDYIEGGELFSLLRKSQRFPNPVAKFYAAEVCLALEYLHSKDIIYRDLKPENILLDKNGHIKITDFGFAKYVPDVTYTLCGTPDYIAPEVVSTKPYNKSIDWWSFGILIYEMLAGYTPFYDSNTMKTYEKILNAELRFPPFFNEDVKDLLSRLITRDLSQRLGNLQNGTEDVKNHPWFKEVVWEKLLSRNIETPYEPPIQQGQGDTSQFDKYPEEDINYGVQGEDPYADLFRDF
|
2.7.11.11
| null |
cell cycle [GO:0007049]; cell division [GO:0051301]; negative regulation of cytoplasmic mRNA processing body assembly [GO:0010607]; phosphorylation [GO:0016310]; protein kinase A signaling [GO:0010737]; Ras protein signal transduction [GO:0007265]; regulation of macroautophagy [GO:0016241]
|
cAMP-dependent protein kinase complex [GO:0005952]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, cAMP subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.11;
| null | null | null | null | null |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06245
|
KAPB_YEAST
|
MEFVAERAQPVGQTIQQQNVNTYGQGVLQPHHDLQQRQQQQQQRQHQQLLTSQLPQKSLVSKGKYTLHDFQIMRTLGTGSFGRVHLVRSVHNGRYYAIKVLKKQQVVKMKQVEHTNDERRMLKLVEHPFLIRMWGTFQDARNIFMVMDYIEGGELFSLLRKSQRFPNPVAKFYAAEVILALEYLHAHNIIYRDLKPENILLDRNGHIKITDFGFAKEVQTVTWTLCGTPDYIAPEVITTKPYNKSVDWWSLGVLIYEMLAGYTPFYDTTPMKTYEKILQGKVVYPPYFHPDVVDLLSKLITADLTRRIGNLQSGSRDIKAHPWFSEVVWERLLAKDIETPYEPPITSGIGDTSLFDQYPEEQLDYGIQGDDPYAEYFQDF
|
2.7.11.11
| null |
invasive growth in response to glucose limitation [GO:0001403]; negative regulation of cytoplasmic mRNA processing body assembly [GO:0010607]; negative regulation of cytoplasmic translation [GO:2000766]; phosphorylation [GO:0016310]; protein kinase A signaling [GO:0010737]; Ras protein signal transduction [GO:0007265]
|
cAMP-dependent protein kinase complex [GO:0005952]; chromatin [GO:0000785]; cytosol [GO:0005829]; nucleus [GO:0005634]; P-body [GO:0000932]
|
AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, cAMP subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.11;
| null | null | null | null | null |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06276
|
CHLE_HUMAN
|
MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCVGL
|
3.1.1.8
| null |
acetylcholine catabolic process [GO:0006581]; choline metabolic process [GO:0019695]; cocaine metabolic process [GO:0050783]; learning [GO:0007612]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of synaptic transmission [GO:0050805]; neuroblast differentiation [GO:0014016]; peptide hormone processing [GO:0016486]; response to alkaloid [GO:0043279]; response to folic acid [GO:0051593]; response to glucocorticoid [GO:0051384]; xenobiotic metabolic process [GO:0006805]
|
blood microparticle [GO:0072562]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nuclear envelope lumen [GO:0005641]; plasma membrane [GO:0005886]
|
acetylcholinesterase activity [GO:0003990]; amyloid-beta binding [GO:0001540]; catalytic activity [GO:0003824]; choline binding [GO:0033265]; cholinesterase activity [GO:0004104]; enzyme binding [GO:0019899]; hydrolase activity, acting on ester bonds [GO:0016788]; identical protein binding [GO:0042802]
|
PF08674;PF00135;
|
3.40.50.1820;
|
Type-B carboxylesterase/lipase family
|
PTM: N-glycosylated. No other PTM detected (PubMed:20946535). The major N-glycan structures are of the complex diantennary type with 1 and 2 N-acetylneuraminic acid molecules (Neu5Ac) making up approximately 33% and 47% of the total N-glycans, respectively. Only low amounts of fucosylated diantennary N-glycans are detected (approximately 2%). Triantennary N-glycans with or without fucose amount to approximately 13%, whereas 5% of the total N-glycans are of the oligomannosidic or hybrid type. {ECO:0000269|PubMed:12869558, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15667209, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:17768338, ECO:0000269|PubMed:18203274, ECO:0000269|PubMed:18975951, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:20946535}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:19542320}.
|
CATALYTIC ACTIVITY: Reaction=an acylcholine + H2O = a carboxylate + choline + H(+); Xref=Rhea:RHEA:21964, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:35287; EC=3.1.1.8; Evidence={ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:19452557};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18 uM for butyrylthiocholine (at 25 degrees Celsius) {ECO:0000269|PubMed:25054547};
| null | null | null |
FUNCTION: Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters. {ECO:0000269|PubMed:19452557, ECO:0000269|PubMed:19542320}.
|
Homo sapiens (Human)
|
P06278
|
AMY_BACLI
|
MKQQKRLYARLLTLLFALIFLLPHSAAAAANLNGTLMQYFEWYMPNDGQHWKRLQNDSAYLAEHGITAVWIPPAYKGTSQADVGYGAYDLYDLGEFHQKGTVRTKYGTKGELQSAIKSLHSRDINVYGDVVINHKGGADATEDVTAVEVDPADRNRVISGEHRIKAWTHFHFPGRGSTYSDFKWHWYHFDGTDWDESRKLNRIYKFQGKAWDWEVSNENGNYDYLMYADIDYDHPDVAAEIKRWGTWYANELQLDGFRLDAVKHIKFSFLRDWVNHVREKTGKEMFTVAEYWQNDLGALENYLNKTNFNHSVFDVPLHYQFHAASTQGGGYDMRKLLNSTVVSKHPLKAVTFVDNHDTQPGQSLESTVQTWFKPLAYAFILTRESGYPQVFYGDMYGTKGDSQREIPALKHKIEPILKARKQYAYGAQHDYFDHHDIVGWTREGDSSVANSGLAALITDGPGGAKRMYVGRQNAGETWHDITGNRSEPVVINSEGWGEFHVNGGSVSIYVQR
|
3.2.1.1
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551}; Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551}; COFACTOR: Name=Na(+); Xref=ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551}; Note=Binds 1 sodium ion per subunit. {ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551};
|
carbohydrate metabolic process [GO:0005975]
|
extracellular space [GO:0005615]
|
alpha-amylase activity [GO:0004556]; calcium ion binding [GO:0005509]
|
PF09154;PF00128;
|
2.40.30.140;3.20.20.80;2.60.40.1180;
|
Glycosyl hydrolase 13 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14632998}.
|
CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:11997021, ECO:0000269|PubMed:12915728, ECO:0000269|PubMed:14632998};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Active up to pH 11.;
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Active up to 100 degrees Celsius.;
| null |
Bacillus licheniformis
|
P06280
|
AGAL_HUMAN
|
MQLRNPELHLGCALALRFLALVSWDIPGARALDNGLARTPTMGWLHWERFMCNLDCQEEPDSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQLANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENLADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIGGPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENTMQMSLKDLL
|
3.2.1.22
| null |
glycoside catabolic process [GO:0016139]; glycosphingolipid catabolic process [GO:0046479]; glycosylceramide catabolic process [GO:0046477]; negative regulation of nitric oxide biosynthetic process [GO:0045019]; negative regulation of nitric-oxide synthase activity [GO:0051001]; oligosaccharide metabolic process [GO:0009311]
|
azurophil granule lumen [GO:0035578]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]
|
alpha-galactosidase activity [GO:0004557]; catalytic activity [GO:0003824]; galactoside binding [GO:0016936]; hydrolase activity [GO:0016787]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102]
|
PF16499;PF17450;
|
3.20.20.70;2.60.40.1180;
|
Glycosyl hydrolase 27 family
| null |
SUBCELLULAR LOCATION: Lysosome.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22; Evidence={ECO:0000269|PubMed:26415523, ECO:0000269|PubMed:27211852}; CATALYTIC ACTIVITY: Reaction=a globoside Gb3Cer (d18:1(4E)) + H2O = a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + D-galactose; Xref=Rhea:RHEA:21112, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377, ChEBI:CHEBI:17950, ChEBI:CHEBI:18313; Evidence={ECO:0000269|PubMed:10838196, ECO:0000269|PubMed:8804427}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21113; Evidence={ECO:0000305|PubMed:10838196, ECO:0000305|PubMed:8804427}; CATALYTIC ACTIVITY: Reaction=a globoside Gb3Cer + H2O = a beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + D-galactose; Xref=Rhea:RHEA:48020, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377, ChEBI:CHEBI:79208, ChEBI:CHEBI:88154; Evidence={ECO:0000269|PubMed:10838196, ECO:0000269|PubMed:8804427}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48021; Evidence={ECO:0000305|PubMed:10838196, ECO:0000305|PubMed:8804427};
| null | null | null | null |
FUNCTION: Catalyzes the hydrolysis of glycosphingolipids and participates in their degradation in the lysosome. {ECO:0000269|PubMed:10838196, ECO:0000269|PubMed:8804427}.
|
Homo sapiens (Human)
|
P06281
|
RENI1_MOUSE
|
MDRRRMPLWALLLLWSPCTFSLPTRTATFERIPLKKMPSVREILEERGVDMTRLSAEWGVFTKRPSLTNLTSPVVLTNYLNTQYYGEIGIGTPPQTFKVIFDTGSANLWVPSTKCSRLYLACGIHSLYESSDSSSYMENGSDFTIHYGSGRVKGFLSQDSVTVGGITVTQTFGEVTELPLIPFMLAKFDGVLGMGFPAQAVGGVTPVFDHILSQGVLKEEVFSVYYNRGSHLLGGEVVLGGSDPQHYQGNFHYVSISKTDSWQITMKGVSVGSSTLLCEEGCAVVVDTGSSFISAPTSSLKLIMQALGAKEKRIEEYVVNCSQVPTLPDISFDLGGRAYTLSSTDYVLQYPNRRDKLCTLALHAMDIPPPTGPVWVLGATFIRKFYTEFDRHNNRIGFALAR
|
3.4.23.15
| null |
amyloid-beta metabolic process [GO:0050435]; angiotensin maturation [GO:0002003]; cell maturation [GO:0048469]; cellular response to xenobiotic stimulus [GO:0071466]; drinking behavior [GO:0042756]; hormone-mediated signaling pathway [GO:0009755]; juxtaglomerular apparatus development [GO:0072051]; male gonad development [GO:0008584]; mesonephros development [GO:0001823]; regulation of blood pressure [GO:0008217]; regulation of blood volume by renin-angiotensin [GO:0002016]; regulation of MAPK cascade [GO:0043408]; renin-angiotensin regulation of aldosterone production [GO:0002018]; response to cAMP [GO:0051591]; response to cGMP [GO:0070305]; response to immobilization stress [GO:0035902]; response to lipopolysaccharide [GO:0032496]; response to organic substance [GO:0010033]; response to xenobiotic stimulus [GO:0009410]
|
apical part of cell [GO:0045177]; extracellular space [GO:0005615]; membrane [GO:0016020]
|
aspartic-type endopeptidase activity [GO:0004190]; endopeptidase activity [GO:0004175]; insulin-like growth factor receptor binding [GO:0005159]; signaling receptor binding [GO:0005102]
|
PF07966;PF00026;
|
2.40.70.10;
|
Peptidase A1 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9030738}. Membrane {ECO:0000250|UniProtKB:P00797}. Note=Associated to membranes via binding to ATP6AP2. {ECO:0000250|UniProtKB:P00797}.
|
CATALYTIC ACTIVITY: Reaction=Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I.; EC=3.4.23.15; Evidence={ECO:0000250|UniProtKB:P00797};
| null | null | null | null |
FUNCTION: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney. {ECO:0000269|PubMed:6370686}.
|
Mus musculus (Mouse)
|
P06292
|
RBL_MARPO
|
MSPQTETKAGVGFKAGVKDYRLTYYTPDYETKDTDILAAFRMTPQPGVPAEEAGNAVAAESSTGTWTTVWTDGLTNLDRYKGRCYDIDPVPGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYTKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFVAEAIYKSQAETGEIKGHYLNATAGTCEEMLKRAACARELGVPIVMHDYLTGGFTANTSLAFYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHAGTVVGKLEGDRQVTLGFVDLLRDDYIEKDRSRGIYFTQDWVSLPGVFPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVSLEACVQARNEGRDLAREGNEIIREACKWSPELSAACEIWKEIKFEFDIIDTL
|
4.1.1.39
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
|
photorespiration [GO:0009853]; reductive pentose-phosphate cycle [GO:0019253]
|
chloroplast [GO:0009507]
|
magnesium ion binding [GO:0000287]; monooxygenase activity [GO:0004497]; ribulose-bisphosphate carboxylase activity [GO:0016984]
|
PF00016;PF02788;
|
3.20.20.110;3.30.70.150;
|
RuBisCO large chain family, Type I subfamily
|
PTM: The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Plastid, chloroplast.
|
CATALYTIC ACTIVITY: Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, ChEBI:CHEBI:58272; EC=4.1.1.39; CATALYTIC ACTIVITY: Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate + 2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033, ChEBI:CHEBI:58272;
| null | null | null | null |
FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
|
Marchantia polymorpha (Common liverwort) (Marchantia aquatica)
|
P06298
|
COLI1_XENLA
|
MFRPLWGCFLAILGICIFHIGEVQSQCWESSRCADLSSEDGVLECIKACKTDLSAESPVFPGNGHLQPLSESIRKYVMTHFRWNKFGRRNSTGNDGSNTGYKREDISSYPVFSLFPLSDQNAPGDNMEEEPLDRQENKRAYSMEHFRWGKPVGRKRRPIKVYPNGVEEESAESYPMELRRELSLELDYPEIDLDEDIEDNEVESALTKKNGNYRMHHFRWGSPPKDKRYGGFMTPERSQTPLMTLFKNAIIKNSHKKGQ
| null | null |
neuropeptide signaling pathway [GO:0007218]; regulation of corticosterone secretion [GO:2000852]
|
extracellular space [GO:0005615]; secretory granule [GO:0030141]
|
G protein-coupled receptor binding [GO:0001664]; neuropeptide hormone activity [GO:0005184]
|
PF00976;PF08384;PF08035;
| null |
POMC family
|
PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01193}. Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored in separate granules in hypothalamic POMC neurons, suggesting that secretion may be under the control of different regulatory mechanisms. {ECO:0000250|UniProtKB:P01193}.
| null | null | null | null | null |
FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release cortisol.; FUNCTION: [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Beta-endorphin]: Endogenous orexigenic opiate.; FUNCTION: [Met-enkephalin]: Endogenous opiate.
|
Xenopus laevis (African clawed frog)
|
P06299
|
COLI2_XENLA
|
MFRPTGGCSLAILGVFIFHIGEVQSQCWESSRCADLSSEDGILECIKACKMDLSAESPVFPGNGHLQPLSESIRKYVMTHFRWNKFGRRNNTGNDGSSGGYKREDISNYPVLNLFPSSDNQNAQGDNMEEEPMDRQENKRAYSMEHFRWGKPVGRKRRPIKVYPNGVEEESAESFPMELRRELSLELDYPEIDLDEDIEDNEVERALTKKNGNYRMHHFRWGSPPKDKRYGGFMTPERSQTPLMTLFKNAIIKNTHKKGL
| null | null |
neuropeptide signaling pathway [GO:0007218]; regulation of corticosterone secretion [GO:2000852]
|
extracellular space [GO:0005615]; secretory granule [GO:0030141]
|
G protein-coupled receptor binding [GO:0001664]; neuropeptide hormone activity [GO:0005184]
|
PF00976;PF08384;PF08035;
| null |
POMC family
|
PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01193}. Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored in separate granules in hypothalamic POMC neurons, suggesting that secretion may be under the control of different regulatory mechanisms. {ECO:0000250|UniProtKB:P01193}.
| null | null | null | null | null |
FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release cortisol.; FUNCTION: [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin by increasing melanin production in melanocytes.; FUNCTION: [Beta-endorphin]: Endogenous orexigenic opiate.; FUNCTION: [Met-enkephalin]: Endogenous opiate.
|
Xenopus laevis (African clawed frog)
|
P06300
|
PDYN_RAT
|
MAWSRLMLAACLLVIPSEVAADCLSLCSLCAVRTQDGPHPINPLICSLECQDLVPPSEEWETCRGFWSFLTLTASGLHGKDDLENEVALEEGYTALTKLLEPLLKELEKGQLLTSVSEEKLRGLSSRFGNGRESELLGTDLMNDEAAQAGTLHFNEEDLRKQAKRYGGFLRKYPKRSSEMTGDEDRGQDGDQVGHEDLYKRYGGFLRRIRPKLKWDNQKRYGGFLRRQFKVVTRSQENPNTYSEDLDV
| null | null |
chemical synaptic transmission [GO:0007268]; neuropeptide signaling pathway [GO:0007218]; response to immobilization stress [GO:0035902]; response to nicotine [GO:0035094]; sensory perception [GO:0007600]
|
axon terminus [GO:0043679]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; dense core granule [GO:0031045]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuronal cell body [GO:0043025]; neuronal dense core vesicle [GO:0098992]; neuronal dense core vesicle lumen [GO:0099013]; plasma membrane [GO:0005886]; synaptic vesicle [GO:0008021]
|
opioid peptide activity [GO:0001515]; opioid receptor binding [GO:0031628]
|
PF01160;
| null |
Opioid neuropeptide precursor family
|
PTM: The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity). {ECO:0000250}.; FUNCTION: Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opioid activity, it is 700 times more potent than Leu-enkephalin (By similarity). {ECO:0000250}.; FUNCTION: Leumorphin has a typical opioid activity and may have anti-apoptotic effect. {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
P06302
|
PTMA_RAT
|
MSDAAVDTSSEITTKDLKEKKEVVEEAENGRDAPANGNAQNEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAPTGKRVAEDDEDDDVETKKQKKTDEDD
| null | null |
cell differentiation [GO:0030154]; chromatin organization [GO:0006325]; negative regulation of apoptotic process [GO:0043066]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of transcription by RNA polymerase II [GO:0045944]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor binding [GO:0140297]; histone binding [GO:0042393]; histone chaperone activity [GO:0140713]; ion binding [GO:0043167]
|
PF03247;
| null |
Pro/parathymosin family
|
PTM: Covalently linked to a small RNA of about 20 nucleotides. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections.
|
Rattus norvegicus (Rat)
|
P06307
|
CCKN_HUMAN
|
MNSGVCLCVLMAVLAAGALTQPVPPADPAGSGLQRAEEAPRRQLRVSQRTDGESRAHLGALLARYIQQARKAPSGRMSIVKNLQNLDPSHRISDRDYMGWMDFGRRSAEEYEYPS
| null | null |
axonogenesis [GO:0007409]; digestion [GO:0007586]; eating behavior [GO:0042755]; neuron migration [GO:0001764]; signal transduction [GO:0007165]
|
axon [GO:0030424]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
hormone activity [GO:0005179]; neuropeptide hormone activity [GO:0005184]; peptide hormone receptor binding [GO:0051428]
|
PF00918;
| null |
Gastrin/cholecystokinin family
|
PTM: The precursor is cleaved by proteases to produce a number of active cholecystokinins.; PTM: [Cholecystokinin-5]: The precursor is cleaved by ACE, which removes the Gly-Arg-Arg peptide at the C-terminus, leading to mature hormone. {ECO:0000269|PubMed:10336644, ECO:0000269|PubMed:9371719}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:37453717}.
| null | null | null | null | null |
FUNCTION: This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion. {ECO:0000250|UniProtKB:Q9TS44}.
|
Homo sapiens (Human)
|
P06312
|
KV401_HUMAN
|
MVLQTQVFISLLLWISGAYGDIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSTP
| null | null |
adaptive immune response [GO:0002250]; immune response [GO:0006955]
|
blood microparticle [GO:0072562]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; immunoglobulin complex [GO:0019814]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]
|
PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
| null | null | null | null | null |
FUNCTION: V segment of the variable domain of immunoglobulins light chain that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
|
Homo sapiens (Human)
|
P06332
|
CD4_MOUSE
|
MCRAISLRRLLLLLLQLSQLLAVTQGKTLVLGKEGESAELPCESSQKKITVFTWKFSDQRKILGQHGKGVLIRGGSPSQFDRFDSKKGAWEKGSFPLIINKLKMEDSQTYICELENRKEEVELWVFKVTFSPGTSLLQGQSLTLTLDSNSKVSNPLTECKHKKGKVVSGSKVLSMSNLRVQDSDFWNCTVTLDQKKNWFGMTLSVLGFQSTAITAYKSEGESAEFSFPLNFAEENGWGELMWKAEKDSFFQPWISFSIKNKEVSVQKSTKDLKLQLKETLPLTLKIPQVSLQFAGSGNLTLTLDKGTLHQEVNLVVMKVAQLNNTLTCEVMGPTSPKMRLTLKQENQEARVSEEQKVVQVVAPETGLWQCLLSEGDKVKMDSRIQVLSRGVNQTVFLACVLGGSFGFLGFLGLCILCCVRCRHQQRQAARMSQIKRLLSEKKTCQCPHRMQKSHNLI
| null | null |
adaptive immune response [GO:0002250]; calcium-mediated signaling [GO:0019722]; cell adhesion [GO:0007155]; cell surface receptor signaling pathway [GO:0007166]; cellular response to granulocyte macrophage colony-stimulating factor stimulus [GO:0097011]; defense response to Gram-negative bacterium [GO:0050829]; helper T cell enhancement of adaptive immune response [GO:0035397]; interleukin-15-mediated signaling pathway [GO:0035723]; macrophage differentiation [GO:0030225]; maintenance of protein location in cell [GO:0032507]; positive regulation of calcium ion transport into cytosol [GO:0010524]; positive regulation of calcium-mediated signaling [GO:0050850]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of monocyte differentiation [GO:0045657]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of T cell activation [GO:0050870]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of viral entry into host cell [GO:0046598]; T cell activation [GO:0042110]; T cell differentiation [GO:0030217]; T cell selection [GO:0045058]
|
cell surface [GO:0009986]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; external side of plasma membrane [GO:0009897]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]
|
coreceptor activity [GO:0015026]; immunoglobulin binding [GO:0019865]; interleukin-16 binding [GO:0042011]; interleukin-16 receptor activity [GO:0042012]; MHC class II protein binding [GO:0042289]; MHC class II protein complex binding [GO:0023026]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein tyrosine kinase binding [GO:1990782]; signaling receptor binding [GO:0005102]; zinc ion binding [GO:0008270]
|
PF05790;PF09191;PF00047;PF12104;
|
2.60.40.10;1.20.5.900;
| null |
PTM: Palmitoylation and association with LCK contribute to the enrichment of CD4 in lipid rafts. {ECO:0000250|UniProtKB:P01730}.; PTM: Phosphorylated by PKC; phosphorylation plays an important role for CD4 internalization. {ECO:0000269|PubMed:2512251}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01730}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01730}.
| null | null | null | null | null |
FUNCTION: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are derived from extracellular proteins while class I peptides are derived from cytosolic proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class II presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of T-helper cells. In other cells such as macrophages or NK cells, plays a role in differentiation/activation, cytokine expression and cell migration in a TCR/LCK-independent pathway. Participates in the development of T-helper cells in the thymus and triggers the differentiation of monocytes into functional mature macrophages. {ECO:0000250|UniProtKB:P01730, ECO:0000269|PubMed:16709847, ECO:0000269|PubMed:1832488, ECO:0000269|PubMed:2784195, ECO:0000269|PubMed:3262426}.
|
Mus musculus (Mouse)
|
P06339
|
HA15_MOUSE
|
MLLFAHLLQLLVSATVPTQSSPHSLRYFTTAVSRPGLGEPRFIIVGYVDDTQFVRFDSDAENPRMEPRARWIEQEGPEYWERETWKARDMGRNFRVNLRTLLGYYNQSNDESHTLQWMYGCDVGPDGRLLRGYCQEAYDGQDYISLNEDLRSWTANDIASQISKHKSEAVDEAHQQRAYLQGPCVEWLHRYLRLGNETLQRSDPPKAHVTHHPRSEDEVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWAAVVVPLGKEQYYTCHVYHEGLPEPLTLRWEPPPSTVSNMVIIAVLVVLGAVIILGAVVAFVMKRRRHIGVKGCYAHVLGSKSFQTSDWPQKA
| null | null |
antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib via ER pathway, TAP-dependent [GO:0002489]; immune response [GO:0006955]; inner ear development [GO:0048839]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; T cell mediated cytotoxicity [GO:0001913]
|
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]
|
peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102]
|
PF07654;PF00129;
|
2.60.40.10;3.30.500.10;
|
MHC class I family
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Involved in the presentation of foreign antigens to the immune system.
|
Mus musculus (Mouse)
|
P06340
|
DOA_HUMAN
|
MALRAGLVLGFHTLMTLLSPQEAGATKADHMGSYGPAFYQSYGASGQFTHEFDEEQLFSVDLKKSEAVWRLPEFGDFARFDPQGGLAGIAAIKAHLDILVERSNRSRAINVPPRVTVLPKSRVELGQPNILICIVDNIFPPVINITWLRNGQTVTEGVAQTSFYSQPDHLFRKFHYLPFVPSAEDVYDCQVEHWGLDAPLLRHWELQVPIPPPDAMETLVCALGLAIGLVGFLVGTVLIIMGTYVSSVPR
| null | null |
adaptive immune response [GO:0002250]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; negative regulation of antigen processing and presentation of peptide antigen via MHC class II [GO:0002587]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of immune response [GO:0050778]; positive regulation of T cell activation [GO:0050870]; regulation of T cell differentiation [GO:0045580]
|
late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; MHC class II protein complex [GO:0042613]; plasma membrane [GO:0005886]
|
MHC class II protein complex binding [GO:0023026]; MHC class II receptor activity [GO:0032395]; peptide antigen binding [GO:0042605]
|
PF07654;PF00993;
|
2.60.40.10;
|
MHC class II family
| null |
SUBCELLULAR LOCATION: Endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Note=Complexes with HLA-DM molecule during intracellular transport and in endosomal/lysosomal compartments. Heterotetramerization is necessary to exit the ER.
| null | null | null | null | null |
FUNCTION: Important modulator in the HLA class II restricted antigen presentation pathway by interaction with the HLA-DM molecule in B-cells. Modifies peptide exchange activity of HLA-DM.
|
Homo sapiens (Human)
|
P06342
|
HB2Q_MOUSE
|
MALQIPSLLLSAAVVVLMVLSSPRTEGGNSERHFVAQLKGECYFTNGTQRIRSVNRYIYNREEWVRFDSDVGEYRAVTELGRPDAEYWNSQPEILERTRAEVDTVCRHNYEGVETHTSLRRLEQPNVAISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDWTFQVLVMLEMTPHQGEVYTCHVEHPSLKSPITVEWRAQSESARSKMLSGIGGCVLGVIFLGLGLFIRHRSQKGPRGPPPAGLLQ
| null | null |
adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; immune response [GO:0006955]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of immune response [GO:0050778]; positive regulation of T cell activation [GO:0050870]
|
cell surface [GO:0009986]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; MHC class II protein complex [GO:0042613]; multivesicular body [GO:0005771]; plasma membrane [GO:0005886]
|
MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein-containing complex binding [GO:0044877]
|
PF07654;PF00969;
|
2.60.40.10;
|
MHC class II family
|
PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null | null |
Mus musculus (Mouse)
|
P06343
|
HB2K_MOUSE
|
MALQIPSLLLLAAVVVLTVLSSPGTEGGNSERHFVHQFQPFCYFTNGTQRIRLVIRYIYNREEYVRFDSDVGEYRAVTELGRPDAEYWNKQYLERTRAELDTVCRHNYEKTETPTSLRRLEQPSVVISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDWTFQVLVMLEMTPRRGEVYTCHVEHPSLKSPITVEWRAQSESARSKMLSGIGGCVLGVIFLGLGLFIRHRSQKGPRGPPPAGLLQ
| null | null |
adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; immune response [GO:0006955]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of immune response [GO:0050778]; positive regulation of T cell activation [GO:0050870]
|
cell surface [GO:0009986]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; MHC class II protein complex [GO:0042613]; multivesicular body [GO:0005771]; plasma membrane [GO:0005886]
|
MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein-containing complex binding [GO:0044877]
|
PF07654;PF00969;
|
2.60.40.10;
|
MHC class II family
|
PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null | null |
Mus musculus (Mouse)
|
P06345
|
HB2S_MOUSE
|
MALQIPSLLLSAAVVVLMVLSSPGTEGGDSERHFVFQFKGECYFTNGTQRIRSVDRYIYNREEYLRFDSDVGEYRAVTELGRPDAEYYNKQYLEQTRAELDTVCRHNYEGVETHTSLRRLEQPNVVISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLISNGDWTFQVLVMLEMTPRRGEVYTCHVEHPSLKSPITVEWRAQSESARSKMLSGIGGCVLGVIFLGLGLFIRHRSQKGPRGPPPAGLLQ
| null | null |
adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; immune response [GO:0006955]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of immune response [GO:0050778]; positive regulation of T cell activation [GO:0050870]
|
cell surface [GO:0009986]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; MHC class II protein complex [GO:0042613]; multivesicular body [GO:0005771]; plasma membrane [GO:0005886]
|
MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein-containing complex binding [GO:0044877]
|
PF07654;PF00969;
|
2.60.40.10;
|
MHC class II family
|
PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null | null |
Mus musculus (Mouse)
|
P06346
|
HB2F_MOUSE
|
AAVVVLMVLSSPGTEGGNSERHFVSQFKGECYFTNGTQRIRSVDRYIYNREEYLRFDSDVGEYRAVTELGRSDAEYYNKQYLERTRAELDTVCRHNYEGVETPTSLRRLEQPNVVISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDWTFQVLVMLEMAPRRGEVYTCHVEHPSLKSPITVEWRAQSESARSKMLSGIGGCVLGVIFLGLGLFIRYRSQKGPRGPPPAGLLQ
| null | null |
adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; immune response [GO:0006955]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of immune response [GO:0050778]; positive regulation of T cell activation [GO:0050870]
|
cell surface [GO:0009986]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; MHC class II protein complex [GO:0042613]; multivesicular body [GO:0005771]; plasma membrane [GO:0005886]
|
MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein-containing complex binding [GO:0044877]
|
PF07654;PF00969;
|
2.60.40.10;
|
MHC class II family
|
PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null | null |
Mus musculus (Mouse)
|
P06349
|
H1T_RAT
|
MSETAPAASSTLVPAPVEKPATKRRGKKPGMATARKPRGFSVSKLIPEALSMSQERAGMSLAALKKALAAAGYDVEKNNSRIKLALKRLVNKGVLVQTKGTGASGSFKLSKKAASGNDKGKGKKSASAKAKKLGLSRASRSPKSSKTKVVKKPKATPTKGSGSRRKTKGAKGLQQRKSPAKARATNSNSGKSKMVMQKTDLRKAAGRK
| null | null |
binding of sperm to zona pellucida [GO:0007339]; cell differentiation [GO:0030154]; chromosome condensation [GO:0030261]; flagellated sperm motility [GO:0030317]; negative regulation of DNA recombination [GO:0045910]; nucleosome assembly [GO:0006334]; spermatogenesis [GO:0007283]
|
condensed nuclear chromosome [GO:0000794]; nucleosome [GO:0000786]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; nucleosomal DNA binding [GO:0031492]; structural constituent of chromatin [GO:0030527]
|
PF00538;
|
1.10.10.10;
|
Histone H1/H5 family
|
PTM: Phosphorylated in early spermatids. {ECO:0000269|PubMed:19043117}.; PTM: Citrullination at Arg-56 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance. {ECO:0000250|UniProtKB:P43275}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Testis-specific histone H1 that forms less compacted chromatin compared to other H1 histone subtypes. Formation of more relaxed chromatin may be required to promote chromatin architecture required for proper chromosome regulation during meiosis, such as homologous recombination. Histones H1 act as linkers that bind to nucleosomes and compact polynucleosomes into a higher-order chromatin configuration. {ECO:0000250|UniProtKB:P22492}.
|
Rattus norvegicus (Rat)
|
P06350
|
H1_ONCMY
|
MAEVAPAPAAAAPAKAPKKKAAAKPKKAGPSVGELIVKAVSASKERSGVSLAALKKSLAAGGYDVEKNNSRVKIAVKSLVTKGTLVQTKGTGASGSFKLNKKAVEAKKPAKKAAAPKAKKVAAKKPAAAKKPKKVAAKKAVAAKKSPKKAKKPATPKKAAKSPKKVKKPAAAAKKAAKSPKKATKAAKPKAAKPKAAKAKKAAPKKK
| null | null |
defense response to bacterium [GO:0042742]; nucleosome assembly [GO:0006334]
|
extracellular region [GO:0005576]; nucleosome [GO:0000786]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; structural constituent of chromatin [GO:0030527]
|
PF00538;
|
1.10.10.10;
|
Histone H1/H5 family
| null |
SUBCELLULAR LOCATION: Nucleus. Chromosome.; SUBCELLULAR LOCATION: [Oncorhyncin II]: Secreted.
| null | null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable up to 80 degrees Celsius.;
|
FUNCTION: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. {ECO:0000269|PubMed:12969798}.; FUNCTION: Oncorhyncin II has antibacterial activity against Gram-positive and Gram-negative bacteria at submicromolar concentrations. Potentially important role in mucosal defense. {ECO:0000269|PubMed:12969798}.
|
Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
|
P06367
|
RS14A_YEAST
|
MSNVVQARDNSQVFGVARIYASFNDTFVHVTDLSGKETIARVTGGMKVKADRDESSPYAAMLAAQDVAAKCKEVGITAVHVKIRATGGTRTKTPGPGGQAALRALARSGLRIGRIEDVTPVPSDSTRKKGGRRGRRL
| null | null |
cytoplasmic translation [GO:0002181]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; ribosomal small subunit assembly [GO:0000028]; translation [GO:0006412]
|
90S preribosome [GO:0030686]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; small-subunit processome [GO:0032040]
|
mRNA binding [GO:0003729]; structural constituent of ribosome [GO:0003735]
|
PF00411;
|
3.30.420.80;
|
Universal ribosomal protein uS11 family
|
PTM: N-terminally acetylated by acetyltransferase NatA. {ECO:0000269|PubMed:10601260, ECO:0000269|PubMed:1544921}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus, nucleolus {ECO:0000269|PubMed:15590835}.
| null | null | null | null | null |
FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). uS11 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (PubMed:15590835). {ECO:0000269|PubMed:15590835, ECO:0000305|PubMed:22096102}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06394
|
K1C10_BOVIN
|
MSVRYSSSKQYSSSRSGGGGGGGSSLRISSSKGSLGGGYSSGGFSGGSFSRGSSAGGCFGGSSSIYGGGLGSGFGGGYGSSFGGSYGGSFGGGYGGGGFGGGSFGGGSFGGGLGGGFGDGGLISGNQKITMQNLNDRLASYLDKVRALEESNYELEVKIKEWYEKYGNSRQREPRDYSKYYQTIDDLKNQIFNLTTDNANILIQVDNARLAADDFRLKYENEVTLRQSVEADINGLRRVLDELTLTKTDLEMQIESLTEELAYLKKNHEEEMRDLQNVSTGDVNVEMNAAPGVDLTELLNNMRSQYEQLAEKNRRDAEAWFNEKSKELTTEINSNLEQVSSHKSEITELRRTIQGLEIELQSQLALKQSLEASLAETEGRYCVQLSQIQSQISSLEEQLQQIRAETECQNAEYQQLLDIKIRLENEIQTYRSLLEGEGSSGGGSYGGGRGYGGSSGGGGGGYGGGSSSGGYGGGSSSGGGHGGSSGGSYGGGSSSGGGHGGGSSSGGHKSTTTGSVGESSSKGPRY
| null | null |
epidermis development [GO:0008544]; epithelial cell differentiation [GO:0030855]; intermediate filament organization [GO:0045109]; positive regulation of epidermis development [GO:0045684]; protein heterotetramerization [GO:0051290]
|
cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular region [GO:0005576]; keratin filament [GO:0045095]
|
protein heterodimerization activity [GO:0046982]; structural constituent of skin epidermis [GO:0030280]
|
PF00038;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250|UniProtKB:P13645}. Cell surface {ECO:0000250|UniProtKB:P13645}. Cytoplasm {ECO:0000250|UniProtKB:P02535}.
| null | null | null | null | null |
FUNCTION: Plays a role in the establishment of the epidermal barrier on plantar skin (By similarity). Involved in the maintenance of cell layer development and keratin filament bundles in suprabasal cells of the epithelium (By similarity). {ECO:0000250|UniProtKB:P02535}.
|
Bos taurus (Bovine)
|
P06396
|
GELS_HUMAN
|
MAPHRPAPALLCALSLALCALSLPVRAATASRGASQAGAPQGRVPEARPNSMVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGGVASGFKHVVPNEVVVQRLFQVKGRRVVRATEVPVSWESFNNGDCFILDLGNNIHQWCGSNSNRYERLKATQVSKGIRDNERSGRARVHVSEEGTEPEAMLQVLGPKPALPAGTEDTAKEDAANRKLAKLYKVSNGAGTMSVSLVADENPFAQGALKSEDCFILDHGKDGKIFVWKGKQANTEERKAALKTASDFITKMDYPKQTQVSVLPEGGETPLFKQFFKNWRDPDQTDGLGLSYLSSHIANVERVPFDAATLHTSTAMAAQHGMDDDGTGQKQIWRIEGSNKVPVDPATYGQFYGGDSYIILYNYRHGGRQGQIIYNWQGAQSTQDEVAASAILTAQLDEELGGTPVQSRVVQGKEPAHLMSLFGGKPMIIYKGGTSREGGQTAPASTRLFQVRANSAGATRAVEVLPKAGALNSNDAFVLKTPSAAYLWVGTGASEAEKTGAQELLRVLRAQPVQVAEGSEPDGFWEALGGKAAYRTSPRLKDKKMDAHPPRLFACSNKIGRFVIEEVPGELMQEDLATDDVMLLDTWDQVFVWVGKDSQEEEKTEALTSAKRYIETDPANRDRRTPITVVKQGFEPPSFVGWFLGWDDDYWSVDPLDRAMAELAA
| null | null |
actin filament capping [GO:0051693]; actin filament depolymerization [GO:0030042]; actin filament organization [GO:0007015]; actin filament polymerization [GO:0030041]; actin filament severing [GO:0051014]; actin polymerization or depolymerization [GO:0008154]; amyloid fibril formation [GO:1990000]; barbed-end actin filament capping [GO:0051016]; cardiac muscle cell contraction [GO:0086003]; cell projection assembly [GO:0030031]; cellular response to type II interferon [GO:0071346]; central nervous system development [GO:0007417]; cilium assembly [GO:0060271]; hepatocyte apoptotic process [GO:0097284]; negative regulation of viral entry into host cell [GO:0046597]; phagocytosis, engulfment [GO:0006911]; positive regulation of actin nucleation [GO:0051127]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:2001269]; positive regulation of gene expression [GO:0010628]; positive regulation of keratinocyte apoptotic process [GO:1902174]; positive regulation of protein processing in phagocytic vesicle [GO:1903923]; protein destabilization [GO:0031648]; regulation of establishment of T cell polarity [GO:1903903]; regulation of plasma membrane raft polarization [GO:1903906]; regulation of podosome assembly [GO:0071801]; regulation of receptor clustering [GO:1903909]; relaxation of cardiac muscle [GO:0055119]; renal protein absorption [GO:0097017]; response to muscle stretch [GO:0035994]; sequestering of actin monomers [GO:0042989]; striated muscle atrophy [GO:0014891]
|
actin cap [GO:0030478]; actin cytoskeleton [GO:0015629]; blood microparticle [GO:0072562]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lumen [GO:1904813]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; podosome [GO:0002102]; sarcoplasm [GO:0016528]; secretory granule lumen [GO:0034774]
|
actin binding [GO:0003779]; actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; myosin II binding [GO:0045159]; phosphatidylinositol 3-kinase catalytic subunit binding [GO:0036313]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]
|
PF00626;
|
3.40.20.10;
|
Villin/gelsolin family
|
PTM: Phosphorylation on Tyr-86, Tyr-409, Tyr-465, Tyr-603 and Tyr-651 in vitro is induced in presence of phospholipids. {ECO:0000269|PubMed:10210201}.
|
SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton.; SUBCELLULAR LOCATION: [Isoform 1]: Secreted.
| null | null | null | null | null |
FUNCTION: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed (PubMed:19666512). Plays a role in ciliogenesis (PubMed:20393563). {ECO:0000269|PubMed:19666512, ECO:0000269|PubMed:20393563}.
|
Homo sapiens (Human)
|
P06399
|
FIBA_RAT
|
MLSLRVACLILSLASTVWTADTGTTSEFIEAGGDIRGPRIVERQPSQCKETDWPFCSDEDWNHKCPSGCRMKGLIDEANQDFTNRINKLKNSLFDFQKNNKDSNSLTRNIMEYLRGDFANANNFDNTFGQVSEDLRRRIQILKRKVIEKAQQIQVLQKDVRDQLIDMKRLEVDIDIKIRSCKGSCSRSVSREINLKDYEGQQKQLEQVIAKDLLPAKDRQYLPAIKMSPVPDLVPGSFKSQLQEGPPEWKALTEMRQMRMELERPGKDGASRGDLPGDSRGDSATRGPGSKIENPMTPGHGGSGYWRPGSSGSGSDGNWGSGTTGSDDTGTWGAGSSRPSSGSGNLKPSNPDWGEFSEFGGSSSPATRKEYHTGKLVTSKGDKELLIGNEKVTSTGTSTTRRSCSKTITKTVLGNDGHREVVKEVVTSDDGSDCGDGMDLGLTHSFSGRLDELSRMHPELGSFYDSRFGSLTSNFKEFGSKTSDSDIFTDIENPSSHVPEFSSSSKTSTVRKQVTKSYKMADEAASEAHQEGDTRTTKRGRARTMRDCDDVLQTHPSGAQNGIFSIKLPGSSKIFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDKGEGEFWLGNDYLHLLTLRGSVLRVELEDWAGKEAYAEYHFRVGSEAEGYALQVSSYQGTAGDALMEGSVEEGTEYTSHSNMQFSTFDRDADQWEENCAEVYGGGWWYNSCQAANLNGIYYPGGTYDPRNNSPYEIENGVLWVPFRGADYSLWAVRMKIRPLVGQ
| null | null |
acute-phase response [GO:0006953]; adaptive immune response [GO:0002250]; blood coagulation [GO:0007596]; blood coagulation, common pathway [GO:0072377]; blood coagulation, fibrin clot formation [GO:0072378]; cell-matrix adhesion [GO:0007160]; cellular response to granulocyte colony-stimulating factor [GO:1990643]; cellular response to interleukin-6 [GO:0071354]; cellular response to organic cyclic compound [GO:0071407]; envenomation resulting in modulation of blood coagulation in another organism [GO:0044468]; fibrinolysis [GO:0042730]; induction of bacterial agglutination [GO:0043152]; innate immune response [GO:0045087]; liver regeneration [GO:0097421]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; plasminogen activation [GO:0031639]; platelet aggregation [GO:0070527]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of exocytosis [GO:0045921]; positive regulation of heterotypic cell-cell adhesion [GO:0034116]; positive regulation of peptide hormone secretion [GO:0090277]; positive regulation of protein secretion [GO:0050714]; positive regulation of smooth muscle cell migration [GO:0014911]; positive regulation of vasoconstriction [GO:0045907]; protein polymerization [GO:0051258]; protein-containing complex assembly [GO:0065003]; response to calcium ion [GO:0051592]; response to cycloheximide [GO:0046898]; response to estradiol [GO:0032355]; response to genistein [GO:0033595]; response to growth hormone [GO:0060416]; response to insulin [GO:0032868]; response to thyroid hormone [GO:0097066]; response to toxic substance [GO:0009636]; response to X-ray [GO:0010165]
|
blood microparticle [GO:0072562]; cell cortex [GO:0005938]; cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; fibrinogen complex [GO:0005577]; platelet alpha granule [GO:0031091]; synapse [GO:0045202]
|
extracellular matrix structural constituent [GO:0005201]; metal ion binding [GO:0046872]; signaling receptor binding [GO:0005102]; structural molecule activity [GO:0005198]
|
PF08702;PF12160;PF00147;
|
1.20.5.50;3.90.215.10;4.10.530.10;
| null |
PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.; PTM: Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P02671}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02671}.
| null | null | null | null | null |
FUNCTION: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways. {ECO:0000250|UniProtKB:E9PV24}.
|
Rattus norvegicus (Rat)
|
P06400
|
RB_HUMAN
|
MPPKTPRKTAATAAAAAAEPPAPPPPPPPEEDPEQDSGPEDLPLVRLEFEETEEPDFTALCQKLKIPDHVRERAWLTWEKVSSVDGVLGGYIQKKKELWGICIFIAAVDLDEMSFTFTELQKNIEISVHKFFNLLKEIDTSTKVDNAMSRLLKKYDVLFALFSKLERTCELIYLTQPSSSISTEINSALVLKVSWITFLLAKGEVLQMEDDLVISFQLMLCVLDYFIKLSPPMLLKEPYKTAVIPINGSPRTPRRGQNRSARIAKQLENDTRIIEVLCKEHECNIDEVKNVYFKNFIPFMNSLGLVTSNGLPEVENLSKRYEEIYLKNKDLDARLFLDHDKTLQTDSIDSFETQRTPRKSNLDEEVNVIPPHTPVRTVMNTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFAKAVGQGCVEIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLERCEHRIMESLAWLSDSPLFDLIKQSKDREGPTDHLESACPLNLPLQNNHTAADMYLSPVRSPKKKGSTTRVNSTANAETQATSAFQTQKPLKSTSLSLFYKKVYRLAYLRLNTLCERLLSEHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAVQETFKRVLIKEEEYDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIEGSDEADGSKHLPGESKFQQKLAEMTSTRTRMQKQKMNDSMDTSNKEEK
| null | null |
aortic valve morphogenesis [GO:0003180]; cell differentiation [GO:0030154]; cell division [GO:0051301]; cell morphogenesis involved in neuron differentiation [GO:0048667]; cellular response to insulin stimulus [GO:0032869]; cellular response to xenobiotic stimulus [GO:0071466]; chondrocyte differentiation [GO:0002062]; chromatin remodeling [GO:0006338]; chromosome organization [GO:0051276]; digestive tract development [GO:0048565]; enucleate erythrocyte differentiation [GO:0043353]; epithelial cell proliferation [GO:0050673]; G1/S transition of mitotic cell cycle [GO:0000082]; glial cell apoptotic process [GO:0034349]; glial cell proliferation [GO:0014009]; hepatocyte apoptotic process [GO:0097284]; heterochromatin formation [GO:0031507]; maintenance of mitotic sister chromatid cohesion [GO:0034088]; myoblast differentiation [GO:0045445]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell growth [GO:0030308]; negative regulation of cold-induced thermogenesis [GO:0120163]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of gene expression [GO:0010629]; negative regulation of glial cell proliferation [GO:0060253]; negative regulation of hepatocyte apoptotic process [GO:1903944]; negative regulation of inflammatory response [GO:0050728]; negative regulation of myofibroblast differentiation [GO:1904761]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of protein serine/threonine kinase activity [GO:0071901]; negative regulation of smoothened signaling pathway [GO:0045879]; negative regulation of tau-protein kinase activity [GO:1902948]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron apoptotic process [GO:0051402]; neuron maturation [GO:0042551]; neuron projection development [GO:0031175]; positive regulation of collagen fibril organization [GO:1904028]; positive regulation of extracellular matrix organization [GO:1903055]; positive regulation of macrophage differentiation [GO:0045651]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription regulatory region DNA binding [GO:2000679]; protein localization to chromosome, centromeric region [GO:0071459]; Ras protein signal transduction [GO:0007265]; regulation of cell cycle [GO:0051726]; regulation of centromere complex assembly [GO:0090230]; regulation of DNA-templated transcription [GO:0006355]; regulation of lipid kinase activity [GO:0043550]; regulation of mitotic cell cycle [GO:0007346]; sister chromatid biorientation [GO:0031134]; skeletal muscle cell differentiation [GO:0035914]; smoothened signaling pathway [GO:0007224]; spermatogenesis [GO:0007283]; striated muscle cell differentiation [GO:0051146]; tissue homeostasis [GO:0001894]; transcription by RNA polymerase II [GO:0006366]
|
chromatin [GO:0000785]; chromatin lock complex [GO:0061793]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]; Rb-E2F complex [GO:0035189]; spindle [GO:0005819]; SWI/SNF complex [GO:0016514]
|
disordered domain specific binding [GO:0097718]; DNA-binding transcription factor binding [GO:0140297]; identical protein binding [GO:0042802]; importin-alpha family protein binding [GO:0061676]; kinase binding [GO:0019900]; molecular adaptor activity [GO:0060090]; phosphoprotein binding [GO:0051219]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription corepressor activity [GO:0003714]; ubiquitin protein ligase binding [GO:0031625]
|
PF11934;PF01858;PF01857;PF08934;
|
1.10.472.140;6.10.140.1380;6.10.250.530;1.10.472.10;
|
Retinoblastoma protein (RB) family
|
PTM: Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at Ser-567 in G1, thereby releasing E2F1 which is then able to activate cell growth. Dephosphorylated at the late M phase. SV40 large T antigen, HPV E7 and adenovirus E1A bind to the underphosphorylated, active form of pRb. Phosphorylation at Thr-821 and Thr-826 promotes interaction between the C-terminal domain C and the Pocket domain, and thereby inhibits interactions with heterodimeric E2F/DP transcription factor complexes. Dephosphorylated at Ser-795 by calcineruin upon calcium stimulation. CDK3/cyclin-C-mediated phosphorylation at Ser-807 and Ser-811 is required for G0-G1 transition. Phosphorylated by CDK1 and CDK2 upon TGFB1-mediated apoptosis. {ECO:0000269|PubMed:10499802, ECO:0000269|PubMed:8114739}.; PTM: N-terminus is methylated by METTL11A/NTM1 (By similarity). Monomethylation at Lys-810 by SMYD2 enhances phosphorylation at Ser-807 and Ser-811, and promotes cell cycle progression. Monomethylation at Lys-860 by SMYD2 promotes interaction with L3MBTL1. {ECO:0000250, ECO:0000269|PubMed:15084261, ECO:0000269|PubMed:15809340, ECO:0000269|PubMed:16360038, ECO:0000269|PubMed:17380128, ECO:0000269|PubMed:1756735, ECO:0000269|PubMed:20870719, ECO:0000269|PubMed:22787429}.; PTM: Acetylated during keratinocyte differentiation. Acetylation at Lys-873 and Lys-874 regulates subcellular localization. Can be deacetylated by SIRT1. {ECO:0000269|PubMed:20940255}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20940255}. Note=During keratinocyte differentiation, acetylation by KAT2B/PCAF is required for nuclear localization. {ECO:0000269|PubMed:20940255}.
| null | null | null | null | null |
FUNCTION: Tumor suppressor that is a key regulator of the G1/S transition of the cell cycle (PubMed:10499802). The hypophosphorylated form binds transcription regulators of the E2F family, preventing transcription of E2F-responsive genes (PubMed:10499802). Both physically blocks E2Fs transactivating domain and recruits chromatin-modifying enzymes that actively repress transcription (PubMed:10499802). Cyclin and CDK-dependent phosphorylation of RB1 induces its dissociation from E2Fs, thereby activating transcription of E2F responsive genes and triggering entry into S phase (PubMed:10499802). RB1 also promotes the G0-G1 transition upon phosphorylation and activation by CDK3/cyclin-C (PubMed:15084261). Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity). {ECO:0000250|UniProtKB:P13405, ECO:0000250|UniProtKB:P33568, ECO:0000269|PubMed:10499802, ECO:0000269|PubMed:15084261}.; FUNCTION: (Microbial infection) In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity. {ECO:0000269|PubMed:1316611, ECO:0000269|PubMed:17974914, ECO:0000269|PubMed:18701596, ECO:0000269|PubMed:2839300, ECO:0000269|PubMed:8892909}.
|
Homo sapiens (Human)
|
P06401
|
PRGR_HUMAN
|
MTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQRVLSPLMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYLRPDSEASQSPQYSFESLPQKICLICGDEASGCHYGVLTCGSCKVFFKRAMEGQHNYLCAGRNDCIVDKIRRKNCPACRLRKCCQAGMVLGGRKFKKFNKVRVVRALDAVALPQPVGVPNESQALSQRFTFSPGQDIQLIPPLINLLMSIEPDVIYAGHDNTKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCMKVLLLLNTIPLEGLRSQTQFEEMRSSYIRELIKAIGLRQKGVVSSSQRFYQLTKLLDNLHDLVKQLHLYCLNTFIQSRALSVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK
| null | null |
cell-cell signaling [GO:0007267]; glandular epithelial cell maturation [GO:0002071]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; lung alveolus development [GO:0048286]; maintenance of protein location in nucleus [GO:0051457]; negative regulation of gene expression [GO:0010629]; negative regulation of phosphorylation [GO:0042326]; ovulation from ovarian follicle [GO:0001542]; paracrine signaling [GO:0038001]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription by RNA polymerase II [GO:0045944]; progesterone receptor signaling pathway [GO:0050847]; regulation of DNA-templated transcription [GO:0006355]; regulation of epithelial cell proliferation [GO:0050678]; regulation of transcription by RNA polymerase II [GO:0006357]; signal transduction [GO:0007165]; tertiary branching involved in mammary gland duct morphogenesis [GO:0060748]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
|
ATPase binding [GO:0051117]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; enzyme binding [GO:0019899]; estrogen response element binding [GO:0034056]; G protein-coupled receptor activity [GO:0004930]; identical protein binding [GO:0042802]; nuclear receptor activity [GO:0004879]; nuclear steroid receptor activity [GO:0003707]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; signaling receptor binding [GO:0005102]; steroid binding [GO:0005496]; transcription coactivator binding [GO:0001223]; zinc ion binding [GO:0008270]
|
PF00104;PF02161;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR3 subfamily
|
PTM: Phosphorylated on multiple serine sites. Several of these sites are hormone-dependent. Phosphorylation on Ser-294 occurs preferentially on isoform B, is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388. Phosphorylation on Ser-102 and Ser-345 also requires induction by hormone. Basal phosphorylation on Ser-81, Ser-162, Ser-190 and Ser-400 is increased in response to progesterone and can be phosphorylated in vitro by the CDK2-A1 complex. Increased levels of phosphorylation on Ser-400 also in the presence of EGF, heregulin, IGF, PMA and FBS. Phosphorylation at this site by CDK2 is ligand-independent, and increases nuclear translocation and transcriptional activity. Phosphorylation at Ser-162 and Ser-294, but not at Ser-190, is impaired during the G(2)/M phase of the cell cycle. Phosphorylation on Ser-345 by ERK1/2 MAPK is required for interaction with SP1. {ECO:0000269|PubMed:10628747, ECO:0000269|PubMed:10655479, ECO:0000269|PubMed:11110801, ECO:0000269|PubMed:15572662, ECO:0000269|PubMed:15798179, ECO:0000269|PubMed:17020914, ECO:0000269|PubMed:17173941, ECO:0000269|PubMed:17347654, ECO:0000269|PubMed:17717077, ECO:0000269|PubMed:18202149, ECO:0000269|PubMed:7476977, ECO:0000269|PubMed:8702648, ECO:0000269|PubMed:9171245}.; PTM: Sumoylation is hormone-dependent and represses transcriptional activity. Sumoylation on all three sites is enhanced by PIAS3. Desumoylated by SENP1. Sumoylation on Lys-388, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-294. {ECO:0000269|PubMed:10628747, ECO:0000269|PubMed:10655479, ECO:0000269|PubMed:15798179, ECO:0000269|PubMed:17020914, ECO:0000269|PubMed:17173941, ECO:0000269|PubMed:17347654, ECO:0000269|PubMed:17717077, ECO:0000269|PubMed:18202149, ECO:0000269|PubMed:8702648}.; PTM: Ubiquitination is hormone-dependent and represses sumoylation on the same site. Promoted by MAPK-mediated phosphorylation on Ser-294. {ECO:0000269|PubMed:10628747, ECO:0000269|PubMed:10655479, ECO:0000269|PubMed:15798179, ECO:0000269|PubMed:17173941, ECO:0000269|PubMed:17717077, ECO:0000269|PubMed:18202149, ECO:0000269|PubMed:8702648}.; PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation. {ECO:0000269|PubMed:22031296}.
|
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleoplasmic shuttling is both hormone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G(1) and G(2)/M phases.; SUBCELLULAR LOCATION: [Isoform A]: Nucleus. Cytoplasm. Note=Mainly nuclear.; SUBCELLULAR LOCATION: [Isoform 4]: Mitochondrion outer membrane {ECO:0000269|PubMed:23518922}.
| null | null | null | null | null |
FUNCTION: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Depending on the isoform, progesterone receptor functions as a transcriptional activator or repressor. {ECO:0000269|PubMed:10757795, ECO:0000269|PubMed:1587864, ECO:0000269|PubMed:9407067, ECO:0000305}.; FUNCTION: [Isoform A]: Ligand-dependent transdominant repressor of steroid hormone receptor transcriptional activity including repression of its isoform B, MR and ER. Transrepressional activity may involve recruitment of corepressor NCOR2. {ECO:0000269|PubMed:7969170, ECO:0000269|PubMed:8180103, ECO:0000269|PubMed:8264658, ECO:0000305, ECO:0000305|PubMed:10757795}.; FUNCTION: [Isoform B]: Transcriptional activator of several progesteron-dependent promoters in a variety of cell types. Involved in activation of SRC-dependent MAPK signaling on hormone stimulation. {ECO:0000269|PubMed:7969170}.; FUNCTION: [Isoform 4]: Increases mitochondrial membrane potential and cellular respiration upon stimulation by progesterone.
|
Homo sapiens (Human)
|
P06437
|
GB_HHV1K
|
MHQGAPSWGRRWFVVWALLGLTLGVLVASAAPTSPGTPGVAAATQAANGGPATPAPPPLGAAPTGDPKPKKNKKPKNPTPPRPAGDNATVAAGHATLREHLRDIKAENTDANFYVCPPPTGATVVQFEQPRRCPTRPEGQNYTEGIAVVFKENIAPYKFKATMYYKDVTVSQVWFGHRYSQFMGIFEDRAPVPFEEVIDKINAKGVCRSTAKYVRNNLETTAFHRDDHETDMELKPANAATRTSRGWHTTDLKYNPSRVEAFHRYGTTVNCIVEEVDARSVYPYDEFVLATGDFVYMSPFYGYREGSHTEHTTYAADRFKQVDGFYARDLTTKARATAPTTRNLLTTPKFTVAWDWVPKRPSVCTMTKWQEVDEMLRSEYGGSFRFSSDAISTTFTTNLTEYPLSRVDLGDCIGKDARDAMDRIFARRYNATHIKVGQPQYYQANGGFLIAYQPLLSNTLAELYVREHLREQSRKPPNPTPPPPGASANASVERIKTTSSIEFARLQFTYNHIQRHVNDMLGRVAIAWCELQNHELTLWNEARKLNPNAIASVTVGRRVSARMLGDVMAVSTCVPVAADNVIVQNSMRISSRPGACYSRPLVSFRYEDQGPLVEGQLGENNELRLTRDAIEPCTVGHRRYFTFGGGYVYFEEYAYSHQLSRADITTVSTFIDLNITMLEDHEFVPLEVYTRHEIKDSGLLDYTEVQRRNQLHDLRFADIDTVIHADANAAMFAGLGAFFEGMGDLGRAVGKVVMGIVGGVVSAVSGVSSFMSNPFGALAVGLLVLAGLAAAFFAFRYVMRLQSNPMKALYPLTTKELKNPTNPDASGEGEEGGDFDEAKLAEAREMIRYMALVSAMERTEHKAKKKGTSALLSAKVTDMVMRKRRNTNYTQVPNKDGDADEDDL
| null | null |
symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062]
|
host cell endosome membrane [GO:0044175]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
|
identical protein binding [GO:0042802]
|
PF17416;PF17417;PF00606;
|
1.20.5.1890;2.30.29.100;2.30.30.1230;6.10.250.3280;
|
Herpesviridae glycoprotein B family
|
PTM: The cytoplasmic tail is phosphorylated by the viral kinase US3. Phosphorylation may be linked to a down-regulation of gB expression on cell surface. {ECO:0000269|PubMed:18945776, ECO:0000269|PubMed:19158241}.; PTM: ubiquitinated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-Rule:MF_04032}.
| null | null | null | null | null |
FUNCTION: Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress. Also plays a role, together with gK, in virus-induced cell-to-cell fusion (syncytia formation). {ECO:0000255|HAMAP-Rule:MF_04032, ECO:0000269|PubMed:17299053}.
|
Human herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1)
|
P06441
|
POLG_HAVLA
|
MNMSKQGIFQTVGSGLDHILSLADIEEEQMIQSVDRTAVTGASYFTSVDQSSVHTAEVGSHQIEPLKTSVDKPGSKKTQGEKFFLIHSADWLTTHALFHEVAKLDVVKLLYNEQFAVQGLLRYHTYARFGIEIQVQINPTPFQQGGLICAMVPGDQSYGSIASLTVYPHGLLNCNINNVVRIKVPFIYTRGAYHFKDPQYPVWELTIRVWSELNIGTGTSAYTSLNVLARFTDLELHGLTPLSTQMMRNEFRVSTTENVVNLSNYEDARAKMSFALDQEDWKSDPSQGGGIKITHFTTWTSIPTLAAQFPFNASDSVGQQIKVIPVDPYFFQMTNTNPDQKCITALASICQMFCFWRGDLVFDFQVFPTKYHSGRLLFCFVPGNELIDVTGITLKQATTAPCAVMDITGVQSTLRFRVPWISDTPYRVNRYTKSAHQKGEYTAIGKLIVYCYNRLTSPSNVASHVRVNVYLSAINLECFAPLYHAMDVTTQVGDDSGGFSTTVSTEQNVPDPQVGITTMRDLKGKANRGKMDVSGVQAPRGSYQQQLNDPVLAKKVPETFPELKPGESRHTSDHMSIYKFMGRSHFLCTFTFNSNNKEYTFPITLSSTSNPPHGLPSTLRWFFNLFQLYRGPLDLTIIITGATDVDGMAWFTPVGLAVDPWVEKESALSIDYKTALGAVRFNTRRTGNIQIRLPWYSYLYAVSGALDGLGDKTDSTFGLFLFEIANYNHSDEYLSFSCYLSVTEQSEFYFPRAPLNSNAMLSTESMMSRIAAGDLESSVDDPRSEEDRRFESHIECRKPYKELRLEVGKQRLKYAQEELSNEVLPPPRKMKGLFSQAKISLFYTEEHEIMKFSWRGVTADTRALRRFGFSLAAGRSVWTLEMDAGVLTGRLIRLNDEKWTEMKDDKIVSLIEKFTSNKYWSKVNFPHGMLDLEEIAANSKDFPNMSETDLCFLLHWLNPKKINLADRMLGLSGVQEIKEQGVGLIAECRTFLDSIAGTLKSMMFGFHHSVTVEIINTVLCFVKSGILLYVIQQLNQDEHSHIIGLLRVMNYADIGCSVISCGKVFSKMLETVFNWQMDSRMMELRTQSFSNWLRDICSGITIFKSFKDAIYWLYTKLKDFYEVNYGKKKDILNILKDNQQKIEKAIEEADNFCILQIQDVEKFDQYQKGVDLIQKLRTVHSMAQVDPNLGVHLSPLRDCIARVHQKLKNLGSINQAMVTRCEPVVCYLYGKRGGGKSLTSIALATKICKHYGVEPEKNIYTKPVASDYWDGYSGQLVCIIDDIGQNTTDEDWSDFCQLVSGCPMRLNMASLEEKGRHFSSPFIIATSNWSNPSPKTVYVKEAIDRRLHFKVEVKPASFFKNPHNDMLNVNLAKTNDAIKDMSCVDLIMDGHNISLMDLLSSLVMTVEIRKQNMSEFMELWSQGISDDDNDSAVAEFFQSFPSGEPSNWKLSSFFQSVTNHKWVAVGAAVGILGVLVGGWFVYKHFSRKEEEPIPAEGVYHGVTKPKQVIKLDADPVESQSTLEIAGLVRKNLVQFGVGEKNGCVRWVMNALGVKDDWLLVPSHAYKFEKDYEMMEFYFNRGGTYYSISAGNVVIQSLDVGFQDVVLMKVPTIPKFRDITQHFIKKGDVPRALNRLATLVTTVNGTPMLISEGPLKMEEKATYVHKKNDGTTVDLTVDQAWRGKGEGLPGMCGGALVSSNQSIQNAILGIHVAGGNSILVAKLVTQEMFQNIDKKIESQRIMKVEFTQCSMNVVSKTLFRKSPIHHHIDKTMINFPAAMPFSKAEIDPMAMMLSKYSLPIVEEPEDYKEASVFYQNKIVGKTQLVDDFLDLDMAITGAPGIDAINMDSSPGFPYVQEKLTKRDLIWLDENGLLLGVHPRLAQRILFNTVMMENCSDLDVVFTTCPKDELRPLEKVLESKTRAIDACPLDYTILCRMYWGPAISYFHLNPGFHTGVAIGIDPDRQWDELFKTMIRFGDVGLDLDFSAFDASLSPFMIREAGRIMSELSGTPSHFGTALINTIIYSKHLLYNCCYHVCGSMPSGSPCTALLNSIINNINLYYVFSKIFGKSPVFFCQALRILCYGDDVLIVFSRDVQIDNLDLIGQKIVDEFKKLGMTATSADKNVPQLKPVSELTFLKRSFNLVEDRIRPAISEKTIWSLMAWQRSNAEFEQNLENAQWFAFMHGYEFYQKFYYFVQSCLEKEMIEYRLKSYDWWRMRFYDQCFICDLS
|
2.7.7.48; 3.4.22.28; 3.6.1.15
| null |
DNA-templated transcription [GO:0006351]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity [GO:0039545]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell cytoplasmic vesicle membrane [GO:0044162]; host cell mitochondrial outer membrane [GO:0044193]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618]
|
ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule activity [GO:0005198]
|
PF20758;PF12944;PF00548;PF00680;PF00073;PF00910;
|
1.20.960.20;2.60.120.20;3.30.70.270;2.40.10.10;
|
Picornaviridae polyprotein family
|
PTM: [Genome polyprotein]: Specific enzymatic cleavages by viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates are produced, such as P1-2A which is a functional precursor of the structural proteins, VP0 which is a VP4-VP2 precursor, VP1-2A precursor, 3ABC precursor which is a stable and catalytically active precursor of 3A, 3B and 3C proteins, 3AB and 3CD precursors. The assembly signal 2A is removed from VP1-2A by a host protease, possibly host Cathepsin L. This cleavage occurs over a region of 3 amino-acids probably generating VP1 proteins with heterogeneous C-termini. {ECO:0000250|UniProtKB:P08617}.; PTM: [Capsid protein VP0]: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and is followed by a conformational change of the particle. {ECO:0000250|UniProtKB:P03303}.; PTM: [Protein VP1-2A]: The assembly signal 2A is removed from VP1-2A by a host protease, possibly host Cathepsin L in naked virions. This cleavage does not occur in enveloped virions. This cleavage occurs over a region of 3 amino-acids probably generating VP1 proteins with heterogeneous C-termini. {ECO:0000250|UniProtKB:P08617}.; PTM: [Viral protein genome-linked]: VPg is uridylylated prior to priming replication into VPg-pUpU. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP4]: Unlike other picornaviruses, does not seem to be myristoylated. {ECO:0000250|UniProtKB:P08617}.
|
SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion {ECO:0000250|UniProtKB:P08617}. Note=Present in the full mature virion. The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protein 2B]: Host membrane {ECO:0000250|UniProtKB:P08617}; Peripheral membrane protein {ECO:0000250|UniProtKB:P08617}. Note=Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protein 2C]: Host membrane {ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08617}. Note=Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. May associate with membranes through a N-terminal amphipathic helix. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protein 3ABC]: Host membrane {ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion outer membrane {ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08617}. Note=Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protein 3AB]: Host membrane {ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein {ECO:0000255}. Note=Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protein 3A]: Host membrane {ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein {ECO:0000255}. Note=Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Viral protein genome-linked]: Virion {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase 3D-POL]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P08617}; Peripheral membrane protein {ECO:0000250|UniProtKB:P08617}; Cytoplasmic side {ECO:0000250|UniProtKB:P08617}. Note=Interacts with membranes in a complex with viral protein 3AB. Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum. {ECO:0000250|UniProtKB:P08617}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000250|UniProtKB:P08617, ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P08617}; CATALYTIC ACTIVITY: Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.; EC=3.4.22.28; Evidence={ECO:0000255|PROSITE-ProRule:PRU01222};
| null | null | null | null |
FUNCTION: [Capsid protein VP1]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP2]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP3]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP0]: VP0 precursor is a component of the immature procapsids. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP4]: Plays a role in the assembly of the 12 pentamers into an icosahedral structure. Has not been detected in mature virions, supposedly owing to its small size. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein VP1-2A]: Precursor component of immature procapsids that corresponds to an extended form of the structural protein VP1. After maturation, possibly by the host Cathepsin L, the assembly signal 2A is cleaved to give rise to the mature VP1 protein. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 2B]: Functions as a viroporin. Affects membrane integrity and causes an increase in membrane permeability. Involved in host intracellular membrane rearrangements probably to give rise to the viral factories. Does not disrupt calcium homeostasis or glycoprotein trafficking. Antagonizes the innate immune response of the host by suppressing IFN-beta synthesis, which it achieves by interfering with the RIG-I/IFIH1 pathway. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 2BC]: Affects membrane integrity and causes an increase in membrane permeability. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 2C]: Associates with and induces structural rearrangements of intracellular membranes. Displays RNA-binding activity. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 3ABC]: The precursor 3ABC is targeted to the mitochondrial membrane where protease 3C activity cleaves and inhibits the host antiviral protein MAVS, thereby disrupting activation of IRF3 through the IFIH1/MDA5 pathway. In vivo, the protease activity of 3ABC precursor is more efficient in cleaving the 2BC precursor than that of protein 3C. The 3ABC precursor may therefore play a role in the proteolytic processing of the polyprotein. Possible viroporin. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 3AB]: Interacts with the 3CD precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Since the 3AB precursor contains the hydrophobic domain 3A, it probably anchors the whole viral replicase complex to intracellular membranes on which viral RNA synthesis occurs. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 3A]: May serve as membrane anchor to the 3AB and 3ABC precursors via its hydrophobic domain. May interact with RNA. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Viral protein genome-linked]: Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome. {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease. Cleaves IKBKG/NEMO to impair innate immune signaling. Cleaves host PABPC1 which may participate in the switch of viral translation to RNA synthesis. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 3CD]: Interacts with the 3AB precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Disrupts TLR3 signaling by degrading the host adapter protein TICAM1/TRIF. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals. {ECO:0000250|UniProtKB:P08617}.
|
Human hepatitis A virus genotype IA (isolate LA) (HHAV) (Human hepatitis A virus (isolate Human/Northern California/LA/1974))
|
P06442
|
POLG_HAVCR
|
MNMSKQGIFQTVGSGLDHILSLADIEEEQMIQSVVRTAVTGASYFTSVDQSSVHTAEVGLHQIEPLKTSVDKPSSKKTQGEKFFLIHSADWLTTHALFHEVAKLDVVKLLYNEQFAVQGLLRYHTYARFGIEIQVQINPTPFQQGGLICAMVPSDQSYGSIASLTVYPHGLLNCNINNVVRIKVPFIYTRGAYHFKDPQYPVWELTIRVWSELNIGTGTSAYTSLNVLARFTDLELHGLTPLSTQMMRNEFRVSTTENVVNLSNYEDARAKMSFALDQEDWKSDPSQGGGIKITHFTTWTSIPTLAAQFPFNASDSVGQQIKVIPVDPYFFQMTNTNPDQKCITALASICQMFCFWRGDLVFDFQVFPTKYHSGRLLFCFVPGNELIDVTGITLKQATTAPCAVMDITGVQSTLRFRVPWISDTPYRVNRYTKSAHQKGEYTAIGKLIVYCYNRLTSPSNVASHVRVNVYLSAINLECFAPLYHAMDVTTQVGDDSGGFSTTVSTEQNVPDPQVGITTMKDLKGKANRGKMDVSGVQAPVGAITTIEDPALAKKVPETFPELKPGESRHTSDHMSIYKFMGRSHFLCTFTFNSNNKEYTFPITLSSTSNPPHGLPSTLRWFFNLFQLYRGPLDLTIIITGATDVDGMAWFTPVGLAVDTPWVEKESALSIDYKTALGAVRFNTRRTGNIQIRLPWYSYLYAVSGALDGLGDKTDSTFGLVSIQIANYNHSDEYLSFSCYLSVTQQSEFYFPRAPLNSNAMLSTESMMSRIAAGDLESSVDDPRSEEDRRFESHIECRKPYKELRLEVGKQRLKYAQEELSNEVLPPPRKMKGLFSQAKISLFYTEEHEIMKF
| null | null |
protein complex oligomerization [GO:0051259]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062]
|
host cell membrane [GO:0033644]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618]
|
monoatomic ion channel activity [GO:0005216]; structural molecule activity [GO:0005198]
|
PF12944;PF00073;
|
2.60.120.20;
|
Picornaviridae polyprotein family
|
PTM: [Genome polyprotein]: Specific enzymatic cleavages by viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates are produced, such as P1-2A which is a functional precursor of the structural proteins, VP0 which is a VP4-VP2 precursor, VP1-2A precursor, 3ABC precursor which is a stable and catalytically active precursor of 3A, 3B and 3C proteins, 3AB and 3CD precursors. The assembly signal 2A is removed from VP1-2A by a host protease, possibly host Cathepsin L. This cleavage occurs over a region of 3 amino-acids probably generating VP1 proteins with heterogeneous C-termini. {ECO:0000250|UniProtKB:P08617}.; PTM: [Capsid protein VP0]: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and is followed by a conformational change of the particle. {ECO:0000250|UniProtKB:P03303}.; PTM: [Protein VP1-2A]: The assembly signal 2A is removed from VP1-2A by a host protease, possibly host Cathepsin L in naked virions. This cleavage does not occur in enveloped virions. This cleavage occurs over a region of 3 amino-acids probably generating VP1 proteins with heterogeneous C-termini. {ECO:0000250|UniProtKB:P08617}.; PTM: Viral protein genome-linked: VPg is uridylylated prior to priming replication into VPg-pUpU. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP4]: Unlike other picornaviruses, does not seem to be myristoylated. {ECO:0000250|UniProtKB:P08617}.
|
SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion {ECO:0000250|UniProtKB:P08617}. Note=Present in the full mature virion. The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protein 2B]: Host membrane {ECO:0000250|UniProtKB:P08617}; Peripheral membrane protein {ECO:0000250|UniProtKB:P08617}. Note=Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. {ECO:0000250|UniProtKB:P08617}.
| null | null | null | null | null |
FUNCTION: [Capsid protein VP1]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP2]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP3]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP0]: VP0 precursor is a component of the immature procapsids. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP4]: Plays a role in the assembly of the 12 pentamers into an icosahedral structure. Has not been detected in mature virions, supposedly owing to its small size. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein VP1-2A]: Precursor component of immature procapsids that corresponds to an extended form of the structural protein VP1. After maturation, possibly by the host Cathepsin L, the assembly signal 2A is cleaved to give rise to the mature VP1 protein. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 2BC]: Affects membrane integrity and causes an increase in membrane permeability. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 2B]: Functions as a viroporin. Affects membrane integrity and causes an increase in membrane permeability. Involved in host intracellular membrane rearrangements probably to give rise to the viral factories. Does not disrupt calcium homeostasis or glycoprotein trafficking. Antagonizes the innate immune response of the host by suppressing IFN-beta synthesis, which it achieves by interfering with the RIG-I/IFIH1 pathway. {ECO:0000250|UniProtKB:P08617}.
|
Human hepatitis A virus genotype IA (isolate CR326) (HHAV) (Human hepatitis A virus (isolate Human/Costa Rica/CR326/1960))
|
P06445
|
ENV_RMCFV
|
MACSTFSKPLKDKINPWGPLIILGILIRAGVSVQHDSPHKVFNVTWRVTNLMTGQTANATSLLGTMTDAFPKLYFDLCDLVGDYWDDPEPDIGDGCRTPGGRRRTRLYDFYVCPGHTVPIGCGGPGEGYCGKWGCETTGQAYWKPSSSWDLISLKRGNTPKDQGPCYDSSVSSDIKGATPGGRCNPLVLEFTDAGKKASWDGPKVWGLRLYRSTGTDPVTRFSLTRRVLNIGPRVPIGPNPVIIDQLPPSRPVQIMLPRPPQPPPPGAASIVPETAPPSQQPGTGDRLLNLVDGAYQALNLTSPDKTQECWLCLVAEPPYYEGVAVLGTYSNHTSAPTNCSVASQHKLTLSEVTGQGLCIGTVPKTHQALCNTTLKTNKGSYYLVAPAGTTWACNTGLTPCLSATVLNRTTDYCVLVELWPRVTYHPPSYVYSQFEKSYRHKREPVSLTLALLLGGLTMGGIAAGVGTGTTALVATQQFQQLHAAVQDDLKEVEKSITNLEKSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYADHTGLVRDSMAKLRERLTQRQKLFESSQGWFEGLFNRSPWFTTLISTIMGPLIILLLILLFGPCILNRLVQFVKDRISVVQALVLTQQYHQLKPLEYEPQ
| null | null |
fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062]
|
host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
| null |
PF00429;
|
1.10.287.210;3.90.310.10;
| null |
PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. The R-peptide is released from the C-terminus of the cytoplasmic tail of the TM protein upon particle formation as a result of proteolytic cleavage by the viral protease. Cleavage of this peptide is required for TM to become fusogenic (By similarity). {ECO:0000250}.; PTM: The CXXC motif is highly conserved across a broad range of retroviral envelope proteins. It is thought to participate in the formation of a labile disulfide bond possibly with the CX6CC motif present in the transmembrane protein. Isomerization of the intersubunit disulfide bond to an SU intrachain disulfide bond is thought to occur upon receptor recognition in order to allow membrane fusion (By similarity). {ECO:0000250}.; PTM: The transmembrane protein is palmitoylated. {ECO:0000250}.; PTM: The R-peptide is palmitoylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein. Host cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=The surface protein is not anchored to the viral envelope, but associates with the virion surface through its binding to TM. Both proteins are thought to be concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [R-peptide]: Host cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=The R-peptide is membrane-associated through its palmitate. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity). {ECO:0000250}.; FUNCTION: The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). {ECO:0000250}.
|
Rauscher mink cell focus-inducing virus
|
P06446
|
MATRX_SENDZ
|
MADIYRFPKFSYEDNGTVEPLPLRTGPDKKAIPHIRIVKVGDPPKHGVRYLDLLLLGFFETPKQTTNLGSVSDLTEPTSYSICGSGSLPIGVAKYYGTDQELLKACTDLRITVRRTVRAGEMIVYMVDSIGAPLLPWSGRLRQGMIFNANKVALAPQCLPVDKDIRLRVVFVNGTSLGAITIAKIPKTLADLALPNSISVNLLVTLKTGISTEQKGVLPVLDDQGEKKLNFMVHLGLIRRKVGKIYSVEYCKSKIERMRLIFSLGLIGGISFHVQVNGTLSKTFMSQLAWKRAVCFPLMDVNPHMNMVIWAASVEITGVDAVFQPAIPRDFRYYPNVVAKNIGRIRKL
| null | null |
viral budding via host ESCRT complex [GO:0039702]
|
host cell cytoplasm [GO:0030430]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423]
|
structural constituent of virion [GO:0039660]
|
PF00661;
|
2.70.20.60;2.70.20.50;
|
Morbillivirus/respirovirus/rubulavirus M protein family
|
PTM: A large portion is phosphorylated in the cytoplasm, but not in virion. However, this phosphorylation is not essential for virus replication. {ECO:0000269|PubMed:9281516}.
|
SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm {ECO:0000269|PubMed:6285608}. Host cell membrane {ECO:0000269|PubMed:6285608}; Peripheral membrane protein {ECO:0000269|PubMed:6285608}; Cytoplasmic side {ECO:0000269|PubMed:6285608}. Note=During bud formation, associates at the inner side of the plasma membrane of infected cells.
| null | null | null | null | null |
FUNCTION: Plays a crucial role in virion assembly and budding. Forms a shell at the inner face of the plasma membrane and concentrates the HN and F glycoproteins. Acts as a negative regulator for transcription and replication by sticking to the nucleocapsid. This effect might be regulated by the cytoplasmic interaction with tubulin that dissociates the M protein from the nucleocapsid.
|
Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ))
|
P06447
|
L_SENDZ
|
MDGQESSQNPSDILYPECHLNSPIVRGKIAQLHVLLDVNQPYRLKDDSIINITKHKIRNGGLSPRQIKIRSLGKALQRTIKDLDRYTFEPYPTYSQELLRLDIPEICDKIRSVFAVSDRLTRELSSGFQDLWLNIFKQLGNIEGREGYDPLQDIGTIPEITDKYSRNRWYRPFLTWFSIKYDMRWMQKTRPGGPLDTSNSHNLLECKSYTLVTYGDLVMILNKLTLTGYILTPELVLMYCDVVEGRWNMSAAGHLDKKSIGITSKGEELWELVDSLFSSLGEEIYNVIALLEPLSLALIQLNDPVIPLRGAFMRHVLTELQTVLTSRDVYTDAEADTIVESLLAIFHGTSIDEKAEIFSFFRTFGHPSLEAVTAADKVRAHMYAQKAIKLKTLYECHAVFCTIIINGYRERHGGQWPPCDFPDHVCLELRNAQGSNTAISYECAVDNYTSFIGFKFRKFIEPQLDEDLTIYMKDKALSPRKEAWDSVYPDSNLYYKAPESEETRRLIEVFINDENFNPEEIINYVESGDWLKDEEFNISYSLKEKEIKQEGRLFAKMTYKMRAVQVLAETLLAKGIGELFRENGMVKGEIDLLKRLTTLSVSGVPRTDSVYNNSKSSEKRNEGMENKNSGGYWDEKKRSRHEFKATDSSTDGYETLSCFLTTDLKKYCLNWRFESTALFGQRCNEIFGFKTFFNWMHPVLERCTIYVGDPYCPVADRMHRQLQDHADSGIFIHNPRGGIEGYCQKLWTLISISAIHLAAVRVGVRVSAMVQGDNQAIAVTSRVPVAQTYKQKKNHVYEEITKYFGALRHVMFDVGHELKLNETIISSKMFVYSKRIYYDGKILPQCLKALTKCVFWSETLVDENRSACSNISTSIAKAIENGYSPILGYCIALYKTCQQVCISLGMTINPTISPTVRDQYFKGKNWLRCAVLIPANVGGFNYMSTSRCFVRNIGDPAVAALADLKRFIRADLLDKQVLYRVMNQEPGDSSFLDWASDPYSCNLPHSQSITTIIKNITARSVLQESPNPLLSGLFTETSGEEDLNLASFLMDRKVILPRVAHEILGNSLTGVREAIAGMLDTTKSLVRASVRKGGLSYGILRRLVNYDLLQYETLTRTLRKPVKDNIEYEYMCSVELAVGLRQKMWIHLTYGRPIHGLETPDPLELLRGIFIEGSEVCKLCRSEGADPIYTWFYLPDNIDLDTLTNGCPAIRIPYFGSATDERSEAQLGYVRNLSKPAKAAIRIAMVYTWAYGTDEISWMEAALIAQTRANLSLENLKLLTPVSTSTNLSHRLKDTATQMKFSSATLVRASRFITISNDNMALKEAGESKDTNLVYQQIMLTGLSLFEFNMRYKKGSLGKPLILHLHLNNGCCIMESPQEANIPPRSTLDLEITQENNKLIYDPDPLKDVDLELFSKVRDVVHTVDMTYWSDDEVIRATSICTAMTIADTMSQLDRDNLKEMIALVNDDDVNSLITEFMVIDVPLFCSTFGGILVNQFAYSLYGLNIRGREEIWGHVVRILKDTSHAVLKVLSNALSHPKIFKRFWNAGVVEPVYGPNLSNQDKILLALSVCEYSVDLFMHDWQGGVPLEIFICDNDPDVADMRRSSFLARHLAYLCSLAEISRDGPRLESMNSLERLESLKSYLELTFLDDPVLRYSQLTGLVIKVFPSTLTYIRKSSIKVLRTRGIGVPEVLEDWDPEADNALLDGIAAEIQQNIPLGHQTRAPFWGLRVSKSQVLRLRGYKEITRGEIGRSGVGLTLPFDGRYLSHQLRLFGINSTSCLKALELTYLLSPLVDKDKDRLYLGEGAGAMLSCYDATLGPCINYYNSGVYSCDVNGQRELNIYPAEVALVGKKLNNVTSLGQRVKVLFNGNPGSTWIGNDECEALIWNELQNSSIGLVHCDMEGGDHKDDQVVLHEHYSVIRIAYLVGDRDVVLISKIAPRLGTDWTRQLSLYLRYWDEVNLIVLKTSNPASTEMYLLSRHPKSDIIEDSKTVLASLLPLSKEDSIKIEKWILIEKAKAHEWVTRELREGSSSSGMLRPYHQALQTFGFEPNLYKLSRDFLSTMNIADTHNCMIAFNRVLKDTIFEWARITESDKRLKLTGKYDLYPVRDSGKLKTISRRLVLSWISLSMSTRLVTGSFPDQKFEARLQLGIVSLSSREIRNLRVITKTLLDRFEDIIHSITYRFLTKEIKILMKILGAVKMFGARQNEYTTVIDDGSLGDIEPYDSS
|
2.1.1.375; 2.7.7.48; 2.7.7.88; 3.6.1.-
| null | null |
host cell cytoplasm [GO:0030430]; virion component [GO:0044423]
|
ATP binding [GO:0005524]; GTPase activity [GO:0003924]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; RNA-dependent RNA polymerase activity [GO:0003968]
|
PF14318;PF00946;
| null |
Paramyxovirus L protein family
| null |
SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + 2 S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + H(+) + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:65376, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16798, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156483, ChEBI:CHEBI:156484; EC=2.1.1.375; Evidence={ECO:0000269|PubMed:15574411}; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:65380, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16801, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156482, ChEBI:CHEBI:156484; Evidence={ECO:0000269|PubMed:15574411}; CATALYTIC ACTIVITY: Reaction=a 5'-end triphospho-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + GDP + H(+) = a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + diphosphate; Xref=Rhea:RHEA:65436, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16799, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58189, ChEBI:CHEBI:156484, ChEBI:CHEBI:156503; EC=2.7.7.88; Evidence={ECO:0000250|UniProtKB:P28887}; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:65440, Rhea:RHEA-COMP:16798, Rhea:RHEA-COMP:16801, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156482, ChEBI:CHEBI:156483; Evidence={ECO:0000250|UniProtKB:P03523}; CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P28887};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6 for mRNA (guanine-N(7)-)-methyltransferase activity.;
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius.;
|
FUNCTION: RNA-directed RNA polymerase that catalyzes the transcription of viral mRNAs, their capping and polyadenylation. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The viral polymerase binds to the genomic RNA at the 3' leader promoter, and transcribes subsequently all viral mRNAs with a decreasing efficiency. The first gene is the most transcribed, and the last the least transcribed. The viral phosphoprotein acts as a processivity factor. Capping is concommitant with initiation of mRNA transcription. Indeed, a GDP polyribonucleotidyl transferase (PRNTase) adds the cap structure when the nascent RNA chain length has reached few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and facilitates subsequent guanine-N-7 methylation, both activities being carried by the viral polymerase. Polyadenylation of mRNAs occur by a stuttering mechanism at a slipery stop site present at the end viral genes. After finishing transcription of a mRNA, the polymerase can resume transcription of the downstream gene. {ECO:0000250|UniProtKB:P03523, ECO:0000269|PubMed:11080486, ECO:0000269|PubMed:15574411}.; FUNCTION: RNA-directed RNA polymerase that catalyzes the replication of viral genomic RNA. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The replicase mode is dependent on intracellular N protein concentration. In this mode, the polymerase replicates the whole viral genome without recognizing transcriptional signals, and the replicated genome is not caped or polyadenylated. {ECO:0000250|UniProtKB:P03523}.
|
Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ))
|
P06454
|
PTMA_HUMAN
|
MSDAAVDTSSEITTKDLKEKKEVVEEAENGRDAPANGNAENEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAESATGKRAAEDDEDDDVDTKKQKTDEDD
| null | null |
DNA-templated transcription [GO:0006351]; negative regulation of apoptotic process [GO:0043066]; positive regulation of transcription by RNA polymerase II [GO:0045944]
|
cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription factor binding [GO:0140297]; histone binding [GO:0042393]; ion binding [GO:0043167]
|
PF03247;
| null |
Pro/parathymosin family
|
PTM: Covalently linked to a small RNA of about 20 nucleotides. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections.
|
Homo sapiens (Human)
|
P06463
|
VE6_HPV18
|
MARFEDPTRRPYKLPDLCTELNTSLQDIEITCVYCKTVLELTEVFEFAFKDLFVVYRDSIPHAACHKCIDFYSRIRELRHYSDSVYGDTLEKLTNTGLYNLLIRCLRCQKPLNPAEKLRHLNEKRRFHNIAGHYRGQCHSCCNRARQERLQRRRETQV
| null | null |
DNA-templated transcription [GO:0006351]; negative regulation of DNA-templated transcription [GO:0045892]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity [GO:0039548]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]
|
DNA binding [GO:0003677]; PDZ domain binding [GO:0030165]; zinc ion binding [GO:0008270]
|
PF00518;
|
3.30.240.40;
|
Papillomaviridae E6 protein family
| null |
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04006}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04006}.
| null | null | null | null | null |
FUNCTION: Plays a major role in the induction and maintenance of cellular transformation. Acts mainly as an oncoprotein by stimulating the destruction of many host cell key regulatory proteins. E6 associates with host UBE3A/E6-AP ubiquitin-protein ligase, and inactivates tumor suppressors TP53 and TP73 by targeting them to the 26S proteasome for degradation. In turn, DNA damage and chromosomal instabilities increase and lead to cell proliferation and cancer development. The complex E6/E6AP targets several other substrates to degradation via the proteasome including host DLG1 or NFX1, a repressor of human telomerase reverse transcriptase (hTERT). The resulting increased expression of hTERT prevents the shortening of telomere length leading to cell immortalization. Other cellular targets including BAK1, Fas-associated death domain-containing protein (FADD) and procaspase 8, are degraded by E6/E6AP causing inhibition of apoptosis. E6 also inhibits immune response by interacting with host IRF3 and TYK2. These interactions prevent IRF3 transcriptional activities and inhibit TYK2-mediated JAK-STAT activation by interferon alpha resulting in inhibition of the interferon signaling pathway. {ECO:0000255|HAMAP-Rule:MF_04006}.
|
Human papillomavirus type 18
|
P06467
|
HBAZ_MOUSE
|
MSLMKNERAIIMSMWEKMAAQAEPIGTETLERLFCSYPQTKTYFPHFDLHHGSQQLRAHGFKIMTAVGDAVKSIDNLSSALTKLSELHAYILRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSILTEKYR
| null | null |
carbon dioxide transport [GO:0015670]; erythrocyte maturation [GO:0043249]; hydrogen peroxide catabolic process [GO:0042744]; negative regulation of transcription by RNA polymerase II [GO:0000122]; oxygen transport [GO:0015671]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: The zeta chain is an alpha-type chain of mammalian embryonic hemoglobin. {ECO:0000250}.
|
Mus musculus (Mouse)
|
P06473
|
GB_HCMVA
|
MESRIWCLVVCVNLCIVCLGAAVSSSSTSHATSSTHNGSHTSRTTSAQTRSVYSQHVTSSEAVSHRANETIYNTTLKYGDVVGVNTTKYPYRVCSMAQGTDLIRFERNIICTSMKPINEDLDEGIMVVYKRNIVAHTFKVRVYQKVLTFRRSYAYIYTTYLLGSNTEYVAPPMWEIHHINKFAQCYSSYSRVIGGTVFVAYHRDSYENKTMQLIPDDYSNTHSTRYVTVKDQWHSRGSTWLYRETCNLNCMLTITTARSKYPYHFFATSTGDVVYISPFYNGTNRNASYFGENADKFFIFPNYTIVSDFGRPNAAPETHRLVAFLERADSVISWDIQDEKNVTCQLTFWEASERTIRSEAEDSYHFSSAKMTATFLSKKQEVNMSDSALDCVRDEAINKLQQIFNTSYNQTYEKYGNVSVFETSGGLVVFWQGIKQKSLVELERLANRSSLNITHRTRRSTSDNNTTHLSSMESVHNLVYAQLQFTYDTLRGYINRALAQIAEAWCVDQRRTLEVFKELSKINPSAILSAIYNKPIAARFMGDVLGLASCVTINQTSVKVLRDMNVKESPGRCYSRPVVIFNFANSSYVQYGQLGEDNEILLGNHRTEECQLPSLKIFIAGNSAYEYVDYLFKRMIDLSSISTVDSMIALDIDPLENTDFRVLELYSQKELRSSNVFDLEEIMREFNSYKQRVKYVEDKVVDPLPPYLKGLDDLMSGLGAAGKAVGVAIGAVGGAVASVVEGVATFLKNPFGAFTIILVAIAVVIITYLIYTRQRRLCTQPLQNLFPYLVSADGTTVTSGSTKDTSLQAPPSYEESVYNSGRKGPGPPSSDASTAAPPYTNEQAYQMLLALARLDAEQRAQQNGTDSLDGQTGTQDKGQKPNLLDRLRHRKNGYRHLKDSDEEENV
| null | null |
symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062]
|
host cell endosome membrane [GO:0044175]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
| null |
PF17416;PF17417;PF00606;PF12154;
|
1.20.5.1890;2.30.29.100;2.30.30.1230;6.10.250.3280;
|
Herpesviridae glycoprotein B family
|
PTM: A proteolytic cleavage by host furin generates two subunits that remain linked by disulfide bonds. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-Rule:MF_04032}.
| null | null | null | null | null |
FUNCTION: Envelope glycoprotein that plays a role in host cell entry, cell to-cell virus transmission, and fusion of infected cells. May be involved in the initial attachment via binding to heparan sulfate together with the gM/gN complex that binds heparin with higher affinity. Interacts with host integrin ITGB1, PDGFRA and EGFR that likely serve as postattachment entry receptors. Participates also in the fusion of viral and cellular membranes leading to virus entry into the host cell. Membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. {ECO:0000269|PubMed:12433371, ECO:0000269|PubMed:19193805}.
|
Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
|
P06487
|
GI_HHV11
|
MPCRPLQGLVLVGLWVCATSLVVRGPTVSLVSNSFVDAGALGPDGVVEEDLLILGELRFVGDQVPHTTYYDGGVELWHYPMGHKCPRVVHVVTVTACPRRPAVAFALCRATDSTHSPAYPTLELNLAQQPLLRVQRATRDYAGVYVLRVWVGDAPNASLFVLGMAIAAEGTLAYNGSAYGSCDPKLLPSSAPRLAPASVYQPAPNQASTPSTTTSTPSTTIPAPSTTIPAPQASTTPFPTGDPKPQPPGVNHEPPSNATRATRDSRYALTVTQIIQIAIPASIIALVFLGSCICFIHRCQRRYRRSRRPIYSPQMPTGISCAVNEAAMARLGAELKSHPSTPPKSRRRSSRTPMPSLTAIAEESEPAGAAGLPTPPVDPTTPTPTPPLLV
| null | null |
virus-mediated perturbation of host defense response [GO:0019049]
|
host cell [GO:0043657]; host cell Golgi apparatus [GO:0044177]; host cell junction [GO:0044156]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
| null |
PF01688;
| null |
Alphaherpesvirinae glycoprotein I family
| null |
SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:18596102}; Single-pass membrane protein {ECO:0000255}. Host cell membrane {ECO:0000269|PubMed:16537585}; Single-pass type I membrane protein {ECO:0000255}. Host cell junction {ECO:0000269|PubMed:11134295, ECO:0000269|PubMed:16537585}. Host Golgi apparatus, host trans-Golgi network {ECO:0000269|PubMed:16537585}. Note=During virion morphogenesis, this protein probably accumulates in the trans-Golgi where secondary envelopment occurs. The heterodimer gE/gI then redistributes to cell junctions to promote cell-cell spread later in the infection. {ECO:0000269|PubMed:11134295}.
| null | null | null | null | null |
FUNCTION: In epithelial cells, the heterodimer gE/gI is required for the cell-to-cell spread of the virus, by sorting nascent virions to cell junctions. Once the virus reaches the cell junctions, virus particles can spread to adjacent cells extremely rapidly through interactions with cellular receptors that accumulate at these junctions. Implicated in basolateral spread in polarized cells. In neuronal cells, gE/gI is essential for the anterograde spread of the infection throughout the host nervous system. Together with US9, the heterodimer gE/gI is involved in the sorting and transport of viral structural components toward axon tips. {ECO:0000269|PubMed:11134295, ECO:0000269|PubMed:14734541, ECO:0000269|PubMed:2831396}.; FUNCTION: The heterodimer gE/gI serves as a receptor for the Fc part of human IgG. Dissociation of gE/gI from IgG occurs at acidic pH. May thus be involved in anti-HSV antibodies bipolar bridging, followed by intracellular endocytosis and degradation, thereby interfering with host Ig-mediated immune responses.
|
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
|
P06492
|
VP16_HHV11
|
MDLLVDELFADMNADGASPPPPRPAGGPKNTPAAPPLYATGRLSQAQLMPSPPMPVPPAALFNRLLDDLGFSAGPALCTMLDTWNEDLFSALPTNADLYRECKFLSTLPSDVVEWGDAYVPERTQIDIRAHGDVAFPTLPATRDGLGLYYEALSRFFHAELRAREESYRTVLANFCSALYRYLRASVRQLHRQAHMRGRDRDLGEMLRATIADRYYRETARLARVLFLHLYLFLTREILWAAYAEQMMRPDLFDCLCCDLESWRQLAGLFQPFMFVNGALTVRGVPIEARRLRELNHIREHLNLPLVRSAATEEPGAPLTTPPTLHGNQARASGYFMVLIRAKLDSYSSFTTSPSEAVMREHAYSRARTKNNYGSTIEGLLDLPDDDAPEEAGLAAPRLSFLPAGHTRRLSTAPPTDVSLGDELHLDGEDVAMAHADALDDFDLDMLGDGDSPGPGFTPHDSAPYGALDMADFEFEQMFTDALGIDEYGG
| null | null |
biological process involved in interaction with host [GO:0051701]; DNA-templated viral transcription [GO:0039695]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein-containing complex assembly [GO:0065003]; regulation of viral transcription [GO:0046782]
|
host cell cytoplasm [GO:0030430]; host cell cytoplasmic vesicle [GO:0044161]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; replication compartment [GO:0046809]; transcription regulator complex [GO:0005667]; viral tegument [GO:0019033]
|
core promoter sequence-specific DNA binding [GO:0001046]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor binding [GO:0140297]; molecular function activator activity [GO:0140677]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; structural constituent of virion [GO:0039660]; transcription coactivator activity [GO:0003713]
|
PF02232;PF12149;
|
1.10.1290.10;
|
Herpesviridae tegument protein VP16 protein family
| null |
SUBCELLULAR LOCATION: Virion tegument {ECO:0000250|UniProtKB:P04486}. Host nucleus {ECO:0000250|UniProtKB:P04486}.
| null | null | null | null | null |
FUNCTION: In the early stage of viral replication, acts as a transcriptional activator of immediate-early (IE) gene products (alpha-genes), which is released by invading virions (PubMed:12826401, PubMed:23029222). Recruits P-TEFb to the viral alpha-gene promoters and overcomes transcriptional inhibition by ICP22 to promote transcription of IE genes (PubMed:15654739, PubMed:23029222). VP16-induced complex represents a regulatory switch: when it is on, it promotes IE-gene expression and thus lytic infection, and when it is off, it limits IE-gene transcription favoring latent infection (PubMed:12826401). Acts as a key activator of lytic infection by initiating the lytic program through the assembly of the transcriptional regulatory VP16-induced complex composed of VP16 and two cellular factors, HCFC1 and POU2F1 (PubMed:10398682). This complex recognizes the core motif 'TAATGARAT' in alpha-gene promoters (PubMed:12826401). In the late stage of viral replication, VP16, as a tegument, is involved in viral assembly (PubMed:19279114). {ECO:0000269|PubMed:10398682, ECO:0000269|PubMed:12826401, ECO:0000269|PubMed:15654739, ECO:0000269|PubMed:19279114, ECO:0000269|PubMed:23029222}.; FUNCTION: May play a role in the aggregation of tegument proteins around nucleocapsids during virus morphogenesis. {ECO:0000305}.
|
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
|
P06493
|
CDK1_HUMAN
|
MEDYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFLSMDLKKYLDSIPPGQYMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHEVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNTFPKWKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYFNDLDNQIKKM
|
2.7.11.22; 2.7.11.23
| null |
animal organ regeneration [GO:0031100]; apoptotic process [GO:0006915]; cell division [GO:0051301]; cell migration [GO:0016477]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to organic cyclic compound [GO:0071407]; centrosome cycle [GO:0007098]; chromosome condensation [GO:0030261]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; epithelial cell differentiation [GO:0030855]; ERK1 and ERK2 cascade [GO:0070371]; fibroblast proliferation [GO:0048144]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; Golgi disassembly [GO:0090166]; microtubule cytoskeleton organization [GO:0000226]; microtubule cytoskeleton organization involved in mitosis [GO:1902850]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; mitotic nuclear membrane disassembly [GO:0007077]; negative regulation of apoptotic process [GO:0043066]; negative regulation of gene expression [GO:0010629]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; positive regulation of cardiac muscle cell proliferation [GO:0060045]; positive regulation of DNA replication [GO:0045740]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; positive regulation of gene expression [GO:0010628]; positive regulation of mitochondrial ATP synthesis coupled electron transport [GO:1905448]; positive regulation of mitotic sister chromatid segregation [GO:0062033]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of protein localization to nucleus [GO:1900182]; pronuclear fusion [GO:0007344]; protein localization to kinetochore [GO:0034501]; protein phosphorylation [GO:0006468]; protein-containing complex assembly [GO:0065003]; regulation of circadian rhythm [GO:0042752]; regulation of embryonic development [GO:0045995]; regulation of Schwann cell differentiation [GO:0014038]; response to activity [GO:0014823]; response to amine [GO:0014075]; response to axon injury [GO:0048678]; response to cadmium ion [GO:0046686]; response to copper ion [GO:0046688]; response to ethanol [GO:0045471]; response to toxic substance [GO:0009636]; response to xenobiotic stimulus [GO:0009410]; rhythmic process [GO:0048511]; ventricular cardiac muscle cell development [GO:0055015]
|
centrosome [GO:0005813]; chromosome, telomeric region [GO:0000781]; cyclin A2-CDK1 complex [GO:0097122]; cyclin B1-CDK1 complex [GO:0097125]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; midbody [GO:0030496]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle microtubule [GO:0005876]
|
ATP binding [GO:0005524]; chromatin binding [GO:0003682]; cyclin binding [GO:0030332]; cyclin-dependent protein kinase activity [GO:0097472]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; histone kinase activity [GO:0035173]; Hsp70 protein binding [GO:0030544]; kinase activity [GO:0016301]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353]; virus receptor activity [GO:0001618]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily
|
PTM: Phosphorylation at Thr-161 by CAK/CDK7 activates kinase activity (PubMed:20360007). Phosphorylation at Thr-14 and Tyr-15 by PKMYT1 prevents nuclear translocation (PubMed:7569953). Phosphorylation at Tyr-15 by WEE1 and WEE2 inhibits the protein kinase activity and acts as a negative regulator of entry into mitosis (G2 to M transition) (PubMed:20360007). Phosphorylation by PKMYT1 and WEE1 takes place during mitosis to keep CDK1-cyclin-B complexes inactive until the end of G2 (PubMed:20360007, PubMed:7569953). By the end of G2, PKMYT1 and WEE1 are inactivated, but CDC25A and CDC25B are activated (PubMed:20360007). Dephosphorylation by active CDC25A and CDC25B at Thr-14 and Tyr-15, leads to CDK1 activation at the G2-M transition (PubMed:20360007). Phosphorylation at Tyr-15 by WEE2 during oogenesis is required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, leading to prevent meiotic reentry (PubMed:29606300). Phosphorylation by WEE2 is also required for metaphase II exit during egg activation to ensure exit from meiosis in oocytes and promote pronuclear formation (PubMed:29606300). Phosphorylated at Tyr-4 by PKR/EIF2AK2 upon genotoxic stress (PubMed:20395957). This phosphorylation triggers CDK1 polyubiquitination and subsequent proteolysis, thus leading to G2 arrest (PubMed:20395957). In response to UV irradiation, phosphorylation at Tyr-15 by PRKCD activates the G2/M DNA damage checkpoint (PubMed:19917613). {ECO:0000269|PubMed:19917613, ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:20395957, ECO:0000269|PubMed:29606300, ECO:0000269|PubMed:7569953}.; PTM: Polyubiquitinated upon genotoxic stress. {ECO:0000269|PubMed:20395957}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11440}. Cytoplasm {ECO:0000250|UniProtKB:P11440}. Mitochondrion {ECO:0000269|PubMed:19917720}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm, cytoskeleton, spindle. Note=Cytoplasmic during the interphase. Colocalizes with SIRT2 on centrosome during prophase and on splindle fibers during metaphase of the mitotic cell cycle. Reversibly translocated from cytoplasm to nucleus when phosphorylated before G2-M transition when associated with cyclin-B1. Accumulates in mitochondria in G2-arrested cells upon DNA-damage.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; Evidence={ECO:0000269|PubMed:19202191, ECO:0000269|PubMed:2188730, ECO:0000269|PubMed:23355470, ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:26829474, ECO:0000269|PubMed:30704899}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; Evidence={ECO:0000269|PubMed:23355470, ECO:0000269|PubMed:26829474, ECO:0000269|PubMed:30704899}; CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23; Evidence={ECO:0000250|UniProtKB:P11440};
| null | null | null | null |
FUNCTION: Plays a key role in the control of the eukaryotic cell cycle by modulating the centrosome cycle as well as mitotic onset; promotes G2-M transition via association with multiple interphase cyclins (PubMed:16407259, PubMed:16933150, PubMed:17459720, PubMed:18356527, PubMed:19509060, PubMed:19917720, PubMed:20171170, PubMed:20935635, PubMed:20937773, PubMed:21063390, PubMed:2188730, PubMed:23355470, PubMed:2344612, PubMed:23601106, PubMed:23602554, PubMed:25556658, PubMed:26829474, PubMed:27814491, PubMed:30139873, PubMed:30704899). Phosphorylates PARVA/actopaxin, APC, AMPH, APC, BARD1, Bcl-xL/BCL2L1, BRCA2, CALD1, CASP8, CDC7, CDC20, CDC25A, CDC25C, CC2D1A, CENPA, CSNK2 proteins/CKII, FZR1/CDH1, CDK7, CEBPB, CHAMP1, DMD/dystrophin, EEF1 proteins/EF-1, EZH2, KIF11/EG5, EGFR, FANCG, FOS, GFAP, GOLGA2/GM130, GRASP1, UBE2A/hHR6A, HIST1H1 proteins/histone H1, HMGA1, HIVEP3/KRC, KAT5, LMNA, LMNB, LBR, LATS1, MAP1B, MAP4, MARCKS, MCM2, MCM4, MKLP1, MLST8, MYB, NEFH, NFIC, NPC/nuclear pore complex, PITPNM1/NIR2, NPM1, NCL, NUCKS1, NPM1/numatrin, ORC1, PRKAR2A, EEF1E1/p18, EIF3F/p47, p53/TP53, NONO/p54NRB, PAPOLA, PLEC/plectin, RB1, TPPP, UL40/R2, RAB4A, RAP1GAP, RBBP8/CtIP, RCC1, RPS6KB1/S6K1, KHDRBS1/SAM68, ESPL1, SKI, BIRC5/survivin, STIP1, TEX14, beta-tubulins, MAPT/TAU, NEDD1, VIM/vimentin, TK1, FOXO1, RUNX1/AML1, SAMHD1, SIRT2, CGAS and RUNX2 (PubMed:16407259, PubMed:16933150, PubMed:17459720, PubMed:18356527, PubMed:19202191, PubMed:19509060, PubMed:19917720, PubMed:20171170, PubMed:20935635, PubMed:20937773, PubMed:21063390, PubMed:2188730, PubMed:23355470, PubMed:2344612, PubMed:23601106, PubMed:23602554, PubMed:25556658, PubMed:26829474, PubMed:27814491, PubMed:30704899, PubMed:32351706, PubMed:34741373). CDK1/CDC2-cyclin-B controls pronuclear union in interphase fertilized eggs (PubMed:18480403, PubMed:20360007). Essential for early stages of embryonic development (PubMed:18480403, PubMed:20360007). During G2 and early mitosis, CDC25A/B/C-mediated dephosphorylation activates CDK1/cyclin complexes which phosphorylate several substrates that trigger at least centrosome separation, Golgi dynamics, nuclear envelope breakdown and chromosome condensation (PubMed:18480403, PubMed:20360007, PubMed:2188730, PubMed:2344612, PubMed:30139873). Once chromosomes are condensed and aligned at the metaphase plate, CDK1 activity is switched off by WEE1- and PKMYT1-mediated phosphorylation to allow sister chromatid separation, chromosome decondensation, reformation of the nuclear envelope and cytokinesis (PubMed:18480403, PubMed:20360007). Phosphorylates KRT5 during prometaphase and metaphase (By similarity). Inactivated by PKR/EIF2AK2- and WEE1-mediated phosphorylation upon DNA damage to stop cell cycle and genome replication at the G2 checkpoint thus facilitating DNA repair (PubMed:20360007). Reactivated after successful DNA repair through WIP1-dependent signaling leading to CDC25A/B/C-mediated dephosphorylation and restoring cell cycle progression (PubMed:20395957). Catalyzes lamin (LMNA, LMNB1 and LMNB2) phosphorylation at the onset of mitosis, promoting nuclear envelope breakdown (PubMed:2188730, PubMed:2344612, PubMed:37788673). In proliferating cells, CDK1-mediated FOXO1 phosphorylation at the G2-M phase represses FOXO1 interaction with 14-3-3 proteins and thereby promotes FOXO1 nuclear accumulation and transcription factor activity, leading to cell death of postmitotic neurons (PubMed:18356527). The phosphorylation of beta-tubulins regulates microtubule dynamics during mitosis (PubMed:16371510). NEDD1 phosphorylation promotes PLK1-mediated NEDD1 phosphorylation and subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation (PubMed:19509060). In addition, CC2D1A phosphorylation regulates CC2D1A spindle pole localization and association with SCC1/RAD21 and centriole cohesion during mitosis (PubMed:20171170). The phosphorylation of Bcl-xL/BCL2L1 after prolongated G2 arrest upon DNA damage triggers apoptosis (PubMed:19917720). In contrast, CASP8 phosphorylation during mitosis prevents its activation by proteolysis and subsequent apoptosis (PubMed:20937773). This phosphorylation occurs in cancer cell lines, as well as in primary breast tissues and lymphocytes (PubMed:20937773). EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing (PubMed:20935635). CALD1 phosphorylation promotes Schwann cell migration during peripheral nerve regeneration (By similarity). CDK1-cyclin-B complex phosphorylates NCKAP5L and mediates its dissociation from centrosomes during mitosis (PubMed:26549230). Regulates the amplitude of the cyclic expression of the core clock gene BMAL1 by phosphorylating its transcriptional repressor NR1D1, and this phosphorylation is necessary for SCF(FBXW7)-mediated ubiquitination and proteasomal degradation of NR1D1 (PubMed:27238018). Phosphorylates EML3 at 'Thr-881' which is essential for its interaction with HAUS augmin-like complex and TUBG1 (PubMed:30723163). Phosphorylates CGAS during mitosis, leading to its inhibition, thereby preventing CGAS activation by self DNA during mitosis (PubMed:32351706). {ECO:0000250|UniProtKB:P11440, ECO:0000250|UniProtKB:P39951, ECO:0000269|PubMed:16371510, ECO:0000269|PubMed:16407259, ECO:0000269|PubMed:16933150, ECO:0000269|PubMed:17459720, ECO:0000269|PubMed:18356527, ECO:0000269|PubMed:18480403, ECO:0000269|PubMed:19202191, ECO:0000269|PubMed:19509060, ECO:0000269|PubMed:19917720, ECO:0000269|PubMed:20171170, ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:20395957, ECO:0000269|PubMed:20935635, ECO:0000269|PubMed:20937773, ECO:0000269|PubMed:21063390, ECO:0000269|PubMed:2188730, ECO:0000269|PubMed:23355470, ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:23601106, ECO:0000269|PubMed:23602554, ECO:0000269|PubMed:25556658, ECO:0000269|PubMed:26549230, ECO:0000269|PubMed:26829474, ECO:0000269|PubMed:27238018, ECO:0000269|PubMed:27814491, ECO:0000269|PubMed:30139873, ECO:0000269|PubMed:30704899, ECO:0000269|PubMed:30723163, ECO:0000269|PubMed:32351706, ECO:0000269|PubMed:34741373, ECO:0000269|PubMed:37788673}.; FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. {ECO:0000269|PubMed:21516087}.
|
Homo sapiens (Human)
|
P06494
|
ERBB2_RAT
|
MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNRDPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQLAPVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTCPYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSDNVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSLRDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHTVPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVARCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATVVGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPSEGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPEYVNQSEVQPQPPLTPEGPLPPVRPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLVPREGTASPPHPSPAFSPAFDNLYYWDQNSSEQGPPPSNFEGTPTAENPEYLGLDVPV
|
2.7.10.1
| null |
cell surface receptor signaling pathway [GO:0007166]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to growth factor stimulus [GO:0071363]; ERBB2-EGFR signaling pathway [GO:0038134]; ERBB2-ERBB3 signaling pathway [GO:0038133]; ERBB2-ERBB4 signaling pathway [GO:0038135]; estrous cycle [GO:0044849]; glial cell differentiation [GO:0010001]; heart development [GO:0007507]; immature T cell proliferation in thymus [GO:0033080]; intracellular signal transduction [GO:0035556]; liver development [GO:0001889]; mammary gland involution [GO:0060056]; motor neuron axon guidance [GO:0008045]; myelination [GO:0042552]; negative regulation of apoptotic process [GO:0043066]; negative regulation of immature T cell proliferation in thymus [GO:0033088]; nervous system development [GO:0007399]; neurogenesis [GO:0022008]; neuromuscular junction development [GO:0007528]; neuron differentiation [GO:0030182]; neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0099645]; oligodendrocyte differentiation [GO:0048709]; peripheral nervous system development [GO:0007422]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phosphorylation [GO:0016310]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell growth [GO:0030307]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of gene expression [GO:0010628]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of Ras protein signal transduction [GO:0046579]; positive regulation of Rho protein signal transduction [GO:0035025]; positive regulation of transcription by RNA polymerase I [GO:0045943]; positive regulation of translation [GO:0045727]; regulation of cell differentiation [GO:0045595]; regulation of cell population proliferation [GO:0042127]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of microtubule-based process [GO:0032886]; response to axon injury [GO:0048678]; response to progesterone [GO:0032570]; response to xenobiotic stimulus [GO:0009410]; Schwann cell development [GO:0014044]; semaphorin-plexin signaling pathway [GO:0071526]; signal transduction [GO:0007165]; skeletal muscle tissue development [GO:0007519]; sympathetic nervous system development [GO:0048485]; tongue development [GO:0043586]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]; wound healing [GO:0042060]
|
apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; ERBB3:ERBB2 complex [GO:0038143]; lateral loop [GO:0043219]; microvillus [GO:0005902]; myelin sheath [GO:0043209]; neuromuscular junction [GO:0031594]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; receptor complex [GO:0043235]; ruffle membrane [GO:0032587]; semaphorin receptor complex [GO:0002116]
|
ATP binding [GO:0005524]; coreceptor activity [GO:0015026]; DNA binding [GO:0003677]; ErbB-3 class receptor binding [GO:0043125]; Hsp90 protein binding [GO:0051879]; identical protein binding [GO:0042802]; protein heterodimerization activity [GO:0046982]; protein tyrosine kinase activity [GO:0004713]; protein-containing complex binding [GO:0044877]; receptor tyrosine kinase binding [GO:0030971]; RNA polymerase I core binding [GO:0001042]; signaling receptor binding [GO:0005102]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; transmembrane signaling receptor activity [GO:0004888]; ubiquitin protein ligase binding [GO:0031625]
|
PF00757;PF14843;PF07714;PF01030;PF21314;
|
1.20.5.100;4.10.1140.10;3.80.20.20;1.10.510.10;
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Protein kinase superfamily, Tyr protein kinase family, EGF receptor subfamily
|
PTM: Autophosphorylated. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Ligand-binding increases phosphorylation on tyrosine residues. Signaling via SEMA4C promotes phosphorylation at Tyr-1250. Dephosphorylated by PTPN12. {ECO:0000250|UniProtKB:P04626}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04626}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P04626}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626}. Early endosome {ECO:0000250|UniProtKB:P04626}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P04626}. Nucleus {ECO:0000250|UniProtKB:P04626}. Note=Translocation to the nucleus requires endocytosis, probably endosomal sorting and is mediated by importin beta-1/KPNB1. Also detected in endosome-to-TGN retrograde vesicles. Internalized from the cell membrane in response to EGF stimulation. {ECO:0000250|UniProtKB:P04626}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). Interacts (preferentially with the tyrosine phosphorylated form) with CPNE3; this interaction occurs at the cell membrane and is increased in a growth factor heregulin-dependent manner (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P04626}.; FUNCTION: In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth (By similarity). {ECO:0000250}.
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Rattus norvegicus (Rat)
|
P06525
|
ADH1_ARATH
|
MSTTGQIIRCKAAVAWEAGKPLVIEEVEVAPPQKHEVRIKILFTSLCHTDVYFWEAKGQTPLFPRIFGHEAGGIVESVGEGVTDLQPGDHVLPIFTGECGECRHCHSEESNMCDLLRINTERGGMIHDGESRFSINGKPIYHFLGTSTFSEYTVVHSGQVAKINPDAPLDKVCIVSCGLSTGLGATLNVAKPKKGQSVAIFGLGAVGLGAAEGARIAGASRIIGVDFNSKRFDQAKEFGVTECVNPKDHDKPIQQVIAEMTDGGVDRSVECTGSVQAMIQAFECVHDGWGVAVLVGVPSKDDAFKTHPMNFLNERTLKGTFFGNYKPKTDIPGVVEKYMNKELELEKFITHTVPFSEINKAFDYMLKGESIRCIITMGA
|
1.1.1.1
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:25447145}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:25447145};
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cellular response to hypoxia [GO:0071456]; formaldehyde catabolic process [GO:0046294]; positive regulation of cellular response to hypoxia [GO:1900039]; response to abscisic acid [GO:0009737]; response to caffeine [GO:0031000]; response to cold [GO:0009409]; response to estradiol [GO:0032355]; response to flooding [GO:0009413]; response to hydrogen peroxide [GO:0042542]; response to hypoxia [GO:0001666]; response to osmotic stress [GO:0006970]; response to salt stress [GO:0009651]; response to sucrose [GO:0009744]; response to water deprivation [GO:0009414]
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cytosol [GO:0005829]; plasma membrane [GO:0005886]
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alcohol dehydrogenase (NAD+) activity [GO:0004022]; alcohol dehydrogenase activity, zinc-dependent [GO:0004024]; nucleotide binding [GO:0000166]; protein homodimerization activity [GO:0042803]; S-(hydroxymethyl)glutathione dehydrogenase activity [GO:0051903]; zinc ion binding [GO:0008270]
|
PF08240;PF00107;
|
3.90.180.10;3.40.50.720;
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Zinc-containing alcohol dehydrogenase family, Class-P subfamily
|
PTM: Glutathionylated. {ECO:0000269|PubMed:16055689}.
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SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:7851777}.
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CATALYTIC ACTIVITY: Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000269|PubMed:23707506, ECO:0000269|PubMed:3377754}; CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH; Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000269|PubMed:23707506, ECO:0000269|PubMed:3377754};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.65 mM for NAD(+) (at pH 10.5 and 25 degrees Celsius) {ECO:0000269|PubMed:23707506}; KM=5.1 mM for ethanol (at pH 10.5 and 25 degrees Celsius) {ECO:0000269|PubMed:23707506}; Vmax=7.9 umol/min/mg enzyme with NAD(+) as substrate (at pH 10.5 and 25 degrees Celsius) {ECO:0000269|PubMed:23707506}; Vmax=70.1 umol/min/mg enzyme with ethanol as substrate (at pH 10.5 and 25 degrees Celsius) {ECO:0000269|PubMed:23707506}; Note=kcat is 328 min(-1) with NAD(+) as substrate (at pH 10.5 and 25 degrees Celsius). {ECO:0000269|PubMed:23707506};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 10.5 (at 25 degrees Celsius). {ECO:0000269|PubMed:23707506};
| null |
FUNCTION: Alcohol dehydrogenase mostly active on ethanol (EtOH), but exhibits broad substrates selectivity for primary and secondary alcohols (e.g. butanol, propyl alcohol, pentanol, isopentanol, ethylene glycol, isopropanol, methanol and tertiary butyl alcohol) (PubMed:23707506). Converts allyl alcohol to highly toxic acryl-aldehyde (PubMed:20508152). Required for survival and acclimation in hypoxic conditions, especially in roots (PubMed:12857811, PubMed:9880346). {ECO:0000269|PubMed:12857811, ECO:0000269|PubMed:20508152, ECO:0000269|PubMed:23707506, ECO:0000269|PubMed:9880346}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
P06534
|
SP0A_BACSU
|
MEKIKVCVADDNRELVSLLSEYIEGQEDMEVIGVAYNGQECLSLFKEKDPDVLVLDIIMPHLDGLAVLERLRESDLKKQPNVIMLTAFGQEDVTKKAVDLGASYFILKPFDMENLVGHIRQVSGNASSVTHRAPSSQSSIIRSSQPEPKKKNLDASITSIIHEIGVPAHIKGYLYLREAISMVYNDIELLGSITKVLYPDIAKKFNTTASRVERAIRHAIEVAWSRGNIDSISSLFGYTVSMTKAKPTNSEFIAMVADKLRLEHKAS
| null |
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
|
asymmetric cell division [GO:0008356]; cell septum assembly [GO:0090529]; detection of stimulus [GO:0051606]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of sporulation resulting in formation of a cellular spore [GO:0045881]; single-species surface biofilm formation [GO:0090606]; sporulation resulting in formation of a cellular spore [GO:0030435]
|
cytosol [GO:0005829]; protein-DNA complex [GO:0032993]
|
calcium ion binding [GO:0005509]; DNA-binding transcription factor activity [GO:0003700]; phosphorelay response regulator activity [GO:0000156]; transcription cis-regulatory region binding [GO:0000976]
|
PF00072;PF08769;
|
3.40.50.2300;1.10.10.10;
| null |
PTM: Phosphorylated by KinA and KinB.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with Spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process. Repressor of abrB, activator of the spoIIa operon. Binds the DNA sequence 5'-TGNCGAA-3' (0A box).
|
Bacillus subtilis (strain 168)
|
P06536
|
GCR_RAT
|
MDSKESLAPPGRDEVPGSLLGQGRGSVMDFYKSLRGGATVKVSASSPSVAAASQADSKQQRILLDFSKGSTSNVQQRQQQQQQQQQQQQQQQQQQQPDLSKAVSLSMGLYMGETETKVMGNDLGYPQQGQLGLSSGETDFRLLEESIANLNRSTSVPENPKSSTSATGCATPTEKEFPKTHSDASSEQQNRKSQTGTNGGSVKLYPTDQSTFDLLKDLEFSAGSPSKDTNESPWRSDLLIDENLLSPLAGEDDPFLLEGNTNEDCKPLILPDTKPKIKDTGDTILSSPSSVALPQVKTEKDDFIELCTPGVIKQEKLGPVYCQASFSGTNIIGNKMSAISVHGVSTSGGQMYHYDMNTASLSQQQDQKPVFNVIPPIPVGSENWNRCQGSGEDSLTSLGALNFPGRSVFSNGYSSPGMRPDVSSPPSSSSAATGPPPKLCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTKKKIKGIQQATAGVSQDTSENPNKTIVPAALPQLTPTLVSLLEVIEPEVLYAGYDSSVPDSAWRIMTTLNMLGGRQVIAAVKWAKAILGLRNLHLDDQMTLLQYSWMFLMAFALGWRSYRQSSGNLLCFAPDLIINEQRMSLPCMYDQCKHMLFVSSELQRLQVSYEEYLCMKTLLLLSSVPKEGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHEVVENLLTYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK
| null | null |
adrenal gland development [GO:0030325]; androgen metabolic process [GO:0008209]; astrocyte differentiation [GO:0048708]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to magnesium ion [GO:0071286]; cellular response to steroid hormone stimulus [GO:0071383]; cellular response to transforming growth factor beta stimulus [GO:0071560]; chromatin remodeling [GO:0006338]; circadian rhythm [GO:0007623]; female pregnancy [GO:0007565]; gene expression [GO:0010467]; glucocorticoid metabolic process [GO:0008211]; glucocorticoid receptor signaling pathway [GO:0042921]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; lung development [GO:0030324]; mammary gland duct morphogenesis [GO:0060603]; maternal behavior [GO:0042711]; microglia differentiation [GO:0014004]; motor behavior [GO:0061744]; muscle atrophy [GO:0014889]; negative regulation of apoptotic process [GO:0043066]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of synaptic plasticity [GO:0031914]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of vascular permeability [GO:0043116]; neuroinflammatory response [GO:0150076]; nucleus localization [GO:0051647]; positive regulation of cell growth involved in cardiac muscle cell development [GO:0061051]; positive regulation of dendritic spine development [GO:0060999]; positive regulation of glucocorticoid receptor signaling pathway [GO:2000324]; positive regulation of glutamate secretion [GO:0014049]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein-containing complex assembly [GO:0065003]; regulation of cell population proliferation [GO:0042127]; regulation of DNA-templated transcription [GO:0006355]; regulation of glucocorticoid biosynthetic process [GO:0031946]; regulation of gluconeogenesis [GO:0006111]; regulation of glucose metabolic process [GO:0010906]; regulation of transcription by RNA polymerase II [GO:0006357]; response to activity [GO:0014823]; response to arsenic-containing substance [GO:0046685]; response to calcium ion [GO:0051592]; response to corticosterone [GO:0051412]; response to dexamethasone [GO:0071548]; response to electrical stimulus [GO:0051602]; response to inactivity [GO:0014854]; response to insulin [GO:0032868]; response to mercury ion [GO:0046689]; synaptic transmission, glutamatergic [GO:0035249]; transcription initiation-coupled chromatin remodeling [GO:0045815]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; postsynaptic density, intracellular component [GO:0099092]; protein-containing complex [GO:0032991]; spindle [GO:0005819]
|
chromatin binding [GO:0003682]; core promoter sequence-specific DNA binding [GO:0001046]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; double-stranded DNA binding [GO:0003690]; estrogen response element binding [GO:0034056]; heat shock protein binding [GO:0031072]; hormone binding [GO:0042562]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; identical protein binding [GO:0042802]; nuclear glucocorticoid receptor activity [GO:0004883]; nuclear receptor activity [GO:0004879]; protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877]; receptor tyrosine kinase binding [GO:0030971]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]; steroid binding [GO:0005496]; steroid hormone binding [GO:1990239]; TBP-class protein binding [GO:0017025]; transcription coactivator activity [GO:0003713]; zinc ion binding [GO:0008270]
|
PF02155;PF00104;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR3 subfamily
|
PTM: Acetylation by CLOCK reduces its binding to glucocorticoid response elements and its transcriptional activity. {ECO:0000250}.; PTM: Increased proteasome-mediated degradation in response to glucocorticoids. {ECO:0000250|UniProtKB:P04150}.; PTM: Phosphorylated in the absence of hormone; becomes hyperphosphorylated in the presence of glucocorticoids. The Ser-224, Ser-246 and Ser-424-phosphorylated forms are mainly cytoplasmic, and the Ser-232-phosphorylated form is nuclear. Phosphorylation at Ser-232 increases transcriptional activity. Phosphorylation at Ser-224, Ser-246 and Ser-424 decreases signaling capacity. Phosphorylation at Ser-424 may protect from glucocorticoid-induced apoptosis. Phosphorylation at Ser-224 and Ser-232 is not required in regulation of chromosome segregation. May be dephosphorylated by PPP5C, attenuates NR3C1 action. {ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537}.; PTM: Sumoylation at Lys-297 and Lys-313 negatively regulates its transcriptional activity. Sumoylation at Lys-721 positively regulates its transcriptional activity in the presence of RWDD3. Sumoylation at Lys-297 and Lys-313 is dispensable whereas sumoylation at Lys-721 is critical for the stimulatory effect of RWDD3 on its transcriptional activity. Heat shock increases sumoylation in a RWDD3-dependent manner. {ECO:0000269|PubMed:23508108}.; PTM: Ubiquitinated; restricts glucocorticoid-mediated transcriptional signaling. {ECO:0000250|UniProtKB:P06537}.
|
SUBCELLULAR LOCATION: [Isoform A]: Cytoplasm {ECO:0000250|UniProtKB:P04150}. Nucleus {ECO:0000250|UniProtKB:P04150}. Mitochondrion {ECO:0000269|PubMed:21730050}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P04150}. Note=After ligand activation, translocates from the cytoplasm to the nucleus (By similarity). In the presence of NR1D1 shows a time-dependent subcellular localization, localizing to the cytoplasm at ZT8 and to the nucleus at ZT20 (By similarity). Lacks this diurnal pattern of localization in the absence of NR1D1, localizing to both nucleus and the cytoplasm at ZT8 and ZT20 (By similarity). {ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537}.
| null | null | null | null | null |
FUNCTION: Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling (PubMed:12917342). Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay (By similarity). Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth (By similarity). In response to induction by transcription factor EGR1/NGFI-A in the hippocampus, may play a role in the behavioral and hypothalamic-pituitary-adrenal responses to stress in offspring (PubMed:15220929). {ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:12917342}.; FUNCTION: [Isoform A]: Has transcriptional activation and repression activity. Mediates glucocorticoid-induced apoptosis. Promotes accurate chromosome segregation during mitosis. May act as a tumor suppressor. May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression. {ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537}.
|
Rattus norvegicus (Rat)
|
P06537
|
GCR_MOUSE
|
MDSKESLAPPGRDEVPSSLLGRGRGSVMDLYKTLRGGATVKVSASSPSVAAASQADSKQQRILLDFSKGSASNAQQQQQQQQQQQQQQQQQPQPDLSKAVSLSMGLYMGETETKVMGNDLGYPQQGQLGLSSGETDFRLLEESIANLNRSTSRPENPKSSTPAAGCATPTEKEFPQTHSDPSSEQQNRKSQPGTNGGSVKLYTTDQSTFDILQDLEFSAGSPGKETNESPWRSDLLIDENLLSPLAGEDDPFLLEGDVNEDCKPLILPDTKPKIQDTGDTILSSPSSVALPQVKTEKDDFIELCTPGVIKQEKLGPVYCQASFSGTNIIGNKMSAISVHGVSTSGGQMYHYDMNTASLSQQQDQKPVFNVIPPIPVGSENWNRCQGSGEDNLTSLGAMNFAGRSVFSNGYSSPGMRPDVSSPPSSSSTATGPPPKLCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTKKKIKGIQQATAGVSQDTSENANKTIVPAALPQLTPTLVSLLEVIEPEVLYAGYDSSVPDSAWRIMTTLNMLGGRQVIAAVKWAKAIPGFRNLHLDDQMTLLQYSWMFLMAFALGWRSYRQASGNLLCFAPDLIINEQRMTLPCMYDQCKHMLFISTELQRLQVSYEEYLCMKTLLLLSSVPKEGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHDVVENLLSYCFQTFLDKSMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK
| null | null |
adrenal gland development [GO:0030325]; astrocyte differentiation [GO:0048708]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to transforming growth factor beta stimulus [GO:0071560]; chromatin remodeling [GO:0006338]; gene expression [GO:0010467]; glucocorticoid metabolic process [GO:0008211]; glucocorticoid receptor signaling pathway [GO:0042921]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; mammary gland duct morphogenesis [GO:0060603]; maternal behavior [GO:0042711]; microglia differentiation [GO:0014004]; motor behavior [GO:0061744]; negative regulation of apoptotic process [GO:0043066]; negative regulation of synaptic plasticity [GO:0031914]; negative regulation of vascular permeability [GO:0043116]; neuroinflammatory response [GO:0150076]; positive regulation of cell growth involved in cardiac muscle cell development [GO:0061051]; positive regulation of dendritic spine development [GO:0060999]; positive regulation of glucocorticoid receptor signaling pathway [GO:2000324]; positive regulation of glutamate secretion [GO:0014049]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell population proliferation [GO:0042127]; regulation of DNA-templated transcription [GO:0006355]; regulation of glucocorticoid biosynthetic process [GO:0031946]; regulation of gluconeogenesis [GO:0006111]; regulation of glucose metabolic process [GO:0010906]; regulation of transcription by RNA polymerase II [GO:0006357]; response to arsenic-containing substance [GO:0046685]; synaptic transmission, glutamatergic [GO:0035249]; transcription initiation-coupled chromatin remodeling [GO:0045815]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; postsynaptic density, intracellular component [GO:0099092]; protein-containing complex [GO:0032991]; spindle [GO:0005819]
|
chromatin binding [GO:0003682]; core promoter sequence-specific DNA binding [GO:0001046]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; double-stranded DNA binding [GO:0003690]; estrogen response element binding [GO:0034056]; heat shock protein binding [GO:0031072]; hormone binding [GO:0042562]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; identical protein binding [GO:0042802]; nuclear glucocorticoid receptor activity [GO:0004883]; nuclear receptor activity [GO:0004879]; protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877]; receptor tyrosine kinase binding [GO:0030971]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]; steroid binding [GO:0005496]; steroid hormone binding [GO:1990239]; TBP-class protein binding [GO:0017025]; transcription coactivator activity [GO:0003713]; zinc ion binding [GO:0008270]
|
PF02155;PF00104;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR3 subfamily
|
PTM: Acetylation by CLOCK reduces its binding to glucocorticoid response elements and its transcriptional activity. {ECO:0000250|UniProtKB:P04150}.; PTM: Increased proteasome-mediated degradation in response to glucocorticoids. {ECO:0000269|PubMed:11555652}.; PTM: Phosphorylated in the absence of hormone; becomes hyperphosphorylated in the presence of glucocorticoids. Phosphorylated in the absence of hormone; becomes hyperphosphorylated in the presence of glucocorticoid. The Ser-221, Ser-243 and Ser-421-phosphorylated forms are mainly cytoplasmic, and the Ser-229-phosphorylated form is nuclear (By similarity). Phosphorylation at Ser-229 increases transcriptional activity (By similarity). Phosphorylation at Ser-221, Ser-243 and Ser-421 decreases signaling capacity (By similarity). Phosphorylation at Ser-421 may protect from glucocorticoid-induced apoptosis (By similarity). Phosphorylation at Ser-221 and Ser-229 is not required in regulation of chromosome segregation (By similarity). May be dephosphorylated by PPP5C, attenuates NR3C1 action (PubMed:21994940). {ECO:0000250|UniProtKB:P04150, ECO:0000269|PubMed:2019585, ECO:0000269|PubMed:21994940}.; PTM: Sumoylation at Lys-294 and Lys-310 negatively regulates its transcriptional activity. Sumoylation at Lys-718 positively regulates its transcriptional activity in the presence of RWDD3. Sumoylation at Lys-294 and Lys-310 is dispensable whereas sumoylation at Lys-718 is critical for the stimulatory effect of RWDD3 on its transcriptional activity. Heat shock increases sumoylation in a RWDD3-dependent manner. {ECO:0000250|UniProtKB:P06536}.; PTM: Ubiquitinated; restricts glucocorticoid-mediated transcriptional signaling. {ECO:0000269|PubMed:11555652}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11278753, ECO:0000269|PubMed:25676786, ECO:0000269|PubMed:27686098}. Nucleus {ECO:0000269|PubMed:10678832, ECO:0000269|PubMed:11278753, ECO:0000269|PubMed:25676786, ECO:0000269|PubMed:27686098}. Note=Cytoplasmic in the absence of ligand, nuclear after ligand-binding (PubMed:11278753). The hormone-occupied receptor undergoes rapid exchange between chromatin and the nucleoplasmic compartment (PubMed:10678832). In the presence of NR1D1 shows a time-dependent subcellular localization, localizing to the cytoplasm at ZT8 and to the nucleus at ZT20 (PubMed:27686098). Lacks this diurnal pattern of localization in the absence of NR1D1, localizing to both nucleus and the cytoplasm at ZT8 and ZT20 (PubMed:27686098). {ECO:0000269|PubMed:10678832, ECO:0000269|PubMed:11278753, ECO:0000269|PubMed:27686098}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000250|UniProtKB:P04150}. Nucleus {ECO:0000250|UniProtKB:P04150}. Mitochondrion {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P04150}. Note=After ligand activation, translocates from the cytoplasm to the nucleus. {ECO:0000250|UniProtKB:P04150}.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus {ECO:0000269|PubMed:20660300}. Cytoplasm {ECO:0000269|PubMed:20660300}. Note=Expressed predominantly in the nucleus with some expression also detected in the cytoplasm. {ECO:0000269|PubMed:20660300}.
| null | null | null | null | null |
FUNCTION: Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling (PubMed:10678832). Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay (By similarity). Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth (PubMed:15037546). {ECO:0000250|UniProtKB:P04150, ECO:0000269|PubMed:10678832, ECO:0000269|PubMed:15037546}.; FUNCTION: [Isoform 1]: Has transcriptional activation and repression activity (By similarity). Mediates glucocorticoid-induced apoptosis (By similarity). Promotes accurate chromosome segregation during mitosis (PubMed:25847991). May act as a tumor suppressor (PubMed:25847991). May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression (PubMed:21994940). {ECO:0000250|UniProtKB:P04150, ECO:0000269|PubMed:21994940, ECO:0000269|PubMed:25847991}.; FUNCTION: [Isoform 3]: Acts as a dominant negative inhibitor of isoform 1 (PubMed:20660300). Has intrinsic transcriptional activity independent of isoform Alpha when both isoforms are coexpressed (By similarity). Loses this transcription modulator function on its own (By similarity). Has no hormone-binding activity (PubMed:20660300). May play a role in controlling glucose metabolism by maintaining insulin sensitivity (PubMed:20660300). Reduces hepatic gluconeogenesis through down-regulation of PEPCK in an isoform Alpha-dependent manner (By similarity). Directly regulates STAT1 expression in isoform Alpha-independent manner (By similarity). {ECO:0000250|UniProtKB:P04150, ECO:0000269|PubMed:20660300}.
|
Mus musculus (Mouse)
|
P06575
|
BINA1_LYSSH
|
MRNLDFIDSFIPTEGKYIRVMDFYNSEYPFCIHAPSAPNGDIMTEICSRENNQYFIFFPTDDGRVIIANRHNGSVFTGEATSVVSDIYTGSPLQFFREVKRTMATYYLAIQNPESATDVRALEPHSHELPSRLYYTNNIENNSNILISNKEQIYLTLPSLPENEQYPKTPVLSGIDDIGPNQSEKSIIGSTLIPCIMVSDFISLGERMKTTPYYYVKHTQYWQSMWSALFPPGSKETKTEKSGITDTSQISMTDGINVSIGADFGLRFGNKTFGIKGGFTYDTKTQITNTSQLLIETTYTREYTNTENFPVRYTGYVLASEFTLHRSDGTQVNTIPWVALNDNYTTIARYPHFASEPLLGNTKIITDDQN
| null | null |
sporulation resulting in formation of a cellular spore [GO:0030435]
| null |
toxin activity [GO:0090729]
|
PF05431;
| null |
Toxin_10 family
|
PTM: Processed by proteases extracted from C.pipiens larval gut; 6 amino acids are removed from the N-terminus while it is estimated about 20 residues are removed from the C-terminus to yield the 40 kDa toxin form that is seen in insects. The 40 kDa form is 50-fold more lethal against tissue culture cells than the precursor form. Larval gut extracts of Aedes aegypti and Anopheles gambiae also generate the same 40 kDa form all of which are toxic in C.pipiens. {ECO:0000269|PubMed:2886104, ECO:0000305|PubMed:3926751}.
|
SUBCELLULAR LOCATION: Spore, perispore {ECO:0000305|PubMed:3926751}.
| null | null | null | null | null |
FUNCTION: Component of a binary toxin active against Culex and some Aedes mosquito larvae; about 1000-fold more toxic against C.quinquefasciatus than A.aegypti (Probable) (PubMed:8419297, Ref.10). This subunit alone is active against C.quinquefasciatus, Anopheles gambiae, A.stephensi and Aedes aegypti mosquito cell lines; non Culex mosquitoes are less sensitive to the toxin (Probable) (PubMed:2886104). Binary toxin internalization into host gut cells requires both proteins (By similarity). {ECO:0000250|UniProtKB:P05516, ECO:0000269|PubMed:2886104, ECO:0000269|PubMed:8419297, ECO:0000269|Ref.10, ECO:0000305|PubMed:3777925, ECO:0000305|PubMed:3926751}.
|
Lysinibacillus sphaericus (Bacillus sphaericus)
|
P06576
|
ATPB_HUMAN
|
MLGFVGRVAAAPASGALRRLTPSASLPPAQLLLRAAPTAVHPVRDYAAQTSPSPKAGAATGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPIKTKQFAPIHAEAPEFMEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHSS
|
7.1.2.2
| null |
angiogenesis [GO:0001525]; ATP biosynthetic process [GO:0006754]; cellular response to interleukin-7 [GO:0098761]; generation of precursor metabolites and energy [GO:0006091]; lipid metabolic process [GO:0006629]; negative regulation of cell adhesion involved in substrate-bound cell migration [GO:0006933]; osteoblast differentiation [GO:0001649]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; proton motive force-driven ATP synthesis [GO:0015986]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; proton transmembrane transport [GO:1902600]; regulation of intracellular pH [GO:0051453]
|
cell surface [GO:0009986]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]; mitochondrial nucleoid [GO:0042645]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase, catalytic core [GO:0005754]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; proton-transporting ATP synthase complex [GO:0045259]; proton-transporting ATP synthase complex, catalytic core F(1) [GO:0045261]
|
angiostatin binding [GO:0043532]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; MHC class I protein binding [GO:0042288]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]
|
PF00006;PF02874;
|
2.40.10.170;3.40.50.300;
|
ATPase alpha/beta chains family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:25168243}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00829}; Matrix side {ECO:0000250|UniProtKB:P00829, ECO:0000269|PubMed:25168243}.
|
CATALYTIC ACTIVITY: Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate; Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2; Evidence={ECO:0000305|PubMed:25168243}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:57722; Evidence={ECO:0000305|PubMed:25168243};
| null | null | null | null |
FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. {ECO:0000269|PubMed:25168243, ECO:0000269|PubMed:36239646}.
|
Homo sapiens (Human)
|
P06583
|
AT1B1_CANLF
|
MARGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYGCLAGIFIGTIQVMLLTISEFKPTYQDRVAPPGLTQIPQIQKTEISFRPNDPKSYEEYVRNIVRFLEKYKDSAQKDEMIFEDCGNMPSEIKERGEFNNERGERKVCRFKLEWLGNCSGINDETYGYRDGKPCVLIKLNRVLGFKPKPPKNESLEAYPVMKYSPYVLPVQCTGKRDEDKDRIGNVEYFGLGGYPGFPLQYYPYYGKLLQPKYLQPLLAVQFTNLTMDTEIRIECKAYGENIGYSEKDRFQGRFDVKIEVKS
| null | null |
cell adhesion [GO:0007155]; innate immune response [GO:0045087]; intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; potassium ion import across plasma membrane [GO:1990573]; sodium ion export across plasma membrane [GO:0036376]
|
apical plasma membrane [GO:0016324]; sarcolemma [GO:0042383]; sodium:potassium-exchanging ATPase complex [GO:0005890]
|
ATPase activator activity [GO:0001671]
|
PF00287;
|
1.20.5.170;2.60.40.1660;
|
X(+)/potassium ATPases subunit beta family
|
PTM: Glutathionylated (By similarity). N-glycosylated (By similarity). {ECO:0000250|UniProtKB:P07340, ECO:0000250|UniProtKB:P14094}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:P07340}; Single-pass type II membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P14094}. Note=Colocalizes with OBSCN at the intercalated disk and sarcolemma in cardiomyocytes. Localizes in long striations at the level of Z and M lines. {ECO:0000250|UniProtKB:P14094}.
| null | null | null | null | null |
FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane (PubMed:22328500). Plays a role in innate immunity by enhancing virus-triggered induction of interferons (IFNs) and interferon stimulated genes (ISGs). Mechanistically, enhances the ubiquitination of TRAF3 and TRAF6 as well as the phosphorylation of TAK1 and TBK1 (By similarity). {ECO:0000250|UniProtKB:P05026, ECO:0000269|PubMed:22328500}.; FUNCTION: Involved in cell adhesion and establishing epithelial cell polarity. {ECO:0000269|PubMed:22328500}.
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
P06585
|
PSBA_PEA
|
MTAILERRDSENLWGRFCNWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANEGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAAVEAPSING
|
1.10.3.9
|
COFACTOR: Note=The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-Rule:MF_01379};
|
photosynthetic electron transport in photosystem II [GO:0009772]; response to herbicide [GO:0009635]
|
chloroplast thylakoid membrane [GO:0009535]; photosystem II [GO:0009523]
|
chlorophyll binding [GO:0016168]; electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity [GO:0045156]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor [GO:0016682]; oxygen evolving activity [GO:0010242]
|
PF00124;
|
1.20.85.10;
|
Reaction center PufL/M/PsbA/D family
|
PTM: Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z. {ECO:0000255|HAMAP-Rule:MF_01379}.; PTM: C-terminally processed by CTPA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth. {ECO:0000255|HAMAP-Rule:MF_01379}.
|
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:1499553, ECO:0000269|PubMed:9407103}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01379}.
|
CATALYTIC ACTIVITY: Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2; Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757, ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01379};
| null | null | null | null |
FUNCTION: This is one of the two reaction center proteins of photosystem II.; FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. {ECO:0000255|HAMAP-Rule:MF_01379}.
|
Pisum sativum (Garden pea) (Lathyrus oleraceus)
|
P06596
|
PA21B_CANLF
|
MKFLVLAALLTVAAAEGGISPRAVWQFRNMIKCTIPESDPLKDYNDYGCYCGLGGSGTPVDELDKCCQTHDHCYSEAKKLDSCKFLLDNPYTKIYSYSCSGSEITCSSKNKDCQAFICNCDRSAAICFSKAPYNKEHKNLDTKKYC
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P00593}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00593};
|
antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; arachidonic acid secretion [GO:0050482]; defense response to Gram-positive bacterium [GO:0050830]; fatty acid biosynthetic process [GO:0006633]; innate immune response in mucosa [GO:0002227]; lipid catabolic process [GO:0016042]; phosphatidylcholine metabolic process [GO:0046470]; phosphatidylglycerol metabolic process [GO:0046471]; phospholipid metabolic process [GO:0006644]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of podocyte apoptotic process [GO:1904635]
|
cell surface [GO:0009986]; extracellular space [GO:0005615]
|
bile acid binding [GO:0032052]; calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family
|
PTM: Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically. {ECO:0000250|UniProtKB:P04054}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04054}. Note=Secreted from pancreatic acinar cells in its inactive form. {ECO:0000250|UniProtKB:P04054}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:P04054, ECO:0000250|UniProtKB:P04055, ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036}; CATALYTIC ACTIVITY: Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate; Xref=Rhea:RHEA:54456, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:64489; Evidence={ECO:0000250|UniProtKB:P04054}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000250|UniProtKB:P04054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000250|UniProtKB:P04054}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72841, ChEBI:CHEBI:75158; Evidence={ECO:0000250|UniProtKB:P04054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920; Evidence={ECO:0000250|UniProtKB:P04054}; CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:78097, ChEBI:CHEBI:85217; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=H2O + N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = (9Z,12Z)-octadecadienoate + H(+) + N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:56424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:85334, ChEBI:CHEBI:85335; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56425; Evidence={ECO:0000250|UniProtKB:P04055};
| null | null | null | null |
FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines. May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation in the intestinal tract. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (By similarity). May act in an autocrine and paracrine manner (By similarity). Has anti-helminth activity in a process regulated by gut microbiota. Upon helminth infection of intestinal epithelia, directly affects phosphatidylethanolamine contents in the membrane of helminth larvae, likely controlling an array of phospholipid-mediated cellular processes such as membrane fusion and cell division while providing for better immune recognition, ultimately reducing larvae integrity and infectivity (By similarity). {ECO:0000250|UniProtKB:P04054, ECO:0000250|UniProtKB:P04055, ECO:0000250|UniProtKB:Q9Z0Y2}.
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
P06602
|
EVE_DROME
|
MHGYRTYNMESHHAHHDASPVDQKPLVVDLLATQYGKPQTPPPSPNECLSSPDNSLNGSRGSEIPADPSVRRYRTAFTRDQLGRLEKEFYKENYVSRPRRCELAAQLNLPESTIKVWFQNRRMKDKRQRIAVAWPYAAVYSDPAFAASILQAAANSVGMPYPPYAPAAAAAAAAAAAVATNPMMATGMPPMGMPQMPTMQMPGHSGHAGHPSPYGQYRYTPYHIPARPAPPHPAGPHMHHPHMMGSSATGSSYSAGAAGLLGALPSATCYTGLGVGVPKTQTPPLDLQSSSSPHSSTLSLSPVGSDHAKVFDRSPVAQSAPSVPAPAPLTTTSPLPAPGLLMPSAKRPASDMSPPPTTTVIAEPKPKLFKPYKTEA
| null | null |
adult heart development [GO:0007512]; blastoderm segmentation [GO:0007350]; cephalic furrow formation [GO:0007376]; germ-band extension [GO:0007377]; heart morphogenesis [GO:0003007]; motor neuron axon guidance [GO:0008045]; negative regulation of cardioblast cell fate specification [GO:0009997]; negative regulation of transcription by RNA polymerase II [GO:0000122]; periodic partitioning by pair rule gene [GO:0007366]; positive regulation of transcription by RNA polymerase II [GO:0045944]; posterior head segmentation [GO:0035289]; regulation of axonogenesis [GO:0050770]; regulation of myoblast fusion [GO:1901739]; regulation of transcription by RNA polymerase II [GO:0006357]; trunk segmentation [GO:0035290]
|
nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00046;
|
1.10.10.60;
|
Even-skipped homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: May play a role in determining neuronal identity. May be directly involved in specifying identity of individual neurons. Pair-rule protein required for segmentation; involved in transforming the broad, spatial, aperiodic expression patterns of the gap genes into a system of precise periodic expression patterns of the pair-rule and segmentary polarity genes.
|
Drosophila melanogaster (Fruit fly)
|
P06603
|
TBA1_DROME
|
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTVGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADQCTGLQGFLIFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLVTYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGMDSGDGEGEGAEEY
|
3.6.5.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363};
|
lysosome localization [GO:0032418]; microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]
|
astral microtubule [GO:0000235]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; microtubule [GO:0005874]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; spindle [GO:0005819]
|
GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200]
|
PF00091;PF03953;
|
1.10.287.600;3.30.1330.20;3.40.50.1440;
|
Tubulin family
|
PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000250}.; PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling (By similarity). During the early stages of oogenesis lky/Alpha-tubulin N-acetyltransferase 2 is the main acetyltransferase responsible for Lys-40 acetylation in germline cells while Atat/alpha-tubulin N-acetyltransferase 1 is the main acetyltransferase responsible for Lys-40 acetylation in somatic cells (PubMed:36342916). {ECO:0000250, ECO:0000250|UniProtKB:P91910, ECO:0000269|PubMed:36342916}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P68363};
| null | null | null | null |
FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
|
Drosophila melanogaster (Fruit fly)
|
P06604
|
TBA2_DROME
|
MRECISVHIGQAGVQIGNACWELYCLEHGIQPDGHMPSDKTVGGGDDSFSTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDVVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYMNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISVEKAYHEQLTVAEITNACFEPANQMVKCDPRRGKYMACCMLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFAEAREDLAALEKDYEEVGIDSTTELGEDEEY
|
3.6.5.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363};
|
microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; unidimensional cell growth [GO:0009826]
|
cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; microtubule [GO:0005874]; spindle microtubule [GO:0005876]
|
GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200]
|
PF00091;PF03953;
|
1.10.287.600;3.30.1330.20;3.40.50.1440;
|
Tubulin family
|
PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000250}.; PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling (By similarity). During the early stages of oogenesis lky/Alpha-tubulin N-acetyltransferase 2 is the main acetyltransferase responsible for Lys-40 acetylation in germline cells while Atat/alpha-tubulin N-acetyltransferase 1 is the main acetyltransferase responsible for Lys-40 acetylation in somatic cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P06603, ECO:0000250|UniProtKB:P91910}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P68363};
| null | null | null | null |
FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
|
Drosophila melanogaster (Fruit fly)
|
P06605
|
TBA3_DROME
|
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTVGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADQCTGLQGFLIFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFAVYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLVTYAPVISAEKAYHEQLSVAEITNACFEPANQMVKVDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGMDSGDGEGEGAEEY
|
3.6.5.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363};
|
microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; sperm axoneme assembly [GO:0007288]; spermatogenesis [GO:0007283]
|
cytoplasm [GO:0005737]; microtubule [GO:0005874]; perinuclear region of cytoplasm [GO:0048471]
|
GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; myosin binding [GO:0017022]; structural constituent of cytoskeleton [GO:0005200]
|
PF00091;PF03953;
|
1.10.287.600;3.30.1330.20;3.40.50.1440;
|
Tubulin family
|
PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000250}.; PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling (By similarity). During the early stages of oogenesis lky/Alpha-tubulin N-acetyltransferase 2 is the main acetyltransferase responsible for Lys-40 acetylation in germline cells while Atat/alpha-tubulin N-acetyltransferase 1 is the main acetyltransferase responsible for Lys-40 acetylation in somatic cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P06603, ECO:0000250|UniProtKB:P91910}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P68363};
| null | null | null | null |
FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
|
Drosophila melanogaster (Fruit fly)
|
P06606
|
TBA4_DROME
|
MREVVSIQIGQCGIQIGNACWELYLLEHGINLDGSLKTKEELTASGSSASVGHDTSANDARTFFTETGNGKQVPRSIFVDLEPTVIDDVRNGCMRELYHPEQLISGKEDAANNYARGRYSIGKEVIDRVTSRLQKIAEQCDSLQGFLIFHSLGGGTGSGFTSLLVERLSTDYSKKCKLDFAVYPSPKVSTAVVEPYNALLTTHSTMDHSDCVFMVDNEAIYDICNNSLGVDRPAYRNLNRLIAQIVSSTTASLRFSGSMNVDLNEFQTNLVPFPRIHFPLVAYAPLMSAERSAHEQHAITTLTNACFESSNMMVKCDPRAGKFMACCMLYRGDVVPKDVNAAVSAIKSKRHIQFVDWCPTGFKIGINYEKPAFVPDGDLAKTSRACCMLSNTTAISVAFSNLSYKFDLMFKKRAFVHWYVGEGMEEGEFTEARENIAVLERDFEEVGLDNAEEGGDEDFDEF
|
3.6.5.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363};
|
central nervous system development [GO:0007417]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic cleavage [GO:0040016]; female pronucleus assembly [GO:0035038]; microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; mitotic spindle organization [GO:0007052]; mRNA transport [GO:0051028]; nuclear division [GO:0000280]; nuclear migration by microtubule mediated pushing forces [GO:0098863]; peripheral nervous system development [GO:0007422]; pronuclear migration [GO:0035046]; sperm aster formation [GO:0035044]
|
cortical microtubule [GO:0055028]; cytoplasm [GO:0005737]; microtubule [GO:0005874]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; spindle [GO:0005819]
|
GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200]
|
PF00091;PF03953;
|
1.10.287.600;3.30.1330.20;3.40.50.1440;
|
Tubulin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P68363};
| null | null | null | null |
FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
|
Drosophila melanogaster (Fruit fly)
|
P06607
|
VIT3_DROME
|
MMSLRICLLATCLLVAAHASKDASNDRLKPTKWLTATELENVPSLNDITWERLENQPLEQGAKVIEKIYHVGQIKHDLTPSFVPSPSNVPVWIIKSNGQKVECKLNNYVETAKAQPGFGEDEVTIVLTGLPKTSPAQQKAMRRLIQAYVQKYNLQQLQKNAQEQQQQLKSSDYDYTSSEEAADQWKSAKAASGDLIIIDLGSTLTNFKRYAMLDVLNTGAMIGQTLIDLTNKGVPQEIIHLIGQGISAHVAGAAGNKYTAQTGHKLRRITGLDPAKVLSKRPQILGGLSRGDADFVDAIHTSTFAMGTPIRCGDVDFYPNGPSTGVPGSENVIEAVARATRYFAESVRPGSERNFPAVPANSLKQYKEQDGFGKRAYMGLQIDYDLRGDYILEVNAKSPFGQRSPAHKQAAYHGMHHAQN
| null | null |
embryo development ending in birth or egg hatching [GO:0009792]; lipid catabolic process [GO:0016042]; regulation of embryonic development [GO:0045995]; response to bacterium [GO:0009617]; sex differentiation [GO:0007548]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; P granule [GO:0043186]
|
serine hydrolase activity [GO:0017171]
|
PF00151;
|
3.40.50.1820;
|
AB hydrolase superfamily, Lipase family
|
PTM: Tyrosine sulfation occurs in the female only and plays an essential functional role. {ECO:0000269|PubMed:3922974}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Vitellogenin is the major yolk protein of eggs where it is used as a food source during embryogenesis. Vitellogenins and their receptor yl/yolkless are required for maintenance of microtubule plus-end orientation towards the posterior pole of oocytes (PubMed:33891588). Involved in polarized localization of germ plasm components, such as osk mRNA and vas protein, to the oocyte posterior cortex (PubMed:33891588). Receptor-mediated endocytosis by yl/yolkless is crucial for actin reorganization, mediated by osk isoform A/Long, required to anchor germ plasm components to the oocyte cortex (PubMed:33891588). {ECO:0000269|PubMed:33891588}.
|
Drosophila melanogaster (Fruit fly)
|
P06609
|
BTUC_ECOLI
|
MLTLARQQQRQNIRWLLCLSVLMLLALLLSLCAGEQWISPGDWFTPRGELFVWQIRLPRTLAVLLVGAALAISGAVMQALFENPLAEPGLLGVSNGAGVGLIAAVLLGQGQLPNWALGLCAIAGALIITLILLRFARRHLSTSRLLLAGVALGIICSALMTWAIYFSTSVDLRQLMYWMMGGFGGVDWRQSWLMLALIPVLLWICCQSRPMNMLALGEISARQLGLPLWFWRNVLVAATGWMVGVSVALAGAIGFIGLVIPHILRLCGLTDHRVLLPGCALAGASALLLADIVARLALAAAELPIGVVTATLGAPVFIWLLLKAGR
| null | null |
cobalamin transport [GO:0015889]
|
ATP-binding cassette (ABC) transporter complex [GO:0043190]; BtuCD complex [GO:1990193]; cobalamin transport complex [GO:1990191]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
ABC-type vitamin B12 transporter activity [GO:0015420]; identical protein binding [GO:0042802]; transmembrane transporter activity [GO:0022857]
|
PF01032;
|
1.10.3470.10;
|
Binding-protein-dependent transport system permease family, FecCD subfamily
| null |
SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Involved in the translocation of the substrate across the membrane.
|
Escherichia coli (strain K12)
|
P06611
|
BTUD_ECOLI
|
MSIVMQLQDVAESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTPPFATPVWHYLTLHQHDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQITPQANPAGQLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYGMNFRRLDIEGHRMLISTI
|
7.6.2.8
| null |
cobalamin transport [GO:0015889]
|
ATP-binding cassette (ABC) transporter complex [GO:0043190]; BtuCD complex [GO:1990193]; cobalamin transport complex [GO:1990191]; extrinsic component of membrane [GO:0019898]; membrane [GO:0016020]
|
ABC-type vitamin B12 transporter activity [GO:0015420]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]
|
PF00005;
|
3.40.50.300;
|
ABC transporter superfamily, Vitamin B12 importer (TC 3.A.1.13.1) family
| null |
SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein.
|
CATALYTIC ACTIVITY: Reaction=an R-cob(III)alamin(out) + ATP + H2O = ADP + an R-cob(III)alamin(in) + H(+) + phosphate; Xref=Rhea:RHEA:17873, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:140785, ChEBI:CHEBI:456216; EC=7.6.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01005};
| null | null | null | null |
FUNCTION: Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Responsible for energy coupling to the transport system. {ECO:0000255|HAMAP-Rule:MF_01005}.
|
Escherichia coli (strain K12)
|
P06612
|
TOP1_ECOLI
|
MGKALVIVESPAKAKTINKYLGSDYVVKSSVGHIRDLPTSGSAAKKSADSTSTKTAKKPKKDERGALVNRMGVDPWHNWEAHYEVLPGKEKVVSELKQLAEKADHIYLATDLDREGEAIAWHLREVIGGDDARYSRVVFNEITKNAIRQAFNKPGELNIDRVNAQQARRFMDRVVGYMVSPLLWKKIARGLSAGRVQSVAVRLVVEREREIKAFVPEEFWEVDASTTTPSGEALALQVTHQNDKPFRPVNKEQTQAAVSLLEKARYSVLEREDKPTTSKPGAPFITSTLQQAASTRLGFGVKKTMMMAQRLYEAGYITYMRTDSTNLSQDAVNMVRGYISDNFGKKYLPESPNQYASKENSQEAHEAIRPSDVNVMAESLKDMEADAQKLYQLIWRQFVACQMTPAKYDSTTLTVGAGDFRLKARGRILRFDGWTKVMPALRKGDEDRILPAVNKGDALTLVELTPAQHFTKPPARFSEASLVKELEKRGIGRPSTYASIISTIQDRGYVRVENRRFYAEKMGEIVTDRLEENFRELMNYDFTAQMENSLDQVANHEAEWKAVLDHFFSDFTQQLDKAEKDPEEGGMRPNQMVLTSIDCPTCGRKMGIRTASTGVFLGCSGYALPPKERCKTTINLVPENEVLNVLEGEDAETNALRAKRRCPKCGTAMDSYLIDPKRKLHVCGNNPTCDGYEIEEGEFRIKGYDGPIVECEKCGSEMHLKMGRFGKYMACTNEECKNTRKILRNGEVAPPKEDPVPLPELPCEKSDAYFVLRDGAAGVFLAANTFPKSRETRAPLVEELYRFRDRLPEKLRYLADAPQQDPEGNKTMVRFSRKTKQQYVSSEKDGKATGWSAFYVDGKWVEGKK
|
5.6.2.1
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:10681504, ECO:0000269|PubMed:21482796}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10681504, ECO:0000269|PubMed:21482796}; Note=Binds two Mg(2+) ions per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+). {ECO:0000269|PubMed:10681504, ECO:0000269|PubMed:21482796};
|
DNA topological change [GO:0006265]
|
chromosome [GO:0005694]; cytosol [GO:0005829]
|
DNA binding [GO:0003677]; DNA topoisomerase activity [GO:0003916]; DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917]; metal ion binding [GO:0046872]
|
PF21372;PF08272;PF01131;PF01751;PF01396;
|
2.20.25.10;3.40.50.140;3.30.65.10;1.10.460.10;2.70.20.10;1.10.290.10;
|
Type IA topoisomerase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00952, ECO:0000269|PubMed:10681504, ECO:0000269|PubMed:14604525, ECO:0000269|PubMed:21482796, ECO:0000269|PubMed:9497321};
| null | null | null | null |
FUNCTION: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. {ECO:0000255|HAMAP-Rule:MF_00952, ECO:0000269|PubMed:10681504, ECO:0000269|PubMed:21482796, ECO:0000269|PubMed:9497321}.
|
Escherichia coli (strain K12)
|
P06616
|
ERA_ECOLI
|
MSIDKSYCGFIAIVGRPNVGKSTLLNKLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHMEEKRAINRLMNKAASSSIGDVELVIFVVEGTRWTPDDEMVLNKLREGKAPVILAVNKVDNVQEKADLLPHLQFLASQMNFLDIVPISAETGLNVDTIAAIVRKHLPEATHHFPEDYITDRSQRFMASEIIREKLMRFLGAELPYSVTVEIERFVSNERGGYDINGLILVEREGQKKMVIGNKGAKIKTIGIEARKDMQEMFEAPVHLELWVKVKSGWADDERALRSLGYVDDL
| null | null |
protein phosphorylation [GO:0006468]; ribosomal small subunit assembly [GO:0000028]; ribosomal small subunit biogenesis [GO:0042274]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; guanosine tetraphosphate binding [GO:0097216]; ribosomal small subunit binding [GO:0043024]; RNA binding [GO:0003723]; rRNA binding [GO:0019843]; small ribosomal subunit rRNA binding [GO:0070181]
|
PF07650;PF01926;
|
3.30.300.20;3.40.50.300;
|
TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Era GTPase family
|
PTM: Autophosphorylated. {ECO:0000269|PubMed:8919456}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8282709}. Cell inner membrane {ECO:0000269|PubMed:8282709}; Peripheral membrane protein {ECO:0000269|PubMed:8282709}; Cytoplasmic side {ECO:0000269|PubMed:8282709}. Note=Binding is GDP or GTP-dependent, slightly more protein is bound in the presence of GTP than GDP.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15.4 uM for GTP (for His-tagged protein at pH 8.0, 5 mM MgCl(2)) {ECO:0000269|PubMed:2105934, ECO:0000269|PubMed:8919456}; KM=9 uM for GTP (for overexpressed protein at pH 8.0, 5 mM MgCl(2)) {ECO:0000269|PubMed:2105934, ECO:0000269|PubMed:8919456};
| null | null | null |
FUNCTION: An essential GTPase that binds both GDP and GTP, with nucleotide exchange occurring on the order of seconds whereas hydrolysis occurs on the order of minutes. Plays a role in numerous processes, including cell cycle regulation, energy metabolism, as a chaperone for 16S rRNA processing and 30S ribosomal subunit biogenesis. One of at least 4 proteins (Era, RbfA, RimM and RsgA/YjeQ) that assist in the late assembly stage of the 30S ribosomal subunit. Its presence in the 30S subunit may prevent translation initiation. Seems to be critical for maintaining cell growth and cell divison rates; a dramatic reduction in Era protein levels temporarily arrests cell growth just before cytokinesis (at the predivisional two-cell stage) and delays cell division. Era mutant era1 suppresses some temperature-sensitive mutations that affect DNA replication and chromosome partitioning and segregation. The dominant-negative Era-de mutant which is missing residues in a putative effector region, is unable to complement the disruption mutant; upon overproduction it shows a significant decrease in cell viability and a synthetic lethal phenotype in the presence of acetate. Era function probably overlaps RbfA (PubMed:16825789). Binds to the pre-30S ribosomal subunit through several stages of protein assembly (PubMed:20188109). {ECO:0000269|PubMed:12753192, ECO:0000269|PubMed:16825789, ECO:0000269|PubMed:20188109, ECO:0000269|PubMed:9515700}.
|
Escherichia coli (strain K12)
|
P06621
|
CBPG_PSES6
|
MRPSIHRTAIAAVLATAFVAGTALAQKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAAAGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGKNLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDLIQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITGKASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNWTIAKAGNVSNIIPASATLNADVRYARNEDFDAAMKTLEERAQQKKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAYYKEAGGTLGVEERTGGGTDAAYAALSGKPVIESLGLPGFGYHSDKAEYVDISAIPRRLYMAARLIMDLGAGK
|
3.4.17.11
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:9083113}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:9083113};
|
proteolysis [GO:0006508]
| null |
carboxypeptidase activity [GO:0004180]; metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]
|
PF07687;PF01546;
|
3.30.70.360;3.40.630.10;
|
Peptidase M20A family
| null | null |
CATALYTIC ACTIVITY: Reaction=Release of C-terminal glutamate residues from a wide range of N-acylating moieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl and pteroyl groups.; EC=3.4.17.11;
| null | null | null | null |
FUNCTION: Catalyzes the hydrolysis of reduced and non-reduced folates to pteroates and L-glutamate. This enzyme has a broad specificity.
|
Pseudomonas sp. (strain RS-16)
|
P06623
|
CN37_BOVIN
|
MSSSGAKDKPELQFPFLQDEETVATLQECKTLFILRGLPGSGKSTLARFIVDKYRDGTKMVSADSYKITPGARGSFSEEYKQLDEDLAACCRRDFRVLVLDDTNHERERLEQLFELADQYQYQVVLVEPKTAWRLDCAQLKEKNQWQLSADDLKKLKPGLEKDFLPLYFGWFLTKKSSAALWKTGQTFLEELGNHKAFKKELRHFVSGDEPREKIELVTYFGKRPPGVLHCTTKFCDYGKAAGAEEYAQQDVVKKSYCKAFTLTISALFVTPKTTGARVELSEQQLALWPNDVDKLSPSDNLPRGSRAHITLGCAGDVEAVQTGIDLLEIVRQEKGGSRGEEVGELSRGKLYSLGSGRWMLSLAKKMEVRAIFTGYYGKGKAVPIRSGRKGGSFQSCTII
|
3.1.4.37
| null |
cyclic nucleotide catabolic process [GO:0009214]
|
cytoplasm [GO:0005737]; melanosome [GO:0042470]; membrane [GO:0016020]
|
2',3'-cyclic-nucleotide 3'-phosphodiesterase activity [GO:0004113]; RNA binding [GO:0003723]
|
PF13671;PF05881;
|
3.90.1740.10;3.40.50.300;
|
2H phosphoesterase superfamily, CNPase family
|
PTM: Met-1 may be removed after translation.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P16330}; Lipid-anchor {ECO:0000250|UniProtKB:P16330}. Melanosome {ECO:0000250|UniProtKB:P09543}. Note=Firmly bound to membrane structures of brain white matter. {ECO:0000250|UniProtKB:P16330}.
|
CATALYTIC ACTIVITY: Reaction=a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 2'-phosphate + H(+); Xref=Rhea:RHEA:14489, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:66954, ChEBI:CHEBI:78552; EC=3.1.4.37; Evidence={ECO:0000269|PubMed:6272743};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.1 mM for AMP {ECO:0000269|PubMed:6272743}; KM=0.4 mM for GMP {ECO:0000269|PubMed:6272743}; KM=6.3 mM for CMP {ECO:0000269|PubMed:6272743}; KM=7.1 mM for UMP {ECO:0000269|PubMed:6272743};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6 (in the presence of both hexadecyltrimethylammonium bromide and serum albumin). {ECO:0000269|PubMed:6272743};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:6272743};
|
FUNCTION: Catalyzes the formation of 2'-nucleotide products from 2',3'-cyclic substrates (PubMed:6272743). May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin (By similarity). {ECO:0000250|UniProtKB:P16330, ECO:0000269|PubMed:6272743}.
|
Bos taurus (Bovine)
|
P06624
|
MIP_BOVIN
|
MWELRSASFWRAICAEFFASLFYVFFGLGASLRWAPGPLHVLQVALAFGLALATLVQAVGHISGAHVNPAVTFAFLVGSQMSLLRAICYMVAQLLGAVAGAAVLYSVTPPAVRGNLALNTLHPGVSVGQATIVEIFLTLQFVLCIFATYDERRNGRLGSVALAVGFSLTLGHLFGMYYTGAGMNPARSFAPAILTRNFTNHWVYWVGPVIGAGLGSLLYDFLLFPRLKSVSERLSILKGSRPSESNGQPEVTGEPVELKTQAL
| null | null |
gap junction-mediated intercellular transport [GO:1990349]; lens development in camera-type eye [GO:0002088]; positive regulation of cell adhesion [GO:0045785]; protein homotetramerization [GO:0051289]; visual perception [GO:0007601]; water transport [GO:0006833]
|
apical plasma membrane [GO:0016324]; endoplasmic reticulum [GO:0005783]; gap junction [GO:0005921]; plasma membrane [GO:0005886]
|
calmodulin binding [GO:0005516]; structural constituent of eye lens [GO:0005212]; water channel activity [GO:0015250]
|
PF00230;
|
1.20.1080.10;
|
MIP/aquaporin (TC 1.A.8) family
|
PTM: Subject to partial proteolytic cleavage in the eye lens core. Partial proteolysis promotes interactions between tetramers from adjoining membranes (By similarity). {ECO:0000250}.; PTM: Fatty acylated at Met-1 and Lys-238. The acyl modifications, in decreasing order of ion abundance, are: oleoyl (C18:1) > palmitoyl (C16:0) > stearoyl (C18:0) > eicosenoyl (C20:1) > dihomo-gamma-linolenoyl (C20:3) > palmitoleoyl (C16:1) > eicosadienoyl (C20:2). {ECO:0000269|PubMed:27378310}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30301}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6J8I9}. Cell junction, gap junction {ECO:0000250|UniProtKB:P30301}.
| null | null | null | null | null |
FUNCTION: Water channel (PubMed:23893133). Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core (By similarity). Plays a role in cell-to-cell adhesion and facilitates gap junction coupling. {ECO:0000250|UniProtKB:P30301, ECO:0000250|UniProtKB:Q6J8I9, ECO:0000269|PubMed:23893133}.
|
Bos taurus (Bovine)
|
P06632
|
DKGA_CORSC
|
MTVPSIVLNDGNSIPQLGYGVFKVPPADTQRAVEEALEVGYRHIDTAAIYGNEEGVGAAIAASGIARDDLFITTKLWNDRHDGDEPAAAIAESLAKLALDQVDLYLVHWPTPAADNYVHAWEKMIELRAAGLTRSIGVSNHLVPHLERIVAATGVVPAVNQIELHPAYQQREITDWAAAHDVKIESWGPLGQGKYDLFGAEPVTAAAAAHGKTPAQAVLRWHLQKGFVVFPKSVRRERLEENLDVFDFDLTDTEIAAIDAMDPGDGSGRVSAHPDEVD
|
1.1.1.346
| null |
L-ascorbic acid biosynthetic process [GO:0019853]
|
cytoplasm [GO:0005737]
|
oxidoreductase activity [GO:0016491]
|
PF00248;
|
3.20.20.100;
|
Aldo/keto reductase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=2-dehydro-L-idonate + NADP(+) = 2,5-didehydro-D-gluconate + H(+) + NADPH; Xref=Rhea:RHEA:35111, ChEBI:CHEBI:11449, ChEBI:CHEBI:15378, ChEBI:CHEBI:36602, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.346;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=26 mM for 2,5-diketo-D-gluconate {ECO:0000269|PubMed:3597405}; KM=10 uM for NADPH {ECO:0000269|PubMed:3597405};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.4. Active over a broad pH range. {ECO:0000269|PubMed:3597405};
| null |
FUNCTION: Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates. 25DKGR-A exhibits a greater selectivity for the substrate and higher thermal stability than 25DKGR-B.
|
Corynebacterium sp. (strain ATCC 31090)
|
P06634
|
DED1_YEAST
|
MAELSEQVQNLSINDNNENGYVPPHLRGKPRSARNNSSNYNNNNGGYNGGRGGGSFFSNNRRGGYGNGGFFGGNNGGSRSNGRSGGRWIDGKHVPAPRNEKAEIAIFGVPEDPNFQSSGINFDNYDDIPVDASGKDVPEPITEFTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLMACAQTGSGKTGGFLFPVLSESFKTGPSPQPESQGSFYQRKAYPTAVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYLVLDEADRMLDMGFEPQIRHIVEDCDMTPVGERQTLMFSATFPADIQHLARDFLSDYIFLSVGRVGSTSENITQKVLYVENQDKKSALLDLLSASTDGLTLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAATLLVATAVAARGLDIPNVTHVINYDLPSDVDDYVHRIGRTGRAGNTGLATAFFNSENSNIVKGLHEILTEANQEVPSFLKDAMMSAPGSRSNSRRGGFGRNNNRDYRKAGGASAGGWGSSRSRDNSFRGGSGWGSDSKSSGWGNSGGSNNSSWW
|
3.6.4.13
| null |
cell differentiation [GO:0030154]; positive regulation of formation of translation preinitiation complex [GO:1901195]; spliceosomal complex disassembly [GO:0000390]; translational initiation [GO:0006413]
|
cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; eukaryotic initiation factor 4G binding [GO:0031370]; mRNA binding [GO:0003729]; RNA helicase activity [GO:0003724]; RNA strand annealing activity [GO:0033592]; translation initiation factor activity [GO:0003743]
|
PF00270;PF00271;
|
3.40.50.300;
|
DEAD box helicase family, DDX3/DED1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.34 mM for ATP {ECO:0000269|PubMed:15201868, ECO:0000269|PubMed:18332124};
| null | null | null |
FUNCTION: ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes. Has weak ATP-dependent affinity for dsRNA, but strong ATP-dependent affinity for ssRNA. Acts as a virus host factor involved in the replication of the MBV and the L-A viruses by promoting the negative-strand RNA synthesis. May be involved in recognition of the preinitiation complex and DNA binding of the RNA polymerase III and play a role in mRNA splicing. {ECO:0000269|PubMed:10364207, ECO:0000269|PubMed:11069307, ECO:0000269|PubMed:14671320, ECO:0000269|PubMed:14763975, ECO:0000269|PubMed:15064363, ECO:0000269|PubMed:15201868, ECO:0000269|PubMed:16216083, ECO:0000269|PubMed:18332124, ECO:0000269|PubMed:1996139, ECO:0000269|PubMed:7835345, ECO:0000269|PubMed:9045610, ECO:0000269|PubMed:9144215}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06636
|
HBA3_XENLA
|
MTLTDSDKAAVVALWGKIAPQANAIGAEALERLFLSYPQTKTYFSHFDLSHGSADLANHGGKVVNALGEAAKHIDDLDAALSTLSDLHAYNLRVDPGNFKLLSHTIQVTLAIHFHKEFDAATQAAWDKFLAEVATVLTSKYR
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: This is a larval (tadpole) alpha-globin.
|
Xenopus laevis (African clawed frog)
|
P06637
|
HBA4_XENLA
|
MTLTDSDKAAIVALWGKIAPQASAIGAEALERLFLSYPQTKTYFSHFDVSHGSADLSNHGGKVVNALGEAAKHIDDLDSALSTLSDLHAYNLRIDPGNFKLLSHTIQVTLAIHFHKEFDAATQAAWDKFLAEVATVLTSKYR
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: This is a larval (tadpole) alpha-globin.
|
Xenopus laevis (African clawed frog)
|
P06652
|
MPIP_SCHPO
|
MDSPLSSLSFTNTLSGKRNVLRPAARELKLMSDRNANQELDFFFPKSKHIASTLVDPFGKTCSTASPASSLAADMSMNMHIDESPALPTPRRTLFRSLSCTVETPLANKTIVSPLPESPSNDALTESYFFRQPASKYSITQDSPRVSSTIAYSFKPKASIALNTTKSEATRSSLSSSSFDSYLRPNVSRSRSSGNAPPFLRSRSSSSYSINKKKGTSGGQATRHLTYALSRTCSQSSNTTSLLESCLTDDTDDFELMSDHEDTFTMGKVADLPESSVELVEDAASIQRPNSDFGACNDNSLDDLFQASPIKPIDMLPKINKDIAFPSLKVRSPSPMAFAMQEDAEYDEQDTPVLRRTQSMFLNSTRLGLFKSQDLVCVTPKQSTKESERFISSHVEDLSLPCFAVKEDSLKRITQETLLGLLDGKFKDIFDKCIIIDCRFEYEYLGGHISTAVNLNTKQAIVDAFLSKPLTHRVALVFHCEHSAHRAPHLALHFRNTDRRMNSHRYPFLYYPEVYILHGGYKSFYENHKNRCDPINYVPMNDASHVMTCTKAMNNFKRNATFMRTKSYTFGQSVLASPDVNDSPTAMHSLSTLRRF
|
3.1.3.48
| null |
cell division [GO:0051301]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic G2 cell size control checkpoint signaling [GO:0031569]; mitotic intra-S DNA damage checkpoint signaling [GO:0031573]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; positive regulation of G2/MI transition of meiotic cell cycle [GO:0110032]; regulation of cell cycle switching, mitotic to meiotic cell cycle [GO:0110044]; regulation of cell size [GO:0008361]; response to mitotic G2 DNA damage checkpoint signaling [GO:0072435]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
phosphoprotein phosphatase activity [GO:0004721]; protein tyrosine phosphatase activity [GO:0004725]
|
PF00581;
|
3.40.250.10;
|
MPI phosphatase family
|
PTM: Phosphorylated by srk1 in the N-terminus; phosphorylation promotes nuclear exclusion. {ECO:0000269|PubMed:15629716}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15629716}. Nucleus {ECO:0000269|PubMed:15629716}. Note=Accumulates in the nucleus in cycling cells; nuclear localization is the highest in G2. {ECO:0000269|PubMed:15629716}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000250|UniProtKB:P30303};
| null | null | null | null |
FUNCTION: Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic and meiotic progression (PubMed:3955656, PubMed:7498766, Ref.3). Directly dephosphorylates cdc2 and stimulates its kinase activity (By similarity). Required for the G2/M transition of the cell cycle (PubMed:15629716). Required for induction of meiosis II (PubMed:7498766, Ref.3). {ECO:0000250|UniProtKB:P30305, ECO:0000269|PubMed:15629716, ECO:0000269|PubMed:3955656, ECO:0000269|Ref.3}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
P06681
|
CO2_HUMAN
|
MGPLMVLFCLLFLYPGLADSAPSCPQNVNISGGTFTLSHGWAPGSLLTYSCPQGLYPSPASRLCKSSGQWQTPGATRSLSKAVCKPVRCPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVCDNGAGHCPNPGISLGAVRTGFRFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPICRQPYSYDFPEDVAPALGTSFSHMLGATNPTQKTKESLGRKIQIQRSGHLNLYLLLDCSQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSVLNDNSRDMTEVISSLENANYKDHENGTGTNTYAALNSVYLMMNNQMRLLGMETMAWQEIRHAIILLTDGKSNMGGSPKTAVDHIREILNINQKRNDYLDIYAIGVGKLDVDWRELNELGSKKDGERHAFILQDTKALHQVFEHMLDVSKLTDTICGVGNMSANASDQERTPWHVTIKPKSQETCRGALISDQWVLTAAHCFRDGNDHSLWRVNVGDPKSQWGKEFLIEKAVISPGFDVFAKKNQGILEFYGDDIALLKLAQKVKMSTHARPICLPCTMEANLALRRPQGSTCRDHENELLNKQSVPAHFVALNGSKLNINLKMGVEWTSCAEVVSQEKTMFPNLTDVREVVTDQFLCSGTQEDESPCKGESGGAVFLERRFRFFQVGLVSWGLYNPCLGSADKNSRKRAPRSKVPPPRDFHINLFRMQPWLRQHLGDVLNFLPL
|
3.4.21.43
| null |
complement activation [GO:0006956]; complement activation, classical pathway [GO:0006958]; innate immune response [GO:0045087]; positive regulation of apoptotic cell clearance [GO:2000427]; proteolysis [GO:0006508]; response to bacterium [GO:0009617]; response to lipopolysaccharide [GO:0032496]; response to nutrient [GO:0007584]; response to thyroid hormone [GO:0097066]
|
classical-complement-pathway C3/C5 convertase complex [GO:0005601]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]
|
PF00084;PF00089;PF00092;
|
2.10.70.10;2.40.10.10;3.40.50.410;
|
Peptidase S1 family
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to form C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha-chain to form C5a and C5b.; EC=3.4.21.43;
| null | null | null | null |
FUNCTION: Component C2 which is part of the classical pathway of the complement system is cleaved by activated factor C1 into two fragments: C2b and C2a. C2a, a serine protease, then combines with complement factor C4b to generate the C3 or C5 convertase.
|
Homo sapiens (Human)
|
P06683
|
CO9_MOUSE
|
MASGMAITLALAIFALGVNAQMPIPVSREEQEQHYPIPIDCRMSPWSNWSECDPCLKQRFRSRSILAFGQFNGKSCVDVLGDRQGCEPTQECEEIQENCGNDFQCETGRCIKRRLLCNGDNDCGDYSDENDCDDDPRTPCRDRVAEESELGLTAGYGINILGMEPLRTPFDNEFYNGLCDRVRDEKTYYRKPWNVVSLIYETKADKSFRTENYDEHLEVFKAINREKTSNFNADFALKFSATEVPEKGAGEVSPAEHSSKPTNISAKFKFSYFMGKNFRRLSSYFSQSKKMFVHLRGVVQLGRFVMRNRDVVLRSTFLDDVKALPTSYEKGEYFGFLETYGTHYSTSGSLGGQYEIVYVLDKASMKEKGVDLNDVKHCLGFNMDLRIPLQDDLKDASVTASVNADGCIKTDNGKTVNITRDNIIDDVISFIRGGTREQAILLKEKILRGDKTFDKTDFANWASSLANAPALISQRMSPIYNLIPLKIKDAYIKKQNLEKAVEDYIDEFSTKRCYPCLNGGTIILLDGQCLCSCPMMFRGMACEIHQKI
| null | null |
cell killing [GO:0001906]; complement activation [GO:0006956]; complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; killing of cells of another organism [GO:0031640]; positive regulation of immune response [GO:0050778]; protein homooligomerization [GO:0051260]
|
extracellular space [GO:0005615]; membrane attack complex [GO:0005579]; other organism cell membrane [GO:0044218]; plasma membrane [GO:0005886]
| null |
PF00057;PF01823;PF00090;
|
2.10.25.10;4.10.400.10;2.20.100.10;
|
Complement C6/C7/C8/C9 family
|
PTM: Initially, positions and connectivity of disulfide bonds were based on peptide sequencing done for the human protein. The high-resolution crystal structure for the mouse protein corrected the positions and connectivities of some disulfide bonds (PubMed:30111885). The distance between Cys-55 and Cys-92 in the monomeric mouse protein precludes formation of a disulfide bond, contrary to what is seen in the structure of the human polymeric form of the protein (Probable). {ECO:0000269|PubMed:30111885, ECO:0000305|PubMed:30111885}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02748}. Target cell membrane {ECO:0000250|UniProtKB:P02748}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P02748}. Note=Secreted as soluble monomer. Oligomerizes at target membranes, forming a pre-pore. A conformation change then leads to the formation of a 100 Angstrom diameter pore. {ECO:0000250|UniProtKB:P02748}.
| null | null | null | null | null |
FUNCTION: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C9 is the pore-forming subunit of the MAC. {ECO:0000250|UniProtKB:P02748}.
|
Mus musculus (Mouse)
|
P06684
|
CO5_MOUSE
|
MGLWGILCLLIFLDKTWGQEQTYVISAPKILRVGSSENVVIQVHGYTEAFDATLSLKSYPDKKVTFSSGYVNLSPENKFQNAALLTLQPNQVPREESPVSHVYLEVVSKHFSKSKKIPITYNNGILFIHTDKPVYTPDQSVKIRVYSLGDDLKPAKRETVLTFIDPEGSEVDIVEENDYTGIISFPDFKIPSNPKYGVWTIKANYKKDFTTTGTAYFEIKEYVLPRFSVSIELERTFIGYKNFKNFEITVKARYFYNKVVPDAEVYAFFGLREDIKDEEKQMMHKATQAAKLVDGVAQISFDSETAVKELSYNSLEDLNNKYLYIAVTVTESSGGFSEEAEIPGVKYVLSPYTLNLVATPLFVKPGIPFSIKAQVKDSLEQAVGGVPVTLMAQTVDVNQETSDLETKRSITHDTDGVAVFVLNLPSNVTVLKFEIRTDDPELPEENQASKEYEAVAYSSLSQSYIYIAWTENYKPMLVGEYLNIMVTPKSPYIDKITHYNYLILSKGKIVQYGTREKLFSSTYQNINIPVTQNMVPSARLLVYYIVTGEQTAELVADAVWINIEEKCGNQLQVHLSPDEYVYSPGQTVSLDMVTEADSWVALSAVDRAVYKVQGNAKRAMQRVFQALDEKSDLGCGAGGGHDNADVFHLAGLTFLTNANADDSHYRDDSCKEILRSKRNLHLLRQKIEEQAAKYKHSVPKKCCYDGARVNFYETCEERVARVTIGPLCIRAFNECCTIANKIRKESPHKPVQLGRIHIKTLLPVMKADIRSYFPESWLWEIHRVPKRKQLQVTLPDSLTTWEIQGIGISDNGICVADTLKAKVFKEVFLEMNIPYSVVRGEQIQLKGTVYNYMTSGTKFCVKMSAVEGICTSGSSAASLHTSRPSRCVFQRIEGSSSHLVTFTLLPLEIGLHSINFSLETSFGKDILVKTLRVVPEGVKRESYAGVILDPKGIRGIVNRRKEFPYRIPLDLVPKTKVERILSVKGLLVGEFLSTVLSKEGINILTHLPKGSAEAELMSIAPVFYVFHYLEAGNHWNIFYPDTLSKRQSLEKKIKQGVVSVMSYRNADYSYSMWKGASASTWLTAFALRVLGQVAKYVKQDENSICNSLLWLVEKCQLENGSFKENSQYLPIKLQGTLPAEAQEKTLYLTAFSVIGIRKAVDICPTMKIHTALDKADSFLLENTLPSKSTFTLAIVAYALSLGDRTHPRFRLIVSALRKEAFVKGDPPIYRYWRDTLKRPDSSVPSSGTAGMVETTAYALLASLKLKDMNYANPIIKWLSEEQRYGGGFYSTQDTINAIEGLTEYSLLLKQIHLDMDINVAYKHEGDFHKYKVTEKHFLGRPVEVSLNDDLVVSTGYSSGLATVYVKTVVHKISVSEEFCSFYLKIDTQDIEASSHFRLSDSGFKRIIACASYKPSKEESTSGSSHAVMDISLPTGIGANEEDLRALVEGVDQLLTDYQIKDGHVILQLNSIPSRDFLCVRFRIFELFQVGFLNPATFTVYEYHRPDKQCTMIYSISDTRLQKVCEGAACTCVEADCAQLQAEVDLAISADSRKEKACKPETAYAYKVRITSATEENVFVKYTATLLVTYKTGEAADENSEVTFIKKMSCTNANLVKGKQYLIMGKEVLQIKHNFSFKYIYPLDSSTWIEYWPTDTTCPSCQAFVENLNNFAEDLFLNSCE
| null | null |
complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; in utero embryonic development [GO:0001701]; inflammatory response [GO:0006954]; killing of cells of another organism [GO:0031640]; positive regulation of angiogenesis [GO:0045766]
|
extracellular space [GO:0005615]; membrane attack complex [GO:0005579]
|
endopeptidase inhibitor activity [GO:0004866]
|
PF00207;PF07703;PF07677;PF01821;PF21309;PF17790;PF01835;PF17791;PF17789;PF01759;PF07678;
|
1.50.10.20;2.20.130.20;2.40.50.120;2.60.120.1540;2.60.40.1930;2.60.40.1940;6.20.50.160;2.60.40.690;1.20.91.20;2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled.; FUNCTION: [C5a anaphylatoxin]: Derived from proteolytic degradation of complement C5, C5a anaphylatoxin is a mediator of local inflammatory process. Binding to the receptor C5AR1 induces a variety of responses including intracellular calcium release, contraction of smooth muscle, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes. C5a is also a potent chemokine which stimulates the locomotion of polymorphonuclear leukocytes and directs their migration toward sites of inflammation. {ECO:0000250|UniProtKB:P01031}.
|
Mus musculus (Mouse)
|
P06685
|
AT1A1_RAT
|
MGKGVGRDKYEPAAVSEHGDKKSKKAKKERDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTPARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIRSATEEEPPNDDLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEDVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAEEIEHFIHLITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWFALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIEVCCGSVMEMREKYTKIVEIPFNSTNKYQLSIHKNPNASEPKHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLLLPDEQFPEGFQFDTDEVNFPVDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVNQVNPRDAKACVVHGSDLKDMTSEELDDILRYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIVGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPFHLLGIRETWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGAALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY
|
7.2.2.13
| null |
cardiac muscle contraction [GO:0060048]; cellular response to mechanical stimulus [GO:0071260]; cellular response to steroid hormone stimulus [GO:0071383]; energy coupled proton transmembrane transport, against electrochemical gradient [GO:0015988]; establishment or maintenance of transmembrane electrochemical gradient [GO:0010248]; heart contraction [GO:0060047]; intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; membrane hyperpolarization [GO:0060081]; membrane repolarization [GO:0086009]; negative regulation of glucocorticoid biosynthetic process [GO:0031947]; negative regulation of heart contraction [GO:0045822]; osmosensory signaling pathway [GO:0007231]; positive regulation of heart contraction [GO:0045823]; positive regulation of striated muscle contraction [GO:0045989]; potassium ion import across plasma membrane [GO:1990573]; potassium ion transport [GO:0006813]; proton transmembrane transport [GO:1902600]; regulation of blood pressure [GO:0008217]; regulation of cardiac muscle cell contraction [GO:0086004]; regulation of sodium ion transport [GO:0002028]; regulation of the force of heart contraction [GO:0002026]; relaxation of cardiac muscle [GO:0055119]; response to glycoside [GO:1903416]; response to xenobiotic stimulus [GO:0009410]; sodium ion export across plasma membrane [GO:0036376]; sodium ion homeostasis [GO:0055078]; sodium ion transport [GO:0006814]; transmembrane transport [GO:0055085]
|
apical plasma membrane [GO:0016324]; axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; caveola [GO:0005901]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; intercalated disc [GO:0014704]; lateral plasma membrane [GO:0016328]; melanosome [GO:0042470]; membrane [GO:0016020]; organelle membrane [GO:0031090]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; protein-containing complex [GO:0032991]; sarcolemma [GO:0042383]; sodium:potassium-exchanging ATPase complex [GO:0005890]; sperm flagellum [GO:0036126]; T-tubule [GO:0030315]
|
ADP binding [GO:0043531]; ankyrin binding [GO:0030506]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; P-type potassium transmembrane transporter activity [GO:0008556]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]; phosphatase activity [GO:0016791]; phosphatidylinositol 3-kinase binding [GO:0043548]; potassium ion binding [GO:0030955]; protein domain specific binding [GO:0019904]; protein heterodimerization activity [GO:0046982]; protein kinase binding [GO:0019901]; protein-folding chaperone binding [GO:0051087]; sodium ion binding [GO:0031402]; steroid hormone binding [GO:1990239]
|
PF13246;PF00689;PF00690;PF00122;
|
3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIC subfamily
|
PTM: Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-943 by PKA modulates the response of ATP1A1 to PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity. {ECO:0000269|PubMed:10473631, ECO:0000269|PubMed:17939993, ECO:0000269|PubMed:7510709, ECO:0000269|PubMed:7775468, ECO:0000269|PubMed:9435504}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8VDN2}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:16914892}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P05023}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:29499166}. Melanosome {ECO:0000250|UniProtKB:P05023}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.13; Evidence={ECO:0000269|PubMed:17939993, ECO:0000269|PubMed:30388404}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18354; Evidence={ECO:0000269|PubMed:30388404};
| null | null | null | null |
FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients (PubMed:30388404). Could also be part of an osmosensory signaling pathway that senses body-fluid sodium levels and controls salt intake behavior as well as voluntary water intake to regulate sodium homeostasis (By similarity). {ECO:0000250|UniProtKB:Q8VDN2, ECO:0000269|PubMed:30388404}.
|
Rattus norvegicus (Rat)
|
P06686
|
AT1A2_RAT
|
MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGALLCFLAYGILAAMEDEPSNDNLYLGIVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGQTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALSRIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPFNSTNKYQLSIHEREDSPQSHVLVMKGAPERILDRCSTILVQGKEIPLDKEMQDAFQNAYMELGGLGERVLGFCQLNLPSGKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPREAKACVVHGSDLKDMTSEQLDEILRDHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNSQTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRTTNDLEDSYGQEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETALAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY
|
7.2.2.13
| null |
adult locomotory behavior [GO:0008344]; amygdala development [GO:0021764]; ATP metabolic process [GO:0046034]; behavioral fear response [GO:0001662]; cardiac muscle contraction [GO:0060048]; cellular response to mechanical stimulus [GO:0071260]; cellular response to steroid hormone stimulus [GO:0071383]; energy coupled proton transmembrane transport, against electrochemical gradient [GO:0015988]; intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; L-ascorbic acid metabolic process [GO:0019852]; locomotion [GO:0040011]; locomotory exploration behavior [GO:0035641]; membrane depolarization [GO:0051899]; monoatomic cation transmembrane transport [GO:0098655]; negative regulation of calcium ion transmembrane transport [GO:1903170]; negative regulation of calcium:sodium antiporter activity [GO:1903280]; negative regulation of cytosolic calcium ion concentration [GO:0051481]; negative regulation of heart contraction [GO:0045822]; negative regulation of striated muscle contraction [GO:0045988]; neuronal action potential propagation [GO:0019227]; neurotransmitter uptake [GO:0001504]; olfactory cortex development [GO:0021989]; potassium ion import across plasma membrane [GO:1990573]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; proton transmembrane transport [GO:1902600]; regulation of blood pressure [GO:0008217]; regulation of cardiac muscle cell contraction [GO:0086004]; regulation of cardiac muscle contraction by calcium ion signaling [GO:0010882]; regulation of muscle contraction [GO:0006937]; regulation of respiratory gaseous exchange by nervous system process [GO:0002087]; regulation of smooth muscle contraction [GO:0006940]; regulation of striated muscle contraction [GO:0006942]; regulation of the force of heart contraction [GO:0002026]; regulation of vasoconstriction [GO:0019229]; relaxation of cardiac muscle [GO:0055119]; response to auditory stimulus [GO:0010996]; response to glycoside [GO:1903416]; response to nicotine [GO:0035094]; response to potassium ion [GO:0035864]; sodium ion export across plasma membrane [GO:0036376]; sodium ion transmembrane transport [GO:0035725]; sodium ion transport [GO:0006814]; visual learning [GO:0008542]
|
caveola [GO:0005901]; cell projection [GO:0042995]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; intercalated disc [GO:0014704]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; organelle membrane [GO:0031090]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; sarcolemma [GO:0042383]; sodium:potassium-exchanging ATPase complex [GO:0005890]; T-tubule [GO:0030315]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled monoatomic cation transmembrane transporter activity [GO:0019829]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]; potassium ion binding [GO:0030955]; protein heterodimerization activity [GO:0046982]; protein-folding chaperone binding [GO:0051087]; sodium ion binding [GO:0031402]; steroid binding [GO:0005496]; steroid hormone binding [GO:1990239]
|
PF13246;PF00689;PF00690;PF00122;PF00702;
|
3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIC subfamily
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.13;
| null | null | null | null |
FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.
|
Rattus norvegicus (Rat)
|
P06687
|
AT1A3_RAT
|
MGDKKDDKSSPKKSKAKERRDLDDLKKEVAMTEHKMSVEEVCRKYNTDCVQGLTHSKAQEILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAGTEDDPSGDNLYLGIVLAAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIREGEKMQVNAEEVVVGDLVEIKGGDRVPADLRIISAHGCKVDNSSLTGESEPQTRSPDCTHDNPLETRNITFFSTNCVEGTARGVVVATGDRTVMGRIATLASGLEVGKTPIAIEIEHFIQLITGVAVFLGVSFFILSLILGYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGTSFDKSSHTWVALSHIAGLCNRAVFKGGQDNIPVLKRDVAGDASESALLKCIELSSGSVKLMRERNKKVAEIPFNSTNKYQLSIHETEDPNDNRYLLVMKGAPERILDRCATILLQGKEQPLDEEMKEAFQNAYLELGGLGERVLGFCHYYLPEEQFPKGFAFDCDDVNFTTDNLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVIHGTDLKDFTSEQIDEILQNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIMANIPLPLGTITILCIDLGTDMVPAISLAYEAAESDIMKRQPRNPRTDKLVNERLISMAYGQIGMIQALGGFFSYFVILAENGFLPGNLVGIRLNWDDRTVNDLEDSYGQQWTYEQRKVVEFTCHTAFFVSIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMDVALRMYPLKPSWWFCAFPYSFLIFVYDEIRKLILRRNPGGWVEKETYY
|
7.2.2.13
| null |
adult locomotory behavior [GO:0008344]; cardiac muscle contraction [GO:0060048]; cellular response to amyloid-beta [GO:1904646]; cellular response to retinoic acid [GO:0071300]; cellular response to thyroid hormone stimulus [GO:0097067]; cerebral cortex development [GO:0021987]; intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; ionotropic glutamate receptor signaling pathway [GO:0035235]; memory [GO:0007613]; neurogenesis [GO:0022008]; neuron projection maintenance [GO:1990535]; potassium ion import across plasma membrane [GO:1990573]; potassium ion transport [GO:0006813]; proton transmembrane transport [GO:1902600]; regulation of cardiac muscle cell membrane potential [GO:0086036]; response to xenobiotic stimulus [GO:0009410]; sodium ion export across plasma membrane [GO:0036376]; sodium ion transport [GO:0006814]; transmission of nerve impulse [GO:0019226]; visual learning [GO:0008542]
|
axon [GO:0030424]; calyx of Held [GO:0044305]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; dendritic spine head [GO:0044327]; dendritic spine neck [GO:0044326]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; myelin sheath [GO:0043209]; neuron to neuron synapse [GO:0098984]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; organelle membrane [GO:0031090]; photoreceptor inner segment [GO:0001917]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; presynaptic membrane [GO:0042734]; protein-containing complex [GO:0032991]; sarcolemma [GO:0042383]; sodium:potassium-exchanging ATPase complex [GO:0005890]; synapse [GO:0045202]
|
amyloid-beta binding [GO:0001540]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; D1 dopamine receptor binding [GO:0031748]; heparan sulfate proteoglycan binding [GO:0043395]; metal ion binding [GO:0046872]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]; P-type sodium:potassium-exchanging transporter activity involved in regulation of cardiac muscle cell membrane potential [GO:0086037]; protein-folding chaperone binding [GO:0051087]
|
PF13246;PF00689;PF00690;PF00122;
|
3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIC subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.13;
| null | null | null | null |
FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.
|
Rattus norvegicus (Rat)
|
P06700
|
SIR2_YEAST
|
MTIPHMKYAVSKTSENKVSNTVSPTQDKDAIRKQPDDIINNDEPSHKKIKVAQPDSLRETNTTDPLGHTKAALGEVASMELKPTNDMDPLAVSAASVVSMSNDVLKPETPKGPIIISKNPSNGIFYGPSFTKRESLNARMFLKYYGAHKFLDTYLPEDLNSLYIYYLIKLLGFEVKDQALIGTINSIVHINSQERVQDLGSAISVTNVEDPLAKKQTVRLIKDLQRAINKVLCTRLRLSNFFTIDHFIQKLHTARKILVLTGAGVSTSLGIPDFRSSEGFYSKIKHLGLDDPQDVFNYNIFMHDPSVFYNIANMVLPPEKIYSPLHSFIKMLQMKGKLLRNYTQNIDNLESYAGISTDKLVQCHGSFATATCVTCHWNLPGERIFNKIRNLELPLCPYCYKKRREYFPEGYNNKVGVAASQGSMSERPPYILNSYGVLKPDITFFGEALPNKFHKSIREDILECDLLICIGTSLKVAPVSEIVNMVPSHVPQVLINRDPVKHAEFDLSLLGYCDDIAAMVAQKCGWTIPHKKWNDLKNKNFKCQEKDKGVYVVTSDEHPKTL
|
2.3.1.286
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:23307867}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:23307867};
|
chromatin organization [GO:0006325]; double-strand break repair via nonhomologous end joining [GO:0006303]; establishment of protein-containing complex localization to telomere [GO:0097695]; heterochromatin formation [GO:0031507]; negative regulation of DNA amplification [GO:1904524]; negative regulation of DNA recombination [GO:0045910]; negative regulation of DNA replication [GO:0008156]; rDNA heterochromatin formation [GO:0000183]; regulation of DNA stability [GO:0097752]; regulatory ncRNA-mediated gene silencing [GO:0031047]; silent mating-type cassette heterochromatin formation [GO:0030466]; sister chromatid cohesion [GO:0007062]; subtelomeric heterochromatin formation [GO:0031509]; telomere tethering at nuclear periphery [GO:0034398]
|
chromatin silencing complex [GO:0005677]; chromosome, telomeric region [GO:0000781]; heterochromatin [GO:0000792]; nuclear inner membrane [GO:0005637]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; rDNA heterochromatin [GO:0033553]; RENT complex [GO:0030869]
|
metal ion binding [GO:0046872]; NAD+ binding [GO:0070403]; NAD-dependent histone deacetylase activity [GO:0017136]; NAD-dependent histone H3K14 deacetylase activity [GO:0032041]; NAD-dependent histone H3K9 deacetylase activity [GO:0046969]; NAD-dependent histone H4K16 deacetylase activity [GO:0046970]; transcription corepressor activity [GO:0003714]; transferase activity [GO:0016740]
|
PF04574;PF02146;
|
1.20.120.1710;3.30.1600.10;3.40.50.1220;
|
Sirtuin family, Class I subfamily
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:9214640}. Note=Associated with nucleolar chromatin. Preferentially bound to the spacer regions of the rDNA repeats through its interaction with NET1.
|
CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=2.3.1.286; Evidence={ECO:0000255|PROSITE-ProRule:PRU00236};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=29.3 uM for NAD(+) {ECO:0000269|PubMed:15274642}; KM=239 uM for a synthetic histone H3K9 acetyllysine peptide {ECO:0000269|PubMed:15274642}; KM=420 uM for a synthetic histone H3K14 acetyllysine peptide {ECO:0000269|PubMed:15274642}; KM=140 uM for a synthetic histone H4K5 acetyllysine peptide {ECO:0000269|PubMed:15274642}; KM=54 uM for a synthetic histone H4K8 acetyllysine peptide {ECO:0000269|PubMed:15274642}; KM=105 uM for a synthetic histone H4K12 acetyllysine peptide {ECO:0000269|PubMed:15274642}; KM=17 uM for a synthetic histone H4K16 acetyllysine peptide {ECO:0000269|PubMed:15274642};
| null | null | null |
FUNCTION: NAD-dependent deacetylase, which participates in a wide range of cellular events including chromosome silencing, chromosome segregation, DNA recombination and the determination of life span. Involved in transcriptional repression of the silent mating-type loci HML and HMR and telomeric silencing via its association with SIR3 and SIR4. Plays a central role in ribosomal DNA (rDNA) silencing via its association with the RENT complex, preventing hyperrecombination, and repressing transcription from foreign promoters, which contributes to extending life span. Probably represses transcription via the formation of heterochromatin structure, which involves the compaction of chromatin fiber into a more condensed form, although this complex in at least one case can still bind euchromatic levels of positive transcription regulators. Although it displays some NAD-dependent histone deacetylase activity on histone H3K9Ac and H3K14Ac and histone H4K16Ac in vitro, such activity is unclear in vivo and may not be essential. {ECO:0000269|PubMed:10693811, ECO:0000269|PubMed:12923057, ECO:0000269|PubMed:15274642, ECO:0000269|PubMed:18086879, ECO:0000269|PubMed:19220062, ECO:0000269|PubMed:9278054}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06701
|
SIR3_YEAST
|
MAKTLKDLDGWQVIITDDQGRVIDDNNRRRSRKRGGENVFLKRISDGLSFGKGESVIFNDNVTETYSVYLIHEIRLNTLNNVVEIWVFSYLRWFELKPKLYYEQFRPDLIKEDHPLEFYKDKFFNEVNKSELYLTAELSEIWLKDFIAVGQILPESQWNDSSIDKIEDRDFLVRYACEPTAEKFVPIDIFQIIRRVKEMEPKQSDEYLKRVSVPVSGQKTNRQVMHKMGVERSSKRLAKKPSMKKIKIEPSADDDVNNGNIPSQRGTSTTHGSISPQEESVSPNISSASPSALTSPTDSSKILQKRSISKELIVSEEIPINSSEQESDYEPNNETSVLSSKPGSKPEKTSTELVDGRENFVYANNPEVSDDGGLEEETDEVSSESSDEAIIPVNKRRGAHGSELSSKIRKIHIQETQEFSKNYTTETDNEMNGNGKPGIPRGNTKIHSMNENPTPEKGNAKMIDFATLSKLKKKYQIILDRFAPDNQVTDSSQLNKLTDEQSSLDVAGLEDKFRKACSSSGRETILSNFNADINLEESIRESLQKRELLKSQVEDFTRIFLPIYDSLMSSQNKLFYITNADDSTKFQLVNDVMDELITSSARKELPIFDYIHIDALELAGMDALYEKIWFAISKENLCGDISLEALNFYITNVPKAKKRKTLILIQNPENLLSEKILQYFEKWISSKNSKLSIICVGGHNVTIREQINIMPSLKAHFTEIKLNKVDKNELQQMIITRLKSLLKPFHVKVNDKKEMTIYNNIREGQNQKIPDNVIVINHKINNKITQLIAKNVANVSGSTEKAFKICEAAVEISKKDFVRKGGLQKGKLVVSQEMVPRYFSEAINGFKDETISKKIIGMSLLMRTFLYTLAQETEGTNRHTLALETVLIKMVKMLRDNPGYKASKEIKKVICGAWEPAITIEKLKQFSWISVVNDLVGEKLVVVVLEEPSASIMVELKLPLEINYAFSMDEEFKNMDCI
| null | null |
DNA replication initiation [GO:0006270]; double-strand break repair via nonhomologous end joining [GO:0006303]; establishment of protein-containing complex localization to telomere [GO:0097695]; heterochromatin formation [GO:0031507]; mitotic DNA replication checkpoint signaling [GO:0033314]; nuclear-transcribed mRNA catabolic process, non-stop decay [GO:0070481]; silent mating-type cassette heterochromatin formation [GO:0030466]; subtelomeric heterochromatin formation [GO:0031509]; telomere tethering at nuclear periphery [GO:0034398]
|
chromatin silencing complex [GO:0005677]; chromosome, telomeric region [GO:0000781]; heterochromatin [GO:0000792]; mitochondrion [GO:0005739]; nuclear origin of replication recognition complex [GO:0005664]; nucleolus [GO:0005730]
|
chromatin binding [GO:0003682]; DNA replication origin binding [GO:0003688]; double-stranded DNA binding [GO:0003690]; identical protein binding [GO:0042802]; nucleic acid binding [GO:0003676]; nucleosome binding [GO:0031491]; single-stranded DNA binding [GO:0003697]
|
PF17872;PF01426;
|
1.10.10.2450;1.10.8.60;2.30.30.490;3.40.50.300;
| null |
PTM: N-terminal acetylation by NatA is important for transcriptional silencing activity. {ECO:0000269|PubMed:15454564}.
|
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR. The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure. Involves the compaction of chromatin fiber into a more condensed form.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06702
|
S10A9_HUMAN
|
MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIEHIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP
| null | null |
activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; apoptotic process [GO:0006915]; astrocyte development [GO:0014002]; autocrine signaling [GO:0035425]; autophagy [GO:0006914]; cell-cell signaling [GO:0007267]; chronic inflammatory response [GO:0002544]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; endothelial cell migration [GO:0043542]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; leukocyte migration involved in inflammatory response [GO:0002523]; modulation of process of another organism [GO:0035821]; neutrophil aggregation [GO:0070488]; neutrophil chemotaxis [GO:0030593]; peptidyl-cysteine S-trans-nitrosylation [GO:0035606]; positive regulation of cell growth [GO:0030307]; positive regulation of inflammatory response [GO:0050729]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of neuron projection development [GO:0010976]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; regulation of cytoskeleton organization [GO:0051493]; regulation of integrin biosynthetic process [GO:0045113]; regulation of respiratory burst involved in inflammatory response [GO:0060264]; regulation of toll-like receptor signaling pathway [GO:0034121]; response to lipopolysaccharide [GO:0032496]; sequestering of zinc ion [GO:0032119]
|
calprotectin complex [GO:1990660]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; S100A9 complex [GO:1990662]; secretory granule lumen [GO:0034774]
|
antioxidant activity [GO:0016209]; arachidonic acid binding [GO:0050544]; calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; microtubule binding [GO:0008017]; RAGE receptor binding [GO:0050786]; Toll-like receptor 4 binding [GO:0035662]; zinc ion binding [GO:0008270]
|
PF01023;
|
1.10.238.10;
|
S-100 family
|
PTM: Phosphorylated. Phosphorylation inhibits activation of tubulin polymerization. {ECO:0000269|PubMed:15331440, ECO:0000269|PubMed:15905572, ECO:0000269|PubMed:2478889}.; PTM: S-nitrosylation of Cys-3 is implicated in LDL(ox)-induced S-nitrosylation of GAPDH at 'Cys-247' through a transnitrosylase mechanism involving a iNOS-S100A8/9 complex (PubMed:25417112). {ECO:0000305|PubMed:25417112}.; PTM: Methylation at His-105 by METTL9 reduces zinc-binding without affecting heterodimerization with S100A8. {ECO:0000250|UniProtKB:P31725}.
|
SUBCELLULAR LOCATION: Secreted. Cytoplasm {ECO:0000269|PubMed:15598812, ECO:0000269|PubMed:8423249}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22489132, ECO:0000269|PubMed:9083090}. Cell membrane {ECO:0000269|PubMed:18786929}; Peripheral membrane protein {ECO:0000305|PubMed:18786929}. Note=Predominantly localized in the cytoplasm. Upon elevation of the intracellular calcium level, translocated from the cytoplasm to the cytoskeleton and the cell membrane (PubMed:18786929). Upon neutrophil activation or endothelial adhesion of monocytes, is secreted via a microtubule-mediated, alternative pathway (PubMed:15598812). {ECO:0000269|PubMed:15598812, ECO:0000269|PubMed:18786929}.
| null | null | null | null | null |
FUNCTION: S100A9 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response (PubMed:12626582, PubMed:15331440, PubMed:16258195, PubMed:19122197, PubMed:20103766, PubMed:21325622, PubMed:8423249). It can induce neutrophil chemotaxis, adhesion, can increase the bactericidal activity of neutrophils by promoting phagocytosis via activation of SYK, PI3K/AKT, and ERK1/2 and can induce degranulation of neutrophils by a MAPK-dependent mechanism (PubMed:12626582, PubMed:15331440, PubMed:20103766). Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions (PubMed:16258195, PubMed:19122197, PubMed:8423249). The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase (PubMed:15331440, PubMed:21325622). Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX (PubMed:15642721, PubMed:22808130). The extracellular functions involve pro-inflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities (PubMed:19534726, PubMed:8423249). Its pro-inflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration (PubMed:15598812, PubMed:21487906). Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER) (PubMed:19402754). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the pro-inflammatory cascade (PubMed:19402754, PubMed:22804476). Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth (PubMed:19087201). Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3 (PubMed:19935772). Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK (PubMed:22363402). Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants (PubMed:21912088, PubMed:22489132). Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread (PubMed:16258195). Has transnitrosylase activity; in oxidatively-modified low-densitity lipoprotein (LDL(ox))-induced S-nitrosylation of GAPDH on 'Cys-247' proposed to transfer the NO moiety from NOS2/iNOS to GAPDH via its own S-nitrosylated Cys-3 (PubMed:25417112). The iNOS-S100A8/A9 transnitrosylase complex is proposed to also direct selective inflammatory stimulus-dependent S-nitrosylation of multiple targets such as ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif (PubMed:25417112). {ECO:0000269|PubMed:12626582, ECO:0000269|PubMed:15331440, ECO:0000269|PubMed:15598812, ECO:0000269|PubMed:15642721, ECO:0000269|PubMed:16258195, ECO:0000269|PubMed:19087201, ECO:0000269|PubMed:19122197, ECO:0000269|PubMed:19402754, ECO:0000269|PubMed:19534726, ECO:0000269|PubMed:19935772, ECO:0000269|PubMed:20103766, ECO:0000269|PubMed:21325622, ECO:0000269|PubMed:21487906, ECO:0000269|PubMed:22363402, ECO:0000269|PubMed:22804476, ECO:0000269|PubMed:22808130, ECO:0000269|PubMed:25417112, ECO:0000269|PubMed:8423249, ECO:0000303|PubMed:21912088, ECO:0000303|PubMed:22489132}.
|
Homo sapiens (Human)
|
P06703
|
S10A6_HUMAN
|
MACPLDQAIGLLVAIFHKYSGREGDKHTLSKKELKELIQKELTIGSKLQDAEIARLMEDLDRNKDQEVNFQEYVTFLGALALIYNEALKG
| null | null |
axonogenesis [GO:0007409]; positive regulation of fibroblast proliferation [GO:0048146]; signal transduction [GO:0007165]
|
collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ruffle [GO:0001726]
|
calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; monoatomic ion transmembrane transporter activity [GO:0015075]; protein homodimerization activity [GO:0042803]; S100 protein binding [GO:0044548]; tropomyosin binding [GO:0005523]; zinc ion binding [GO:0008270]
|
PF01023;
|
1.10.238.10;
|
S-100 family
|
PTM: The N-terminus is blocked.
|
SUBCELLULAR LOCATION: Nucleus envelope. Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
| null | null | null | null | null |
FUNCTION: May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative. {ECO:0000269|PubMed:22399290}.
|
Homo sapiens (Human)
|
P06704
|
CDC31_YEAST
|
MSKNRSSLQSGPLNSELLEEQKQEIYEAFSLFDMNNDGFLDYHELKVAMKALGFELPKREILDLIDEYDSEGRHLMKYDDFYIVMGEKILKRDPLDEIKRAFQLFDDDHTGKISIKNLRRVAKELGETLTDEELRAMIEEFDLDGDGEINENEFIAICTDS
| null | null |
cell division [GO:0051301]; Golgi vesicle transport [GO:0048193]; mRNA export from nucleus [GO:0006406]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; spindle pole body duplication [GO:0030474]
|
cytoplasm [GO:0005737]; half bridge of spindle pole body [GO:0005825]; mitotic spindle pole body [GO:0044732]; nuclear envelope [GO:0005635]; transcription export complex 2 [GO:0070390]
|
calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; microtubule binding [GO:0008017]
|
PF13499;
|
1.10.238.10;
|
Centrin family
| null |
SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:10684247}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:8188750}. Note=Spindle pole body, SPB half- bridge (PubMed:8188750). Interacts with the nuclear pore complex (NPCs) at the nucleus envelope (PubMed:10684247). {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:8188750}.
| null | null | null | null | null |
FUNCTION: Functions as a component of the spindle pole body (SPB) half-bridge (PubMed:10684247, PubMed:11156974, PubMed:12486115, PubMed:14504268, PubMed:8070654). At the SPB, it is recruited by KAR1 and MPS3 to the SPB half-bridge and involved in the initial steps of SPB duplication (PubMed:11156974, PubMed:12486115, PubMed:14504268, PubMed:8070654). Also involved in connection with the protein kinase KIC1 in the maintenance of cell morphology and integrity (PubMed:9813095). May play a role in vesicle-mediated transport, in a VPS13-dependent manner (PubMed:28122955). {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11156974, ECO:0000269|PubMed:12486115, ECO:0000269|PubMed:14504268, ECO:0000269|PubMed:28122955, ECO:0000269|PubMed:8070654, ECO:0000269|PubMed:9813095}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P06709
|
BIRA_ECOLI
|
MKDNTVPLKLIALLANGEFHSGEQLGETLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLNAKQILGQLDGGSVAVLPVIDSTNQYLLDRIGELKSGDACIAEYQQAGRGRRGRKWFSPFGANLYLSMFWRLEQGPAAAIGLSLVIGIVMAEVLRKLGADKVRVKWPNDLYLQDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEESVVNQGWITLQEAGINLDRNTLAAMLIRELRAALELFEQEGLAPYLSRWEKLDNFINRPVKLIIGDKEIFGISRGIDKQGALLLEQDGIIKPWMGGEISLRSAEK
|
6.3.4.15
| null |
biotin biosynthetic process [GO:0009102]; biotin metabolic process [GO:0006768]; protein modification process [GO:0036211]; regulation of DNA-templated transcription [GO:0006355]
|
cytoplasm [GO:0005737]; transcription repressor complex [GO:0017053]
|
ATP binding [GO:0005524]; biotin binding [GO:0009374]; biotin-[acetyl-CoA-carboxylase] ligase activity [GO:0004077]; DNA binding [GO:0003677]; nucleic acid binding [GO:0003676]; protein homodimerization activity [GO:0042803]; transcription cis-regulatory region binding [GO:0000976]
|
PF02237;PF03099;PF08279;
|
2.30.30.100;1.10.10.10;
|
Biotin--protein ligase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H(+) + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:11756, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10505, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57586, ChEBI:CHEBI:83144, ChEBI:CHEBI:456215; EC=6.3.4.15; Evidence={ECO:0000255|HAMAP-Rule:MF_00978, ECO:0000269|PubMed:6129246, ECO:0000269|PubMed:8003500};
| null | null | null | null |
FUNCTION: Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. {ECO:0000255|HAMAP-Rule:MF_00978, ECO:0000269|PubMed:12527300, ECO:0000269|PubMed:2667763, ECO:0000269|PubMed:6129246, ECO:0000269|PubMed:8003500}.
|
Escherichia coli (strain K12)
|
P06710
|
DPO3X_ECOLI
|
MSYQVLARKWRPQTFADVVGQEHVLTALANGLSLGRIHHAYLFSGTRGVGKTSIARLLAKGLNCETGITATPCGVCDNCREIEQGRFVDLIEIDAASRTKVEDTRDLLDNVQYAPARGRFKVYLIDEVHMLSRHSFNALLKTLEEPPEHVKFLLATTDPQKLPVTILSRCLQFHLKALDVEQIRHQLEHILNEEHIAHEPRALQLLARAAEGSLRDALSLTDQAIASGDGQVSTQAVSAMLGTLDDDQALSLVEAMVEANGERVMALINEAAARGIEWEALLVEMLGLLHRIAMVQLSPAALGNDMAAIELRMRELARTIPPTDIQLYYQTLLIGRKELPYAPDRRMGVEMTLLRALAFHPRMPLPEPEVPRQSFAPVAPTAVMTPTQVPPQPQSAPQQAPTVPLPETTSQVLAARQQLQRVQGATKAKKSEPAAATRARPVNNAALERLASVTDRVQARPVPSALEKAPAKKEAYRWKATTPVMQQKEVVATPKALKKALEHEKTPELAAKLAAEAIERDPWAAQVSQLSLPKLVEQVALNAWKEESDNAVCLHLRSSQRHLNNRGAQQKLAEALSMLKGSTVELTIVEDDNPAVRTPLEWRQAIYEEKLAQARESIIADNNIQTLRRFFDAELDEESIRPI
|
2.7.7.7
| null |
DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA-templated DNA replication [GO:0006261]
|
DNA polymerase III complex [GO:0009360]; DNA polymerase III, clamp loader complex [GO:0043846]; replisome [GO:0030894]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA clamp loader activity [GO:0003689]; DNA polymerase processivity factor activity [GO:0030337]; DNA-directed DNA polymerase activity [GO:0003887]; identical protein binding [GO:0042802]; ribonucleoside triphosphate phosphatase activity [GO:0017111]
|
PF13177;PF12169;PF12168;PF12170;
|
1.10.8.60;1.20.272.10;3.30.300.150;3.40.50.300;
|
DnaX/STICHEL family
| null | null |
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7;
| null | null | null | null |
FUNCTION: Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex (PubMed:2040637). DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3'-5' exonuclease activity. The gamma complex (gamma(3),delta,delta') is thought to load beta dimers onto DNA by binding ATP which alters the complex's conformation so it can bind beta sliding clamp dimers and open them at one interface. Primed DNA is recognized, ATP is hydrolyzed releasing the gamma complex and closing the beta sliding clamp ring around the primed DNA (PubMed:9927437). {ECO:0000269|PubMed:2040637}.; FUNCTION: [Isoform tau]: Serves as a scaffold to trimerize the core complex (PubMed:7037770). {ECO:0000305|PubMed:7037770}.; FUNCTION: [Isoform gamma]: Interacts with the delta and delta' subunits to transfer the beta subunit on the DNA (PubMed:9927437). Interacts with ATP, drives ATP-induced conformational changes in the gamma complex that opens the beta sliding clamp ring. After loading of primed DNA ATP is hydrolyzed and the beta sliding clamp ring closes (PubMed:9927437). {ECO:0000269|PubMed:9927437}.
|
Escherichia coli (strain K12)
|
P06715
|
GSHR_ECOLI
|
MTKHYDYIAIGGGSGGIASINRAAMYGQKCALIEAKELGGTCVNVGCVPKKVMWHAAQIREAIHMYGPDYGFDTTINKFNWETLIASRTAYIDRIHTSYENVLGKNNVDVIKGFARFVDAKTLEVNGETITADHILIATGGRPSHPDIPGVEYGIDSDGFFALPALPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNTDGSLTLELEDGRSETVDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDDQVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEKIVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR
|
1.8.1.7
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 1 FAD per subunit.;
|
cell redox homeostasis [GO:0045454]; cellular response to oxidative stress [GO:0034599]; glutathione metabolic process [GO:0006749]
|
cytosol [GO:0005829]; membrane [GO:0016020]
|
FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; glutathione-disulfide reductase (NADP) activity [GO:0004362]; NADP binding [GO:0050661]
|
PF07992;PF02852;
|
3.30.390.30;3.50.50.60;
|
Class-I pyridine nucleotide-disulfide oxidoreductase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=2 glutathione + NADP(+) = glutathione disulfide + H(+) + NADPH; Xref=Rhea:RHEA:11740, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58349; EC=1.8.1.7;
| null | null | null | null |
FUNCTION: Maintains high levels of reduced glutathione in the cytosol.
|
Escherichia coli (strain K12)
|
P06717
|
ELAP_ECOLX
|
MKNITFIFFILLASPLYANGDRLYRADSRPPDEIKRSGGLMPRGHNEYFDRGTQMNINLYDHARGTQTGFVRYDDGYVSTSLSLRSAHLAGQSILSGYSTYYIYVIATAPNMFNVNDVLGVYSPHPYEQEVSALGGIPYSQIYGWYRVNFGVIDERLHRNREYRDRYYRNLNIAPAEDGYRLAGFPPDHQAWREEPWIHHAPQGCGNSSRTITGDTCNEETQNLSTIYLREYQSKVKRQIFSDYQSEVDIYNRIRDEL
| null | null | null |
extracellular space [GO:0005615]
|
toxin activity [GO:0090729]
|
PF01375;
|
1.20.5.240;3.90.210.10;
|
Enterotoxin A family
| null | null | null | null | null | null | null |
FUNCTION: The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.
|
Escherichia coli
|
P06721
|
METC_ECOLI
|
MADKKLDTQLVNAGRSKKYTLGAVNSVIQRASSLVFDSVEAKKHATRNRANGELFYGRRGTLTHFSLQQAMCELEGGAGCVLFPCGAAAVANSILAFIEQGDHVLMTNTAYEPSQDFCSKILSKLGVTTSWFDPLIGADIVKHLQPNTKIVFLESPGSITMEVHDVPAIVAAVRSVVPDAIIMIDNTWAAGVLFKALDFGIDVSIQAATKYLVGHSDAMIGTAVCNARCWEQLRENAYLMGQMVDADTAYITSRGLRTLGVRLRQHHESSLKVAEWLAEHPQVARVNHPALPGSKGHEFWKRDFTGSSGLFSFVLKKKLNNEELANYLDNFSLFSMAYSWGGYESLILANQPEHIAAIRPQGEIDFSGTLIRLHIGLEDVDDLIADLDAGFARIV
|
4.4.1.13; 4.4.1.28
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:3307782, ECO:0000269|PubMed:7049234, ECO:0000269|PubMed:8566238};
|
L-cysteine catabolic process to pyruvate [GO:0019450]; methionine biosynthetic process [GO:0009086]; protein homotetramerization [GO:0051289]; transsulfuration [GO:0019346]
|
cytoplasm [GO:0005737]; protein-containing complex [GO:0032991]
|
alanine racemase activity [GO:0008784]; cystathionine beta-lyase activity [GO:0004121]; cysteine-S-conjugate beta-lyase activity [GO:0047804]; identical protein binding [GO:0042802]; L-cysteine desulfhydrase activity [GO:0080146]; pyridoxal phosphate binding [GO:0030170]
|
PF01053;
|
3.90.1150.10;3.40.640.10;
|
Trans-sulfuration enzymes family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate; Xref=Rhea:RHEA:13965, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199; Evidence={ECO:0000269|PubMed:7049234}; CATALYTIC ACTIVITY: Reaction=H2O + L-cysteine = H(+) + hydrogen sulfide + NH4(+) + pyruvate; Xref=Rhea:RHEA:24931, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29919, ChEBI:CHEBI:35235; EC=4.4.1.28; Evidence={ECO:0000269|PubMed:12883870}; CATALYTIC ACTIVITY: Reaction=an S-substituted L-cysteine + H2O = a thiol + NH4(+) + pyruvate; Xref=Rhea:RHEA:18121, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29256, ChEBI:CHEBI:58717; EC=4.4.1.13; Evidence={ECO:0000269|PubMed:7049234};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.04 mM for L-cystathionine {ECO:0000269|PubMed:7049234}; KM=0.25 mM for L-cystine {ECO:0000269|PubMed:7049234}; Vmax=249 umol/min/mg enzyme with L-cystathionine as substrate {ECO:0000269|PubMed:7049234}; Vmax=263 umol/min/mg enzyme with L-cystine as substrate {ECO:0000269|PubMed:7049234};
|
PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from L-cystathionine: step 1/1. {ECO:0000305}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-9.0. {ECO:0000269|PubMed:7049234};
| null |
FUNCTION: Primarily catalyzes the cleavage of cystathionine to homocysteine, pyruvate and ammonia during methionine biosynthesis (PubMed:7049234). Also exhibits cysteine desulfhydrase activity, producing sulfide from cysteine (PubMed:12883870). In addition, under certain growth conditions, exhibits significant alanine racemase coactivity (PubMed:21193606). {ECO:0000269|PubMed:12883870, ECO:0000269|PubMed:21193606, ECO:0000269|PubMed:7049234}.
|
Escherichia coli (strain K12)
|
P06722
|
MUTH_ECOLI
|
MSQPRPLLSPPETEEQLLAQAQQLSGYTLGELAALVGLVTPENLKRDKGWIGVLLEIWLGASAGSKPEQDFAALGVELKTIPVDSLGRPLETTFVCVAPLTGNSGVTWETSHVRHKLKRVLWIPVEGERSIPLAQRRVGSPLLWSPNEEEDRQLREDWEELMDMIVLGQVERITARHGEYLQIRPKAANAKALTEAIGARGERILTLPRGFYLKKNFTSALLARHFLIQ
| null | null |
DNA modification [GO:0006304]; mismatch repair [GO:0006298]; regulation of DNA recombination [GO:0000018]
|
cytoplasm [GO:0005737]; mismatch repair complex [GO:0032300]
|
DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; T/G mismatch-specific endonuclease activity [GO:0043765]
|
PF02976;
|
3.40.600.10;
|
MutH family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Sequence-specific endonuclease that cleaves unmethylated GATC sequences. It is involved in DNA mismatch repair.
|
Escherichia coli (strain K12)
|
P06726
|
PP71_HCMVA
|
MSQASSSPGEGPSSEAAAISEAEAASGSFGRLHCQVLRLITNVEGGSLEAGRLRLLDLRTNIEVSRPSVLCCFQENKSPHDTVDLTDLNIKGRCVVGEQDRLLVDLNNFGPRRLTPGSENNTVSVLAFALPLDRVPVSGLHLFQSQRRGGEENRPRMEARAIIRRTAHHWAVRLTVTPNWRRRTDSSLEAGQIFVSQFAFRAGAIPLTLVDALEQLACSDPNTYIHKTETDERGQWIMLFLHHDSPHPPTSVFLHFSVYTHRAEVVARHNPYPHLRRLPDNGFQLLIPKSFTLTRIHPEYIVQIQNAFETNQTHDTIFFPENIPGVSIEAGPLPDRVRITLRVTLTGDQAVHLEHRQPLGRIHFFRRGFWTLTPGKPDKIKRPQVQLRAGLFPRSNVMRGAVSEFLPQSPGLPPTEEEEEEEEEDDEDDLSSTPTPTPLSEAMFAGFEEASGDEDSDTQAGLSPALILTGQRRRSGNNGALTLVIPSWHVFASLDDLVPLTVSVQHAALRPTSYLRSDMDGDVRTAADISSTLRSVPAPRPSPISTASTSSTPRSRPRI
| null | null |
DNA-templated viral transcription [GO:0039695]; symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint [GO:0039645]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell endoplasmic reticulum [GO:0044165]; host cell nucleus [GO:0042025]; viral tegument [GO:0019033]
| null |
PF05784;
| null |
Herpesviridae pp71 family
|
PTM: S-nitrosylation limits ability to undermine the cGAS/STING antiviral pathway. {ECO:0000269|PubMed:32581105}.
|
SUBCELLULAR LOCATION: Virion tegument {ECO:0000305}. Host nucleus {ECO:0000269|PubMed:19369322, ECO:0000269|PubMed:9000101}. Host endoplasmic reticulum {ECO:0000269|PubMed:28132838}. Note=Present in the nucleus shortly after infection as well as during the late phase of viral morphogenesis. Detected at nuclear domain 10 (ND10).
| null | null | null | null | null |
FUNCTION: Stimulates viral immediate-early (IE) transcription. Plays a role in the inhibition of the host innate repsonse by targeting STING1 and thus the cGAS-STING pathway (PubMed:28132838, PubMed:32581105). Counteracts also host DAXX-mediated repression of viral transcription. Displaces a DAXX-binding protein, ATRX, from nuclear domain 10 sites (ND10) shortly after infection (PubMed:18922870). Increases the basal level of SUMOylated DAXX in infected cells (PubMed:19369322). Stimulates quiescent cells to re-enter the cell cycle, proceed through G1 and enter the S phase (PubMed:12610120). Interacts with hypophosphorylated forms of RB1 and induces their degradation by the proteasome without involving ubiquitin conjugation (PubMed:12626766). {ECO:0000269|PubMed:12610120, ECO:0000269|PubMed:12626766, ECO:0000269|PubMed:18922870, ECO:0000269|PubMed:19369322, ECO:0000269|PubMed:28132838, ECO:0000269|PubMed:32581105}.
|
Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
|
P06727
|
APOA4_HUMAN
|
MFLKAVVLTLALVAVAGARAEVSADQVATVMWDYFSQLSNNAKEAVEHLQKSELTQQLNALFQDKLGEVNTYAGDLQKKLVPFATELHERLAKDSEKLKEEIGKELEELRARLLPHANEVSQKIGDNLRELQQRLEPYADQLRTQVSTQAEQLRRQLTPYAQRMERVLRENADSLQASLRPHADELKAKIDQNVEELKGRLTPYADEFKVKIDQTVEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRLAPLAEDVRGNLRGNTEGLQKSLAELGGHLDQQVEEFRRRVEPYGENFNKALVQQMEQLRQKLGPHAGDVEGHLSFLEKDLRDKVNSFFSTFKEKESQDKTLSLPELEQQQEQQQEQQQEQVQMLAPLES
| null | null |
acylglycerol homeostasis [GO:0055090]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; chylomicron assembly [GO:0034378]; chylomicron remodeling [GO:0034371]; high-density lipoprotein particle remodeling [GO:0034375]; hydrogen peroxide catabolic process [GO:0042744]; innate immune response in mucosa [GO:0002227]; leukocyte cell-cell adhesion [GO:0007159]; lipid catabolic process [GO:0016042]; lipid homeostasis [GO:0055088]; lipid transport [GO:0006869]; lipoprotein metabolic process [GO:0042157]; negative regulation of plasma lipoprotein oxidation [GO:0034445]; peripheral nervous system axon regeneration [GO:0014012]; phosphatidylcholine metabolic process [GO:0046470]; phospholipid efflux [GO:0033700]; positive regulation of CoA-transferase activity [GO:1905920]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of lipoprotein lipase activity [GO:0051006]; positive regulation of triglyceride catabolic process [GO:0010898]; protein-lipid complex assembly [GO:0065005]; regulation of cholesterol transport [GO:0032374]; regulation of intestinal cholesterol absorption [GO:0030300]; removal of superoxide radicals [GO:0019430]; response to lipid hydroperoxide [GO:0006982]; response to stilbenoid [GO:0035634]; response to triglyceride [GO:0034014]; reverse cholesterol transport [GO:0043691]; triglyceride homeostasis [GO:0070328]; very-low-density lipoprotein particle remodeling [GO:0034372]
|
blood microparticle [GO:0072562]; chylomicron [GO:0042627]; collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; early endosome [GO:0005769]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; high-density lipoprotein particle [GO:0034364]; low-density lipoprotein particle [GO:0034362]; synapse [GO:0045202]; very-low-density lipoprotein particle [GO:0034361]
|
antioxidant activity [GO:0016209]; cholesterol transfer activity [GO:0120020]; copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; lipid transporter activity [GO:0005319]; phosphatidylcholine binding [GO:0031210]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein homodimerization activity [GO:0042803]
|
PF01442;
|
1.20.120.20;
|
Apolipoprotein A1/A4/E family
|
PTM: Phosphorylation sites are present in the extracellular medium.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons.
|
Homo sapiens (Human)
|
P06728
|
APOA4_MOUSE
|
MFLKAAVLTLALVAITGTRAEVTSDQVANVVWDYFTQLSNNAKEAVEQFQKTDVTQQLSTLFQDKLGDASTYADGVHNKLVPFVVQLSGHLAQETERVKEEIKKELEDLRDRMMPHANKVTQTFGENMQKLQEHLKPYAVDLQDQINTQTQEMKLQLTPYIQRMQTTIKENVDNLHTSMMPLATNLKDKFNRNMEELKGHLTPRANELKATIDQNLEDLRRSLAPLTVGVQEKLNHQMEGLAFQMKKNAEELQTKVSAKIDQLQKNLAPLVEDVQSKVKGNTEGLQKSLEDLNRQLEQQVEEFRRTVEPMGEMFNKALVQQLEQFRQQLGPNSGEVESHLSFLEKSLREKVNSFMSTLEKKGSPDQPQALPLPEQAQEQAQEQAQEQVQPKPLES
| null | null |
acylglycerol homeostasis [GO:0055090]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; high-density lipoprotein particle remodeling [GO:0034375]; hydrogen peroxide catabolic process [GO:0042744]; innate immune response in mucosa [GO:0002227]; leukocyte cell-cell adhesion [GO:0007159]; lipid catabolic process [GO:0016042]; lipoprotein metabolic process [GO:0042157]; negative regulation of plasma lipoprotein oxidation [GO:0034445]; peripheral nervous system axon regeneration [GO:0014012]; phosphatidylcholine metabolic process [GO:0046470]; phospholipid efflux [GO:0033700]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of triglyceride catabolic process [GO:0010898]; protein-lipid complex assembly [GO:0065005]; regulation of cholesterol transport [GO:0032374]; regulation of intestinal cholesterol absorption [GO:0030300]; removal of superoxide radicals [GO:0019430]; response to lipid hydroperoxide [GO:0006982]; response to stilbenoid [GO:0035634]; response to triglyceride [GO:0034014]; reverse cholesterol transport [GO:0043691]; triglyceride homeostasis [GO:0070328]; very-low-density lipoprotein particle remodeling [GO:0034372]
|
blood microparticle [GO:0072562]; cell surface [GO:0009986]; chylomicron [GO:0042627]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; high-density lipoprotein particle [GO:0034364]; low-density lipoprotein particle [GO:0034362]; synapse [GO:0045202]; very-low-density lipoprotein particle [GO:0034361]
|
antioxidant activity [GO:0016209]; cholesterol transfer activity [GO:0120020]; copper ion binding [GO:0005507]; phosphatidylcholine binding [GO:0031210]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein homodimerization activity [GO:0042803]
|
PF01442;
|
1.20.120.20;
|
Apolipoprotein A1/A4/E family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons.
|
Mus musculus (Mouse)
|
P06729
|
CD2_HUMAN
|
MSFPCKFVASFLLIFNVSSKGAVSKEITNALETWGALGQDINLDIPSFQMSDDIDDIKWEKTSDKKKIAQFRKEKETFKEKDTYKLFKNGTLKIKHLKTDDQDIYKVSIYDTKGKNVLEKIFDLKIQERVSKPKISWTCINTTLTCEVMNGTDPELNLYQDGKHLKLSQRVITHKWTTSLSAKFKCTAGNKVSKESSVEPVSCPEKGLDIYLIIGICGGGSLLMVFVALLVFYITKRKKQRSRRNDEELETRAHRVATEERGRKPHQIPASTPQNPATSQHPPPPPGHRSQAPSHRPPPPGHRVQHQPQKRPPAPSGTQVHQQKGPPLPRPRVQPKPPHGAAENSLSPSSN
| null | null |
apoptotic process [GO:0006915]; cell surface receptor signaling pathway [GO:0007166]; cell-cell adhesion [GO:0098609]; heterotypic cell-cell adhesion [GO:0034113]; membrane raft polarization [GO:0001766]; natural killer cell activation [GO:0030101]; natural killer cell mediated cytotoxicity [GO:0042267]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of myeloid dendritic cell activation [GO:0030887]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of type II interferon production [GO:0032729]; regulation of T cell differentiation [GO:0045580]; T cell activation [GO:0042110]
|
cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cytoplasmic side of plasma membrane [GO:0009898]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
identical protein binding [GO:0042802]; protein self-association [GO:0043621]; receptor tyrosine kinase binding [GO:0030971]; signaling receptor activity [GO:0038023]; signaling receptor binding [GO:0005102]
|
PF05790;PF07686;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23006327, ECO:0000269|PubMed:2437578}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: CD2 interacts with lymphocyte function-associated antigen CD58 (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T-cells, the cytoplasmic domain is implicated in the signaling function.
|
Homo sapiens (Human)
|
P06730
|
IF4E_HUMAN
|
MATVEPETTPTPNPPTTEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV
| null | null |
behavioral fear response [GO:0001662]; cellular response to dexamethasone stimulus [GO:0071549]; G1/S transition of mitotic cell cycle [GO:0000082]; mRNA export from nucleus [GO:0006406]; negative regulation of neuron differentiation [GO:0045665]; negative regulation of translation [GO:0017148]; neuron differentiation [GO:0030182]; positive regulation of mitotic cell cycle [GO:0045931]; regulation of translation [GO:0006417]; regulation of translation at postsynapse, modulating synaptic transmission [GO:0099578]; stem cell population maintenance [GO:0019827]; translational initiation [GO:0006413]
|
chromatoid body [GO:0033391]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; eukaryotic translation initiation factor 4F complex [GO:0016281]; extracellular exosome [GO:0070062]; glutamatergic synapse [GO:0098978]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; P-body [GO:0000932]; perinuclear region of cytoplasm [GO:0048471]; postsynapse [GO:0098794]; RISC complex [GO:0016442]
|
DNA-binding transcription factor binding [GO:0140297]; enzyme binding [GO:0019899]; eukaryotic initiation factor 4G binding [GO:0031370]; mRNA cap binding [GO:0098808]; RNA 7-methylguanosine cap binding [GO:0000340]; RNA binding [GO:0003723]; RNA cap binding [GO:0000339]; translation initiation factor activity [GO:0003743]
|
PF01652;
|
3.30.760.10;
|
Eukaryotic initiation factor 4E family
|
PTM: Phosphorylation increases the ability of the protein to bind to mRNA caps and to form the eIF4F complex (PubMed:11154262, PubMed:3112145, PubMed:7590282, PubMed:7665584, PubMed:7782323, PubMed:8505316, PubMed:9878069). Phosphorylation also enhances its mRNA transport function (By similarity). Phosphorylation at Ser-209 is not essential for protein synthesis (PubMed:11606200, PubMed:12138083). {ECO:0000250|UniProtKB:P63073, ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:11606200, ECO:0000269|PubMed:12138083, ECO:0000269|PubMed:3112145, ECO:0000269|PubMed:7590282, ECO:0000269|PubMed:7665584, ECO:0000269|PubMed:7782323, ECO:0000269|PubMed:8505316, ECO:0000269|PubMed:9878069}.
|
SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:16157702, ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:24335285, ECO:0000269|PubMed:25923732}. Cytoplasm {ECO:0000269|PubMed:10856257, ECO:0000269|PubMed:12554669, ECO:0000269|PubMed:1384058, ECO:0000269|PubMed:15657436, ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:23471078, ECO:0000269|PubMed:36843541}. Cytoplasm, Stress granule {ECO:0000269|PubMed:21883093}. Nucleus {ECO:0000269|PubMed:10856257, ECO:0000269|PubMed:11423616, ECO:0000269|PubMed:1384058, ECO:0000269|PubMed:23471078, ECO:0000269|PubMed:36843541}. Nucleus speckle {ECO:0000269|PubMed:10648556}. Nucleus, nuclear body {ECO:0000269|PubMed:12554669, ECO:0000269|PubMed:15657436}. Note=Interaction with EIF4ENIF1/4E-T is required for localization to processing bodies (P-bodies) (PubMed:16157702, PubMed:24335285, PubMed:25923732). Imported in the nucleus via interaction with EIF4ENIF1/4E-T via a piggy-back mechanism (PubMed:10856257). Sequestered in the nucleus by EIF4EBP1 and EIF4EBP2 (By similarity). {ECO:0000250|UniProtKB:P63073, ECO:0000269|PubMed:10856257, ECO:0000269|PubMed:16157702, ECO:0000269|PubMed:24335285, ECO:0000269|PubMed:25923732}.
| null | null | null | null | null |
FUNCTION: Acts in the cytoplasm to initiate and regulate protein synthesis and is required in the nucleus for export of a subset of mRNAs from the nucleus to the cytoplasm which promotes processes such as RNA capping, processing and splicing (PubMed:11606200, PubMed:22578813, PubMed:22684010, PubMed:24335285, PubMed:29987188). Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). This protein recognizes and binds the 7-methylguanosine (m7G)-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (PubMed:16271312, PubMed:22578813). Together with EIF4G1, antagonizes the scanning promoted by EIF1-EIF4G1 and is required for TISU translation, a process where the TISU element recognition makes scanning unnecessary (PubMed:29987188). In addition to its role in translation initiation, also acts as a regulator of translation and stability in the cytoplasm (PubMed:24335285). Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression: in the complex, EIF4E mediates the binding to the mRNA cap (By similarity). Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity). In P-bodies, component of a complex that mediates the storage of translationally inactive mRNAs in the cytoplasm and prevents their degradation (PubMed:24335285). May play an important role in spermatogenesis through translational regulation of stage-specific mRNAs during germ cell development (By similarity). As well as its roles in translation, also involved in mRNA nucleocytoplasmic transport (By similarity). Its role in mRNA export from the nucleus to the cytoplasm relies on its ability to bind the m7G cap of RNAs and on the presence of the 50-nucleotide EIF4E sensitivity element (4ESE) in the 3'UTR of sensitive transcripts (By similarity). Interaction with the 4ESE is mediated by LRPPRC which binds simultaneously to both EIF4E and the 4ESE, thereby acting as a platform for assembly for the RNA export complex (By similarity). EIF4E-dependent mRNA export is independent of ongoing protein or RNA synthesis and is also NFX1-independent but is XPO1-dependent with LRPPRC interacting with XPO1 to form an EIF4E-dependent mRNA export complex (By similarity). Alters the composition of the cytoplasmic face of the nuclear pore to promote RNA export by reducing RANBP2 expression, relocalizing nucleoporin NUP214 and increasing expression of RANBP1 and RNA export factors DDX19 and GLE1 (By similarity). Promotes the nuclear export of cyclin CCND1 mRNA (By similarity). Promotes the nuclear export of NOS2/iNOS mRNA (PubMed:23471078). Promotes the nuclear export of MDM2 mRNA (PubMed:22684010). Promotes the export of additional mRNAs, including others involved in the cell cycle (By similarity). In the nucleus, binds to capped splice factor-encoding mRNAs and stimulates their nuclear export to enhance splice factor production by increasing their cytoplasmic availability to the translation machinery (By similarity). May also regulate splicing through interaction with the spliceosome in an RNA and m7G cap-dependent manner (By similarity). Also binds to some pre-mRNAs and may play a role in their recruitment to the spliceosome (By similarity). Promotes steady-state capping of a subset of coding and non-coding RNAs by mediating nuclear export of capping machinery mRNAs including RNMT, RNGTT and RAMAC to enhance their translation (By similarity). Stimulates mRNA 3'-end processing by promoting the expression of several core cleavage complex factors required for mRNA cleavage and polyadenylation, and may also have a direct effect through its interaction with the CPSF3 cleavage enzyme (By similarity). Rescues cells from apoptosis by promoting activation of serine/threonine-protein kinase AKT1 through mRNA export of NBS1 which potentiates AKT1 phosphorylation and also through mRNA export of AKT1 effectors, allowing for increased production of these proteins (By similarity). {ECO:0000250|UniProtKB:P63073, ECO:0000250|UniProtKB:P63074, ECO:0000269|PubMed:11606200, ECO:0000269|PubMed:16271312, ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:22684010, ECO:0000269|PubMed:23471078, ECO:0000269|PubMed:24335285, ECO:0000269|PubMed:29987188}.
|
Homo sapiens (Human)
|
P06731
|
CEAM5_HUMAN
|
MESPSAPPHRWCIPWQRLLLTASLLTFWNPPTTAKLTIESTPFNVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNRQIIGYVIGTQQATPGPAYSGREIIYPNASLLIQNIIQNDTGFYTLHVIKSDLVNEEATGQFRVYPELPKPSISSNNSKPVEDKDAVAFTCEPETQDATYLWWVNNQSLPVSPRLQLSNGNRTLTLFNVTRNDTASYKCETQNPVSARRSDSVILNVLYGPDAPTISPLNTSYRSGENLNLSCHAASNPPAQYSWFVNGTFQQSTQELFIPNITVNNSGSYTCQAHNSDTGLNRTTVTTITVYAEPPKPFITSNNSNPVEDEDAVALTCEPEIQNTTYLWWVNNQSLPVSPRLQLSNDNRTLTLLSVTRNDVGPYECGIQNELSVDHSDPVILNVLYGPDDPTISPSYTYYRPGVNLSLSCHAASNPPAQYSWLIDGNIQQHTQELFISNITEKNSGLYTCQANNSASGHSRTTVKTITVSAELPKPSISSNNSKPVEDKDAVAFTCEPEAQNTTYLWWVNGQSLPVSPRLQLSNGNRTLTLFNVTRNDARAYVCGIQNSVSANRSDPVTLDVLYGPDTPIISPPDSSYLSGANLNLSCHSASNPSPQYSWRINGIPQQHTQVLFIAKITPNNNGTYACFVSNLATGRNNSIVKSITVSASGTSPGLSAGATVGIMIGVLVGVALI
| null | null |
apoptotic process [GO:0006915]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; homotypic cell-cell adhesion [GO:0034109]; negative regulation of anoikis [GO:2000811]; negative regulation of apoptotic process [GO:0043066]; negative regulation of myotube differentiation [GO:0010832]; regulation of immune system process [GO:0002682]; signal transduction [GO:0007165]
|
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; membrane [GO:0016020]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
|
GPI anchor binding [GO:0034235]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; protein tyrosine kinase binding [GO:1990782]
|
PF13895;PF13927;PF07686;
|
2.60.40.10;
|
Immunoglobulin superfamily, CEA family
|
PTM: Complex immunoreactive glycoprotein with a MW of 180 kDa comprising 60% carbohydrate.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10864933, ECO:0000269|PubMed:18086185, ECO:0000269|PubMed:2317824}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10864933, ECO:0000269|PubMed:18086185, ECO:0000269|PubMed:2317824}. Apical cell membrane {ECO:0000269|PubMed:10436421}. Cell surface {ECO:0000269|PubMed:2317824, ECO:0000269|PubMed:2803308}. Note=Localized to the apical glycocalyx surface. {ECO:0000269|PubMed:10436421}.
| null | null | null | null | null |
FUNCTION: Cell surface glycoprotein that plays a role in cell adhesion, intracellular signaling and tumor progression (PubMed:10864933, PubMed:10910050, PubMed:2803308). Mediates homophilic and heterophilic cell adhesion with other carcinoembryonic antigen-related cell adhesion molecules, such as CEACAM6 (PubMed:2803308). Plays a role as an oncogene by promoting tumor progression; induces resistance to anoikis of colorectal carcinoma cells (PubMed:10910050). {ECO:0000269|PubMed:10864933, ECO:0000269|PubMed:10910050, ECO:0000269|PubMed:2803308}.; FUNCTION: (Microbial infection) Receptor for E.coli Dr adhesins. Binding of E.coli Dr adhesins leads to dissociation of the homodimer. {ECO:0000269|PubMed:18086185}.
|
Homo sapiens (Human)
|
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