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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P11217 | PYGM_HUMAN | MSRPLSDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKISGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGHVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCR... | 2.4.1.1 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P00489}; | glycogen catabolic process [GO:0005980]; glycogen metabolic process [GO:0005977] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062] | glycogen phosphorylase activity [GO:0008184]; linear malto-oligosaccharide phosphorylase activity [GO:0102250]; nucleotide binding [GO:0000166]; pyridoxal phosphate binding [GO:0030170]; SHG alpha-glucan phosphorylase activity [GO:0102499] | PF00343; | 3.40.50.2000; | Glycogen phosphorylase family | PTM: Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A. {ECO:0000269|PubMed:1150650}. | null | CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1; Evidence={ECO:0000269|PubMed:1150650, ECO:0000269|Pub... | null | null | null | null | FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis. {ECO:0000269|PubMed:8316268}. | Homo sapiens (Human) |
P11218 | AGI_URTDI | MMMRFLSAVVIMSSAMAVGLVSAQRCGSQGGGGTCPALWCCSIWGWCGDSEPYCGRTCENKCWSGERSDHRCGAAVGNPPCGQDRCCSVHGWCGGGNDYCSGSKCQYRCSSSVRGPRVALSGNSTANSIGNVVVTEPLFDQMFSHRKDCPSQGFYSYHSFLVAAESFPAFGTIGDVATRKREVAAFLAHISQATSGERSDVENPHAWGLCHINTTTVTENDFCTSSDWPCAAGKKYSPRGPIQLTHNFNYGLAGQAIGEDLIQNPDLVEKDPIISFKTALWFWMSQHDNKPSCHDIVLNANSAANRIPNKGVIGNIISRA... | 3.2.1.14 | null | cell wall macromolecule catabolic process [GO:0016998]; chitin catabolic process [GO:0006032]; defense response to fungus [GO:0050832]; killing of cells of another organism [GO:0031640]; polysaccharide catabolic process [GO:0000272] | null | carbohydrate binding [GO:0030246]; chitin binding [GO:0008061]; chitinase activity [GO:0004568]; metal ion binding [GO:0046872] | PF00187;PF00182; | 1.10.530.10;3.30.20.10;3.30.60.10; | null | PTM: Proteolytically processed to yield a very small protein (8.5 kDa, 86 AA) containing only the two chitin-binding domains. | null | CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; | null | null | null | null | FUNCTION: Functions both as a chitinase and as a N-acetyl-D-glucosamine binding lectin. Inhibits the growth of several phytopathogenic chitin-containing fungi. Possesses also insecticidal activity and superantigenic properties. {ECO:0000269|PubMed:10873861}. | Urtica dioica (Great nettle) (Stinging nettle) |
P11223 | SPIKE_IBVB | MLVTPLLLVTLLCALCSAVLYDSSSYVYYYQSAFRPPSGWHLQGGAYAVVNISSEFNNAGSSSGCTVGIIHGGRVVNASSIAMTAPSSGMAWSSSQFCTAHCNFSDTTVFVTHCYKHGGCPLTGMLQQNLIRVSAMKNGQLFYNLTVSVAKYPTFRSFQCVNNLTSVYLNGDLVYTSNETIDVTSAGVYFKAGGPITYKVMREVKALAYFVNGTAQDVILCDGSPRGLLACQYNTGNFSDGFYPFTNSSLVKQKFIVYRENSVNTTCTLHNFIFHNETGANPNPSGVQNIQTYQTKTAQSGYYNFNFSFLSSFVYKESNF... | null | null | endocytosis involved in viral entry into host cell [GO:0075509]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; receptor-mediated virion attachment to host cell [GO:0046813] | host cell endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0044173]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF19209;PF01601;PF19214; | 1.20.5.300; | Gammacoronaviruses spike protein family | PTM: Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host cell furin or furin-like protease to yield the mature S1 and S2 proteins. The cleavage site between S1 and S2 requires the optimal sequence [KR]-X-[KR]-R. Additionally, a second cleavage leads to the relea... | SUBCELLULAR LOCATION: [Spike protein S2]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04098}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04098}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04098}; Single-pass type I membrane protein {ECO:0000255|HAMAP... | null | null | null | null | null | FUNCTION: [Spike protein S1]: Attaches the virion to the host cell membrane by interacting with sialic acids, initiating the infection. {ECO:0000255|HAMAP-Rule:MF_04098, ECO:0000269|PubMed:16537586, ECO:0000269|PubMed:24314633}.; FUNCTION: [Spike protein S2]: Mediates fusion of the virion and cellular membranes by acti... | Avian infectious bronchitis virus (strain Beaudette) (IBV) |
P11224 | SPIKE_CVMA5 | MLFVFILFLPSCLGYIGDFRCIQLVNSNGANVSAPSISTETVEVSQGLGTYYVLDRVYLNATLLLTGYYPVDGSKFRNLALRGTNSVSLSWFQPPYLNQFNDGIFAKVQNLKTSTPSGATAYFPTIVIGSLFGYTSYTVVIEPYNGVIMASVCQYTICQLPYTDCKPNTNGNKLIGFWHTDVKPPICVLKRNFTLNVNADAFYFHFYQHGGTFYAYYADKPSATTFLFSVYIGDILTQYYVLPFICNPTAGSTFAPRYWVTPLVKRQYLFNFNQKGVITSAVDCASSYTSEIKCKTQSMLPSTGVYELSGYTVQPVGVVY... | null | null | endocytosis involved in viral entry into host cell [GO:0075509]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; receptor-mediated virion attachment to host cell [GO:0046813] | host cell endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0044173]; host cell Golgi apparatus [GO:0044177]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | identical protein binding [GO:0042802] | PF16451;PF09408;PF19209;PF01601;PF19214; | 1.20.5.300;3.30.70.1840;2.60.120.960; | Betacoronaviruses spike protein family | PTM: Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host cell furin or another cellular protease to yield the mature S1 and S2 proteins. Additionally, a second cleavage leads to the release of a fusion peptide after viral attachment to host cell receptor. {ECO:0... | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Hos... | null | null | null | null | null | FUNCTION: [Spike protein S1]: Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. Interacts with murine CEACAM1 to mediate viral entry. {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:16014947}.; FUNCTION: [Spike protein S2]: Mediates fusion of the virion and cellu... | Murine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus) |
P11225 | SPIKE_CVMJH | MLFVFILLLPSCLGYIGDFRCIQTVNYNGNNASAPSISTEAVDVSKGRGTYYVLDRVYLNATLLLTGYYPVDGSNYRNLALTGTNTLSLTWFKPPFLSEFNDGIFAKVQNLKTNTPTGATSYFPTIVIGSLFGNTSYTVVLEPYNNIIMASVCTYTICQLPYTPCKPNTNGNRVIGFWHTDVKPPICLLKRNFTFNVNAPWLYFHFYQQGGTFYAYYADKPSATTFLFSVYIGDILTQYFVLPFICTPTAGSTLAPLYWVTPLLKRQYLFNFNEKGVITSAVDCASSYISEIKCKTQSLLPSTGVYDLSGYTVQPVGVVY... | null | null | endocytosis involved in viral entry into host cell [GO:0075509]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; receptor-mediated virion attachment to host cell [GO:0046813] | host cell endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0044173]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF16451;PF09408;PF19209;PF01601;PF19214; | 1.20.5.300;3.30.70.1840;2.60.120.960; | Betacoronaviruses spike protein family | PTM: Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host cell furin or another cellular protease to yield the mature S1 and S2 proteins. Additionally, a second cleavage leads to the release of a fusion peptide after viral attachment to host cell receptor. {ECO:0... | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Hos... | null | null | null | null | null | FUNCTION: [Spike protein S1]: Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. {ECO:0000255|HAMAP-Rule:MF_04099}.; FUNCTION: [Spike protein S2]: Mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model,... | Murine coronavirus (strain JHM) (MHV-JHM) (Murine hepatitis virus) |
P11226 | MBL2_HUMAN | MSLFPSLPLLLLSMVAASYSETVTCEDAQKTCPAVIACSSPGINGFPGKDGRDGTKGEKGEPGQGLRGLQGPPGKLGPPGNPGPSGSPGPKGQKGDPGKSPDGDSSLAASERKALQTEMARIKKWLTFSLGKQVGNKFFLTNGEIMTFEKVKALCVKFQASVATPRNAAENGAIQNLIKEEAFLGITDEKTEGQFVDLTGNRLTYTNWNEGEPNNAGSDEDCVLLLKNGQWNDVPCSTSHLAVCEFPI | null | null | acute-phase response [GO:0006953]; antiviral innate immune response [GO:0140374]; cell surface pattern recognition receptor signaling pathway [GO:0002752]; complement activation, classical pathway [GO:0006958]; complement activation, lectin pathway [GO:0001867]; defense response to bacterium [GO:0042742]; defense respo... | cell surface [GO:0009986]; collagen trimer [GO:0005581]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; multivesicular body [GO:0005771]; serine-type endopeptidase complex [GO:1905370] | calcium-dependent protein binding [GO:0048306]; identical protein binding [GO:0042802]; mannose binding [GO:0005537]; signaling receptor binding [GO:0005102] | PF01391;PF00059; | 3.10.100.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7982896}. | null | null | null | null | null | FUNCTION: Calcium-dependent lectin involved in innate immune defense (PubMed:35102342). Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic ce... | Homo sapiens (Human) |
P11227 | POL_MLVRD | MGQTVTTPLSLTLEHWGDVQRIASNQSVEVKKRRRVTFCPAEWPTFDVGWPQDGTFNLDIILQVKSKVFSPGPHGHPDQVPYIVTWEAIAYEPPSWVKPFVSPKLSLSPTAPILPSGPSTQPPPRSALYPALTPSIKPRPSKPQVLSDNGGPLIDLLTEDPPPYGEQGPSSPDGDGDREEATYTSEIPAPSPMVSRLRGKRDPPAADSTTSRAFPLRLGGNGQLQYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLTTHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGNDGRPTQLPNEVNSAFPLERPDWDY... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; Note=The RT polymerase active site binds 2 magnesium ions. {ECO:0000255|PROSITE-ProRule:PRU00405}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03355}; Note=Binds 1 magnesium ion for ribonu... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; virion a... | host cell late endosome membrane [GO:0044185]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; RNA binding [GO:0003723]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural constituent of virion [GO:0039660]; zinc ion binding ... | PF01140;PF01141;PF02093;PF18697;PF00075;PF17919;PF00665;PF00077;PF00078;PF00098;PF16721; | 1.10.340.70;2.30.30.850;3.10.20.370;3.30.70.270;2.40.70.10;1.10.150.180;3.10.10.10;1.10.375.10;3.30.420.10;4.10.60.10; | Retroviral Pol polyprotein family | PTM: [Gag-Pol polyprotein]: Ubiquitinated by ITCH. Gag can recruit the ubiquitin ligase Itch in an L domain-independent manner to facilitate virus release via a mechanism that involves Gag ubiquitination. {ECO:0000250|UniProtKB:P03332}.; PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yie... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Virion {ECO:0000250|UniProtKB:P03332}. Host cell membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host late endosome membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular ... | 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=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag-Pol, or to Gag-Pol binding host factor... | Radiation murine leukemia virus |
P11229 | ACM1_HUMAN | MNTSAPPAVSPNITVLAPGKGPWQVAFIGITTGLLSLATVTGNLLVLISFKVNTELKTVNNYFLLSLACADLIIGTFSMNLYTTYLLMGHWALGTLACDLWLALDYVASNASVMNLLLISFDRYFSVTRPLSYRAKRTPRRAALMIGLAWLVSFVLWAPAILFWQYLVGERTVLAGQCYIQFLSQPIITFGTAMAAFYLPVTVMCTLYWRIYRETENRARELAALQGSETPGKGGGSSSSSERSQPGAEGSPETPPGRCCRCCRAPRLLQAYSWKEEEEEDEGSMESLTSSEGEEPGSEVVIKMPMVDPEAQAPTKQPPR... | null | null | adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway [GO:0007197]; chemical synaptic transmission [GO:0007268]; cognition [GO:0050890]; G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; G protein-coupled receptor signaling pathway [GO:0007186]; G protein-coupled... | axon terminus [GO:0043679]; cholinergic synapse [GO:0098981]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynaptic membrane [GO:0042734]; Schaffer collateral - CA1 synapse [GO:0098685]; synapse [GO:0045202... | G protein-coupled acetylcholine receptor activity [GO:0016907]; G protein-coupled serotonin receptor activity [GO:0004993]; phosphatidylinositol phospholipase C activity [GO:0004435] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Muscarinic acetylcholine receptor subfamily, CHRM1 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover. | Homo sapiens (Human) |
P11230 | ACHB_HUMAN | MTPGALLMLLGALGAPLAPGVRGSEAEGRLREKLFSGYDSSVRPAREVGDRVRVSVGLILAQLISLNEKDEEMSTKVYLDLEWTDYRLSWDPAEHDGIDSLRITAESVWLPDVVLLNNNDGNFDVALDISVVVSSDGSVRWQPPGIYRSSCSIQVTYFPFDWQNCTMVFSSYSYDSSEVSLQTGLGPDGQGHQEIHIHEGTFIENGQWEIIHKPSRLIQPPGDPRGGREGQRQEVIFYLIIRRKPLFYLVNVIAPCILITLLAIFVFYLPPDAGEKMGLSIFALLTLTVFLLLLADKVPETSLSVPIIIKYLMFTMVLVT... | null | null | acetylcholine receptor signaling pathway [GO:0095500]; behavioral response to nicotine [GO:0035095]; membrane depolarization [GO:0051899]; monoatomic cation transport [GO:0006812]; muscle cell development [GO:0055001]; muscle contraction [GO:0006936]; nervous system process [GO:0050877]; neuromuscular synaptic transmis... | acetylcholine-gated channel complex [GO:0005892]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic specialization membrane [GO:0099634]; synapse [GO:0045202] | acetylcholine binding [GO:0042166]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; channel activity [GO:0015267]; ligand-gated monoatomic ion channel activity [GO:0015276]; transmembrane signaling receptor activity [GO:0004888]; transmitter-gated monoatomic ion channel activity involved ... | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Beta-1/CHRNB1 sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P04758}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P04758}; | null | null | null | null | FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. {ECO:0000269|PubMed:27375219}. | Homo sapiens (Human) |
P11232 | THIO_RAT | MVKLIESKEAFQEALAAAGDKLVVVDFSATWCGPCKMIKPFFHSLCDKYSNVVFLEVDVDDCQDVAADCEVKCMPTFQFYKKGQKVGEFSGANKEKLEATITEFA | null | null | cell redox homeostasis [GO:0045454]; cellular detoxification of hydrogen peroxide [GO:0061692]; cellular response to antibiotic [GO:0071236]; cellular response to glucose stimulus [GO:0071333]; cellular response to hyperoxia [GO:0071455]; cellular response to xenobiotic stimulus [GO:0071466]; negative regulation of pro... | axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular region [GO:0005576]; neuronal cell body [GO:0043025]; nucleus [GO:0005634] | enzyme binding [GO:0019899]; protein homodimerization activity [GO:0042803]; protein-disulfide reductase (NAD(P)) activity [GO:0047134]; protein-disulfide reductase activity [GO:0015035]; thioredoxin-disulfide reductase (NADP) activity [GO:0004791] | PF00085; | 3.40.30.10; | Thioredoxin family | PTM: In the fully reduced protein, both Cys-69 and Cys-73 are nitrosylated in response to nitric oxide (NO). When two disulfide bonds are present in the protein, only Cys-73 is nitrosylated. Cys-73 can serve as donor for nitrosylation of target proteins (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10599}. Cytoplasm {ECO:0000250|UniProtKB:P10599}. Secreted {ECO:0000250|UniProtKB:P10599}. Note=Translocates from the cytoplasm into the nucleus after phorbol 12-myristate 13-acetate induction (PMA). Predominantly in the cytoplasm in non irradiated cells. Radiation ... | null | null | null | null | null | FUNCTION: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (By similarity). Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the respon... | Rattus norvegicus (Rat) |
P11233 | RALA_HUMAN | MAANKPKGQNSLALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQIDILDTAGQEDYAAIRDNYFRSGEGFLCVFSITEMESFAATADFREQILRVKEDENVPFLLVGNKSDLEDKRQVSVEEAKNRAEQWNVNYVETSAKTRANVDKVFFDLMREIRARKMEDSKEKNGKKKRKSLAKRIRERCCIL | 3.6.5.2 | null | cell cycle [GO:0007049]; cell division [GO:0051301]; chemotaxis [GO:0006935]; establishment of protein localization to mitochondrion [GO:0072655]; exocytosis [GO:0006887]; membrane raft localization [GO:0051665]; neural tube closure [GO:0001843]; positive regulation of epidermal growth factor receptor signaling pathway... | cell surface [GO:0009986]; cleavage furrow [GO:0032154]; cytoplasmic vesicle membrane [GO:0030659]; extracellular exosome [GO:0070062]; Flemming body [GO:0090543]; focal adhesion [GO:0005925]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; Schaffer collateral - CA1 synapse [GO:0098685]; synaptic membrane [GO... | ATPase binding [GO:0051117]; Edg-2 lysophosphatidic acid receptor binding [GO:0031755]; G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; myosin binding [GO:0017022]; ubiquitin protein ligase binding [GO:0031625] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Ras family | PTM: Phosphorylated. Phosphorylation at Ser-194 by AURKA/Aurora kinase A, during mitosis, induces RALA localization to the mitochondrion where it regulates mitochondrial fission. {ECO:0000269|PubMed:21822277}.; PTM: Prenylation is essential for membrane localization. The geranylgeranylated form and the farnesylated mut... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17875936, ECO:0000269|PubMed:18756269, ECO:0000269|PubMed:19306925}; Lipid-anchor {ECO:0000269|PubMed:17875936}; Cytoplasmic side. Cleavage furrow {ECO:0000269|PubMed:18756269}. Midbody, Midbody ring {ECO:0000269|PubMed:16213214}. Mitochondrion {ECO:0000269|PubMed... | 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; EC=3.6.5.2; Evidence={ECO:0000269|PubMed:30500825}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000269|PubM... | null | null | null | null | FUNCTION: Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors (PubMed:18756269, PubMed:19306925, PubMed:2... | Homo sapiens (Human) |
P11234 | RALB_HUMAN | MAANKSKGQSSLALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQIDILDTAGQEDYAAIRDNYFRSGEGFLLVFSITEHESFTATAEFREQILRVKAEEDKIPLLVVGNKSDLEERRQVPVEEARSKAEEWGVQYVETSAKTRANVDKVFFDLMREIRTKKMSENKDKNGKKSSKNKKSFKERCCLL | 3.6.5.2 | null | apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cell division [GO:0051301]; cellular response to exogenous dsRNA [GO:0071360]; cellular response to starvation [GO:0009267]; negative regulation of protein binding [GO:0032091]; positive regulation of autophagosome assembly [GO:2000786]; positive regulation of ep... | extracellular exosome [GO:0070062]; midbody [GO:0030496]; plasma membrane [GO:0005886] | ATPase binding [GO:0051117]; G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; ubiquitin protein ligase binding [GO:0031625] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Ras family | PTM: Prenylation is essential for membrane localization. The geranylgeranylated form and the farnesylated mutant does not undergo alternative prenylation in response to geranylgeranyltransferase I inhibitors (GGTIs) and farnesyltransferase I inhibitors (FTIs). {ECO:0000269|PubMed:17875936}.; PTM: The farnesylated form ... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17875936}; Lipid-anchor {ECO:0000269|PubMed:17875936}; Cytoplasmic side {ECO:0000269|PubMed:17875936}. Midbody {ECO:0000269|PubMed:18756269}. Note=During late cytokinesis, enriched at the midbody. {ECO:0000269|PubMed:18756269}. | 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; EC=3.6.5.2; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking (PubMed:10393179, PubMed:17875936, PubMed:18756269). Accomplishes its multiple functions by interacting with distinct downstream e... | Homo sapiens (Human) |
P11245 | ARY2_HUMAN | MDIEAYFERIGYKNSRNKLDLETLTDILEHQIRAVPFENLNMHCGQAMELGLEAIFDHIVRRNRGGWCLQVNQLLYWALTTIGFQTTMLGGYFYIPPVNKYSTGMVHLLLQVTIDGRNYIVDAGSGSSSQMWQPLELISGKDQPQVPCIFCLTEERGIWYLDQIRREQYITNKEFLNSHLLPKKKHQKIYLFTLEPRTIEDFESMNTYLQTSPTSSFITTSFCSLQTPEGVYCLVGFILTYRKFNYKDNTDLVEFKTLTEEEVEEVLRNIFKISLGRNLVPKPGDGSLTI | 2.3.1.118; 2.3.1.5 | null | xenobiotic metabolic process [GO:0006805] | cytosol [GO:0005829] | arylamine N-acetyltransferase activity [GO:0004060]; N-hydroxyarylamine O-acetyltransferase activity [GO:0046990] | PF00797; | 3.30.2140.20; | Arylamine N-acetyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + an arylamine = an N-acetylarylamine + CoA; Xref=Rhea:RHEA:16613, ChEBI:CHEBI:13790, ChEBI:CHEBI:50471, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.5; Evidence={ECO:0000269|PubMed:12222688, ECO:0000269|PubMed:7915226}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + an N-hydroxyary... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.21 uM for 2-aminofluorene (measured with the enzyme encoded by allele NAT2*4) {ECO:0000269|PubMed:7915226}; KM=15.9 uM for 4-aminobiphenyl (measured with the enzyme encoded by allele NAT2*4) {ECO:0000269|PubMed:7915226}; KM=28.6 uM for 3,2-dimethyl-4-aminobipheny... | null | null | null | FUNCTION: Catalyzes the N- or O-acetylation of various arylamine and heterocyclic amine substrates (PubMed:12222688, PubMed:7915226). Participates in the detoxification of a plethora of hydrazine and arylamine drugs, and is able to bioactivate several known carcinogens. {ECO:0000269|PubMed:12222688, ECO:0000269|PubMed:... | Homo sapiens (Human) |
P11247 | PERM_MOUSE | MKLLLALAGLLAPLAMLQTSNGATPALLGEVENSVVLSCMEEAKQLVDRAYKERRESIKRSLQSGSASPTELLFYFKQPVAGTRTAVRAADYLHVALDLLKRKLQPLWPRPFNVTDVLTPAQLNLLSVSSGCAYQDVRVTCPPNDKYRTITGHCNNRRSPTLGASNRAFVRWLPAEYEDGVSMPFGWTPGVNRNGFKVPLARQVSNAIVRFPNDQLTKDQERALMFMQWGQFLDHDITLTPEPATRFSFFTGLNCETSCLQQPPCFPLKIPPNDPRIKNQKDCIPFFRSCPACTRNNITIRNQINALTSFVDASGVYGSE... | 1.11.2.2 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion per monomer. {ECO:0000250}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per monomer. {ECO:0000250}; | defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; hydrogen peroxide catabolic process [GO:0042744]; hypochlorous acid biosynthetic process [GO:0002149]; low-density lipoprotein particle remodeling [GO:0034374]; removal of superoxide radicals [GO:0019430]; respiratory burst involved in... | azurophil granule [GO:0042582]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; secretory granule [GO:0030141] | heme binding [GO:0020037]; heparin binding [GO:0008201]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601] | PF03098; | 1.10.640.10; | Peroxidase family, XPO subfamily | null | SUBCELLULAR LOCATION: Lysosome. | CATALYTIC ACTIVITY: Reaction=chloride + H(+) + H2O2 = H2O + hypochlorous acid; Xref=Rhea:RHEA:28218, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:17996, ChEBI:CHEBI:24757; EC=1.11.2.2; Evidence={ECO:0000269|PubMed:11593004}; | null | null | null | null | FUNCTION: Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that gre... | Mus musculus (Mouse) |
P11260 | LORF1_MOUSE | MAKGKRKNPTNRNQDHSPSSERSTPTPPSPGHPNTTENLDPDLKTFLMMMIEDIKKDFHKSLKDLQESTAKELQALKEKQENTAKQVMEMNKTILELKGEVDTIKKTQSEATLEIETLGKRSGTIDASISNRIQEMEERISGAEDSIENIDTTVKENTKCKRILTQNIQVIQDTMRRPNLRIIGIDENEDFQLKGPANIFNKIIEENFPNIKKEMPMIIQEAYRTPNRLDQKRNSSRHIIIRTTNALNKDRILKAVREKGQVTYKGRPIRITPDFSPETMKARRAWTDVIQTLREHKCQPRLLYPAKLSITIDGETKVFH... | null | null | retrotransposition [GO:0032197] | cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoplasmic stress granule [GO:0010494]; nucleolus [GO:0005730]; ribonucleoprotein complex [GO:1990904] | nucleotide binding [GO:0000166]; single-stranded RNA binding [GO:0003727] | PF17490;PF02994; | 3.30.250.20;3.30.70.1820;1.20.5.390; | Transposase 22 family | PTM: Polyubiquitinated, probably by UBR2, which induces its degradation. {ECO:0000269|PubMed:28806172}. | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9UN81}. Cytoplasm {ECO:0000269|PubMed:28806172}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q9UN81}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9UN81}. Note=Colocalizes with its encoding RNA in cytoplasmic ribonucleopro... | null | null | null | null | null | FUNCTION: Nucleic acid-binding protein which is essential for retrotransposition of LINE-1 elements in the genome. Functions as a nucleic acid chaperone binding its own transcript and therefore preferentially mobilizing the transcript from which they are encoded. {ECO:0000269|PubMed:11134335, ECO:0000269|PubMed:2880617... | Mus musculus (Mouse) |
P11261 | ENV_FLVLB | MEGPTHPKPSKDKTFSWDLMILVGVLLRLDVGMANPSPHQIYNVTWTITNLVTGTKANATSMLGTLTDAFPTMYFDLCDIIGNTWNPSDQEPFPGYGCDQPMRRWQQRNTPFYVCPGHANRKQCGGPQDGFCAVWGCETTGETYWRPTSSWDYITVKKGVTQGIYQCSGGGWCGPCYDKAVHSSITGASEGGRCNPLILQFTQKGRQTSWDGPKSWGLRLYRSGYDPIALFSVSRQVMTITLPQAMGPNLVLPDQKPPSRQSQIESRVTPHHSQGNGGTPGITLVNASIAPLSTPVTPASPKRIGTGNRLINLVQGTYLA... | 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 th... | 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... | 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).... | Feline leukemia virus (strain B/lambda-B1) |
P11267 | ENV_SIVML | MGCLKNQLLIAILLLSVYGIYCTQYVTVFYGVPAWRNATIPLFCATKNRDTWGTTQCLPDNGDYSELALNVTESFDAWENTVTEQAIEDVWQLFETSIKPCVKLSPLCITMRCNKSETDRWGLTKSSTTITTAAPTSAPVSEKLDMVNETSSCIAQNNCTGLEQEQMISCKFNMTGLKRDKTKEYNETWYSTDLVCEQRNSTDNESRCYMNHCNTSVIQESCDKHYWDTIRFRYCAPPGYALLRCNDTNYSGFMPKCSKVVVSSCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNKYYNLTMKCRRPGNKT... | null | null | membrane fusion involved in viral entry into host cell [GO:0039663]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [... | SUBCELLULAR LOCATION: [Transmembrane protein gp41]: 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}. Host endosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=It is p... | null | null | null | null | null | FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 t... | Simian immunodeficiency virus (isolate K78) (SIV-mac) (Simian immunodeficiency virus rhesus monkey) |
P11268 | ENV_MLVRD | MESTTLSKPFKNQVNPWGPLIVLLILGRVNPVALGNSPHQVFNLSWEVTNEDRETVWAITGNHPLWTWWPDLTPDLCMLALHGPSYWGLEYQAPFSPPPGPPCCSGSSGSTPGCSRDCEEPLTSYTPRCNTAWNRLKLSKVTHAHNEGFYVCPGPHRPRWARSCGGPESFYCASWGCETTGRASWKPSSSWDYITVSNNLTSGQATPVCKNNTWCNSLTIRFTSLGKQATSWVTGHWWGLRLYVSGHDPGLIFGIRLKITDSGPRVPIGPNPVLSDQRPPSQPRSPPHSNSTPTETPLTLPEPPPAGVENRLLNLVKGAY... | 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] | metal ion binding [GO:0046872] | 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 th... | 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... | 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).... | Radiation murine leukemia virus |
P11269 | GAG_MLVRD | MGQTVTTPLSLTLEHWGDVQRIASNQSVEVKKRRRVTFCPAEWPTFDVGWPQDGTFNLDIILQVKSKVFSPGPHGHPDQVPYIVTWEAIAYEPPSWVKPFVSPKLSLSPTAPILPSGPSTQPPPRSALYPALTPSIKPRPSKPQVLSDNGGPLIDLLTEDPPPYGEQGPSSPDGDGDREEATYTSEIPAPSPMVSRLRGKRDPPAADSTTSRAFPLRLGGNGQLQYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLTTHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGNDGRPTQLPNEVNSAFPLERPDWDY... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | RNA binding [GO:0003723]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF01140;PF01141;PF02093;PF00098; | 1.10.150.180;1.10.375.10;4.10.60.10; | null | PTM: [Gag polyprotein]: Ubiquitinated by ITCH. Gag can recruit the ubiquitin ligase Itch in an L domain-independent manner to facilitate virus release via a mechanism that involves Gag ubiquitination. {ECO:0000250|UniProtKB:P03332}.; PTM: [Gag polyprotein]: Specific enzymatic cleavages by the viral protease yield matur... | SUBCELLULAR LOCATION: [Gag polyprotein]: Virion {ECO:0000250|UniProtKB:P03332}. Host cell membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P26807}.; SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000250|UniProt... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interacti... | Radiation murine leukemia virus |
P11274 | BCR_HUMAN | MVDPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNFERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQHGAGSSVGDASRPPYRGRSSESSCGVDGDYEDAELNPRFLKDNLIDANGGSRPPWPPLEYQPYQSIYVGGMMEGEGKGPLLRSQSTSEQEKRLTWPRRSYSPRS... | 2.7.11.1 | null | actin cytoskeleton organization [GO:0030036]; activation of GTPase activity [GO:0090630]; brain development [GO:0007420]; cellular response to lipopolysaccharide [GO:0071222]; definitive hemopoiesis [GO:0060216]; focal adhesion assembly [GO:0048041]; homeostasis of number of cells [GO:0048872]; inner ear morphogenesis ... | axon [GO:0030424]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; protein-containing complex [GO:0032991]; Schaffer collateral - CA1 synapse [GO:0098685] | ATP binding [GO:0005524]; GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713] | PF09036;PF00168;PF19057;PF00620;PF00621; | 4.10.280.30;2.60.40.150;1.20.900.10;2.30.29.30;1.10.555.10; | null | PTM: Autophosphorylated. Phosphorylated by FES/FPS on tyrosine residues, leading to down-regulation of the BCR kinase activity. Phosphorylation at Tyr-177 by HCK is important for interaction with GRB2. {ECO:0000269|PubMed:15302586, ECO:0000269|PubMed:9407116}. | SUBCELLULAR LOCATION: Postsynaptic density {ECO:0000250|UniProtKB:Q6PAJ1}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q6PAJ1}. Cell projection, axon {ECO:0000250|UniProtKB:Q6PAJ1}. Synapse {ECO:0000250|UniProtKB:F1LXF1}. | 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; Evidence={ECO:0000269|PubMed:1657398}; Physiologi... | null | null | null | null | FUNCTION: Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein (GAP) domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-re... | Homo sapiens (Human) |
P11275 | KCC2A_RAT | MATITCTRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLKGAILTTMLATRNFSGGKSGG... | 2.7.11.17 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9UQM7}; | angiotensin-activated signaling pathway [GO:0038166]; calcium ion transport [GO:0006816]; calmodulin dependent kinase signaling pathway [GO:0099004]; cellular response to interferon-beta [GO:0035458]; cellular response to type II interferon [GO:0071346]; dendrite morphogenesis [GO:0048813]; dendritic spine development ... | axon [GO:0030424]; calcium- and calmodulin-dependent protein kinase complex [GO:0005954]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendrite cytoplasm [GO:0032839]; dendritic spine [GO:0043197]; glutamatergic postsynaptic density [GO:0099573]; glutamatergic synapse [GO:0098978]; mitochondrion... | ATP binding [GO:0005524]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; glutamate receptor binding [GO:0035254]; GTPase activating protein binding [GO:0032794]; identical protein binding [GO:0042802]; ... | PF08332;PF00069; | 3.10.450.50;6.10.140.620;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily | PTM: Autophosphorylation of Thr-286 following activation by Ca(2+)/calmodulin. Phosphorylation of Thr-286 locks the kinase into an activated state. {ECO:0000250|UniProtKB:Q9UQM7}.; PTM: Palmitoylated (PubMed:23687301). Probably palmitoylated by ZDHHC3 and ZDHHC7 (PubMed:23687301). {ECO:0000269|PubMed:23687301}. | SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:15659234}. Postsynaptic density {ECO:0000269|PubMed:15659234}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q9UQM7}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9UQM7}. Note=Postsynaptic lipid rafts. {ECO:0000269|PubMed:15659234}. | 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=2.7.11.17; Evidence={ECO:0000269|PubMed:11972023}; CATALYTI... | null | null | null | null | FUNCTION: Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in various processes, such as synaptic plasticity, neurotransmitter release and long-term potentiation. Member of the NMDAR signaling complex in excitatory synapses,... | Rattus norvegicus (Rat) |
P11276 | FINC_MOUSE | MLRGPGPGRLLLLAVLCLGTSVRCTEAGKSKRQAQQIVQPQSPVAVSQSKPGCFDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEPEETCFDKYTGNTYKVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDKWRRPHETGGYMLECLCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGNGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCVCTGNGRGEWKCERHALQSASAGSGSFTDVRTAIYQPQTHPQPAPYGHCVTDSGVVYSVGM... | null | null | acute-phase response [GO:0006953]; angiogenesis [GO:0001525]; biological process involved in interaction with symbiont [GO:0051702]; calcium-independent cell-matrix adhesion [GO:0007161]; cell adhesion [GO:0007155]; cell-matrix adhesion [GO:0007160]; cell-substrate junction assembly [GO:0007044]; cellular response to i... | apical plasma membrane [GO:0016324]; basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; fibrinogen complex [GO:0... | extracellular matrix structural constituent [GO:0005201]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; mercury ion binding [GO:0045340]; peptidase activator activity [GO:0016504]; protease binding [GO:0002020]; proteoglycan binding [GO:0043394]; signaling receptor... | PF00039;PF00040;PF00041; | 2.10.70.10;2.10.10.10;2.60.40.10; | null | PTM: Sulfated. {ECO:0000250|UniProtKB:P02751}.; PTM: Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers). {ECO:0000... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:36812915}. | null | null | null | null | null | FUNCTION: Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin (By similarity). Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape healing, and maintenance of cell shape (By similarity). Involved in o... | Mus musculus (Mouse) |
P11277 | SPTB1_HUMAN | MTSATEFENVGNQPPYSRINARWDAPDDELDNDNSSARLFERSRIKALADEREVVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILRFQIQDIVVQTQEGRETRSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDPEDVFTENPDEKSIITYVVAFYHYFSKMKVLAVEGKRVGKVIDHAIETEKMIEKYSGLASDLLTWIEQ... | null | null | actin cytoskeleton organization [GO:0030036]; actin filament capping [GO:0051693]; modification of postsynaptic actin cytoskeleton [GO:0098885] | actin cytoskeleton [GO:0015629]; cell junction [GO:0030054]; cell projection [GO:0042995]; cell surface [GO:0009986]; cortical actin cytoskeleton [GO:0030864]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; postsynapse [GO:009879... | actin binding [GO:0003779]; actin filament binding [GO:0051015]; ankyrin binding [GO:0030506]; structural constituent of cytoskeleton [GO:0005200] | PF00307;PF00435; | 1.20.58.60;1.10.418.10; | Spectrin family | PTM: The first phosphorylation event occurs on Ser-2114, followed by Ser-2125, Ser-2123, Ser-2128, Ser-2117, and Thr-2110. {ECO:0000269|PubMed:15065869}.; PTM: (Microbial infection) Probably cleaved by P.falciparum SERA6; the cleavage results in SPTB solubilization causing the disruption of the actin cytoskeleton and t... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. | null | null | null | null | null | FUNCTION: Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. | Homo sapiens (Human) |
P11279 | LAMP1_HUMAN | MAAPGSARRPLLLLLLLLLLGLMHCASAAMFMVKNGNGTACIMANFSAAFSVNYDTKSGPKNMTFDLPSDATVVLNRSSCGKENTSDPSLVIAFGRGHTLTLNFTRNATRYSVQLMSFVYNLSDTHLFPNASSKEIKTVESITDIRADIDKKYRCVSGTQVHMNNVTVTLHDATIQAYLSNSSFSRGETRCEQDRPSPTTAPPAPPSPSPSPVPKSPSVDKYNVSGTNGTCLLASMGLQLNLTYERKDNTTVTRLLNINPNKTSASGSCGAHLVTLELHSEGTTVLLFQFGMNASSSRFFLQGIQLNTILPDARDPAFKA... | null | null | establishment of protein localization to organelle [GO:0072594]; Golgi to lysosome transport [GO:0090160]; granzyme-mediated programmed cell death signaling pathway [GO:0140507]; lysosomal lumen acidification [GO:0007042]; positive regulation of natural killer cell degranulation [GO:0043323]; positive regulation of nat... | autolysosome [GO:0044754]; autophagosome membrane [GO:0000421]; azurophil granule membrane [GO:0035577]; cytolytic granule membrane [GO:0101004]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; ficolin-1-ric... | enzyme binding [GO:0019899]; ion channel inhibitor activity [GO:0008200]; protein domain specific binding [GO:0019904]; virus receptor activity [GO:0001618] | PF01299;PF21222; | 2.40.160.110; | LAMP family | PTM: O- and N-glycosylated; some of the 18 N-linked glycans are polylactosaminoglycans. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:8323299}.; PTM: (Microbial infection) The glycosylation of Asn-76 is essential for Lassa virus entry into cells. {ECO:0000269... | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:16176980, ECO:0000269|PubMed:17897319}; Single-pass type I membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:16176980}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:16176980}; Single-pass typ... | null | null | null | null | null | FUNCTION: Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, lysosomal pH regulation, autophagy and cholesterol homeostasis (PubMed:37390818). Acts as an important regulator of lysosomal lumen pH regulation by acting as a direct inhibitor of the proton channel TMEM175, facilitating ly... | Homo sapiens (Human) |
P11280 | COLI_NEOVI | SEPGRREGKRSYSMEHFRWGKPVGKKRRPVKVYPNGAEDESAEAFPLEFKRELAGERPEPALGPEGAAEGMAALADLEYGLVAKAEVAEKKDDGPYKMEHFRWGSPGKDKRYGGFMTSEKSQTPLVTLFKNAIIKNAHKKGQ | 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;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 ... | Neovison vison (American mink) (Mustela vison) |
P11283 | POL_MMTVC | MGVSGSKGQKLFVSVLQRLLSERGLHVKESSAIEFYQFLIKVSPWFPEEGGLNLQDWKRVGREMKKYAAEHGTDSIPKQAYPIWLQLREILTEQSDLVLLSAEAKSVTEEELEEGLTGLLSASSQEKTYGTRGTAYAEIDTEVDKLSEHIYDEPYEEKEKADKNEEKDHVRKVKKIVQRKENSEHKRKEKDQKAFLATDWNNDDLSPEDWDDLEEQAAHYHDDDELILPVKRKVDKKKPLALRRKPLPPVGFAGAMAEAREKGDLTFTFPVVFMGESDDDDTPVWEPLPLKTLKELQSAVRTMGPSAPYTLQVVDMVASQ... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.-; 3.6.1.23 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; Note=The RT polymerase active site binds 2 magnesium ions. {ECO:0000255|PROSITE-ProRule:PRU00405}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Magnesium ions are required for NC-dUTPase activity. {ECO:0000305|PubMed:... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; viral genome integration into host DNA [GO:0044826] | viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; dUTP diphosphatase activity [GO:0004170]; nucleotide binding [GO:0000166]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease ac... | PF00692;PF02337;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06817;PF00098;PF14787; | 1.10.10.200;1.10.1200.30;2.70.40.10;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;2.30.30.10;1.10.150.490;3.30.420.10;4.10.60.10; | null | PTM: [Protease]: Released by autocatalytic processing. {ECO:0000250|UniProtKB:P03365}.; PTM: [Gag-Pro-Pol polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000269|PubMed:2542570}.; PTM: [Gag-Pro-Pol polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transpor... | SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000250|UniProtKB:P10258}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000250|UniProtKB:P10258}.; SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion {ECO:0000250|UniProtKB:P10258}. | 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=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=... | null | null | null | null | FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.; FUNCTION: Nucleocapsid protein p14: Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs. {ECO:0000305}.; FUNCTION: [Capsid protein p27]: Capsid protein.... | Mouse mammary tumor virus (strain C3H) (MMTV) |
P11284 | GAG_MMTVC | MGVSGSKGQKLFVSVLQRLLSERGLHVKESSAIEFYQFLIKVSPWFPEEGGLNLQDWKRVGREMKKYAAEHGTDSIPKQAYPIWLQLREILTEQSDLVLLSAEAKSVTEEELEEGLTGLLSASSQEKTYGTRGTAYAEIDTEVDKLSEHIYDEPYEEKEKADKNEEKDHVRKVKKIVQRKENSEHKRKEKDQKAFLATDWNNDDLSPEDWDDLEEQAAHYHDDDELILPVKRKVDKKKPLALRRKPLPPVGFAGAMAEAREKGDLTFTFPVVFMGESDDDDTPVWEPLPLKTLKELQSAVRTMGPSAPYTLQVVDMVASQ... | null | null | viral budding via host ESCRT complex [GO:0039702] | viral nucleocapsid [GO:0019013] | DNA binding [GO:0003677]; nucleotide binding [GO:0000166]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF02337;PF00607;PF19317;PF00098;PF14787; | 1.10.1200.30;1.10.375.10;1.10.150.490;4.10.60.10; | null | PTM: [Gag polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral particles. {ECO:0000269|PubMed:2542570}.; PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield mature... | SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000250|UniProtKB:P10258}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000250|UniProtKB:P10258}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion {ECO:0000250|UniProtKB:P10258}. | null | null | null | null | null | FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.; FUNCTION: [Nucleocapsid protein p14]: Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs. {ECO:0000305}.; FUNCTION: [Capsid protein p27]: Capsid protei... | Mouse mammary tumor virus (strain C3H) (MMTV) |
P11308 | ERG_HUMAN | MASTIKEALSVVSEDQSLFECAYGTPHLAKTEMTASSSSDYGQTSKMSPRVPQQDWLSQPPARVTIKMECNPSQVNGSRNSPDECSVAKGGKMVGSPDTVGMNYGSYMEEKHMPPPNMTTNERRVIVPADPTLWSTDHVRQWLEWAVKEYGLPDVNILLFQNIDGKELCKMTKDDFQRLTPSYNADILLSHLHYLRETPLPHLTSDDVDKALQNSPRLMHARNTGGAAFIFPNTSVYPEATQRITTRPDLPYEPPRRSAWTGHGHPTPQSKAAQPSPSTVPKTEDQRPQLDPYQILGPTSSRLANPGSGQIQLWQFLLEL... | null | null | cell differentiation [GO:0030154]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein phosphorylation [GO:0006468]; regulation of transcription by RNA polymerase II [GO:0006357]; signal transduction [GO:0007165] | chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904] | chromatin binding [GO:0003682]; 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]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequenc... | PF00178;PF02198; | 1.10.150.50;1.10.10.10; | ETS family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237, ECO:0000269|PubMed:17289661}. Cytoplasm {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. | null | null | null | null | null | FUNCTION: Transcriptional regulator. May participate in transcriptional regulation through the recruitment of SETDB1 histone methyltransferase and subsequent modification of local chromatin structure. | Homo sapiens (Human) |
P11309 | PIM1_HUMAN | MLLSKINSLAHLRAAPCNDLHATKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLALRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLHSLSPGPSK | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15525646, ECO:0000269|PubMed:15657054, ECO:0000269|PubMed:15808862}; | apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cellular detoxification [GO:1990748]; cellular response to type II interferon [GO:0071346]; negative regulation of apoptotic process [GO:0043066]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of innate immune ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; manganese ion binding [GO:0030145]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activator activity [GO:0043539]; protein serine/threonine kinase activity [GO:0004674]; ribosomal small subunit binding [GO:0043024]; transcription factor binding [GO:0008134] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, PIM subfamily | PTM: Autophosphorylated on both serine/threonine and tyrosine residues. Phosphorylated. Interaction with PPP2CA promotes dephosphorylation. {ECO:0000269|PubMed:12473674}.; PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000269|PubMed:12473674, ECO:0000269|PubMed:15798097}. | SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane. | 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; Evidence={ECO:0000269|PubMed:15525646, ECO:000026... | null | null | null | null | FUNCTION: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis (PubMed:15528381, PubMed:1825810, PubMed:31548394). Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulat... | Homo sapiens (Human) |
P11310 | ACADM_HUMAN | MAAGFGRCCRVLRSISRFHWRSQHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAIS... | 1.3.8.7 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23}; | cardiac muscle cell differentiation [GO:0055007]; carnitine biosynthetic process [GO:0045329]; carnitine metabolic process, CoA-linked [GO:0019254]; fatty acid beta-oxidation [GO:0006635]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; glycogen biosynthetic process [GO:0005978]; liver development ... | axon [GO:0030424]; cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | acyl-CoA dehydrogenase activity [GO:0003995]; flavin adenine dinucleotide binding [GO:0050660]; identical protein binding [GO:0042802]; medium-chain fatty acyl-CoA dehydrogenase activity [GO:0070991] | PF00441;PF02770;PF02771; | 1.10.540.10;2.40.110.10;1.20.140.10; | Acyl-CoA dehydrogenase family | PTM: Acetylated. Could occur at proximity of the cofactor-binding sites and reduce the catalytic activity. Could be deacetylated by SIRT3. {ECO:0000269|PubMed:24121500}. | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:16020546}. | CATALYTIC ACTIVITY: Reaction=a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:14477, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:5830... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=175 uM for butyryl-CoA {ECO:0000269|PubMed:8823175}; KM=15 uM for hexanoyl-CoA {ECO:0000269|PubMed:8823175}; KM=3.4 uM for octanoyl-CoA {ECO:0000269|PubMed:8823175}; KM=2.5 uM for decanoyl-CoA {ECO:0000269|PubMed:8823175}; KM=2.5 uM for dodecanoyl-CoA {ECO:0000269|... | PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation. {ECO:0000269|PubMed:2251268}. | null | null | FUNCTION: Medium-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (PubMed:1970566, PubMed:21237683, PubMed:2251... | Homo sapiens (Human) |
P11325 | SYLM_YEAST | MLSRPSSRFLSTKRGPGPAVKKLIAIGEKWKQKTTRGLPKQDTLNSGSKYILCQFPYPSGALHIGHLRVYVISDSLNRFYKQKGYNVIHPMGWDAFGLPAENAAIERSINPAIWTRDNIAKMKQQMQSMLANFDWDREITTCDPEYYKFTQWIFLKLFENGLAYRKEAEINWDPVDMTVLANEQVDAQGRSWRSGAIVEKKQLKQWFLGITKFAPKLKKHLNQLKDWPSNVKQMQKNWIGESVGAELVFKVADPKFENLIVFTTRPETLFAVQYVALALDHPIVQKYCEEMPDLKEFIQKSDQLPNDTKEGFQLPNIKAV... | 6.1.1.4 | null | Group I intron splicing [GO:0000372]; leucyl-tRNA aminoacylation [GO:0006429]; mitochondrial translation [GO:0032543]; mRNA processing [GO:0006397] | cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | aminoacyl-tRNA editing activity [GO:0002161]; ATP binding [GO:0005524]; leucine-tRNA ligase activity [GO:0004823]; pre-mRNA intronic binding [GO:0097157] | PF00133;PF13603; | 3.40.50.620; | Class-I aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:1990003}. | CATALYTIC ACTIVITY: Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427, ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4; Evidence={ECO:0000269|PubMed:1... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.1 uM for leucine {ECO:0000269|PubMed:1990003}; KM=1.02 uM for tRNA {ECO:0000269|PubMed:1990003}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-9.5. {ECO:0000269|PubMed:1990003}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:1990003}; | FUNCTION: Catalyzes the attachment of leucine to tRNA(Leu) in the mitochondrion. {ECO:0000269|PubMed:1990003}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11344 | TYRO_MOUSE | MFLAVLYCLLWSFQISDGHFPRACASSKNLLAKECCPPWMGDGSPCGQLSGRGSCQDILLSSAPSGPQFPFKGVDDRESWPSVFYNRTCQCSGNFMGFNCGNCKFGFGGPNCTEKRVLIRRNIFDLSVSEKNKFFSYLTLAKHTISSVYVIPTGTYGQMNNGSTPMFNDINIYDLFVWMHYYVSRDTLLGGSEIWRDIDFAHEAPGFLPWHRLFLLLWEQEIRELTGDENFTVPYWDWRDAENCDICTDEYLGGRHPENPNLLSPASFFSSWQIICSRSEEYNSHQVLCDGTPEGPLLRNPGNHDKAKTPRLPSSADVEF... | 1.14.18.1 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:Q9ZP19}; Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q9ZP19}; | cell population proliferation [GO:0008283]; melanin biosynthetic process [GO:0042438]; pigmentation [GO:0043473]; response to blue light [GO:0009637]; response to cAMP [GO:0051591]; response to UV [GO:0009411]; response to vitamin D [GO:0033280]; thymus development [GO:0048538] | melanosome [GO:0042470]; melanosome membrane [GO:0033162]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471] | copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; tyrosinase activity [GO:0004503] | PF00264; | 1.10.1280.10; | Tyrosinase family | PTM: Glycosylated. {ECO:0000269|PubMed:1537333}. | SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000250|UniProtKB:P14679}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P14679}. Melanosome {ECO:0000269|PubMed:26620560}. Note=Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38. {ECO:0000269|PubMed:26620560}. | CATALYTIC ACTIVITY: Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; Xref=Rhea:RHEA:34287, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504, ChEBI:CHEBI:57924; EC=1.14.18.1; Evidence={ECO:0000269|PubMed:1537333}; CATALYTIC ACTIVITY: Reaction=L-tyrosine + O2 = H2O + L-dopaquinone; Xref=Rhea:RHEA:18117, ChEBI:CHE... | null | null | null | null | FUNCTION: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds (PubMed:2517217). Catalyzes the initial and rate limiting step in the cascade of reactions leading to melanin production from tyrosine (PubMed:1537333, PubMed:2517217, PubMed:35469... | Mus musculus (Mouse) |
P11345 | RAF1_RAT | MEHIQGAWKTISNGFGLKDAVFDGSSCISPTIVQQFGYQRRASDDGKLTDSSKTSNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLQEHKGKKARLDWNTDAASLIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDWSNIRQLLLFPNSTASDSGVPAPPSFTMRRMRESVSRMPASSQHRYSTPHAFTFNTSSPSSEGSLSQRQRSTSTPNVHMVSTTLPVDSRMIEDAIRSHSESASPSALSSSPNNLSPTGWSQPKTPVPAQRERAP... | 2.7.11.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; | cell differentiation [GO:0030154]; death-inducing signaling complex assembly [GO:0071550]; ERBB2-ERBB3 signaling pathway [GO:0038133]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; face development [GO:0060324]; heart development [GO:0007507]; insulin receptor signaling pathway [GO:0008... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143] | adenylate cyclase activator activity [GO:0010856]; adenylate cyclase binding [GO:0008179]; ATP binding [GO:0005524]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; mitogen-activated protein kinase kinase binding [GO:00... | PF00130;PF00069;PF02196; | 3.30.60.20;1.10.510.10; | Protein kinase superfamily, TKL Ser/Thr protein kinase family, RAF subfamily | PTM: Phosphorylation at Thr-269, Ser-338, Tyr-341, Thr-491 and Ser-494 results in its activation. Phosphorylation at Ser-29, Ser-43, Ser-289, Ser-296, Ser-301 and Ser-642 by MAPK1/ERK2 results in its inactivation. Phosphorylation at Ser-259 induces the interaction with YWHAZ and inactivates kinase activity. Dephosphory... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with RGS14 and BRAF in both the cytoplasm and membranes. Phosphorylation at Ser-259 impairs its membrane accumulation. Recruited to the cell membrane by the active Ras protein... | 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; Evidence={ECO:0000250|UniProtKB:P04049}; Physiolo... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformatio... | Rattus norvegicus (Rat) |
P11346 | KRAF1_DROME | MSSESSTEGDSDLYDPLAEELHNVQLVKHVTRENIDALNAKFANLQEPPAMYLIEYQELTSKLHELEAKEQELMERLNSQDQQEDSSLVERFKEQPHYQNQTQILQQQRQLARVHHGNDLTDSLGSQPGSQCGTLTRQPKILLRAHLPNQQRTSVEVISGVRLCDALMKALKLRQLTPDMCEVSTTHSGRHIIPWHTDIGTLHVEEIFVRLLDKFPIRTHIKHQIIRKTFFSLVFCEGCRRLLFTGFYCSQCNFRFHQRCANRVPMLCQPFPMDSYYQLLLAENPDNGVGFPGRGTAVRFNMSSRSRSRRCSSSGSSSSS... | 2.7.11.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; | border follicle cell migration [GO:0007298]; cellular response to starvation [GO:0009267]; compound eye photoreceptor development [GO:0042051]; dorsal appendage formation [GO:0046843]; dorsal/ventral axis specification, ovarian follicular epithelium [GO:0008069]; epidermal growth factor receptor signaling pathway [GO:0... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; kinase binding [GO:0019900]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00130;PF07714;PF02196; | 3.30.60.20;1.10.510.10; | Protein kinase superfamily, TKL Ser/Thr protein kinase family, RAF subfamily | PTM: Extensively phosphorylated 1 to 2 hours after egg laying. {ECO:0000269|PubMed:18327897, ECO:0000269|PubMed:8423783}. | 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; Evidence={ECO:0000250|UniProtKB:P15056}; CATALYTI... | null | null | null | null | FUNCTION: Serine/threonine kinase required in the early embryo for the formation of terminal structure (PubMed:3135183, PubMed:8423783). Also required during the proliferation of imaginal cells (PubMed:3135183). May act downstream of Ras85D in the tor signal transduction pathway (PubMed:8423783). During larval developm... | Drosophila melanogaster (Fruit fly) |
P11348 | DHPR_RAT | MAASGEARRVLVYGGRGALGSRCVQAFRARNWWVASIDVVENEEASASVIVKMTDSFTEQADQVTAEVGKLLGDQKVDAILCVAGGWAGGNAKSKSLFKNCDLMWKQSIWTSTISSHLATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGKNSGMPSGAAAIAVLPVTLDTPMNRKSMPEADFSSWTPLEFLVETFHDWITGNKRPNSGSLIQVVTTDGKTELTPAYF | 1.5.1.34 | null | cellular response to xenobiotic stimulus [GO:0071466]; L-phenylalanine catabolic process [GO:0006559]; liver development [GO:0001889]; response to aluminum ion [GO:0010044]; response to glucagon [GO:0033762]; response to lead ion [GO:0010288]; tetrahydrobiopterin biosynthetic process [GO:0006729] | cytoplasm [GO:0005737] | 6,7-dihydropteridine reductase activity [GO:0004155]; identical protein binding [GO:0042802]; NADH binding [GO:0070404]; NADPH binding [GO:0070402] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=5,6,7,8-tetrahydropteridine + NAD(+) = 6,7-dihydropteridine + H(+) + NADH; Xref=Rhea:RHEA:17869, ChEBI:CHEBI:15378, ChEBI:CHEBI:28889, ChEBI:CHEBI:30156, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.5.1.34; Evidence={ECO:0000269|PubMed:1898002}; PhysiologicalDirection=right-to-left; Xref=Rhea... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 uM for NADH {ECO:0000269|PubMed:1898002}; Note=kcat is 156 sec(-1) for NADH. {ECO:0000269|PubMed:1898002}; | null | null | null | FUNCTION: Catalyzes the conversion of quinonoid dihydrobiopterin into tetrahydrobiopterin. {ECO:0000269|PubMed:1898002}. | Rattus norvegicus (Rat) |
P11349 | NARH_ECOLI | MKIRSQVGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGQGFPTDWENQEKYKGGWIRKINGKLQPRMGNRAMLLGKIFANPHLPGIDDYYEPFDFDYQNLHTAPEGSKSQPIARPRSLITGERMAKIEKGPNWEDDLGGEFDKLAKDKNFDNIQKAMYSQFENTFMMYLPRLCEHCLNPACVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGKSEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADAIERAASTENEKDLYQRQLDVFLDPNDPKVIEQAIKDGIPLS... | 1.7.5.1 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:12910261, ECO:0000269|PubMed:14725769}; Note=Binds 3 [4Fe-4S] clusters per subunit. {ECO:0000269|PubMed:12910261, ECO:0000269|PubMed:14725769}; COFACTOR: Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000269|PubMed:1291... | anaerobic electron transport chain [GO:0019645]; anaerobic respiration [GO:0009061]; nitrate assimilation [GO:0042128]; nitrate metabolic process [GO:0042126] | membrane [GO:0016020]; NarGHI complex [GO:0044799] | 3 iron, 4 sulfur cluster binding [GO:0051538]; 4 iron, 4 sulfur cluster binding [GO:0051539]; electron transfer activity [GO:0009055]; metal ion binding [GO:0046872]; nitrate reductase activity [GO:0008940] | PF13247;PF14711; | 3.30.70.20;1.10.3650.10; | null | null | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=a quinol + nitrate = a quinone + H2O + nitrite; Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.7.5.1; | null | null | null | null | FUNCTION: The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum co... | Escherichia coli (strain K12) |
P11350 | NARI_ECOLI | MQFLNMFFFDIYPYIAGAVFLIGSWLRYDYGQYTWRAASSQMLDRKGMNLASNLFHIGILGIFVGHFFGMLTPHWMYEAWLPIEVKQKMAMFAGGASGVLCLIGGVLLLKRRLFSPRVRATTTGADILILSLLVIQCALGLLTIPFSAQHMDGSEMMKLVGWAQSVVTFHGGASQHLDGVAFIFRLHLVLGMTLFLLFPFSRLIHIWSVPVEYLTRKYQLVRARH | 1.7.5.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:12910261}; Note=Binds 2 heme groups per subunit. Heme 1, called the proximal or heme Bp in PubMed:12910261, is located at the cytoplasmic interface, heme 2, called the distal or heme Bd, is located at the periplasmic interface. Electrons are tran... | anaerobic electron transport chain [GO:0019645]; anaerobic respiration [GO:0009061]; nitrate assimilation [GO:0042128]; nitrate metabolic process [GO:0042126] | membrane [GO:0016020]; NarGHI complex [GO:0044799]; nitrate reductase complex [GO:0009325]; plasma membrane [GO:0005886] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; nitrate reductase activity [GO:0008940] | PF02665; | 1.20.950.20; | null | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000305|PubMed:15919996}. | CATALYTIC ACTIVITY: Reaction=a quinol + nitrate = a quinone + H2O + nitrite; Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.7.5.1; | null | null | null | null | FUNCTION: The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit. | Escherichia coli (strain K12) |
P11352 | GPX1_MOUSE | MCAARLSAAAQSTVYAFSARPLTGGEPVSLGSLRGKVLLIENVASLUGTTIRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEILNSLKYVRPGGGFEPNFTLFEKCEVNGEKAHPLFTFLRNALPTPSDDPTALMTDPKYIIWSPVCRNDIAWNFEKFLVGPDGVPVRRYSRRFRTIDIEPDIETLLSQQSGNS | 1.11.1.12; 1.11.1.9 | null | angiogenesis involved in wound healing [GO:0060055]; apoptotic process [GO:0006915]; arachidonic acid metabolic process [GO:0019369]; biological process involved in interaction with symbiont [GO:0051702]; blood vessel endothelial cell migration [GO:0043534]; cell redox homeostasis [GO:0045454]; cellular response to glu... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; Lewy body [GO:0097413]; mitochondrion [GO:0005739] | glutathione peroxidase activity [GO:0004602]; peroxidase activity [GO:0004601]; phospholipid-hydroperoxide glutathione peroxidase activity [GO:0047066]; SH3 domain binding [GO:0017124] | PF00255; | 3.40.30.10; | Glutathione peroxidase family | PTM: During periods of oxidative stress, Sec-47 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine. {ECO:0000269|PubMed:21420488}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10754271, ECO:0000269|PubMed:9126277}. Mitochondrion {ECO:0000269|PubMed:10754271, ECO:0000269|PubMed:9126277}. | CATALYTIC ACTIVITY: Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O; Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9; Evidence={ECO:0000269|PubMed:10754271, ECO:0000269|PubMed:21420488, ECO:0000269|PubMed:36608588, ECO:0000269|PubMed:9126277, E... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14 uM for H(2)O(2) (at 25 degrees Celsius, in 0.1 M phosphate buffer, pH 7.0) {ECO:0000269|PubMed:21420488}; KM=29 uM for tert-butylperoxide (at 25 degrees Celsius, in 0.1 M phosphate buffer, pH 7.0) {ECO:0000269|PubMed:21420488}; Vmax=319 mM/min/mg enzyme toward H... | null | null | null | FUNCTION: Catalyzes the reduction of hydroperoxides in a glutathione-dependent manner thus regulating cellular redox homeostasis (PubMed:10754271, PubMed:21420488, PubMed:36608588, PubMed:9126277, PubMed:9195979, PubMed:9712879). Can reduce small soluble hydroperoxides such as H2O2, cumene hydroperoxide and tert-butyl ... | Mus musculus (Mouse) |
P11353 | HEM6_YEAST | MPAPQDPRNLPIRQQMEALIRRKQAEITQGLESIDTVKFHADTWTRGNDGGGGTSMVIQDGTTFEKGGVNVSVVYGQLSPAAVSAMKADHKNLRLPEDPKTGLPVTDGVKFFACGLSMVIHPVNPHAPTTHLNYRYFETWNQDGTPQTWWFGGGADLTPSYLYEEDGQLFHQLHKDALDKHDTALYPRFKKWCDEYFYITHRKETRGIGGIFFDDYDERDPQEILKMVEDCFDAFLPSYLTIVKRRKDMPYTKEEQQWQAIRRGRYVEFNLIYDRGTQFGLRTPGSRVESILMSLPEHASWLYNHHPAPGSREAKLLEVT... | 1.3.3.3 | null | heme biosynthetic process [GO:0006783]; protoporphyrinogen IX biosynthetic process [GO:0006782] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | coproporphyrinogen oxidase activity [GO:0004109]; protein homodimerization activity [GO:0042803] | PF01218; | 3.40.1500.10; | Aerobic coproporphyrinogen-III oxidase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:3516695}. | CATALYTIC ACTIVITY: Reaction=coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX; Xref=Rhea:RHEA:18257, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:57307, ChEBI:CHEBI:57309; EC=1.3.3.3; Evidence={ECO:0000269|PubMed:3516695}; PhysiologicalDirection=lef... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.05 uM for coproporphyrinogen {ECO:0000269|PubMed:3516695}; | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1. {ECO:0000305|PubMed:3516695}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.6. {ECO:0000269|PubMed:3516695}; | null | FUNCTION: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX. {ECO:0000269|PubMed:3516695}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11362 | FGFR1_HUMAN | MWSWKCLLFWAVLVTATLCTARPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQDSVPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTD... | 2.7.10.1 | null | angiogenesis [GO:0001525]; auditory receptor cell development [GO:0060117]; branching involved in salivary gland morphogenesis [GO:0060445]; calcium ion homeostasis [GO:0055074]; cardiac muscle cell proliferation [GO:0060038]; cell maturation [GO:0048469]; cell migration [GO:0016477]; cell projection assembly [GO:00300... | cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; extracellular region [GO:0005576]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; fibroblast growth factor binding [GO:0017134]; fibroblast growth factor receptor activity [GO:0005007]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; protein tyrosine kinase activity [GO:0004713]; receptor-receptor interac... | PF07679;PF00047;PF07714; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Fibroblast growth factor receptor subfamily | PTM: Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer and proceeds in a highly ordered manner. Initi... | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Nucleus. Cytoplasm, cytosol. Cytoplasmic vesicle. Note=After ligand binding, both receptor and ligand are rapidly internalized. Can translocate to the nucleus after internalization, or by translocation from the endoplasmic reticulum or Golgi appa... | 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:PRU100... | null | null | null | null | FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and correct axial organization during embryonic developm... | Homo sapiens (Human) |
P11373 | CUTI1_COLGL | MKFLSVLSLAITLAAAAPVEVETGVALETRQSSTRNELETGSSSACPKVIYIFARASTEPGNMGISAGPIVADALERIYGANNVWVQGVGGPYLADLASNFLPDGTSSAAINEARRLFTLANTKCPNAAIVSGGYSQGTAVMAGSISGLSTTIKNQIKGVVLFGYTKNLQNLGRIPNFETSKTEVYCDIADAVCYGTLFILPAHFLYQTDAAVAAPRFLQARIG | 3.1.1.74 | null | null | extracellular region [GO:0005576] | cutinase activity [GO:0050525] | PF01083; | 3.40.50.1820; | Cutinase family | PTM: The 2 disulfide bonds play a critical role in holding the catalytic residues in juxta-position; reduction of the disulfide bridges results in the complete inactivation of the enzyme. {ECO:0000305|Ref.1}.; PTM: The N-terminus is blocked. {ECO:0000269|PubMed:17043825}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17043825}. | CATALYTIC ACTIVITY: Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109, ECO:0000305|PubMed:17043825}; | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:17043825). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:17043825). Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initi... | Colletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata) |
P11378 | STP2_MOUSE | MDTKMQSLPTTHPHPHSSSRPQSHTSNQCNQCTCSHHCRSCSQAGHAGSSSSPSPGPPMKHPKPSVHSRHSPARPSHRGSCPKNRKTFEGKVSKRKAVRRRKRTHRAKRRSSGRRYK | null | null | acrosome reaction [GO:0007340]; binding of sperm to zona pellucida [GO:0007339]; flagellated sperm motility [GO:0030317]; penetration of zona pellucida [GO:0007341]; positive regulation of protein processing [GO:0010954]; sperm DNA condensation [GO:0035092]; spermatogenesis [GO:0007283] | male germ cell nucleus [GO:0001673]; nucleosome [GO:0000786]; nucleus [GO:0005634] | DNA binding [GO:0003677]; zinc ion binding [GO:0008270] | PF01254; | null | Nuclear transition protein 2 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15163613}. Chromosome {ECO:0000269|PubMed:28366643}. Note=Loaded onto the nucleosomes of condensing spermatids (PubMed:28366643). Inclusion of the H2AB1-H2BC1/TH2B dimer into chromatin opens the nucleosomes, releasing the nucleosomal DNA ends and allowing the invasion o... | null | null | null | null | null | FUNCTION: Plays a key role in the replacement of histones to protamine in the elongating spermatids of mammals (PubMed:15083521, PubMed:15163613, PubMed:15189834, PubMed:28366643). In condensing spermatids, loaded onto the nucleosomes, where it promotes the recruitment and processing of protamines, which are responsibl... | Mus musculus (Mouse) |
P11383 | RBL_WHEAT | MSPQTETKAGVGFKAGVKDYKLTYYTPEYETKDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVAGEDSQWICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTTLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRM... | 4.1.1.39 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.; | 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 between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover. {ECO:0000269|PubMed:1733975}. | 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-phosphoglyce... | 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 (PubMed:2928307). Both reactions occur simultaneously and in competition at the same ... | Triticum aestivum (Wheat) |
P11384 | SECR_RAT | MEPLLPTPPLLLLLLLLLSSSFVLPAPPRTPRHSDGTFTSELSRLQDSARLQRLLQGLVGKRSEEDTENIPENSVARPKPLEDQLCLLWSNTQALQDWLLPRLSLDGSLSLWLPPGPRPAVDHSEWTETTRQPR | null | null | brain development [GO:0007420]; dentate gyrus development [GO:0021542]; diet induced thermogenesis [GO:0002024]; embryonic digestive tract development [GO:0048566]; hippocampus development [GO:0021766]; intracellular water homeostasis [GO:0009992]; negative regulation of gastrin-induced gastric acid secretion [GO:19036... | extracellular space [GO:0005615] | digestive hormone activity [GO:0046659]; G protein-coupled receptor binding [GO:0001664]; hormone activity [GO:0005179]; signaling receptor binding [GO:0005102] | PF00123; | null | Glucagon family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19805236, ECO:0000269|PubMed:3047699}. | null | null | null | null | null | FUNCTION: Hormone involved in different processes, such as regulation of the pH of the duodenal content, food intake and water homeostasis (PubMed:19805236, PubMed:3047699, PubMed:7958688, PubMed:8568688, PubMed:9655680). Exerts its biological effects by binding to secretin receptor (SCTR), a G-protein coupled receptor... | Rattus norvegicus (Rat) |
P11387 | TOP1_HUMAN | MSGDHLHNDSQIEADFRLNDSHKHKDKHKDREHRHKEHKKEKDREKSKHSNSEHKDSEKKHKEKEKTKHKDGSSEKHKDKHKDRDKEKRKEEKVRASGDAKIKKEKENGFSSPPQIKDEPEDDGYFVPPKEDIKPLKRPRDEDDADYKPKKIKTEDTKKEKKRKLEEEEDGKLKKPKNKDKDKKVPEPDNKKKKPKKEEEQKWKWWEEERYPEGIKWKFLEHKGPVFAPPYEPLPENVKFYYDGKVMKLSPKAEEVATFFAKMLDHEYTTKEIFRKNFFKDWRKEMTNEEKNIITNLSKCDFTQMSQYFKAQTEARKQMS... | 5.6.2.1 | null | chromatin remodeling [GO:0006338]; chromosome segregation [GO:0007059]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; DNA replication [GO:0006260]; DNA topological change [GO:0006265]; embryonic cleavage [GO:0040016]; peptidyl-serine phosphorylation [GO:0018105]; phosphorylation [... | chromosome [GO:0005694]; fibrillar center [GO:0001650]; male germ cell nucleus [GO:0001673]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; P-body [GO:0000932]; perikaryon [GO:0043204]; protein-DNA complex [GO:0032993] | ATP binding [GO:0005524]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA binding, bending [GO:0008301]; DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917]; double-stranded DNA binding [GO:0003690]; protein domain specific binding [GO:0019904]; protein serine/threonine kin... | PF14370;PF01028;PF02919; | 1.10.132.10;2.170.11.10;1.10.10.41; | Type IB topoisomerase family | PTM: Sumoylated. Lys-117 is the main site of sumoylation. Sumoylation plays a role in partitioning TOP1 between nucleoli and nucleoplasm. Levels are dramatically increased on camptothecin (CPT) treatment. {ECO:0000269|PubMed:12149243}.; PTM: Phosphorylation at Ser-506 by CK2 increases binding to supercoiled DNA and sen... | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12149243}. Nucleus, nucleoplasm {ECO:0000269|PubMed:12149243}. Note=Diffuse nuclear localization with some enrichment in nucleoli. On CPT treatment, cleared from nucleoli into nucleoplasm. Sumoylated forms found in both nucleoplasm and nucleoli. | CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10130, ECO:0000269|PubMed:14594810, ECO:0000269|PubMed:16033260, ECO:0000269|PubMed:2833744}; | null | null | null | null | FUNCTION: Releases the supercoiling and torsional tension of DNA 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... | Homo sapiens (Human) |
P11388 | TOP2A_HUMAN | MEVSPLQPVNENMQVNKIKKNEDAKKRLSVERIYQKKTQLEHILLRPDTYIGSVELVTQQMWVYDEDVGINYREVTFVPGLYKIFDEILVNAADNKQRDPKMSCIRVTIDPENNLISIWNNGKGIPVVEHKVEKMYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETASREYKKMFKQTWMDNMGRAGEMELKPFNGEDYTCITFQPDLSKFKMQSLDKDIVALMVRRAYDIAGSTKDVKVFLNGNKLPVKGFRSYVDMYLKDKLDETGNSLKVIHEQVNHRWEVCLTMSEKGFQQISFVNSIATS... | 5.6.2.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:19222228, ECO:0000305|PubMed:19697956, ECO:0000305|PubMed:22323612, ECO:0000305|PubMed:22841979}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305|PubMed:19222228, ECO:0000305|PubMed:19697956, ECO:0000305|PubMed:22323612, ECO:0000305|... | apoptotic chromosome condensation [GO:0030263]; chromosome segregation [GO:0007059]; DNA damage response [GO:0006974]; DNA ligation [GO:0006266]; DNA topological change [GO:0006265]; embryonic cleavage [GO:0040016]; female meiotic nuclear division [GO:0007143]; hematopoietic progenitor cell differentiation [GO:0002244]... | chromosome, centromeric region [GO:0000775]; condensed chromosome [GO:0000793]; cytoplasm [GO:0005737]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex [GO:0009330]; male germ cell nucleus [GO:0001673]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing com... | ATP binding [GO:0005524]; ATP-dependent activity, acting on DNA [GO:0008094]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA binding, bending [GO:0008301]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]; magnesium ion binding [GO:0000287]; protein heterodimerization ... | PF00204;PF00521;PF08070;PF02518;PF01751;PF16898; | 3.30.1360.40;3.30.1490.30;3.30.230.10;3.40.50.670;3.30.565.10;3.90.199.10;1.10.268.10; | Type II topoisomerase family | PTM: Phosphorylation has no effect on catalytic activity. However, phosphorylation at Ser-1106 by CSNK1D/CK1 promotes DNA cleavable complex formation. {ECO:0000269|PubMed:10942766, ECO:0000269|PubMed:18062778, ECO:0000269|PubMed:19043076, ECO:0000269|Ref.11}.; PTM: (Microbial infection) Deubiquitinated by Epstein-Barr ... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9155056}. Nucleus, nucleoplasm {ECO:0000269|PubMed:8299728}. Nucleus {ECO:0000269|PubMed:17567603, ECO:0000269|PubMed:22013166, ECO:0000269|PubMed:8299728, ECO:0000269|PubMed:9155056}. Nucleus, nucleolus {ECO:0000269|PubMed:9155056}. | CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995, ECO:0000269|PubMed:19222228, ECO:0000269|PubMed:19697956}; | null | null | null | null | FUNCTION: Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand (PubMed:17567603, PubMed:18790802, PubMed:22013166, PubMed:22323612)... | Homo sapiens (Human) |
P11403 | FGF4_MOUSE | MAKRGPTTGTLLPRVLLALVVALADRGTAAPNGTRHAELGHGWDGLVARSLARLPVAAQPPQAAVRSGAGDYLLGLKRLRRLYCNVGIGFHLQVLPDGRIGGVHADTRDSLLELSPVQRGVVSIFGVASRFFVAMSSRGKLFGVPFFTDECKFKEILLPNNYNAYESYAYPGMFMALSKNGRTKKGNRVSPTMKVTHFLPRL | null | null | animal organ morphogenesis [GO:0009887]; apoptotic process [GO:0006915]; apoptotic process involved in morphogenesis [GO:0060561]; cartilage condensation [GO:0001502]; cell differentiation [GO:0030154]; cell population proliferation [GO:0008283]; cellular response to leukemia inhibitory factor [GO:1990830]; chondroblas... | cytoplasm [GO:0005737]; extracellular space [GO:0005615] | fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083] | PF00167; | 2.80.10.50; | Heparin-binding growth factors family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. Is essential for survival of the postimplantation mouse embryo. Required for normal limb and cardiac valve development during embryogenesis. May play a role in embryonic molar tooth bud developmen... | Mus musculus (Mouse) |
P11404 | FABPH_MOUSE | MADAFVGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDTITIKTQSTFKNTEINFQLGIEFDEVTADDRKVKSLVTLDGGKLIHVQKWNGQETTLTRELVDGKLILTLTHGSVVSTRTYEKEA | null | null | brown fat cell differentiation [GO:0050873]; cholesterol homeostasis [GO:0042632]; intracellular lipid transport [GO:0032365]; long-chain fatty acid transport [GO:0015909]; phospholipid homeostasis [GO:0055091]; positive regulation of long-chain fatty acid import into cell [GO:0140214]; positive regulation of phospholi... | cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634]; sarcoplasm [GO:0016528] | cytoskeletal protein binding [GO:0008092]; fatty acid binding [GO:0005504]; icosatetraenoic acid binding [GO:0050543]; long-chain fatty acid binding [GO:0036041]; long-chain fatty acid transporter activity [GO:0005324]; oleic acid binding [GO:0070538] | PF00061; | 2.40.128.20; | Calycin superfamily, Fatty-acid binding protein (FABP) family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. | Mus musculus (Mouse) |
P11407 | PA2BC_VIPAA | MRTLWIVAVCLIGVEGSLLEFGMMILGETGKNPLTSYSFYGCYCGVGGKGTPKDATDRCCFVHDCCYGNLPDCSPKTDRYKYHRENGAIVCGKGTSCENRICECDRAAAICFRKNLKTYNYIYRNYPDILCKEESEKC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. Host cytoplasm, host cytosol {ECO:0000250}. | 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:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that acts as a presynaptic neurotoxin, an inhibitor of blood coagulation, and has been found to bind with high affinity to intracellular proteins. The response of indirectly stimulated neuromuscular preparations to ammodytoxin (Atx) is triphasic. The first phase, the transi... | Vipera ammodytes ammodytes (Western sand viper) |
P11411 | G6PD_LEUME | MVSEIKTLVTFFGGTGDLAKRKLYPSVFNLYKKGYLQKHFAIVGTARQALNDDEFKQLVRDSIKDFTDDQAQAEAFIEHFSYRAHDVTDAASYAVLKEAIEEAADKFDIDGNRIFYMSVAPRFFGTIAKYLKSEGLLADTGYNRLMIEKPFGTSYDTAAELQNDLENAFDDNQLFRIDHYLGKEMVQNIAALRFGNPIFDAAWNKDYIKNVQVTLSEVLGVEERAGYYDTAGALLDMIQNHTMQIVGWLAMEKPESFTDKDIRAAKNAAFNALKIYDEAEVNKYFVRAQYGAGDSADFKPYLEELDVPADSKNNTFIAGE... | 1.1.1.363 | null | glucose metabolic process [GO:0006006]; pentose-phosphate shunt, oxidative branch [GO:0009051] | cytosol [GO:0005829] | glucose-6-phosphate dehydrogenase activity [GO:0004345]; NADP binding [GO:0050661] | PF02781;PF00479; | 3.40.50.720; | Glucose-6-phosphate dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + NAD(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADH; Xref=Rhea:RHEA:38215, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57955, ChEBI:CHEBI:61548; EC=1.1.1.363; Evidence={ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:11106479, ECO:0000269|... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=114 uM for glucose 6-phosphate (with NADP) {ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:9485426}; KM=69 uM for glucose 6-phosphate (with NAD) {ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:9485426}; KM=8 uM for NADP {ECO:0000269|PubMed:11106478, ECO:0000269|P... | PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3. {ECO:0000255|HAMAP-Rule:MF_00966}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.4-8.9. {ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:9485426}; | null | FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone. Can utilize either NADP(+) or NAD(+). {ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:11106479, ECO:0000269|PubMed:1304341, ECO:0000269|PubMed:4396688, ECO:0000269|PubMed:9485426}. | Leuconostoc mesenteroides |
P11412 | G6PD_YEAST | MSEGPVKFEKNTVISVFGASGDLAKKKTFPALFGLFREGYLDPSTKIFGYARSKLSMEEDLKSRVLPHLKKPHGEADDSKVEQFFKMVSYISGNYDTDEGFDELRTQIEKFEKSANVDVPHRLFYLALPPSVFLTVAKQIKSRVYAENGITRVIVEKPFGHDLASARELQKNLGPLFKEEELYRIDHYLGKELVKNLLVLRFGNQFLNASWNRDNIQSVQISFKERFGTEGRGGYFDSIGIIRDVMQNHLLQIMTLLTMERPVSFDPESIRDEKVKVLKAVAPIDTDDVLLGQYGKSEDGSKPAYVDDDTVDKDSKCVTF... | 1.1.1.49 | null | glucose metabolic process [GO:0006006]; NADPH regeneration [GO:0006740]; pentose-phosphate shunt, oxidative branch [GO:0009051]; response to hydrogen peroxide [GO:0042542] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | glucose-6-phosphate dehydrogenase activity [GO:0004345]; NADP binding [GO:0050661] | PF02781;PF00479; | 3.40.50.720; | Glucose-6-phosphate dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349, ChEBI:CHEBI:61548; EC=1.1.1.49; Evidence={ECO:0000250|UniProtKB:P11413}; | null | PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3. {ECO:0000250|UniProtKB:P11413}. | null | null | FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis (By similarity... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11413 | G6PD_HUMAN | MAEQVALSRTQVCGILREELFQGDAFHQSDTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPENTFIVGYARSRLTVADIRKQSEPFFKATPEEKLKLEDFFARNSYVAGQYDDAASYQRLNSHMNALHLGSQANRLFYLALPPTVYEAVTKNIHESCMSQIGWNRIIVEKPFGRDLQSSDRLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTNSDDVRDEKVKVLKCISEVQANNVVLGQYVGNPDGEGEATK... | 1.1.1.49 | null | cellular response to oxidative stress [GO:0034599]; cholesterol biosynthetic process [GO:0006695]; erythrocyte maturation [GO:0043249]; glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; glutathione metabolic process [GO:0006749]; lipid metabolic process [GO:0006629]; NADP metab... | centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020] | glucose binding [GO:0005536]; glucose-6-phosphate dehydrogenase activity [GO:0004345]; identical protein binding [GO:0042802]; NADP binding [GO:0050661]; protein homodimerization activity [GO:0042803] | PF02781;PF00479; | 3.40.50.720; | Glucose-6-phosphate dehydrogenase family | PTM: Acetylated by ELP3 at Lys-403; acetylation inhibits its homodimerization and enzyme activity. Deacetylated by SIRT2 at Lys-403; deacetylation stimulates its enzyme activity. {ECO:0000269|PubMed:24769394, ECO:0000269|PubMed:7857286}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:35122041, ECO:0000269|PubMed:743300}. Membrane; Peripheral membrane protein {ECO:0000269|PubMed:743300}. | CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349, ChEBI:CHEBI:61548; EC=1.1.1.49; Evidence={ECO:0000269|PubMed:15858258, ECO:0000269|PubMed:24769394, ECO:0000269... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.07 uM for NADP {ECO:0000269|PubMed:15858258}; KM=52 uM for glucose 6-phosphate {ECO:0000269|PubMed:15858258}; KM=46.1 uM for glucose 6-phosphate {ECO:0000269|PubMed:38066190}; KM=12.9 uM for NADP {ECO:0000269|PubMed:38066190}; | PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3. {ECO:0000269|PubMed:15858258, ECO:0000269|PubMed:24769394, ECO:0000269|PubMed:26479991, ECO:0000269|PubMed:743300}. | null | null | FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis. {ECO:0000269|... | Homo sapiens (Human) |
P11414 | RPB1_CRIGR | MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDPRQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVDSNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKGHGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEPRYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAAHVIAEDVKLLQFHVATMVDN... | 2.7.7.48; 2.7.7.6; 3.1.13.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P24928}; Note=Two Mg(2+) ions are coordinated by both the catalytic residues and the nucleic acid substrate to enhance substrate recognition and catalytic efficiency. {ECO:0000250|UniProtKB:P24928}; | positive regulation of RNA splicing [GO:0033120]; transcription by RNA polymerase II [GO:0006366] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; RNA polymerase II, core complex [GO:0005665] | DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II activity [GO:0001055] | PF04997;PF00623;PF04983;PF05000;PF04998;PF04992;PF04990;PF05001; | 1.10.132.30;1.10.150.390;2.40.40.20;3.30.1360.140;6.10.250.2940;6.20.50.80;3.30.1490.180;4.10.860.120;1.10.274.100; | RNA polymerase beta' chain family | PTM: The tandem heptapeptide repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat and is mediated, at least, by CDK7 and CDK9. CDK7 phosphorylation of POLR2A associated with DNA... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11674999}. Cytoplasm {ECO:0000250|UniProtKB:P24928}. Chromosome {ECO:0000250|UniProtKB:P24928}. Note=Hypophosphorylated form is mainly found in the cytoplasm, while the hyperphosphorylated and active form is nuclear. Co-localizes with kinase SRPK2 and helicase DDX23 at ... | 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=2.7.7.6; Evidence={ECO:0000250|UniProtKB:P24928}; PhysiologicalDirection=left-to-right; Xref=Rhe... | null | null | null | null | FUNCTION: Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates (By similarity). Pol II-mediated transcription cycle proceeds through transcription initiation,... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
P11415 | QOR_CAVPO | MATGQKLMRAIRVFEFGGPEVLKVQSDVAVPIPKDHQVLIKVHACGINPVETYIRSGTYTRIPLLPYTPGTDVAGVVESIGNDVSAFKKGDRVFTTSTISGGYAEYALASDHTVYRLPEKLDFRQGAAIGIPYFTACRALFHSARAKAGESVLVHGASGGVGLAACQIARAYGLKVLGTAGTEEGQKVVLQNGAHEVFNHRDAHYIDEIKKSIGEKGVDVIIEMLANVNLSNDLKLLSCGGRVIIVGCRGSIEINPRDTMAKESTISGVSLFSSTKEEFQQFASTIQAGMELGWVKPVIGSQYPLEKASQAHENIIHSSG... | 1.6.5.5 | null | protein homotetramerization [GO:0051289]; quinone catabolic process [GO:1901662]; xenobiotic catabolic process [GO:0042178] | cytosol [GO:0005829] | identical protein binding [GO:0042802]; mRNA 3'-UTR binding [GO:0003730]; NADPH binding [GO:0070402]; NADPH:quinone reductase activity [GO:0003960]; structural constituent of eye lens [GO:0005212]; zinc ion binding [GO:0008270] | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family, Quinone oxidoreductase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=2 a quinone + H(+) + NADPH = 2 a 1,4-benzosemiquinone + NADP(+); Xref=Rhea:RHEA:14269, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124, ChEBI:CHEBI:134225; EC=1.6.5.5; Evidence={ECO:0000269|PubMed:1370456, ECO:0000269|PubMed:1420281}; | null | null | null | null | FUNCTION: Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones, such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the best substrates (in vitro). May act in the detoxification of xenobiotics. Interacts with (AU)-rich elements (ARE) in the 3'-... | Cavia porcellus (Guinea pig) |
P11416 | RARA_MOUSE | MASNSSSCPTPGGGHLNGYPVPPYAFFFPPMLGGLSPPGALTSLQHQLPVSGYSTPSPATIETQSSSSEEIVPSPPSPPPLPRIYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHRDKNCIINKVTRNRCQYCRLQKCFDVGMSKESVRNDRNKKKKEAPKPECSESYTLTPEVGELIEKVRKAHQETFPALCQLGKYTTNNSSEQRVSLDIDLWDKFSELSTKCIIKTVEFAKQLPGFTTLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFANQLLPLE... | null | null | apoptotic cell clearance [GO:0043277]; bone development [GO:0060348]; cell differentiation [GO:0030154]; cellular response to corticotropin-releasing hormone stimulus [GO:0071376]; cellular response to estrogen stimulus [GO:0071391]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to retinoic ac... | actin cytoskeleton [GO:0015629]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; RNA polymerase II transcription regulator comp... | alpha-actinin binding [GO:0051393]; chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity [GO:0001217]; heterocyclic compound binding [GO:1901363]; histone deacetylase binding [GO:0042826]; mRNA 5'-UTR binding [... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | PTM: Phosphorylated on serine and threonine residues. Phosphorylation does not change during cell cycle. Phosphorylation on Ser-77 is crucial for the N-terminal AF1 transcriptional activity. Under stress conditions, MAPK8 enhances phosphorylation on Thr-181, Ser-445 and Ser-461 leading to RARA ubiquitination and degrad... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10660575, ECO:0000269|PubMed:12079996}. Cytoplasm {ECO:0000269|PubMed:10660575, ECO:0000269|PubMed:12079996}. Note=Nuclear localization depends on ligand binding, phosphorylation and sumoylation (PubMed:10660575, PubMed:12079996). Translocation to the nucleus is depende... | null | null | null | null | null | FUNCTION: Receptor for retinoic acid (PubMed:17205979). Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes (PubMed:17205979). The RXR/RAR heterodimers bind to the reti... | Mus musculus (Mouse) |
P11420 | DA_DROME | MATSDDEPMHLYEVFQNCFNKIANKQPTGTVGADRGGGGGYHSPYGSLGVENGMYPSDFNSMHDTVNGGNNRYANASTVDQYFDSAAAGSGGAWCQPQMSSANSYMGQSAYQNSGPLSGHSIDQQQQQVHQADGLGMGGGGGGGVGADGMHCPVTTGLPPISSFRPTSGGIGGPGAGQQAPVNVNVNPPAVFNSPQAHNHNHTVQAQHSALSTAGPLGHHSLNHTPHAHSHTLPLPHALPHGHTLPHPHHSQQNSPAVQSSDAFSGAGASVKVAGAGNSSAAALRQQMYMPADQSISSFGSNPSTPVNSPPPLTQSVVGG... | null | null | chaeta morphogenesis [GO:0008407]; female sex determination [GO:0030237]; follicle cell of egg chamber development [GO:0030707]; hindgut development [GO:0061525]; Malpighian tubule tip cell differentiation [GO:0061382]; neuroblast fate determination [GO:0007400]; neuroendocrine cell differentiation [GO:0061101]; neuron... | nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor binding [GO:0140297]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-re... | PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Daughterless/Achaete-scute complex heterodimers act as transcriptional activators of neural cell fates and are involved in sex determination. | Drosophila melanogaster (Fruit fly) |
P11433 | CDC24_YEAST | MAIQTRFASGTSLSDLKPKPSATSISIPMQNVMNKPVTEQDSLFHICANIRKRLEVLPQLKPFLQLAYQSSEVLSERQSLLLSQKQHQELLKSNGANRDSSDLAPTLRSSSISTATSLMSMEGISYTNSNPSATPNMEDTLLTFSMGILPITMDCDPVTQLSQLFQQGAPLCILFNSVKPQFKLPVIASDDLKVCKKSIYDFILGCKKHFAFNDEELFTISDVFANSTSQLVKVLEVVETLMNSSPTIFPSKSKTQQIMNAENQHRHQPQQSSKKHNEYVKIIKEFVATERKYVHDLEILDKYRQQLLDSNLITSEELYM... | null | null | cellular bud site selection [GO:0000282]; chemotropism [GO:0043577]; establishment of cell polarity [GO:0030010]; intracellular signal transduction [GO:0035556]; protein localization to cell cortex [GO:0072697]; regulation of exit from mitosis [GO:0007096]; regulation of pheromone-dependent signal transduction involved... | Cdc24p-Far1p-Gbetagamma complex [GO:0120171]; cell cortex [GO:0005938]; cellular bud neck [GO:0005935]; cellular bud tip [GO:0005934]; cytoplasm [GO:0005737]; division septum [GO:0000935]; incipient cellular bud site [GO:0000131]; mating projection tip [GO:0043332]; nucleus [GO:0005634]; PAR polarity complex [GO:012015... | guanyl-nucleotide exchange factor activity [GO:0005085] | PF06395;PF15411;PF00621; | 1.10.418.10;1.20.900.10;2.30.29.30; | null | null | null | null | null | null | null | null | FUNCTION: Promotes the exchange of CDC42-bound GDP by GTP. Controls the polarity of calmodulin, and the calcium regulatory process of bud emergence. CDC24 may be involved in the initial selection and organization of the budding site. {ECO:0000269|PubMed:17460121}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11436 | AMIE_PSEAE | MRHGDISSSNDTVGVAVVNYKMPRLHTAAEVLDNARKIAEMIVGMKQGLPGMDLVVFPEYSLQGIMYDPAEMMETAVAIPGEETEIFSRACRKANVWGVFSLTGERHEEHPRKAPYNTLVLIDNNGEIVQKYRKIIPWCPIEGWYPGGQTYVSEGPKGMKISLIICDDGNYPEIWRDCAMKGAELIVRCQGYMYPAKDQQVMMAKAMAWANNCYVAVANAAGFDGVYSYFGHSAIIGFDGRTLGECGEEEMGIQYAQLSLSQIRDARANDQSQNHLFKILHRGYSGLQASGDGDRGLAECPFEFYRTWVTDAEKARENVE... | 3.5.1.4 | null | amide catabolic process [GO:0043605]; beta-alanine biosynthetic process via 3-ureidopropionate [GO:0033396]; carbon utilization [GO:0015976] | null | amidase activity [GO:0004040]; beta-ureidopropionase activity [GO:0003837]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides [GO:0016811]; indoleacetamide hydrolase activity [GO:0043864] | PF00795; | 3.60.110.10; | Carbon-nitrogen hydrolase superfamily, Aliphatic amidase family | null | null | CATALYTIC ACTIVITY: Reaction=a monocarboxylic acid amide + H2O = a monocarboxylate + NH4(+); Xref=Rhea:RHEA:12020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:35757, ChEBI:CHEBI:83628; EC=3.5.1.4; | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of short-chain aliphatic amides to their corresponding organic acids with release of ammonia. Enables the organism to use acetamide as both carbon and nitrogen source.; FUNCTION: Also exhibits in vitro acyl transferase activity, transferring the acyl moiety of short-chain amides to hy... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
P11438 | LAMP1_MOUSE | MAAPGARRPLLLLLLAGLAHGASALFEVKNNGTTCIMASFSASFLTTYETANGSQIVNISLPASAEVLKNGSSCGKENVSDPSLTITFGRGYLLTLNFTKNTTRYSVQHMYFTYNLSDTEHFPNAISKEIYTMDSTTDIKADINKAYRCVSDIRVYMKNVTVVLRDATIQAYLSSGNFSKEETHCTQDGPSPTTGPPSPSPPLVPTNPTVSKYNVTGNNGTCLLASMALQLNITYLKKDNKTVTRAFNISPNDTSSGSCGINLVTLKVENKNRALELQFGMNASSSLFFLQGVRLNMTLPDALVPTFSISNHSLKALQAT... | null | null | autophagic cell death [GO:0048102]; establishment of protein localization to organelle [GO:0072594]; Golgi to lysosome transport [GO:0090160]; granzyme-mediated programmed cell death signaling pathway [GO:0140507]; lysosomal lumen acidification [GO:0007042]; positive regulation of natural killer cell degranulation [GO:... | alveolar lamellar body [GO:0097208]; autolysosome [GO:0044754]; autophagosome membrane [GO:0000421]; cell surface [GO:0009986]; cytolytic granule [GO:0044194]; cytolytic granule membrane [GO:0101004]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; endosome [GO:0005768]; endosome membrane [GO:00100... | enzyme binding [GO:0019899]; ion channel inhibitor activity [GO:0008200]; protein domain specific binding [GO:0019904] | PF01299;PF21222; | 2.40.160.110; | LAMP family | PTM: O- and N-glycosylated; some of the N-glycans attached to LAMP-1 are polylactosaminoglycans. {ECO:0000250|UniProtKB:P11279}. | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein {ECO:... | null | null | null | null | null | FUNCTION: Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, lysosomal pH regulation, autophagy and cholesterol homeostasis (PubMed:15121881). Acts as an important regulator of lysosomal lumen pH regulation by acting as a direct inhibitor of the proton channel TMEM175, facilitating ly... | Mus musculus (Mouse) |
P11439 | TOXA_PSEAE | MHLTPHWIPLVASLGLLAGGSFASAAEEAFDLWNECAKACVLDLKDGVRSSRMSVDPAIADTNGQGVLHYSMVLEGGNDALKLAIDNALSITSDGLTIRLEGGVEPNKPVRYSYTRQARGSWSLNWLVPIGHEKPSNIKVFIHELNAGNQLSHMSPIYTIEMGDELLAKLARDATFFVRAHESNEMQPTLAISHAGVSVVMAQAQPRREKRWSEWASGKVLCLLDPLDGVYNYLAQQRCNLDDTWEGKIYRVLAGNPAKHDLDIKPTVISHRLHFPEGGSLAALTAHQACHLPLETFTRHRQPRGWEQLEQCGYPVQRLV... | 2.4.2.36 | null | null | null | NAD+-diphthamide ADP-ribosyltransferase activity [GO:0047286]; nucleotidyltransferase activity [GO:0016779]; toxin activity [GO:0090729] | PF09101;PF09009;PF09102; | 2.60.120.200;3.90.175.10;3.90.1350.10; | null | PTM: The 8 cysteines participate in intrachain disulfide bonds. | null | CATALYTIC ACTIVITY: Reaction=diphthamide-[translation elongation factor 2] + NAD(+) = H(+) + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2] + nicotinamide; Xref=Rhea:RHEA:11820, Rhea:RHEA-COMP:10174, Rhea:RHEA-COMP:10175, ChEBI:CHEBI:15378, ChEBI:CHEBI:16692, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=121 uM for NAD; Note=For ADP-ribosyltransferase activity of the catalytic fragment 399-605.; | null | null | null | FUNCTION: An NAD-dependent ADP-ribosyltransferase (ADPRT). Catalyzes the transfer of the ADP ribosyl moiety of oxidized NAD (NAD(+)) onto eukaryotic elongation factor 2 (eEF-2) thus arresting protein synthesis (PubMed:18276581, PubMed:2170123). Has an LD(50) of 65 ng/ml against the human lung epithelial cell line C38 (... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
P11440 | CDK1_MOUSE | MEDYIKIEKIGEGTYGVVYKGRHRVTGQIVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFLSMDLKKYLDSIPPGQFMDSSLVKSYLHQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHEVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNTFPKWKPGSLASHVKNLDENGLDLLSKMLVYDPAKRISGKMALKHPYFDDLDNQIKKM | 2.7.11.22; 2.7.11.23 | null | animal organ regeneration [GO:0031100]; apoptotic process [GO:0006915]; cell division [GO:0051301]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to organic cyclic compound [GO:0071407]; chromosome condensation [GO:0030261]; epithelial cell differentiation [GO:0030855]; fibroblast proliferation... | centrosome [GO:0005813]; cyclin A2-CDK1 complex [GO:0097122]; cyclin B1-CDK1 complex [GO:0097125]; cytosol [GO:0005829]; midbody [GO:0030496]; mitochondrial matrix [GO:0005759]; 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]; pr... | 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. Phosphorylation at Thr-14 and Tyr-15 by PKMYT1 prevents nuclear translocation. 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). Phosphorylati... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17942597}. Cytoplasm {ECO:0000269|PubMed:17942597}. Mitochondrion {ECO:0000269|PubMed:17942597}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P06493}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P06493}. Note=Colo... | 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:36264786}; CATALYTI... | 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:16007079, PubMed:17700700, PubMed:17942597, PubMed:22405274). Phosphorylates PARVA/actopaxin, APC, AMPH, A... | Mus musculus (Mouse) |
P11441 | UBL4A_HUMAN | MQLTVKALQGRECSLQVPEDELVSTLKQLVSEKLNVPVRQQRLLFKGKALADGKRLSDYSIGPNSKLNLVVKPLEKVLLEEGEAQRLADSPPPQVWQLISKVLARHFSAADASRVLEQLQRDYERSLSRLTLDDIERLASRFLHPEVTETMEKGFSK | null | null | post-translational protein targeting to endoplasmic reticulum membrane [GO:0006620]; protein modification process [GO:0036211]; regulation of protein stability [GO:0031647]; tail-anchored membrane protein insertion into ER membrane [GO:0071816]; ubiquitin-dependent protein catabolic process [GO:0006511] | BAT3 complex [GO:0071818]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | protein-folding chaperone binding [GO:0051087]; ubiquitin-like protein transferase activity [GO:0019787] | PF17840;PF00240; | null | null | PTM: Polyubiquitinated. Ubiquitination by AMFR and deubiquitination by USP13 may regulate the interaction between the BAG6/BAT3 complex and SGTA and therefore may regulate client proteins fate. {ECO:0000269|PubMed:24424410}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20676083, ECO:0000269|PubMed:21636303}. Nucleus {ECO:0000269|PubMed:21636303}. | null | null | null | null | null | FUNCTION: As part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, maintains misfolded and hydrophobic patches-containing proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they under... | Homo sapiens (Human) |
P11442 | CLH1_RAT | MAQILPIRFQEHLQLQNLGINPANIGFSTLTMESDKFICIREKVGEQAQVVIIDMNDPSNPIRRPISADSAIMNPASKVIALKAGKTLQIFNIEMKSKMKAHTMTDDVTFWKWISLNTVALVTDNAVYHWSMEGESQPVKMFDRHSSLAGCQIINYRTDAKQKWLLLTGISAQQNRVVGAMQLYSVDRKVSQPIEGHAASFAQFKMEGNAEESTLFCFAVRGQAGGKLHIIEVGTPPTGNQPFPKKAVDVFFPPEAQNDFPVAMQISEKHDVVFLITKYGYIHLYDLETGTCIYMNRISGETIFVTAPHEATAGIIGVNR... | null | null | amyloid-beta clearance by transcytosis [GO:0150093]; autophagy [GO:0006914]; clathrin coat assembly [GO:0048268]; clathrin coat disassembly [GO:0072318]; clathrin-dependent endocytosis [GO:0072583]; Golgi organization [GO:0007030]; intracellular protein transport [GO:0006886]; mitotic cell cycle [GO:0000278]; mitotic s... | clathrin coat [GO:0030118]; clathrin coat of coated pit [GO:0030132]; clathrin coat of trans-Golgi network vesicle [GO:0030130]; clathrin complex [GO:0071439]; clathrin-coated endocytic vesicle [GO:0045334]; clathrin-coated endocytic vesicle membrane [GO:0030669]; clathrin-coated pit [GO:0005905]; clathrin-coated vesic... | ankyrin binding [GO:0030506]; clathrin light chain binding [GO:0032051]; disordered domain specific binding [GO:0097718]; double-stranded RNA binding [GO:0003725]; heat shock protein binding [GO:0031072]; low-density lipoprotein particle receptor binding [GO:0050750]; peptide binding [GO:0042277]; protein kinase bindin... | PF00637;PF09268;PF13838;PF01394; | 1.25.40.730;2.130.10.110;1.25.40.10; | Clathrin heavy chain family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Melanosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15858577}. Note=Cytoplasmic face of coated pits and vesicles. In complex ... | null | null | null | null | null | FUNCTION: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network (By similarity). Acts as a component of the TACC3/ch-TOG/clathrin complex proposed to contribute to st... | Rattus norvegicus (Rat) |
P11454 | ENTF_ECOLI | MSQHLPLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGEVWQWVDDALTFELPEIIDLRTNIDPHGTAQALMQADLQQDLRVDSGKPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTWLRGEPTPASPFTPFADVVEEYQQYRESEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFTDGEFRQLATQLSGVQRTDLALALAALWLGRLCNRMDYAAGFIFMRRLGSAALTATGPVLNVLPLGIHIAAQETLPELATRLAAQLKKM... | 6.2.1.72; 6.3.2.14 | COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000269|PubMed:10375542, ECO:0000269|PubMed:1826089, ECO:0000269|PubMed:26762461, ECO:0000269|PubMed:27597544, ECO:0000269|PubMed:9485415}; Note=Binds 1 phosphopantetheine covalently. {ECO:0000269|PubMed:10375542, ECO:0000269|PubMed:26762461... | amino acid activation for nonribosomal peptide biosynthetic process [GO:0043041]; carboxylic acid metabolic process [GO:0019752]; enterobactin biosynthetic process [GO:0009239] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; enterobactin synthetase complex [GO:0009366]; plasma membrane [GO:0005886] | 2,3-dihydroxybenzoate-serine ligase activity [GO:0047527]; ATP binding [GO:0005524]; nucleotidyltransferase activity [GO:0016779]; phosphopantetheine binding [GO:0031177] | PF00501;PF00668;PF00550;PF00975; | 3.30.300.30;3.40.50.980;3.40.50.1820;3.30.559.10;3.30.559.30; | ATP-dependent AMP-binding enzyme family, EntF subfamily | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-EntF by EntD (PubMed:9485415). Holo-EntF so formed is then acylated with seryl-AMP (PubMed:9485415). {ECO:0000269|PubMed:9485415}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10692387}. Note=Membrane-associated. {ECO:0000269|PubMed:10692387}. | CATALYTIC ACTIVITY: Reaction=3 2,3-dihydroxybenzoate + 6 ATP + 3 L-serine = 6 AMP + 6 diphosphate + enterobactin + 4 H(+); Xref=Rhea:RHEA:30571, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:36654, ChEBI:CHEBI:77805, ChEBI:CHEBI:456215; EC=6.3.2.14; Evidence={ECO:0000269|PubMed... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.26 mM for L-serine {ECO:0000269|PubMed:1338974}; KM=0.75 mM for ATP {ECO:0000269|PubMed:1338974}; KM=5 mM for O-acetyl-L-serine {ECO:0000269|PubMed:1338974}; KM=8 mM for L-beta-chloroalanine {ECO:0000269|PubMed:1338974}; KM=3.1 mM for S-methyl-L-cysteine {ECO:000... | PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis. {ECO:0000269|PubMed:1826089, ECO:0000269|PubMed:216414, ECO:0000269|PubMed:9485415}. | null | null | FUNCTION: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine (PubMed:1338974, PubMed:1826089, PubMed:216414, PubMed:9485415). EntF catalyzes the activation of L-serine via ATP-dependent PPi exchange reaction to form ser... | Escherichia coli (strain K12) |
P11458 | NADA_ECOLI | MSVMFDPDTAIYPFPPKPTPLSIDEKAYYREKIKRLLKERNAVMVAHYYTDPEIQQLAEETGGCISDSLEMARFGAKHPASTLLVAGVRFMGETAKILSPEKTILMPTLQAECSLDLGCPVEEFNAFCDAHPDRTVVVYANTSAAVKARADWVVTSSIAVELIDHLDSLGEKIIWAPDKHLGRYVQKQTGGDILCWQGACIVHDEFKTQALTRLQEEYPDAAILVHPESPQAIVDMADAVGSTSQLIAAAKTLPHQRLIVATDRGIFYKMQQAVPDKELLEAPTAGEGATCRSCAHCPWMAMNGLQAIAEALEQEGSNHE... | 2.5.1.72 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_00567, ECO:0000269|PubMed:15898769, ECO:0000269|PubMed:15967443, ECO:0000269|PubMed:18674537}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-Rule:MF_00567, ECO:0000269|PubMed:15898769, ECO:0000269|PubMed:1596744... | 'de novo' NAD biosynthetic process from aspartate [GO:0034628] | cytosol [GO:0005829] | 4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; quinolinate synthetase A activity [GO:0008987] | PF02445; | 3.40.50.10800; | Quinolinate synthase family, Type 1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00567, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate; Xref=Rhea:RHEA:25888, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29959, ChEBI:CHEBI:43474, ChEBI:CHEBI:57642, ChEBI:CHEBI:77875; EC=2.5.1.72; Evidence={ECO:0000255|HAMAP-Rule:MF_00567, ECO:0000269|P... | null | PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00567, ECO:0000269|PubMed:10648170}. | null | null | FUNCTION: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. {ECO:0000255|HAMAP-Rule:MF_00567, ECO:0000269|PubMed:10648170, ECO:0000269|PubMed:15898769, ECO:0000269|PubMed:15967443, ECO:0000269|PubMed:18674537}. | Escherichia coli (strain K12) |
P11461 | FATA_VIBA7 | MTHQVATCHKKQSFSGKPTLSRIALLVALQISASALPISITHAEEQADESITVYGQANEAYAAGKISKASSIGMLGDKDFLDTPFNAIGYTDKHIQDQHAQDISDVISASDPSVFTSGETGLNKESFKIRGFSSDIGDVMFNGLYGIAPYYRSSPEMYQRIDVLKGPASLLNGMPPNGSVGGSINLVTKRAQEAPITSFTGTYMSDSQFGGHIDIGRRFGENEQFGVRFNGVFRDGDASVDGQSRKAQLASLSLDWRNDIALIEADLYFSTERVDGPNRGLSIASGVDVPSPPSSDTLLSPSWAYNDSEDKGMMIRAELD... | null | null | null | cell outer membrane [GO:0009279] | siderophore uptake transmembrane transporter activity [GO:0015344]; signaling receptor activity [GO:0038023] | PF07715;PF00593; | 2.40.170.20;2.170.130.10; | TonB-dependent receptor family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|PROSITE-ProRule:PRU01360, ECO:0000269|PubMed:3968037}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU01360}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 nM for ferric-anguibactin {ECO:0000269|PubMed:17259629}; | null | null | null | FUNCTION: Involved in the uptake of iron in complex with the siderophore anguibactin. Binds and transports ferric-anguibactin from the cell surface to the periplasm. {ECO:0000269|PubMed:17259629, ECO:0000269|PubMed:2830268}. | Vibrio anguillarum (strain ATCC 68554 / 775) (Listonella anguillarum) |
P11464 | PSG1_HUMAN | MGTLSAPPCTQRIKWKGLLLTASLLNFWNLPTTAQVTIEAEPTKVSEGKDVLLLVHNLPQNLTGYIWYKGQMRDLYHYITSYVVDGEIIIYGPAYSGRETAYSNASLLIQNVTREDAGSYTLHIIKGDDGTRGVTGRFTFTLHLETPKPSISSSNLNPRETMEAVSLTCDPETPDASYLWWMNGQSLPMTHSLKLSETNRTLFLLGVTKYTAGPYECEIRNPVSASRSDPVTLNLLPKLPKPYITINNLNPRENKDVLNFTCEPKSENYTYIWWLNGQSLPVSPRVKRPIENRILILPSVTRNETGPYQCEIRDRYGGIR... | null | null | female pregnancy [GO:0007565]; regulation of immune system process [GO:0002682]; signal transduction [GO:0007165] | cell surface [GO:0009986]; extracellular region [GO:0005576]; plasma membrane [GO:0005886] | protein tyrosine kinase binding [GO:1990782] | PF13895;PF13927;PF07686; | 2.60.40.10; | Immunoglobulin superfamily, CEA family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | null | Homo sapiens (Human) |
P11466 | OCTC_RAT | MENQLAKSIEERTFQYQDSLPPLPVPSLEESLKKYLESVKPFANEDEYKKTEEIVQKFQDGVGKTLHQKLLERAKGKRNWLEEWWLNVAYLDVRIPSQLNVNFVGPSPHFEHYWPAREGTQLERGSILLWHNLNYWQLLRREKLPVHKSGNTPLDMNQFRMLFSTCKVPGITRDSIMNYFKTESEGHCPTHIAVLCRGRAFVFDVLHDGCLITPPELLRQLTYIYQKCWNEPVGPSIAALTSEERTRWAKAREYLIGLDPENLTLLEKIQSSLFVYSIEDTSPHATPENFSQVFEMLLGGDPAVRWGDKSYNLISFANGI... | 2.3.1.137 | null | carnitine metabolic process [GO:0009437]; coenzyme A metabolic process [GO:0015936]; fatty acid beta-oxidation [GO:0006635]; fatty acid metabolic process [GO:0006631]; fatty acid transport [GO:0015908]; generation of precursor metabolites and energy [GO:0006091]; long-chain fatty acid transport [GO:0015909]; medium-cha... | peroxisome [GO:0005777] | carnitine O-octanoyltransferase activity [GO:0008458] | PF00755; | 3.30.559.10;1.10.275.20;3.30.559.70; | Carnitine/choline acetyltransferase family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(R)-carnitine + octanoyl-CoA = CoA + O-octanoyl-(R)-carnitine; Xref=Rhea:RHEA:17177, ChEBI:CHEBI:16347, ChEBI:CHEBI:18102, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386; EC=2.3.1.137; Evidence={ECO:0000250|UniProtKB:Q9UKG9}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine + 4,8-dimethylnonanoyl-CoA = CoA... | null | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. | null | null | FUNCTION: Beta-oxidation of fatty acids. The highest activity concerns the C6 to C10 chain length substrate. {ECO:0000250|UniProtKB:Q9UKG9}. | Rattus norvegicus (Rat) |
P11473 | VDR_HUMAN | MEAMAASTSLPDPGDFDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKALFTCPFNGDCRITKDNRRHCQACRLKRCVDIGMMKEFILTDEEVQRKREMILKRKEEEALKDSLRPKLSEEQQRIIAILLDAHHKTYDPTYSDFCQFRPPVRVNDGGGSHPSRPNSRHTPSFSGDSSSSCSDHCITSSDMMDSSSFSNLDLSEEDSDDPSVTLELSQLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTSEDQIVLLKSSAIEVIMLRSNESFTMDDMSWTCGNQDYKYRVSDVTKAGHSLELIEPLIKFQVGL... | null | null | apoptotic process involved in mammary gland involution [GO:0060057]; bile acid signaling pathway [GO:0038183]; calcium ion transport [GO:0006816]; cell differentiation [GO:0030154]; cell morphogenesis [GO:0000902]; decidualization [GO:0046697]; intestinal absorption [GO:0050892]; intracellular calcium ion homeostasis [... | chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; receptor complex [GO:0043235]; RNA polymerase II transcription regulator complex [GO:0090575] | calcitriol binding [GO:1902098]; DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; lithocholic acid binding [GO:1902121]; lithocholic acid receptor activity [GO:0038186]; nuclear receptor activity [GO:0004879]; nuclear retinoid X receptor binding [GO:0046965];... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:12145331, ECO:0000269|PubMed:16207705, ECO:0000269|PubMed:28698609}. Cytoplasm {ECO:0000269|PubMed:12145331, ECO:0000269|PubMed:16207705, ECO:0000269|PubMed:28698609}. Note=Localizes mainly to the nucleus (PubMed:12145331, PubMed:28... | null | null | null | null | null | FUNCTION: Nuclear receptor for calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells (PubMed:10678179, PubMed:15728261, PubMed:16913708, PubMed:28698609). Enters the nucleus upon vitamin D3 binding where it forms heterodimers with the retinoid X receptor/RXR (PubMed:28698609). The... | Homo sapiens (Human) |
P11474 | ERR1_HUMAN | MSSQVVGIEPLYIKAEPASPDSPKGSSETETEPPVALAPGPAPTRCLPGHKEEEDGEGAGPGEQGGGKLVLSSLPKRLCLVCGDVASGYHYGVASCEACKAFFKRTIQGSIEYSCPASNECEITKRRRKACQACRFTKCLRVGMLKEGVRLDRVRGGRQKYKRRPEVDPLPFPGPFPAGPLAVAGGPRKTAAPVNALVSHLLVVEPEKLYAMPDPAGPDGHLPAVATLCDLFDREIVVTISWAKSIPGFSSLSLSDQMSVLQSVWMEVLVLGVAQRSLPLQDELAFAEDLVLDEEGARAAGLGELGAALLQLVRRLQALR... | null | null | intracellular steroid hormone receptor signaling pathway [GO:0030518]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; fibrillar center [GO:0001650]; intercellular bridge [GO:0045171]; microtubule cytoskeleton [GO:0015630]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; estrogen response element binding [GO:0034056]; nuclear receptor activity [GO:0004879]; nuclear steroid receptor activity [GO:0003707]; protein domain specific binding [GO:0019904]... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | PTM: Phosphorylation on Ser-19 enhances sumoylation on Lys-14 increasing repression of transcriptional activity. {ECO:0000269|PubMed:17676930, ECO:0000269|PubMed:18063693}.; PTM: Sumoylated with SUMO2. Main site is Lys-14 which is enhanced by phosphorylation on Ser-19, cofactor activation, and by interaction with PIAS4... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:18063693, ECO:0000269|PubMed:21190936}. Cytoplasm {ECO:0000269|PubMed:21190936}. Note=Co-localizes to the cytoplasm only in presence of MAPK15. {ECO:0000269|PubMed:21190936}. | null | null | null | null | null | FUNCTION: Binds to an ERR-alpha response element (ERRE) containing a single consensus half-site, 5'-TNAAGGTCA-3'. Can bind to the medium-chain acyl coenzyme A dehydrogenase (MCAD) response element NRRE-1 and may act as an important regulator of MCAD promoter. Binds to the C1 region of the lactoferrin gene promoter. Req... | Homo sapiens (Human) |
P11475 | ERR2_RAT | MSSEDRHLGSSCGSFIKTEPSSPSSGIDALSHHSPSGSSDASGGFGMALGTHANGLDSPPMFAGAGLGGNPCRKSYEDCTSGIMEDSAIKCEYMLNAIPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRLDSENSPYLSLQISPPAKKPLTKIVSYLLVAEPDKLYAMPPDDVPEGDIKALTTLCDLADRELVFLISWAKHIPGFSNLTLGDQMSLLQSAWMEILILGIVYRSLPYDDKLAYAEDYIMDEEHSRLVGLLEL... | null | null | cell dedifferentiation [GO:0043697]; cell population proliferation [GO:0008283]; embryonic placenta development [GO:0001892]; in utero embryonic development [GO:0001701]; inner ear development [GO:0048839]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; negative regulation of DNA-templated trans... | condensed chromosome [GO:0000793]; cytoplasm [GO:0005737]; integrator complex [GO:0032039]; nucleus [GO:0005634] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; estrogen response element b... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | PTM: Acetylated by PCAF/KAT2 (in vitro). {ECO:0000250|UniProtKB:O95718}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q61539}. Cytoplasm {ECO:0000250|UniProtKB:Q61539}. Chromosome {ECO:0000250|UniProtKB:Q61539}. | null | null | null | null | null | FUNCTION: Transcription factor that binds a canonical ESRRB recognition (ERRE) sequence 5'TCAAGGTCA-3' localized on promoter and enhancer of targets genes regulating their expression or their transcription activity (By similarity). Plays a role, in a LIF independent manner, in maintainance of self-renewal and pluripote... | Rattus norvegicus (Rat) |
P11477 | DEFA1_MOUSE | MKKLVLLFALVLLGFQVQADSIQNTDEETKTEEQPGEEDQAVSVSFGDPEGTSLQEESLRDLVCYCRSRGCKGRERMNGTCRKGHLLYTLCCR | null | null | antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cellular response to lipopolysaccharide [GO:0071222]; defense response to bacterium [GO:0042742]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive... | extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | null | PF00323;PF00879; | null | Alpha-defensin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Probably contributes to the antimicrobial barrier function of the small bowel mucosa. Has antibacterial activity against attenuated mutants of S.typhimurium. | Mus musculus (Mouse) |
P11480 | TBAE_PHYPO | MREILSIHIGQAGAQVGNACWELYCLEHGIKPDGQMPSDKSVGGGDDAFNTFFSETSSGKHVPRAIFLDLEPTVIDEIRTGTYRQLFHPEQLITGKEDAANNYARGHYTVGKELVDLCLDRVRKLADQCSGLQGFLVFHSVGGGTGSGFGSLLLERLSVDYGKKSKLDFCVYPSPQVSTAVVEPYNSVLSTHGLLEHTDVAFMLDNEAIYDLCKRSLDIERPSYANLNRLVAQVISSLTTSLRFDGALNVDITEFQTNLVPYPRIHFMLASYAPVISAEKAFHEQLSVAELTNTVFDPSSMMAKCDPRHGKYMACCLMYR... | 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] | cytoplasm [GO:0005737]; microtubule [GO:0005874]; nucleus [GO:0005634]; 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: 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 similarit... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Nucleus. Note=Mitosis in the slime mold Plasmodium differs from the process in many eukaryotes. The tubulin chains must be transported to the nuclei for intranuclear assembly of the spindle. | 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:P6836... | 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 a... | Physarum polycephalum (Slime mold) |
P11481 | TBA1_VOLCA | MREVISIHIGQAGIQVGNACWELYCLEHGIQPDGQMPSDKTIGGGDDAFNTFFSETGAGKHVPRCIFLDLEPTVVDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLALDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRSLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDVTEFQTNLVPYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNAAFEPASMMVKCDPRHGKYMACCLMYR... | 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] | cytoplasm [GO:0005737]; microtubule [GO:0005874] | 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 ... | 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:P6836... | 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 a... | Volvox carteri (Green alga) |
P11483 | ACM3_PIG | MTLHNNNTTSPLFPNISSSWIHGPSDAGLPPGTVTHFGSYNISQAAGNFSSPNGTTSDPLGGHTIWQVVFIAFLTGILALVTIIGNILVIVAFKVNKQLKTVNNYFLLSLACADLIIGVISMNLFTTYIIMNRWALGNLACDLWLSIDYVASNASVMNLLVISFDRYFSITRPLTYRAKRTTKRAGVMIGLAWVISFILWAPAILFWQYFVGKRTVPPGECFIQFLSEPTITFGTAIAAFYMPVTIMTILYWRIYKETEKRTKELAGLQASGTEAEAENFVHPTGSSRSCSSYELQQQSLKRSARRKYGRCHFWFTTKSW... | null | null | adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway [GO:0007197]; chemical synaptic transmission [GO:0007268]; G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger [GO:0007... | basolateral plasma membrane [GO:0016323]; dendrite [GO:0030425]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202] | acetylcholine binding [GO:0042166]; G protein-coupled acetylcholine receptor activity [GO:0016907]; G protein-coupled serotonin receptor activity [GO:0004993] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Muscarinic acetylcholine receptor subfamily, CHRM3 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20309}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P20309}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum m... | null | null | null | null | null | FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover. | Sus scrofa (Pig) |
P11484 | SSB1_YEAST | MAEGVFQGAIGIDLGTTYSCVATYESSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKDMKTWPFKVIDVDGNPVIEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAISGLNVLRIINEPTAAAIAYGLGAGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPV... | 3.6.4.10 | null | 'de novo' cotranslational protein folding [GO:0051083]; chaperone cofactor-dependent protein refolding [GO:0051085]; cytoplasmic translation [GO:0002181]; protein refolding [GO:0042026]; regulation of translational fidelity [GO:0006450]; ribosomal subunit export from nucleus [GO:0000054]; rRNA processing [GO:0006364]; ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; calmodulin binding [GO:0005516]; heat shock protein binding [GO:0031072]; protein folding chaperone [GO:0044183]; unfolded protein binding [GO:0051082] | PF00012; | 1.20.1270.10;3.30.30.30;3.30.420.40; | Heat shock protein 70 family, Ssb-type Hsp70 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10347213, ECO:0000269|PubMed:23332755, ECO:0000305|PubMed:1394434}. Note=About 50% of the protein is associated with translating ribosomes, but sufficient Ssb exists in the cell for each ribosome to be associated with at least one Ssb molecule. {ECO:0000269|PubMed:139... | 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=3.6.4.10; Evidence={ECO:0000269|PubMed:9860955}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=270 uM for ATP (at 2.5 mM potassium acetate) {ECO:0000269|PubMed:9860955}; KM=147 uM for ATP (at 100 mM potassium acetate) {ECO:0000269|PubMed:9860955}; Note=kcat is 0.95 min(-1) with ATP as substrate (at 2.5 mM potassium acetate) and 0.81 min(-1) with ATP as subst... | null | null | null | FUNCTION: Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11485 | NRAM_I83A1 | MNPNQKIITIGSICMTIGIISLILQIGNIISIWVSHSIQTGSQNHTGICNQRIITYENSTWVNQTYVNINNTNVVAGKDTTSVTLAGNSSLCPIRGWAIYSKDNSIRIGSKGDVFVIREPFISCSHLECRTFFLTQGALLNDKHSNGTVKDRSPYRALMSCPIGEAPSPYNSRFESVAWSASACHDGMGWLTIGISGPDDGAVAVLKYNGIITETIKSWRKRILRTQESECVCVNGSCFTIMTDGPSNGPASYRIFKIEKGKITKSIELDAPNSHYEECSCYPDTGTVMCVCRDNWHGSNRPWVSFNQNLDYQIGYICSG... | 3.2.1.18 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP-Rule:MF_04071}; | carbohydrate metabolic process [GO:0005975]; viral budding from plasma membrane [GO:0046761] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; metal ion binding [GO:0046872] | PF00064; | 2.120.10.10; | Glycosyl hydrolase 34 family | PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04071}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04071}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04071}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the... | CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; Evidence={ECO:0000255|HAMAP-Rule:MF_04071}; | null | null | null | null | FUNCTION: Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell ... | Influenza A virus (strain A/Chile/1/1983 H1N1) |
P11487 | FGF3_HUMAN | MGLIWLLLLSLLEPGWPAAGPGARLRRDAGGRGGVYEHLGGAPRRRKLYCATKYHLQLHPSGRVNGSLENSAYSILEITAVEVGIVAIRGLFSGRYLAMNKRGRLYASEHYSAECEFVERIHELGYNTYASRLYRTVSSTPGARRQPSAERLWYVSVNGKGRPRRGFKTRRTQKSSLFLPRVLDHRDHEMVRQLQSGLPRPPGKGVQPRRRRQKQSPDNLEPSHVQASRLGSQLEASAH | null | null | anatomical structure morphogenesis [GO:0009653]; animal organ morphogenesis [GO:0009887]; cell differentiation [GO:0030154]; cell-cell signaling [GO:0007267]; fibroblast growth factor receptor signaling pathway [GO:0008543]; negative regulation of cardiac muscle tissue development [GO:0055026]; positive regulation of c... | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083] | PF00167; | 2.80.10.50; | Heparin-binding growth factors family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. Required for normal ear development. {ECO:0000269|PubMed:8663044}. | Homo sapiens (Human) |
P11488 | GNAT1_HUMAN | MGAGASAEEKHSRELEKKLKEDAEKDARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLEECLEFIAIIYGNTLQSILAIVRAMTTLNIQYGDSARQDDARKLMHMADTIEEGTMPKEMSDIIQRLWKDSGIQACFERASEYQLNDSAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGIIETQFSFKDLNFRMFDVGGQRSERKKWIHCFEGVTCIIFIAALSAYDMVLVEDDEVNRMHESLHLFNSICNHRYFATTSIVLFLNKKDVFFEKIKKAHLSICFPDYDGPNTYEDAGNYIKVQFLELNMRRDVKEIYSHMT... | null | null | adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; background adaptation [GO:0120302]; cell population proliferation [GO:0008283]; cellular response to electrical stimulus [GO:0071257]; detection of chemical stimulus involved in sensory perception of bitter taste [GO:0001580]; detec... | apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; heterotrimeric G-protein complex [GO:0005834]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; photoreceptor connecting cilium [GO:0032391]; photoreceptor disc membrane [GO:0097381]; photoreceptor inner segment [GO:0001917]; phot... | acyl binding [GO:0000035]; G protein-coupled receptor binding [GO:0001664]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; protein kinase binding [GO:0019901] | PF00503; | 1.10.400.10;3.40.50.300; | G-alpha family, G(i/o/t/z) subfamily | null | SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P04695}. Membrane {ECO:0000250|UniProtKB:P04695}; Peripheral membrane protein {ECO:0000250|UniProtKB:P04695}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P20612}. Note=Localizes mainly in the outer segment in the da... | null | null | null | null | null | FUNCTION: Functions as a signal transducer for the rod photoreceptor RHO. Required for normal RHO-mediated light perception by the retina (PubMed:22190596). Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs), such as the photoreceptor RHO. The alph... | Homo sapiens (Human) |
P11491 | PPB_YEAST | MMTHTLPSEQTRLVPGSDSSSRPKKRRISKRSKIIVSTVVCIGLLLVLVQLAFPSSFALRSASHKKKNVIFFVTDGMGPASLSMARSFNQHVNDLPIDDILTLDEHFIGSSRTRSSDSLVTDSAAGATAFACALKSYNGAIGVDPHHRPCGTVLEAAKLAGYLTGLVVTTRITDATPASFSSHVDYRWQEDLIATHQLGEYPLGRVVDLLMGGGRSHFYPQGEKASPYGHHGARKDGRDLIDEAQSNGWQYVGDRKNFDSLLKSHGENVTLPFLGLFADNDIPFEIDRDEKEYPSLKEQVKVALGALEKASNEDKDSNGF... | 3.1.3.1; 3.1.3.54; 3.1.7.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions. {ECO:0000250}; | dephosphorylation [GO:0016311]; nicotinamide nucleotide metabolic process [GO:0046496] | fungal-type vacuole membrane [GO:0000329]; periplasmic space [GO:0042597] | alkaline phosphatase activity [GO:0004035]; fructose-2,6-bisphosphate 6-phosphatase activity [GO:0047386]; metal ion binding [GO:0046872] | PF00245; | 1.10.60.40;3.40.720.10; | Alkaline phosphatase family | null | SUBCELLULAR LOCATION: [Repressible alkaline phosphatase]: Vacuole membrane; Single-pass membrane protein. Note=The full-length version is found in lysosome-like vacuoles.; SUBCELLULAR LOCATION: [Soluble alkaline phosphatase]: Cytoplasm. Note=The truncated version of the protein is soluble. | CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042, ECO:0000269|PubMed:16484724}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl dip... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 for farnesyl diphosphatase activity. {ECO:0000269|PubMed:16484724}; | null | FUNCTION: Phosphatase with broad substrate specificity. A truncated (soluble) version of the protein is responsible for the production of (E,E)-farnesol from (E,E)-farnesyl diphosphate. Acts as a fructose-2,6-bisphosphate 6-phosphatase (PubMed:1848184). {ECO:0000269|PubMed:1848184}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11497 | ACACA_RAT | MDEPSPLAKTLELNQHSRFIIGSVSEDNSEDEISNLVKLDLEEKEGSLSPASVSSDTLSDLGISALQDGLAFHMRSSMSGLHLVKQGRDRKKIDSQRDFTVASPAEFVTRFGGNKVIEKVLIANNGIAAVKCMRSIRRWSYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPGGANNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGLRVDWQENDFSKRILNVPQDLYEKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGI... | 6.4.1.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-ProRule:PRU00969}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-ProRule:PRU00969}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:000... | acetyl-CoA metabolic process [GO:0006084]; cellular response to prostaglandin E stimulus [GO:0071380]; fatty acid biosynthetic process [GO:0006633]; lipid biosynthetic process [GO:0008610]; lipid homeostasis [GO:0055088]; lipid metabolic process [GO:0006629]; malonyl-CoA biosynthetic process [GO:2001295]; protein homot... | cytosol [GO:0005829]; mitochondrion [GO:0005739] | acetyl-CoA carboxylase activity [GO:0003989]; ATP binding [GO:0005524]; biotin binding [GO:0009374]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF08326;PF21385;PF02785;PF00289;PF00364;PF01039;PF02786; | 2.40.50.100;3.40.50.20;3.30.1490.20;3.30.470.20;2.40.460.10;3.90.1770.10; | null | PTM: The N-terminus is blocked.; PTM: Phosphorylation on Ser-1262 is required for interaction with BRCA1. {ECO:0000250}.; PTM: Phosphorylation at Ser-79 by AMPK inactivates enzyme activity. Phosphorylated in vitro at Ser-1200 and Ser-1215 by AMPK; the relevance of phosphorylation of these sites in vivo is however uncle... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5SWU9}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000250|UniProtKB:Q13085}; Physi... | null | PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. {ECO:0000250|UniProtKB:Q13085}. | null | null | FUNCTION: Cytosolic enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the first and rate-limiting step of de novo fatty acid biosynthesis. This is a 2 steps reaction starting with the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain followed by the transf... | Rattus norvegicus (Rat) |
P11498 | PYC_HUMAN | MLKFRTVHGGLRLLGIRRTSTAPAASPNVRRLEYKPIKKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENNVDAVHPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEIAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKH... | 6.4.1.1 | COFACTOR: Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000269|PubMed:18297087}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:18297087}; | gluconeogenesis [GO:0006094]; lipid metabolic process [GO:0006629]; NADH metabolic process [GO:0006734]; NADP metabolic process [GO:0006739]; negative regulation of gene expression [GO:0010629]; positive regulation by host of viral process [GO:0044794]; pyruvate metabolic process [GO:0006090]; viral release from host c... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; biotin binding [GO:0009374]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; pyruvate carboxylase activity [GO:0004736] | PF02785;PF00289;PF00364;PF02786;PF00682;PF02436; | 2.40.50.100;3.20.20.70;3.30.470.20;3.10.600.10; | null | PTM: Acetylation of Lys-748 might play a role in catalytic activity regulation. {ECO:0000250|UniProtKB:Q05920}. | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:9585002}. | CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.4.1.1; Evidence={ECO:0000269|PubMed:9585002}; Physiolo... | null | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000305|PubMed:9585002}. | null | null | FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (a... | Homo sapiens (Human) |
P11499 | HS90B_MOUSE | MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKGEKEEEDKEDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKH... | null | null | cellular response to heat [GO:0034605]; cellular response to interleukin-4 [GO:0071353]; chaperone-mediated protein complex assembly [GO:0051131]; negative regulation of apoptotic process [GO:0043066]; negative regulation of complement-dependent cytotoxicity [GO:1903660]; negative regulation of neuron apoptotic process... | apical plasma membrane [GO:0016324]; aryl hydrocarbon receptor complex [GO:0034751]; axonal growth cone [GO:0044295]; basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; cell surface [GO:0009986]; COP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic growth con... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein binding [GO:0043008]; ATP-dependent protein folding chaperone [GO:0140662]; CTP binding [GO:0002135]; dATP binding [GO:0032564]; disordered domain specific binding [GO:0097718]; DNA polymerase binding [GO:0070182]; double-stranded RNA... | PF13589;PF00183; | 3.30.230.80;3.40.50.11260;1.20.120.790;3.30.565.10; | Heat shock protein 90 family | PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro). {ECO:0000250|UniProtKB:P08238}.; PTM: S-nitrosylated; negatively regulates the ATPase activity. {ECO:0000250|UniProtKB:P08238}.; PTM: Phosphorylation at Tyr-301 by SRC is induced by lipopolysaccharide.... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27496612, ECO:0000269|PubMed:27686098}. Melanosome {ECO:0000250|UniProtKB:P08238}. Nucleus {ECO:0000250|UniProtKB:P08238}. Secreted {ECO:0000250|UniProtKB:P08238}. Cell membrane {ECO:0000250|UniProtKB:P08238}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q6AZV1}. N... | null | null | null | null | null | FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the ... | Mus musculus (Mouse) |
P11501 | HS90A_CHICK | MPEAVQTQDQPMEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKDLKINLIPNKHDRTLTIVDTGIGMTKADLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGSYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRLDNGEPLGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPIRLFVEKERDKEVSDDEAEEKEEEKEEKEEKTEDKPEIEDVGSDEEEEKKDGDKKKKKKIKEKYIDEEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWEDHL... | null | null | cellular response to heat [GO:0034605]; positive regulation of cell cycle G2/M phase transition [GO:1902751]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; protein folding [GO:0006457]; protein stabilization [GO:0050821]; respon... | axon [GO:0030424]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; melanosome [GO:0042470]; myelin sheath [GO:0043209]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing ... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; disordered domain specific binding [GO:0097718]; heat shock protein binding [GO:0031072]; Hsp90 protein binding [GO:0051879]; identical protein binding [GO:0042802]; nitric-oxide synthase regulator acti... | PF13589;PF00183; | 3.30.230.80;3.40.50.11260;1.20.120.790;3.30.565.10; | Heat shock protein 90 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07901}. Melanosome {ECO:0000250|UniProtKB:P07900}. | null | null | null | null | null | FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This... | Gallus gallus (Chicken) |
P11505 | AT2B1_RAT | MGDMANNSVAYSGVKNSLKEANHDGDFGITLAELRALMELRSTDALRKIQESYGDVYGICTKLKTSPNEGLSGNPADLERREAVFGKNFIPPKKPKTFLQLVWEALQDVTLIILEIAAIVSLGLSFYQPPEGDNALCGEVSVGEEEGEGETGWIEGAAILLSVVCVVLVTAFNDWSKEKQFRGLQSRIEQEQKFTVIRGGQVIQIPVADITVGDIAQVKYGDLLPADGILIQGNDLKIDESSLTGESDHVKKSLDKDPLLLSGTHVMEGSGRMVVTAVGVNSQTGIIFTLLGAGGEEEEKKDEKKKEKKNKKQDGAIENR... | 7.2.2.10 | null | calcium ion export [GO:1901660]; calcium ion export across plasma membrane [GO:1990034]; cellular response to corticosterone stimulus [GO:0071386]; cellular response to vitamin D [GO:0071305]; intracellular calcium ion homeostasis [GO:0006874]; negative regulation of cytokine production [GO:0001818]; negative regulatio... | apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cytoplasmic side of plasma membrane [GO:0009898]; dendrite membrane [GO:0032590]; dendritic spine membrane [GO:0032591]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; immunological syn... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calcium ion transmembrane transporter activity [GO:0015085]; calmodulin binding [GO:0005516]; metal ion binding [GO:0046872]; P-type calcium transporter activity [GO:0005388]; PDZ domain binding [GO:0030165] | PF12424;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 IIB subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20020}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:16803870}. Synapse {ECO:0000250|UniProtKB:G5E829}. Presynaptic cell membrane {ECO:0000250|UniProtKB:G5E829}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic... | CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000250|UniProtKB:G5E829}; PhysiologicalDirection=left-to-right;... | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of calcium from the cytoplasm to the extracellular space thereby maintaining intracellular calcium homeostasis. Plays a role in blood pressure regulation through regulation of intracellular calcium concentration and nitric oxide production leading to ... | Rattus norvegicus (Rat) |
P11506 | AT2B2_RAT | MGDMTNSDFYSKNQRNESSHGGEFGCSMEELRSLMELRGTEAVVKIKETYGDTESICRRLKTSPVEGLPGTAPDLEKRKQIFGQNFIPPKKPKTFLQLVWEALQDVTLIILEIAAIISLGLSFYHPPGESNEGCATAQGGAEDEGEAEAGWIEGAAILLSVICVVLVTAFNDWSKEKQFRGLQSRIEQEQKFTVVRAGQVVQIPVAEIVVGDIAQIKYGDLLPADGLFIQGNDLKIDESSLTGESDQVRKSVDKDPMLLSGTHVMEGSGRMVVTAVGVNSQTGIIFTLLGAGGEEEEKKDKKGVKKGDGLQLPAADGAAP... | 7.2.2.10 | null | auditory receptor cell stereocilium organization [GO:0060088]; calcium ion transport [GO:0006816]; cell morphogenesis [GO:0000902]; cerebellar granule cell differentiation [GO:0021707]; cerebellar Purkinje cell differentiation [GO:0021702]; cerebellar Purkinje cell layer morphogenesis [GO:0021692]; cerebellum developme... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cilium [GO:0005929]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendritic spine membrane [GO:0032591]; endoplasmic reticulum [GO:0005783]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; intracellular membrane-bounde... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calcium ion binding [GO:0005509]; calcium-dependent ATPase activity [GO:0030899]; calmodulin binding [GO:0005516]; glutamate receptor binding [GO:0035254]; metal ion binding [GO:0046872]; P-type calcium transporter activity [GO:0005388]; P-type calcium tra... | PF12424;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 IIB subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q01814}; Multi-pass membrane protein {ECO:0000255}. Synapse {ECO:0000250|UniProtKB:Q9R0K7}. Apical cell membrane {ECO:0000250|UniProtKB:Q01814}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q01814}; Multi-pass memb... | CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000250|UniProtKB:Q01814, ECO:0000250|UniProtKB:Q9R0K7}; Physiol... | null | null | null | null | FUNCTION: ATP-driven Ca(2+) ion pump involved in the maintenance of basal intracellular Ca(2+) levels in specialized cells of cerebellar circuit and vestibular and cochlear systems. Uses ATP as an energy source to transport cytosolic Ca(2+) ions across the plasma membrane to the extracellular compartment (By similarity... | Rattus norvegicus (Rat) |
P11507 | AT2A2_RAT | MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLA... | 7.2.2.10 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P11607}; | autophagosome assembly [GO:0000045]; autophagosome membrane docking [GO:0016240]; calcium ion import into sarcoplasmic reticulum [GO:1990036]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; calcium ion transport from cytosol to endoplasmic reticulum [GO:1903515]; cardiac muscle hy... | apical ectoplasmic specialization [GO:0061831]; calcium ion-transporting ATPase complex [GO:0090534]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; longitudinal sarcoplasmic reticulum [GO:0014801]; membrane [GO:0... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calcium ion binding [GO:0005509]; enzyme binding [GO:0019899]; lncRNA binding [GO:0106222]; lutropin-choriogonadotropic hormone receptor binding [GO:0031775]; P-type calcium transporter activity [GO:0005388]; P-type calcium transporter activity involved in... | 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 IIA subfamily | PTM: Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity. {ECO:0000250|UniProtKB:P16615}.; PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia, leading to its inactivation. {ECO:0000250|UniProtKB:O55143}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with FLVCR2 at the mitochondrial-ER contact junction. {ECO:0000250|U... | CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000250|UniProtKB:P16615}; PhysiologicalDirection=left-to-right;... | null | null | null | null | FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome ... | Rattus norvegicus (Rat) |
P11509 | CP2A6_HUMAN | MLASGMLLVALLVCLTVMVLMSVWQQRKSKGKLPPGPTPLPFIGNYLQLNTEQMYNSLMKISERYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVVFSNGERAKQLRRFSIATLRDFGVGKRGIEERIQEEAGFLIDALRGTGGANIDPTFFLSRTVSNVISSIVFGDRFDYKDKEFLSLLRMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFQLLQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFIGGTETVSTTLRYGFLLLMKH... | 1.14.14.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; | coumarin catabolic process [GO:0046226]; coumarin metabolic process [GO:0009804]; epoxygenase P450 pathway [GO:0019373]; steroid metabolic process [GO:0008202]; xenobiotic catabolic process [GO:0042178]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | arachidonic acid epoxygenase activity [GO:0008392]; coumarin 7-hydroxylase activity [GO:0008389]; enzyme binding [GO:0019899]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein a... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=1,4-cineole + O2 + reduced [NADPH--hemoprotein reductase] = 2-exo-hydroxy-1,4-cineole + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49160, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.23 uM for coumarin {ECO:0000269|PubMed:16086027}; KM=530 uM for 1,4-cineole {ECO:0000269|PubMed:11695850}; Vmax=3.5 nmol/min/nmol enzyme toward 1,4-cineole {ECO:0000269|PubMed:11695850}; | null | null | null | FUNCTION: Exhibits a high coumarin 7-hydroxylase activity. Can act in the hydroxylation of the anti-cancer drugs cyclophosphamide and ifosphamide. Competent in the metabolic activation of aflatoxin B1. Constitutes the major nicotine C-oxidase. Acts as a 1,4-cineole 2-exo-monooxygenase. Possesses low phenacetin O-deethy... | Homo sapiens (Human) |
P11511 | CP19A_HUMAN | MVLEMLNPIHYNITSIVPEAMPAATMPVLLLTGLFLLVWNYEGTSSIPGPGYCMGIGPLISHGRFLWMGIGSACNYYNRVYGEFMRVWISGEETLIISKSSSMFHIMKHNHYSSRFGSKLGLQCIGMHEKGIIFNNNPELWKTTRPFFMKALSGPGLVRMVTVCAESLKTHLDRLEEVTNESGYVDVLTLLRRVMLDTSNTLFLRIPLDESAIVVKIQGYFDAWQALLIKPDIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLF... | 1.14.14.14 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:19129847}; | androgen catabolic process [GO:0006710]; estrogen biosynthetic process [GO:0006703]; female genitalia development [GO:0030540]; female gonad development [GO:0008585]; mammary gland development [GO:0030879]; negative regulation of chronic inflammatory response [GO:0002677]; negative regulation of macrophage chemotaxis [... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | aromatase activity [GO:0070330]; electron transfer activity [GO:0009055]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen ... | PF00067; | 1.10.630.10; | Cytochrome P450 family | PTM: Phosphorylated in vitro by PKA and PKG/PRKG1. These phosphorylations inhibit the catalytic activity as measured by estrone synthesis from androstenedione (36% decrease for PKA and 30% for PKG/PRKG1). {ECO:0000269|PubMed:27702664}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:2973313}; Multi-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000269|PubMed:2973313}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=3 O2 + 3 reduced [NADPH--hemoprotein reductase] + testosterone = 17beta-estradiol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:38191, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.46 uM for androst-4-ene-3,17-dione {ECO:0000269|PubMed:27702664}; KM=0.044 uM for androst-4-ene-3,17-dione (19-hydroxylation) {ECO:0000269|PubMed:20385561}; KM=21 uM for 19-hydroxyandrost-4-ene-3,17-dione {ECO:0000269|PubMed:20385561}; KM=18 uM for 19-oxo-androst... | PATHWAY: Steroid hormone biosynthesis. {ECO:0000269|PubMed:20385561, ECO:0000269|PubMed:22773874}. | null | null | FUNCTION: A cytochrome P450 monooxygenase that catalyzes the conversion of C19 androgens, androst-4-ene-3,17-dione (androstenedione) and testosterone to the C18 estrogens, estrone and estradiol, respectively (PubMed:27702664, PubMed:2848247). Catalyzes three successive oxidations of C19 androgens: two conventional oxid... | Homo sapiens (Human) |
P11512 | RPO1N_SULAC | MSEKIIRGVKFGVLSPNEIRQMSVTAIITSEVYDEDGTPIEGGVMDPKLGVIEPGQKCPVCGNTLAGCPGHFGHIELIKPVIHIGYVKHIYDFLRSTCWRCGRIKIKEQDLERYKRIYNAIKLRWPSAARRLVEYIKKISIKNLECPHCGEKQFKIKLEKPYNFNEERNGSIVKLSPSEIRDRLERIPDSDVELLGYDPKSSRPEWMILTVLPVPPITIRPSITIESGIRAEDDLTHKLVDIIRLNERLKESIEAGAPQLIIEDLWDLLQYHVATYFDNEIPGLPPAKHRSGRPLRTLAQRLKGKEGRFRGNLSGKRVDF... | 2.7.7.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00863, ECO:0000269|PubMed:34535646, ECO:0000312|PDB:7OK0, ECO:0000312|PDB:7OQ4, ECO:0000312|PDB:7OQY}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00863, ECO:0000269|PubMed:34535646, ECO:0000305|Ref... | DNA-templated transcription [GO:0006351] | cytoplasm [GO:0005737]; DNA-directed RNA polymerase complex [GO:0000428] | DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; magnesium ion binding [GO:0000287]; RNA polymerase II activity [GO:0001055]; zinc ion binding [GO:0008270] | PF04997;PF00623;PF04983;PF05000;PF04998; | 1.10.10.1950;1.10.132.30;2.40.40.20;2.60.40.2940;4.10.320.40;6.10.250.2940;6.20.50.80;3.30.1490.180;4.10.860.120; | RNA polymerase beta' chain family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00863}. | 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=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00863, ECO:0000269|Ref.4}; | null | null | null | null | FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms the clamp head domain. {ECO:0000255|HAMAP-Rule:MF_00863, ECO:0000269|PubMed:34535646, ECO:0000269|Ref.4}. | Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) |
P11513 | RPO2_SULAC | MLDTESRWAIAESFFKTRGLVRQHLDSFNDFLRNKLQQVIYEQGEIVTEVPGLKIKLGKIRYEKPSIRETDKGPMREITPMEARLRNLTYSSPIFLSMIPVENNIEGEPIEIYIGDLPIMLKSVADPTSNLPIDKLIEIGEDPKDPGGYFIVNGSEKVIIAQEDLATNRVLVDYGKSGSNITHVAKVTSSAAGYRVQVMIERLKDSTIQISFATVPGRIPFAIIMRALGFVTDRDIVYAVSLDPQIQNELLPSLEQASSITSAEEALDFIGNRVAIGQKRENRIQKAEQVIDKYFLPHLGTSPEDRKKKGYYLASAVNKI... | 2.7.7.6 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:34535646, ECO:0000305|Ref.4, ECO:0000312|PDB:7OK0, ECO:0000312|PDB:7OQ4, ECO:0000312|PDB:7OQY}; Note=Binds 1 Zn(2+) per subunit. {ECO:0000269|PubMed:34535646, ECO:0000305|Ref.4, ECO:0000312|PDB:7OK0, ECO:0000312|PDB:7OQ4, ECO:0000312|PDB:7OQY}; | DNA-templated transcription [GO:0006351] | cytoplasm [GO:0005737]; DNA-directed RNA polymerase complex [GO:0000428] | DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; ribonucleoside binding [GO:0032549]; RNA polymerase II activity [GO:0001055]; zinc ion binding [GO:0008270] | PF04563;PF04561;PF04565;PF04566;PF04567;PF00562;PF04560; | 2.40.50.150;3.90.1070.20;3.90.1100.10;2.40.270.10;3.90.1800.10;3.90.1110.10; | RNA polymerase beta chain family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B8YB55}. | 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=2.7.7.6; Evidence={ECO:0000269|Ref.4}; | null | null | null | null | FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (Ref.4). This subunit is involved in DNA promoter recognition (By similarity). {ECO:0000250|UniProtKB:B8YB55, ECO:0000269|Ref.4}. | Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) |
P11517 | HBB2_RAT | MVHLTDAEKATVSGLWGKVNADNVGAEALGRLLVVYPWTQRYFSKFGDLSSASAIMGNPQVKAHGKKVINAFNDGLKHLDNLKGTFAHLSELHCDKLHVDPENFRLLGNMIVIVLGHHLGKEFTPCAQAAFQKVVAGVASALAHKYH | null | null | carbon dioxide transport [GO:0015670]; hydrogen peroxide catabolic process [GO:0042744]; nitric oxide transport [GO:0030185]; 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]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; 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: Involved in oxygen transport from the lung to the various peripheral tissues. | Rattus norvegicus (Rat) |
P11530 | DMD_RAT | MLWWEEVEDCYEREDVQKKTFTKWINAQFSKFGKQHIDNLFSDLQDGKRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALQVLQKNNVDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVKNVMKTIMAGLQQTNSEKILLSWVRESTRNYPQVNVLNFTSSWSDGLALNALIHSHRPDLFDWNSVVSQQSATQRLEHAFNIAKCQLGIEKLLDPEDVATTYPDKKSILMYITSLFQVLPQQVSIEAIREVEMLPRPSKVTREEHFQLHHQMHYSQQITVSLAQGYEQTSSSPKPRFKSYAFTQAAYVATSDSSQSPYPS... | null | null | apoptotic process [GO:0006915]; bone development [GO:0060348]; cardiac muscle cell action potential [GO:0086001]; cardiac muscle contraction [GO:0060048]; cell differentiation [GO:0030154]; cerebral cortex development [GO:0021987]; connective tissue development [GO:0061448]; determination of adult lifespan [GO:0008340]... | astrocyte projection [GO:0097449]; axon [GO:0030424]; cell junction [GO:0030054]; cell projection [GO:0042995]; cell surface [GO:0009986]; cell-substrate junction [GO:0030055]; costamere [GO:0043034]; dystrophin-associated glycoprotein complex [GO:0016010]; filopodium [GO:0030175]; filopodium membrane [GO:0031527]; lam... | actin binding [GO:0003779]; dystroglycan binding [GO:0002162]; integrin binding [GO:0005178]; lamin binding [GO:0005521]; myosin binding [GO:0017022]; nitric-oxide synthase binding [GO:0050998]; PDZ domain binding [GO:0030165]; protein-containing complex binding [GO:0044877]; structural constituent of muscle [GO:000830... | PF00307;PF09068;PF09069;PF00435;PF00397;PF00569; | 1.20.58.60;2.20.70.10;3.30.60.90;1.10.418.10;1.10.238.10; | null | null | SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P11531}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11531}; Cytoplasmic side {ECO:0000250|UniProtKB:P11531}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P11531}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P11531}. Note=In muscle c... | null | null | null | null | null | FUNCTION: Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function ... | Rattus norvegicus (Rat) |
P11531 | DMD_MOUSE | MLWWEEVEDCYEREDVQKKTFTKWINAQFSKFGKQHIDNLFSDLQDGKRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQKNNVDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVKNVMKTIMAGLQQTNSEKILLSWVRQSTRNYPQVNVINFTSSWSDGLALNALIHSHRPDLFDWNSVVSQHSATQRLEHAFNIAKCQLGIEKLLDPEDVATTYPDKKSILMYITSLFQVLPQQVSIEAIQEVEMLPRTSSKVTREEHFQLHHQMHYSQQITVSLAQGYEQTSSSPKPRFKSYAFTQAAYVATSDSTQSPYP... | null | null | apoptotic process [GO:0006915]; bone development [GO:0060348]; cardiac muscle cell action potential [GO:0086001]; cerebral cortex development [GO:0021987]; connective tissue development [GO:0061448]; determination of adult lifespan [GO:0008340]; establishment of blood-nerve barrier [GO:0008065]; establishment of glial ... | astrocyte projection [GO:0097449]; axon [GO:0030424]; cell junction [GO:0030054]; cell projection [GO:0042995]; cell-substrate junction [GO:0030055]; dystrophin-associated glycoprotein complex [GO:0016010]; lamellipodium [GO:0030027]; matrix side of mitochondrial inner membrane [GO:0099617]; membrane raft [GO:0045121];... | actin binding [GO:0003779]; integrin binding [GO:0005178]; lamin binding [GO:0005521]; nitric-oxide synthase binding [GO:0050998]; PDZ domain binding [GO:0030165]; protein-containing complex binding [GO:0044877]; zinc ion binding [GO:0008270] | PF00307;PF09068;PF09069;PF00435;PF00397;PF00569; | 1.20.58.60;2.20.70.10;3.30.60.90;1.10.418.10;1.10.238.10; | null | null | SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000269|PubMed:19109891}; Peripheral membrane protein {ECO:0000269|PubMed:19109891}; Cytoplasmic side {ECO:0000269|PubMed:19109891}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19109891}. Postsynaptic cell membrane {ECO:0000269|PubMed:19109891}. Note=In muscle cells,... | null | null | null | null | null | FUNCTION: Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function ... | Mus musculus (Mouse) |
P11532 | DMD_HUMAN | MLWWEEVEDCYEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVKNVMKNIMAGLQQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHAFNIARYQLGIEKLLDPEDVDTTYPDKKSILMYITSLFQVLPQQVSIEAIQEVEMLPRPPKVTKEEHFQLHHQMHYSQQITVSLAQGYERTSSPKPRFKSYAYTQAAYVTTSDPTRSPFPSQ... | null | null | cardiac muscle cell action potential [GO:0086001]; cardiac muscle contraction [GO:0060048]; maintenance of blood-brain barrier [GO:0035633]; motile cilium assembly [GO:0044458]; muscle cell cellular homeostasis [GO:0046716]; muscle cell development [GO:0055001]; muscle organ development [GO:0007517]; negative regulatio... | cell surface [GO:0009986]; cell-substrate junction [GO:0030055]; costamere [GO:0043034]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dystrophin-associated glycoprotein complex [GO:0016010]; filopodium [GO:0030175]; filopodium membrane [GO:0031527]; membrane raft [GO:0045121]; neuron projection terminus [GO:0044306... | actin binding [GO:0003779]; dystroglycan binding [GO:0002162]; myosin binding [GO:0017022]; nitric-oxide synthase binding [GO:0050998]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of muscle [GO:0008307]; vinculin binding [GO:0017166]; zinc ion binding [GO:0008270] | PF00307;PF09068;PF09069;PF00435;PF00397;PF00569; | 1.20.58.60;2.20.70.10;3.30.60.90;1.10.418.10;1.10.238.10; | null | null | SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P11531}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11531}; Cytoplasmic side {ECO:0000250|UniProtKB:P11531}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P11531}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P11531}. Note=In muscle c... | null | null | null | null | null | FUNCTION: Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function ... | Homo sapiens (Human) |
P11536 | E74EB_DROME | MIMVQHLVAASAHNFASQAAASLVNVSSSSSSSSSSSSSSLSLSSSSSSSSLSSATPTPVASPVTPTSPPPAAAAPAEASPPAGAELQEDGQQAKTQEDPTMKDQDMLEKTRQEVKDPVNVEEPGAIVDTESVMARQSPSPVASTKVPESLEEISNKSPPVQEDEEESESVASDCREFKVLYNHLRQQQHHHSPSSPDKTRSTLDDVSKILWERKQQLQRSSVITAAPTLQPQQHQQPMSDIEDEETLEDVDDADADVEADAEDEELLEQYQNGYDSPLDLSLGGATSAAASAAAAASAVSRRRGRTYSGTESDDSAQCE... | null | null | autophagy [GO:0006914]; cell death [GO:0008219]; oogenesis [GO:0048477]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of development, heterochronic [GO:0040034]; regulation of transcription by RNA polymerase II [GO:0006357]; spermatogenesis [GO:0007283] | nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; sequence-specific DNA binding [GO:0043565] | PF00178; | 1.10.10.10; | ETS family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | null | Drosophila melanogaster (Fruit fly) |
P11541 | PDE6A_BOVIN | MGEVTAEEVEKFLDSNVSFAKQYYNLRYRAKVISDLLGPREAAVDFSNYHALNSVEESEIIFDLLRDFQDNLQAEKCVFNVMKKLCFLLQADRMSLFMYRARNGIAELATRLFNVHKDAVLEECLVAPDSEIVFPLDMGVVGHVALSKKIVNVPNTEEDEHFCDFVDTLTEYQTKNILASPIMNGKDVVAIIMVVNKVDGPHFTENDEEILLKYLNFANLIMKVFHLSYLHNCETRRGQILLWSGSKVFEELTDIERQFHKALYTVRAFLNCDRYSVGLLDMTKQKEFFDVWPVLMGEAPPYAGPRTPDGREINFYKVID... | 3.1.4.35 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions. {ECO:0000250}; | cAMP-mediated signaling [GO:0019933]; retina development in camera-type eye [GO:0060041]; visual perception [GO:0007601] | photoreceptor disc membrane [GO:0097381]; photoreceptor outer segment membrane [GO:0042622] | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; metal ion binding [GO:0046872] | PF01590;PF00233; | 3.30.450.40;1.10.1300.10; | Cyclic nucleotide phosphodiesterase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P16499}; Lipid-anchor {ECO:0000250|UniProtKB:P16499}; Cytoplasmic side {ECO:0000250|UniProtKB:P16499}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P16499}. | CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746, ChEBI:CHEBI:58115; EC=3.1.4.35; Evidence={ECO:0000250|UniProtKB:P16499}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958; Evidence={ECO:0000250|UniProtKB:P16499}; | null | null | null | null | FUNCTION: Rod-specific cGMP phosphodiesterase that catalyzes the hydrolysis of 3',5'-cyclic GMP. This protein participates in processes of transmission and amplification of the visual signal. {ECO:0000250|UniProtKB:P16499}. | Bos taurus (Bovine) |
P11542 | LIG4_PHACH | MAFKQLLAALSVALTLQVTQAAPNLDKRVACPDGVHTASNAACCAWFPVLDDIQQNLFHGGQCGAEAHEALRMVFHDSIAISPKLQSQGKFGGGGADGSIITFSSIETTYHPNIGLDEVVAIQKPFIAKHGVTRGDFIAFAGAVGVSNCPGAPQMQFFLGRPEATQAAPDGLVPEPFHTIDQVLARMLDAGGFDEIETVWLLSAHSIAAANDVDPTISGLPFDSTPGQFDSQFFVETQLRGTAFPGKTGIQGTVMSPLKGEMRLQTDHLFARDSRTACEWQSFVNNQTKLQEDFQFIFTALSTLGHDMNAMTDCSEVIPA... | 1.11.1.14 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00297}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000255|PROSITE-ProRule:PRU00297}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 2 calcium ions per subunit.; | cellular response to oxidative stress [GO:0034599]; hydrogen peroxide catabolic process [GO:0042744]; lignin catabolic process [GO:0046274]; response to reactive oxygen species [GO:0000302] | null | diarylpropane peroxidase activity [GO:0016690]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00141;PF11895; | 1.10.520.10;1.10.420.10; | Peroxidase family, Ligninase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + glycolaldehyde + guaiacol + H2O; Xref=Rhea:RHEA:48004, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17071, ChEBI:CHEBI:17098, ChEBI:CHEBI:28591, ChEBI:CHEBI:86963; EC=1.11.1.14; Evidence={... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=85 uM for H(2)O(2) {ECO:0000269|PubMed:3240864}; KM=171 uM for (3,4-dimethoxyphenyl)methanol {ECO:0000269|PubMed:3240864}; | PATHWAY: Secondary metabolite metabolism; lignin degradation. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 2.3. {ECO:0000269|PubMed:3240864}; | null | FUNCTION: Depolymerization of lignin. Catalyzes the C(alpha)-C(beta) cleavage of the propyl side chains of lignin. {ECO:0000269|PubMed:3240864}. | Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum) |
P11544 | PALY_RHOTO | MAPSLDSISHSFANGVASAKQAVNGASTNLAVAGSHLPTTQVTQVDIVEKMLAAPTDSTLELDGYSLNLGDVVSAARKGRPVRVKDSDEIRSKIDKSVEFLRSQLSMSVYGVTTGFGGSADTRTEDAISLQKALLEHQLCGVLPSSFDSFRLGRGLENSLPLEVVRGAMTIRVNSLTRGHSAVRLVVLEALTNFLNHGITPIVPLRGTISASGDLSPLSYIAAAISGHPDSKVHVVHEGKEKILYAREAMALFNLEPVVLGPKEGLGLVNGTAVSASMATLALHDAHMLSLLSQSLTAMTVEAMVGHAGSFHPFLHDVTR... | 4.3.1.25 | null | cinnamic acid biosynthetic process [GO:0009800]; L-phenylalanine catabolic process [GO:0006559] | cytoplasm [GO:0005737] | phenylalanine ammonia-lyase activity [GO:0045548]; tyrosine ammonia-lyase activity [GO:0052883] | PF00221; | 1.20.200.10;1.10.275.10; | PAL/histidase family | PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly. {ECO:0000269|PubMed:15350127}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=L-phenylalanine = (E)-cinnamate + NH4(+); Xref=Rhea:RHEA:21384, ChEBI:CHEBI:15669, ChEBI:CHEBI:28938, ChEBI:CHEBI:58095; EC=4.3.1.25; Evidence={ECO:0000269|PubMed:5102931}; CATALYTIC ACTIVITY: Reaction=L-tyrosine = (E)-4-coumarate + NH4(+); Xref=Rhea:RHEA:24906, ChEBI:CHEBI:12876, ChEBI:CHE... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.29 mM for L-phenylalanine {ECO:0000269|PubMed:5102931, ECO:0000269|Ref.5}; KM=0.18 mM for L-tyrosine {ECO:0000269|PubMed:5102931, ECO:0000269|Ref.5}; | PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis; trans-cinnamate from L-phenylalanine: step 1/1. {ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:5102931, ECO:0000269|Ref.5}; | null | FUNCTION: Catalyzes the non-oxidative deamination of L-phenylalanine and L-tyrosine to form trans-cinnamic acid and p-coumaric acid respectively with similar efficiencies. Facilitates the commitment step in phenylpropanoid pathways that produce secondary metabolites such as lignins, coumarins and flavonoids. {ECO:00002... | Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides) |
P11551 | FUCP_ECOLI | MGNTSIQTQSYRAVDKDAGQSRSYIIPFALLCSLFFLWAVANNLNDILLPQFQQAFTLTNFQAGLIQSAFYFGYFIIPIPAGILMKKLSYKAGIITGLFLYALGAALFWPAAEIMNYTLFLVGLFIIAAGLGCLETAANPFVTVLGPESSGHFRLNLAQTFNSFGAIIAVVFGQSLILSNVPHQSQDVLDKMSPEQLSAYKHSLVLSVQTPYMIIVAIVLLVALLIMLTKFPALQSDNHSDAKQGSFSASLSRLARIRHWRWAVLAQFCYVGAQTACWSYLIRYAVEEIPGMTAGFAANYLTGTMVCFFIGRFTGTWLIS... | null | null | arabinose transmembrane transport [GO:0015751]; fucose metabolic process [GO:0006004]; fucose transmembrane transport [GO:0015756]; galactose transmembrane transport [GO:0015757] | membrane [GO:0016020]; plasma membrane [GO:0005886] | arabinose:proton symporter activity [GO:0015518]; fucose:proton symporter activity [GO:0015535]; galactose:proton symporter activity [GO:0015517] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, FHS transporter (TC 2.A.1.7) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:20877283}; Multi-pass membrane protein {ECO:0000269|PubMed:20877283}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) + L-fucose(in) = H(+)(out) + L-fucose(out); Xref=Rhea:RHEA:29023, ChEBI:CHEBI:2181, ChEBI:CHEBI:15378; Evidence={ECO:0000269|PubMed:22930818, ECO:0000269|PubMed:2829831, ECO:0000269|PubMed:8052131}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29025; Evidence={ECO:0000269|P... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5 for fucose transport. {ECO:0000269|PubMed:2829831}; | null | FUNCTION: Mediates the uptake of L-fucose across the boundary membrane with the concomitant transport of protons into the cell (symport system) (PubMed:2829831, PubMed:8052131). Can also transport L-galactose and D-arabinose, but at reduced rates compared with L-fucose. Is not able to transport L-rhamnose and L-arabino... | Escherichia coli (strain K12) |
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