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 |
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A9JTS5 | STPAP_XENTR | MEAEESSSSVVPLPQDVQSVVRGGFRCLLCGVNIPNRPSLTDHLSGRRHVRLHEERDKRNQQQERSVYVSNFPRETSEEQLRDVFQKISPVRNIVMDKDRGLYAIVEFESKDGMCAALEEPQIKLSGKRLRVKPREKKEFQRKKGGSPRTLQPPDPEALSKELLNCADVEQQIKKLVSLCSPSHHESHLRELLLSLLQETFTEFFPGCQLLPFGSSVNGFEISGCDLDLYLDLGDDEAENVEGKAEKEIQNREESSTDMEVSMEDPETERKEEEMEIGNSKNDEDEDVTPGLSLKGLSSEEILEVVGKVLRHCVPGVHGV... | 2.7.7.19; 2.7.7.52 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9H6E5}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9NVV4}; Note=Binds 1 divalent cation per subunit. {ECO:0000250|UniProtKB:Q9H6E5}; | co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway [GO:0180010]; mRNA polyadenylation [GO:0006378]; snRNA processing [GO:0016180] | mitochondrion [GO:0005739]; mRNA cleavage and polyadenylation specificity factor complex [GO:0005847]; nuclear speck [GO:0016607]; nucleolus [GO:0005730] | ATP binding [GO:0005524]; enzyme-substrate adaptor activity [GO:0140767]; metal ion binding [GO:0046872]; mRNA 3'-UTR binding [GO:0003730]; poly(A) RNA polymerase activity [GO:1990817]; RNA binding [GO:0003723]; RNA uridylyltransferase activity [GO:0050265] | PF03828;PF00076; | 1.10.1410.10;3.30.70.330;3.30.460.10; | DNA polymerase type-B-like family | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H6E5}. Nucleus speckle {ECO:0000250|UniProtKB:Q9H6E5}. | CATALYTIC ACTIVITY: Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide; Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395, ChEBI:CHEBI:173116; EC=2.7.7.52; Evidence={ECO:0000250|UniProtKB:Q9H6E5}; CATALYTIC ACTIVITY: Reaction=A... | null | null | null | null | FUNCTION: Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to ... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A9LLI7 | RP6L2_ARATH | MSDGNMDVDESPVSWKVKSLEKLIDGSSFSSTLSRLSSSSRLIPTSRDFHFYYNFDEFKRPIDEITGTSQSTLATIGDSEQVWGKSMKFPGDVDDVYAEDWLCNVNDELIERFDVSVDEFQRIRKKEKEIGRSVVADDGDDGFQMVYGKKKKPVGNVVTGSAAVNGGGSVIDVKMAERDKNSSGKAKVPFHVPTIKKPQEEYNILVNNANLPFEHVWLERSEDDLRAMHPLEKFSVLDFVDKDVNEMEPVKPLPLEQTPFKFVQEVKDLKELVAKLRSVEEFAVDLEHNQYRSFQGLTCLMQISTRTEDYIVDTFKLRIH... | null | null | exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000467]; gene silencing by RNA-directed DNA methylation [GO:0080188]; histone mRNA catabolic process [GO:0071044]; nuclear polyadenylation-dependent antisense transcript catabolic proces... | cytoplasm [GO:0005737]; nuclear exosome (RNase complex) [GO:0000176]; nucleolus [GO:0005730]; nucleus [GO:0005634] | 3'-5'-RNA exonuclease activity [GO:0000175]; nucleotide binding [GO:0000166]; single-stranded RNA binding [GO:0003727] | PF01612;PF00570; | 1.10.150.80;3.30.420.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18285452}. Nucleus, nucleolus {ECO:0000269|PubMed:18285452}. Cytoplasm {ECO:0000269|PubMed:18285452}. Note=Localizes predominantly in the nucleus. {ECO:0000269|PubMed:18285452}. | null | null | null | null | null | FUNCTION: Acts as an important epigenetic regulator through multiple silencing mechanisms (PubMed:23555312, PubMed:25211139). Involved in association with RRP6L1 in the silencing of the solo LTR locus. Controls levels of non-coding RNAs (ncRNAs) from the solo LTR locus. Seems to function independently of the RNA-mediat... | Arabidopsis thaliana (Mouse-ear cress) |
A9LNK9 | CPSF_ARATH | MEDADGLSFDFEGGLDSGPVQNTASVPVAPPENSSSAAVNVAPTYDHSSATVAGAGRGRSFRQTVCRHWLRGLCMKGDACGFLHQFDKARMPICRFFRLYGECREQDCVYKHTNEDIKECNMYKLGFCPNGPDCRYRHAKLPGPPPPVEEVLQKIQQLTTYNYGTNRLYQARNVAPQLQDRPQGQVPMQGQPQESGNLQQQQQQQPQQSQHQVSQTLIPNPADQTNRTSHPLPQGVNRYFVVKSNNRENFELSVQQGVWATQRSNEAKLNEAFDSVENVILIFSVNRTRHFQGCAKMTSRIGGYIGGGNWKHEHGTAQYG... | 3.1.21.- | null | mRNA 3'-end processing [GO:0031124]; mRNA polyadenylation [GO:0006378]; mRNA splicing, via spliceosome [GO:0000398]; plant-type hypersensitive response [GO:0009626]; positive regulation of plant-type hypersensitive response [GO:0034052]; positive regulation of programmed cell death [GO:0043068]; regulation of mRNA spli... | cytoplasm [GO:0005737]; mRNA cleavage and polyadenylation specificity factor complex [GO:0005847]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | calmodulin binding [GO:0005516]; DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; N6-methyladenosine-containing RNA reader activity [GO:1990247]; RNA binding [GO:0003723]; RNA endonuclease activity [GO:0004521] | PF04146; | 3.10.590.10;4.10.1000.10; | CPSF4/YTH1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16500995, ECO:0000269|PubMed:19573236}. Cytoplasm {ECO:0000269|PubMed:19573236}. Note=Localized in the cytoplasm when not in complex or when associated with CPSF100, but move to the nucleus when associated with the cleavage and polyadenylation specificity factor (CPSF) ... | null | null | null | null | null | FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation. May interact with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition (By similarity). Mediates poly(A) site selection (PubMed:23136375). Binds RNA i... | Arabidopsis thaliana (Mouse-ear cress) |
A9NJG2 | 13S_FAGTA | MSTKLILSFSLCLMVLSCSAQAAQLWPWRKGQDSRPHHGHQQFQQQCDIQRLTASEPSRRVRSEAGVTEIWDHNTPEFRCTGFVAVRYVIQPGGLLLPSYSNAPYITFVEQGRGVQGVVIPGCPETFQSDSEYPQSQRGQHSRESESQESSRGDQHQKIFRVREGDVIPSPAGVVQWTHNDGDQDLISVTLLDANSFHNQLDENVRSFFLAGQSQQGREERRSQQQTREEGGDRQSRESDDVEALIGANILSGFQDEILHELFRDVDRETISKLRGENDQRGFIVQAQDLKLRVPEDSEEGYERQRGDRKRDERGSGRSN... | null | null | null | null | IgE binding [GO:0019863]; IgG binding [GO:0019864]; nutrient reservoir activity [GO:0045735] | PF00190; | 2.60.120.10; | 11S seed storage protein (globulins) family | PTM: Proteolytically processed from a single precursor to produce an acidic and a basic chain that are linked by a disulfide bond. {ECO:0000250|UniProtKB:A0A1L6K371}. | null | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Highly thermostable. Loss of stability only after incubation for 1 hour at 100 degrees Celsius. {ECO:0000269|PubMed:15277744}; | FUNCTION: Seed storage protein. {ECO:0000305}. | Fagopyrum tataricum (Tartarian buckwheat) (Polygonum tataricum) |
A9PCL4 | PRX2_POPTR | MAPIAVGDVLPDGKLAYFDEQDQLQEVSVHSLVAGKKVILFGVPGAFTPTCSLKHVPGFIEKAGELKSKGVTEILCISVNDPFVMKAWAKSYPENKHVKFLADGSATYTHALGLELNLQEKGLGTRSRRFALLVDDLKVKAANIEGGGEFTVSSADDILKDL | 1.11.1.25 | null | cell redox homeostasis [GO:0045454]; cellular response to oxidative stress [GO:0034599]; hydrogen peroxide catabolic process [GO:0042744] | cytoplasm [GO:0005737] | thioredoxin peroxidase activity [GO:0008379] | PF08534; | 3.40.30.10; | Peroxiredoxin family, Prx5 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=[glutaredoxin]-dithiol + a hydroperoxide = [glutaredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62624, Rhea:RHEA-COMP:10729, Rhea:RHEA-COMP:10730, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.25; Evidence={ECO:0000269|PubMed... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50 uM for phosphatidylcholine hydroperoxide {ECO:0000269|PubMed:15032877}; | null | null | null | FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. Plays a role in cell protection against oxidative stress by detoxifying peroxide... | Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa) |
A9Q751 | PCDP1_MOUSE | MEVVKSPMQELQQAKEPFDTMSPLLLKSLVEEPKKRTEVPNHLLESRVYAKLLNNKVIQARPGIVHFGGYEIESKHQQILNIANISDEDTHLHILPPQTKYFQINFEKKEHRLIPGLSLTVTITFSPDEWRYYYDCIRIHCKGDDTLLVPIHAYPVLNNLDFPTFINLSDVFLGESKSYVIPLQCSCPVDFEFHITLLRSHQAFTIEPKSGIIPANGKAKVTVKFTPIQYGMAQIKIQLWISQFNSQPYECVFTGTCYPNMALPLEEFKRLNTRSKKVNVPLEKTTYVQFYPAPAKAKPQKLKEIDYQDLRFPADLSNPF... | null | null | cerebrospinal fluid circulation [GO:0090660]; establishment of localization in cell [GO:0051649]; motile cilium assembly [GO:0044458]; mucociliary clearance [GO:0120197]; sperm flagellum assembly [GO:0120316] | 9+2 motile cilium [GO:0097729]; axoneme [GO:0005930]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; manchette [GO:0002177]; sperm flagellum [GO:0036126] | calmodulin binding [GO:0005516] | null | 2.60.40.10; | PCDP1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:18039845}. Cytoplasm {ECO:0000269|PubMed:18039845, ECO:0000269|PubMed:29690537}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:29690537}. Note=Localizes to the manchette in elongating spermatids in a SPAG17-dependent manner. {ECO:0000269|Pu... | null | null | null | null | null | FUNCTION: May play a role in cilium morphogenesis. {ECO:0000305|PubMed:18039845}. | Mus musculus (Mouse) |
A9QA56 | ABC3H_FELCA | MNPLQEVIFCRQFGNQHRVPKPYYRRKTYLCYQLKLPEGTLIHKDCLRNKKKRHAEMCFIDKIKALTRDTSQRFEIICYITWSPCPFCAEELVAFVKDNPHLSLRIFASRLYVHWRWKYQQGLRHLHASGIPVAVMSLPEFEDCWRNFVDHQDRSFQPWPNLDQYSKSIKRRLGKILTPLNDLRNDFRNLKLE | 3.5.4.38 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9GZX7}; | cytidine to uridine editing [GO:0016554]; defense response to virus [GO:0051607]; DNA cytosine deamination [GO:0070383]; DNA demethylation [GO:0080111]; negative regulation of single stranded viral RNA replication via double stranded DNA intermediate [GO:0045869] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; P-body [GO:0000932] | cytidine deaminase activity [GO:0004126]; deoxycytidine deaminase activity [GO:0047844]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270] | PF18772; | 3.40.140.10; | Cytidine and deoxycytidylate deaminase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q19Q52}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxycytidine in single-stranded DNA + H(+) + H2O = a 2'-deoxyuridine in single-stranded DNA + NH4(+); Xref=Rhea:RHEA:50948, Rhea:RHEA-COMP:12846, Rhea:RHEA-COMP:12847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:85452, ChEBI:CHEBI:133902; EC=3.5.4.38; Evidence... | null | null | null | null | FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA (By similarity). Exhibi... | Felis catus (Cat) (Felis silvestris catus) |
A9QM73 | SMG7_ARATH | MMTLQMDKTTASSSWERAKSIYDEIAELANKRQKAGNPPDPNLLQLLREKYEAIILESHTFSEQHNIEIPLWQLHYKRIEYFRLHINRVLASSTSTAAQNVKGPSKAEQIAQLKLQFRTFLSEATGFYHDMILKIRSKYGLPLGSFSEDQQSQNLSDKDGKELAEVQKALKSCHRCLIYLGDLARYKGMYAEGDSRSRQYASASSYYLQAASLWPASGNPHHQLAIVASYSRDEFVTTYRYFRSLAVEYPFPTARDNLIVAFDKNRQSYEKLFVPSKDSSKRLTGKGRGKGADISLKDATLVAGPEKDKVTIANEMLKAF... | null | null | defense response [GO:0006952]; meiotic cell cycle [GO:0051321]; meiotic spindle assembly [GO:0090306]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; programmed cell death [GO:0012501]; regulation of defense response [GO:0031347] | nucleus [GO:0005634]; P-body [GO:0000932]; telomerase holoenzyme complex [GO:0005697] | telomerase RNA binding [GO:0070034]; telomeric DNA binding [GO:0042162] | PF10374;PF10373; | 1.25.40.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:22974464, ECO:0000269|PubMed:29073135}. | null | null | null | null | null | FUNCTION: Plays multiple roles in growth and development. Involved in nonsense-mediated mRNA decay (NMD). May provide a link to the mRNA degradation machinery to initiate NMD and serve as an adapter for UPF proteins function. Required for meiotic progression through anaphase II of pollen mother cells. May counteract cy... | Arabidopsis thaliana (Mouse-ear cress) |
A9QM74 | IMA8_HUMAN | MPTLDAPEERRRKFKYRGKDVSLRRQQRMAVSLELRKAKKDEQTLKRRNITSFCPDTPSEKTAKGVAVSLTLGEIIKGVNSSDPVLCFQATQTARKMLSQEKNPPLKLVIEAGLIPRMVEFLKSSLYPCLQFEAAWALTNIASGTSEQTRAVVEGGAIQPLIELLSSSNVAVCEQAVWALGNIAGDGPEFRDNVITSNAIPHLLALISPTLPITFLRNITWTLSNLCRNKNPYPCDTAVKQILPALLHLLQHQDSEVLSDACWALSYLTDGSNKRIGQVVNTGVLPRLVVLMTSSELNVLTPSLRTVGNIVTGTDEQTQM... | null | null | blastocyst development [GO:0001824]; epigenetic regulation of gene expression [GO:0040029]; negative regulation of gene expression [GO:0010629]; NLS-bearing protein import into nucleus [GO:0006607]; positive regulation of gene expression [GO:0010628]; protein import into nucleus [GO:0006606] | cytosol [GO:0005829]; female germ cell nucleus [GO:0001674]; NLS-dependent protein nuclear import complex [GO:0042564]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819] | nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139] | PF00514;PF16186;PF01749; | 1.20.5.690;1.25.10.10; | Importin alpha family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20701745, ECO:0000269|PubMed:36647821}. | null | null | null | null | null | FUNCTION: Functions in nuclear protein import. {ECO:0000269|PubMed:36647821}. | Homo sapiens (Human) |
A9QT41 | NEMO_PIG | MSRTPWKSQPCEMVQPSGGPAGDQDVLGEESSLGKPTMLHLPSEQGAPETFQRCLEENQELRDAIRQSNQMLRERCEELQRFQGSQREEKEFLMQKFCEARRLVERLSLEKLELRRQREQALQEVELLKTCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQALESRVRATSEQVRQLENEREALQQQHSVQVDQLRLQSQSMEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIKSSVVSSERNRGLQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQARE... | null | null | DNA damage response [GO:0006974]; phosphorylation [GO:0016310]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of T cell receptor signaling pathway [GO:0050862] | cytoplasm [GO:0005737]; IkappaB kinase complex [GO:0008385]; nucleus [GO:0005634] | K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; kinase activity [GO:0016301]; linear polyubiquitin binding [GO:1990450]; metal ion binding [GO:0046872] | PF16516;PF11577;PF18414; | 1.20.5.390;1.20.5.990; | null | PTM: Phosphorylation at Ser-68 attenuates aminoterminal homodimerization. {ECO:0000250|UniProtKB:Q9Y6K9}.; PTM: Polyubiquitinated on Lys-285 via 'Lys-63'-linked ubiquitin; the ubiquitination is mediated downstream of NOD2 and RIPK2 and probably plays a role in signaling by facilitating interactions with ubiquitin domai... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y6K9}. Nucleus {ECO:0000250|UniProtKB:Q9Y6K9}. Note=Sumoylated NEMO accumulates in the nucleus in response to genotoxic stress. {ECO:0000250|UniProtKB:Q9Y6K9}. | null | null | null | null | null | FUNCTION: Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin plays a key role in IKK activation by multiple signaling recep... | Sus scrofa (Pig) |
A9RA84 | HMGB1_PAPAN | MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEEDEEDEEDEEEEEDEEDEDEEEDDDDE | null | null | adaptive immune response [GO:0002250]; autophagy [GO:0006914]; chemotaxis [GO:0006935]; DNA geometric change [GO:0032392]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; positive regulation of response to external stimulus [GO:0032103]; ... | chromosome [GO:0005694]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endosome [GO:0005768]; extracellular region [GO:0005576]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | bubble DNA binding [GO:0000405]; DNA binding, bending [GO:0008301]; four-way junction DNA binding [GO:0000400]; supercoiled DNA binding [GO:0097100] | PF00505;PF09011; | 1.10.30.10; | HMGB family | PTM: Phosphorylated at serine residues. Phosphorylation in both NLS regions is required for cytoplasmic translocation followed by secretion. {ECO:0000250|UniProtKB:P09429}.; PTM: Acetylated on multiple sites upon stimulation with LPS (By similarity). Acetylation on lysine residues in the nuclear localization signals (N... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09429}. Chromosome {ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}. Cytoplasm {ECO:0000250|UniProtKB:P09429}. Secreted {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}. Cell membrane {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P6315... | null | null | null | null | null | FUNCTION: Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stabi... | Papio anubis (Olive baboon) |
A9RVK2 | M3K1B_PHYPA | MVEERGSSRSSRGGSWGSGEDGGSSHGGKGVPKLSRTVAKKIHKYDVSADHSDYEDDGSVHSTSSSGSRRNPLSKSIIQQQSFRVGANFEEDLKTLYELIGVSKPADLAISASDWQSRGKSIAYSQPLSSPSLSQEHGEASHSNDLKPSIIDFRSEAPAASPRELPVAPVKLDAHERMTYRSDYVNSQPQNHYGRKNSPSQRSPPPESFPAFDSSPSRLGREGYGLHRMQSDPVMPTLGALSPLGTGNAHPESAGSTATRRWSFDLVPGNHEGDYANMSQVVRDNLPSAAVAMPKNGLVRRSPIIRDPNRSNSSVSNPYA... | 2.7.11.25 | null | defense response [GO:0006952]; MAPK cascade [GO:0000165]; phosphorylation [GO:0016310]; response to chitin [GO:0010200] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q39008}. | 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=2.7.11.25; Evidence={ECO:0000250|UniProtKB:Q39008}; CATALYT... | null | null | null | null | FUNCTION: The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for responses to chitin and acts redundantly with MEKK1a. {ECO:0000269|PubMed:27268... | Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens) |
A9S9Q8 | MPK4B_PHYPA | MDVAGAGGGGAADGNIQGVPTHNGEYTQYNIFGNLFEVSRKYVPPIRPIGRGAYGIVCSAVNSETGEEVAIKKIGNAFDNRIDAKRTLREIKLLRHMDHENIVAIRDIIRPPTRENFNDVYIVYELMDTDLHQIIRSNQPLTEDHCQYFLYQLLRGLKYIHSAKVLHRDLKPSNLLLNANCDLKICDFGLARTTSETDFMTEYVVTRWYRAPELLLNCSEYTAAIDVWSVGCIFMELLNREPLFPGRDYVQQLRLITELIGSPEDHDLGFLRSDNARRYIRQLPRFARQPLDRKFPNMGPAAIDLVEHMLRFDPARRITV... | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|RuleBase:RU361165}; | innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; pattern recognition receptor signaling pathway [GO:0002221]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Dually phosphorylated on Thr-201 and Tyr-203, which activates the enzyme. Phosphorylated in response to pathogen-associated molecular pattern (PAMP) chitin and to a lot lesser extent in response to necrotrophic fungus B.cinerea spores. Not phosphorylated in response to osmotic stress. {ECO:0000269|PubMed:27268428}... | 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=2.7.11.24; Evidence={ECO:0000255|RuleBase:RU361165, ECO:000... | null | null | null | null | FUNCTION: The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein may act redundantly with MPK4a in innate immunity triggered by pathogen-associated molecular pa... | Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens) |
A9SIZ6 | D5FAD_PHYPA | MAPHSADTAGLVPSDELRLRTSNSKGPEQEQTLKKYTLEDVSRHNTPADCWLVIWGKVYDVTSWIPNHPGGSLIHVKAGQDSTQLFDSYHPLYVRKMLAKYCIGELVPSAGDDKFKKATLEYADAENEDFYLVVKQRVESYFKSNKINPQIHPHMILKSLFILGGYFASYYLAFFWSSSVLVSLFFALWMGFFAAEVGVSIQHDGNHGSYTKWRGFGYIMGASLDLVGASSFMWRQQHVVGHHSFTNVDNYDPDIRVKDPDVRRVATTQPRQWYHAYQHIYLAVLYGTLALKSIFLDDFLAYFTGSIGPVKVAKMTPLEF... | 1.14.19.30 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:O00767}; | lipid metabolic process [GO:0006629]; long-chain fatty acid biosynthetic process [GO:0042759]; unsaturated fatty acid biosynthetic process [GO:0006636] | membrane [GO:0016020] | di-homo-gamma-linolenate delta5 desaturase activity [GO:0102866]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water [GO:0016717] | PF00173;PF00487; | 3.10.120.10; | Fatty acid desaturase type 1 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=an (8Z,11Z,14Z)-icosatrienoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46260, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:153... | null | null | null | null | FUNCTION: Fatty acid desaturase that introduces a cis double bond at the 5-position in 20-carbon polyunsaturated fatty acids incorporated in a glycerolipid that contain a Delta(8) double bond. {ECO:0000269|PubMed:16728405}. | Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens) |
A9SR33 | M2K1B_PHYPA | MSRRHRTGGLRVAVPKQENSIHRFLTANGVFHDDDIQLDHMGLRVVSSESTAYANPPDAQLSLADLEAVRVLGKGAGGSVQLVRHKWTNDIYALKGIQMNINETVRKQIVQELKINQLTLHQCPYIVKCYHSFYHNGIISIVLEYMDRGSLADIIKQTKQIPEPYLAVISNQVLKGLNYLHQVRHIIHRDIKPSNLLINQKGEVKISDFGVSAVLISSMAQRDTFVGTYTYMSPERLGGQSYAYDSDIWSLGLTILECALGYFPYRPPGQEEGWNNFFMLMELVINQPPVAAPPDKFSPEFCSFIAACIQKRPGDRLSTA... | 2.7.12.2 | null | defense response [GO:0006952]; phosphorylation [GO:0016310]; response to chitin [GO:0010200] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; MAP kinase kinase activity [GO:0004708]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2; Evidence={ECO:0000250|UniProtKB:Q9S7U9}; CATALYTI... | null | null | null | null | FUNCTION: The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for full defense response to fungal pathogen chitin. {ECO:0000269|PubMed:27268428}. | Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens) |
A9SY39 | M3K1A_PHYPA | MIEERGSSRGSREDRGSSRGSSRGSFEDKGSSHDWKGMGGSTPRPRLTRLVAKKDRNYDAKVDSDFDDDSSVHSTSSPRLSPASSDNLSKITIGQQSFRVGGDVDNLKALYEALGATSPAALGIEASDWESRRKSAVYSRPTSPPRVSHDTGQSSYSHDFQFPASRVDSSLESPPLSPRGLAPMSPVRPIEVEWRKHRNNYAKPTISNRPGRENNPLKPSQPPPTMFPQSSGLRTPDPLPPIDTSTSRLGRESLELQNRHTTLGAYSPPGLRKVHSELTGLVSARSDGAGWASDIESAKRNEDLAVASPVFRDNLPSAAV... | 2.7.11.25 | null | defense response [GO:0006952]; MAPK cascade [GO:0000165]; phosphorylation [GO:0016310]; response to chitin [GO:0010200] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q39008}. | 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=2.7.11.25; Evidence={ECO:0000250|UniProtKB:Q39008}; CATALYT... | null | null | null | null | FUNCTION: The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for responses to chitin and acts redundantly with MEKK1b. {ECO:0000269|PubMed:27268... | Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens) |
A9T142 | MPK4A_PHYPA | METSSGTPELKVISTPTYGGHYVKYVVAGTDFEVTARYKPPLRPIGRGAYGIVCSLFDTVTGEEVAVKKIGNAFDNRIDAKRTLREIKLLRHMDHENVVAITDIIRPPTRENFNDVYIVYELMDTDLHQIIRSNQALTEDHCQYFLYQILRGLKYIHSANVLHRDLKPTNLLVNANCDLKIADFGLARTLSETDFMTEYVVTRWYRAPELLLNCSAYTAAIDIWSVGCIFMELLNRSALFPGRDYVHQLRLITELIGTPEDRDLGFLRSDNARRYIKHLPRQSPIPLTQKFRGINRSALDLVEKMLVFDPAKRITVEAAL... | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|RuleBase:RU361165}; | innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; pattern recognition receptor signaling pathway [GO:0002221]; phosphorylation [GO:0016310]; regulation of gene expression [GO:0010468] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Dually phosphorylated on Thr-197 and Tyr-199, which activates the enzyme. Phosphorylated in response to pathogen-associated molecular pattern (PAMP) chitin and in response to necrotrophic fungus B.cinerea spores. Not phosphorylated in response to osmotic stress. {ECO:0000269|PubMed:27268428}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27268428}. Nucleus {ECO:0000269|PubMed:27268428}. Note=Localization to the cytoplasm and nucleus does not change significantly following chitin treatment. {ECO:0000269|PubMed:27268428}. | 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=2.7.11.24; Evidence={ECO:0000255|RuleBase:RU361165, ECO:000... | null | null | null | null | FUNCTION: The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for innate immunity triggered by pathogen-associated molecular patterns (PAMPs). In... | Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens) |
A9TXT1 | CERK1_PHYPA | MKFQMKMKSELCRTYKYWLILLVLWLSGVTQRETGVLIVDADCIPPNGCKALAYYRLKQGDDLEKLQGRFQTNNSEVLAYNPQLVDANSIQAGTNIYLPFDCLCLNGELVHRFSYTVTTNDTAEKVVDVTYQKLTTVGAVRSASNSGDLSSIYSGQSLTIPVRCYCGDPNVDPKYGLFSTYVVQADDQLTSLSTNFSVDADVISKFNSDTRNLSPDSIIFIPSKAANGSFPPFSGYVLGTVHWRSNVGIIVGVVVGGIVLAVLLLFALIFGFKHFRRRKLAKEPTMQQSGLLSSSSMAGSKPSRSGSTMLPVPKSVEFTY... | 2.7.11.1 | null | innate immune response [GO:0045087]; phosphorylation [GO:0016310] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; chitin binding [GO:0008061]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; transmembrane receptor protein kinase activity [GO:0019199] | PF01476;PF07714; | 3.10.350.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A8R7E6}; Single-pass membrane protein {ECO:0000250|UniProtKB:A8R7E6}. | 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:A8R7E6}; CATALYTI... | null | null | null | null | FUNCTION: Lysin motif (LysM) receptor kinase required as a cell surface receptor for chitin elicitor (chitooligosaccharides) signaling leading to innate immunity in response to biotic stresses (By similarity). The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapi... | Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens) |
A9UHW6 | MI4GD_HUMAN | MGEPSREEYKIQSFDAETQQLLKTALKDPGAVDLEKVANVIVDHSLQDCVFSKEAGRMCYAIIQAESKQAGQSVFRRGLLNRLQQEYQAREQLRARSLQGWVCYVTFICNIFDYLRVNNMPMMALVNPVYDCLFRLAQPDSLSKEEEVDCLVLQLHRVGEQLEKMNGQRMDELFVLIRDGFLLPTGLSSLAQLLLLEIIEFRAAGWKTTPAAHKYYYSEVSD | null | null | cap-dependent translational initiation [GO:0002191]; regulation of translational initiation [GO:0006446] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; histone mRNA stem-loop binding complex [GO:0062073]; nucleolus [GO:0005730] | identical protein binding [GO:0042802]; RNA binding [GO:0003723]; translation activator activity [GO:0008494] | PF02854; | 1.25.40.180; | MIF4GD family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18025107}. Nucleus {ECO:0000269|PubMed:18025107}. | null | null | null | null | null | FUNCTION: Functions in replication-dependent translation of histone mRNAs which differ from other eukaryotic mRNAs in that they do not end with a poly-A tail but a stem-loop. May participate in circularizing those mRNAs specifically enhancing their translation. {ECO:0000269|PubMed:18025107}. | Homo sapiens (Human) |
A9ULC7 | OSTA_XENTR | MDPEQNDTKPPFNPICATRQAPYSHEILENLDITGILLFAILTFMTLVSLLVFLEEAYYMYRKIPNPKNSIIIWINAGAMMIATTSCFGMWIPRSTMFTDFTASVFLAVLIHKFQLMLVNECGGRREFLSTFGDTKLKISTGPFCCCCLCLPHKDINRKTLFILKLGTFQFAFLRPVLMFLAVVLWTNGTYMIGNSSAEKATIWINIGVGITTITALWAVGIMFNLVKDNLKEKNIIGKFAVYQFTVILSQLQTSIINILGTTGVISCVPPLPGPSRASYMNQQLLIMEMFLVTVICRVLYRRRYDDKNLLENQETNDNL... | null | null | bile acid and bile salt transport [GO:0015721] | endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803] | PF03619; | null | OST-alpha family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=taurocholate(out) = taurocholate(in); Xref=Rhea:RHEA:71703, ChEBI:CHEBI:36257; Evidence={ECO:0000250|UniProtKB:Q90YM5}; CATALYTIC ACTIVITY: Reaction=prostaglandin E2(out) = prostaglandin E2(in); Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:Q90YM5}; CATALYTIC ACT... | null | null | null | null | FUNCTION: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for the translocation of bile acids (such as taurocholate), steroids (such as estrone sulfate), and eicosanoids (such as prostaglandin E2). {ECO:0000250|UniProtKB:Q90YM5}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A9ULR9 | BACD1_DANRE | MSAEASGSSGGHAVTVSGSSPSSSSHVGEEKPGRSLVSSKYVKLNVGGTLHYTTVQTLSKEDSLLRSICDGSTEVSIDSEGWVVLDRCGRHFSLVLNFLRDGTVPLPDSTRELEEVLKEAQYYRLQGLVQHCLSTLQKRRDVCRGCHIPMITSAKEEQRMIATCRKPVVKLQNNRGNNKYSYTSNSDDNLLKNIELFDKLGLRFNGRVLFIKDVLGDEICCWSFYGEGRKIAEVCCTSIVYATEKKQTKVEFPEARIFEETLNILIYENGRGSGGMALLESGGVSSSGAGQSEEEGAGAGGGDRRVRRIHVRRHIMHDER... | null | null | brain development [GO:0007420]; central nervous system projection neuron axonogenesis [GO:0021952]; head development [GO:0060322]; negative regulation of Rho protein signal transduction [GO:0035024]; neural precursor cell proliferation [GO:0061351]; positive regulation of apoptotic process [GO:0043065]; proteasome-medi... | Cul3-RING ubiquitin ligase complex [GO:0031463]; nucleus [GO:0005634] | ubiquitin-protein transferase activity [GO:0004842] | PF02214; | null | BACURD family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WZ19}. | null | null | null | null | null | FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for synaptic transmission (By similarity). The BCR(KCTD13) E3 ubiquitin ligase complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton a... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A9WCM4 | ENO_CHLAA | MSTLIEAIVAREVLDSRGNPTIEVDVRLESGDVGRAIVPSGASTGAHEALELRDGDKSRYNGKGVLKAVQAVNEDIAEALIGFDAADQIALDQELIALDGTPNKSKLGANAILGVSLAAAKAAAAAFGLPLYRYLGGVYAHVLPVPMMNIMNGGQHATNSTDFQEFMIMPVGAESFREGLRWGAEIYHMLKKVIHDRGFSTTVGDEGGFAPSLPTNDAPLQLIMEAIEKAGYRPGEQIVIALDPATTEIFEDGKYHLKREGRSLSSAEMVDYWVDLVNRYPIISLEDGLAEDDWEGWALLRAKLGDRVQLVGDDFLVTNV... | 4.2.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:26082925}; Note=Binds a second Mg(2+) ion via substrate during catalysis (PubMed:26082925). {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:26082925}; | glycolytic process [GO:0006096] | cell surface [GO:0009986]; extracellular region [GO:0005576]; phosphopyruvate hydratase complex [GO:0000015] | magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634] | PF00113;PF03952; | 3.20.20.120;3.30.390.10; | Enolase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000305|PubMed:26082925}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. {ECO:0000255|HAMAP-Rule:MF_00318}. | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:26082925}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165; Evidence={ECO... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=35 uM for 2-phosphoglycerate (2-PG) at 80 degrees Celsius {ECO:0000269|PubMed:26082925}; KM=158 uM for 2-PG at 25 degrees Celsius {ECO:0000269|PubMed:26082925}; Vmax=50 umol/min/mg enzyme for 2-PG at 80 degrees Celsius {ECO:0000269|PubMed:26082925}; Vmax=9 umol/min... | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00318}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5, thermostable up to 85 degrees Celsius, at 90 degrees it loses about 50% activity (PubMed:26082925). {ECO:0000269|PubMed:26082925}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80 degrees Celsius. {ECO:0000269|PubMed:26082925}; | FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP) (PubMed:26082925). It is essential for the degradation of carbohydrates via glycolysis. {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:26082925}. | Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl) |
A9WGE2 | CCL_CHLAA | MEAVTIVDVAPRDGLQNEPDVLEPATRVELIERLLAAGVPRIEIGSFVNPRQVPQMAGIDQIARMLIERGHNLAARTTNDLFRFTALVPNQRGYELAAAAGLRHVRLVLAASDGLNRANFKRTTAESLIEFSRFALNIRRDGLTFGVAIGAAFGCPFDGYVSPERVRAIAEHAVDIGAGEIILADTTGMAVPTQVAALCRTILDRIPDVTVTLHLHNTRNTGYANAFAAWQVGIRSFDAALGGIGGCPFAPRAVGNIASEDLVHLFNGLGVPTGIDLSALIAASDWLSATLGRPLPALVGKAGPVYPQVVSMAPYLS | 4.1.3.46 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17259315}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:17259315}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:17259315}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17259315}; No... | carbon fixation by 3-hydroxypropionate cycle [GO:0043427]; glyoxylate catabolic process [GO:0009436]; ketone body biosynthetic process [GO:0046951]; leucine catabolic process [GO:0006552] | null | (3R)-citramalyl-CoA lyase activity [GO:0044101]; hydroxymethylglutaryl-CoA lyase activity [GO:0004419]; metal ion binding [GO:0046872]; oxo-acid-lyase activity [GO:0016833]; transferase activity [GO:0016740] | PF00682; | 3.20.20.70; | HMG-CoA lyase family | null | null | CATALYTIC ACTIVITY: Reaction=(3R)-citramalyl-CoA = acetyl-CoA + pyruvate; Xref=Rhea:RHEA:38275, ChEBI:CHEBI:15361, ChEBI:CHEBI:57288, ChEBI:CHEBI:75637; EC=4.1.3.46; Evidence={ECO:0000269|PubMed:17259315}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=70 uM for (R)-citramalyl-CoA {ECO:0000269|PubMed:17259315}; Note=kcat is 1.7 sec(-1) for lyase activity with (R)-citramalyl-CoA as substrate.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7 (at 55 degrees Celsius). {ECO:0000269|PubMed:17259315}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:17259315}; | FUNCTION: Involved in the glyoxylate assimilation cycle used to regenerate acetyl-CoA and produce pyruvate as universal precursor for biosynthesis. Catalyzes the cleavage of (R)-citramalyl-CoA to yield acetyl-CoA and pyruvate. {ECO:0000269|PubMed:17259315}. | Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl) |
A9X1A0 | PI4KB_PAPAN | MGDTVVEPAPLKPTSEPTSGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVKLLRGGVAVSSRGTPLELVNGDGVDSEIRCLDDPPAQIREEEDEMGATVASGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHRKRELPSLSPAPDTGLSPSKRTHQRSKSDATASISLSSNLKRTASNPKVENEDEELSSSTESIDNSFSSPV... | 2.7.1.67 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; | inner ear development [GO:0048839]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310] | Golgi membrane [GO:0000139]; mitochondrial outer membrane [GO:0005741]; rough endoplasmic reticulum membrane [GO:0030867] | 1-phosphatidylinositol 4-kinase activity [GO:0004430]; 14-3-3 protein binding [GO:0071889]; ATP binding [GO:0005524] | PF00454;PF21245; | 1.10.1070.11; | PI3/PI4-kinase family, Type III PI4K subfamily | null | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Rough endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus {ECO:0000250}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.67; Evidence={ECO:0000250|... | null | null | null | null | FUNCTION: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation (By similarity). Involved in Golgi-to-plasma membrane traffickin... | Papio anubis (Olive baboon) |
A9XMT3 | CCLOP_LOTJA | MEGRGFSGLYRNSSEELFLKTVMESPIGMPVPSMEMLGFKNVSQGFRADSEELFKRWLTNGEGYNSSSIGFSSRLSKRISTELVNGSNQLQVGVASDGRNNDKPFIQNNLLANDVSGDFNFPIRDPVDRELQPSNLFLAKAWFLSDQRMTRSRSSELRRRYSEMQNGLATQGIESICMDPQHGAEATKQEVANFNGYNYLSMCELPSQKGSFMSPSNSCSSNFNTPQFGDMDKVSSCVSMLKGTLQRRRLSSQLEKEAAEDDLNGIFYPQEPLFQTGFDQGQENWSNQTPVNVQVDSIGEVKDHGVLQTLEGSTNPVVDG... | null | null | arbuscular mycorrhizal association [GO:0036377]; nodulation [GO:0009877]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; protein homodimerization activity [GO:0042803]; sequence-specific DNA binding [GO:0043565] | null | null | CYCLOPS family | PTM: Phosphorylated at the N-terminus by CCAMK. {ECO:0000269|PubMed:19074278}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19074278}. | null | null | null | null | null | FUNCTION: Involved in symbiotic signaling. Required for root infection by symbiotic rhizobia, infection thread (IT) formation, and nodule development (PubMed:19074278). Probably not involved in nodule organogenesis (PubMed:19074278). Involved in arbuscular mycorrhizal (AM) symbiosis (PubMed:19074278). Required for fung... | Lotus japonicus (Lotus corniculatus var. japonicus) |
A9YTQ3 | AHRR_HUMAN | MPRTMIPPGECTYAGRKRRRPLQKQRPAVGAEKSNPSKRHRDRLNAELDHLASLLPFPPDIISKLDKLSVLRLSVSYLRVKSFFQVVQEQSSRQPAAGAPSPGDSCPLAGSAVLEGRLLLESLNGFALVVSAEGTIFYASATIVDYLGFHQTDVMHQNIYDYIHVDDRQDFCRQLHWAMDPPQVVFGQPPPLETGDDAILGRLLRAQEWGTGTPTEYSAFLTRCFICRVRCLLDSTSGFLTMQFQGKLKFLFGQKKKAPSGAMLPPRLSLFCIAAPVLLPSAAEMKMRSALLRAKPRADTAATADAKVKATTSLCESELH... | null | null | xenobiotic metabolic process [GO:0006805] | aryl hydrocarbon receptor complex [GO:0034751]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; nuclear receptor activity [GO:0004879]; protein dimerization activity [GO:0046983]; transcription cis-regulatory region binding [GO:0000976] | PF00010;PF00989; | 4.10.280.10;3.30.450.20; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17980155}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:17980155}. Note=Predominantly in the nuclear compartment. First cytoplasmic, translocates into the nuclear compartment upon interaction with ARNT in the cytoplasmic compartment. | null | null | null | null | null | FUNCTION: Mediates dioxin toxicity and is involved in regulation of cell growth and differentiation. Represses the transcription activity of AHR by competing with this transcription factor for heterodimer formation with the ARNT and subsequently binding to the xenobiotic response element (XRE) sequence present in the p... | Homo sapiens (Human) |
A9YWR6 | STR2_MEDTR | MKTQGLELETVIDIKHKPVSFTGGLEFESLTYTVTKKKKVDGKWSNEDVDLLHDITGYAPKGCITAVMGPSGAGKSTLLDGLAGRIASGSLKGKVSLDGNSVNASLIKRTSAYIMQEDRLFPMLTVYETLMFAADFRLGPLSAVDKRQRVEKLIEQLGLSSSRNTYIGDEGTRGVSGGERRRVSIGVDIIHGPSLLFLDEPTSGLDSTSALSVIEKLHDIARNGSTVILTIHQPSSRIQLLLDHLIILARGQLMFQGSLKDVGHHLNRMGRKIPKGENPIENLIDVIQEYDQCDFVGVEVLAEFARTGMKPPLLSDMEEI... | 7.6.2.- | null | arbuscular mycorrhizal association [GO:0036377]; response to symbiotic fungus [GO:0009610]; transmembrane transport [GO:0055085] | membrane [GO:0016020]; periarbuscular membrane [GO:0085042]; plasma membrane [GO:0005886] | ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626] | PF01061;PF19055;PF00005; | 3.40.50.300; | ABC transporter superfamily, ABCG family, Stunted arbuscule (STR) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20453115}; Multi-pass membrane protein {ECO:0000255}. Note=Located in the peri-arbuscular membrane of arbuscular mycorrhiza (AM). {ECO:0000269|PubMed:20453115}. | null | null | null | null | null | FUNCTION: Together with STR, required for arbuscule development in arbuscular mycorrhizal symbiosis. {ECO:0000269|PubMed:20453115}. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
A9ZLX4 | RIPR2_COTJA | MSIGSHSFSPGGPNGIIRSQSFAGFSGLQERRSRCNSFIENTSALKKPQAKVKKMHNLGHKNSTTPKEPQPKRVEEVYRALKNGLDEYLEVHQTELDKLTAQLKDMRRNSRLGVLYDLDKQIKAVERYMRRLEFHISKVDELYEAYCIQRRLCDGASKMKQAFAMSPTSKAARESLTEINRSYKEYTENMCTIEAELENLLGEFCIKMKGLAGFARLCPGDQYEIFMRYGRQRWKLKGKIEVNGKQSWDGEEMVFLPLIVGLISIKVTEVKGLATHILVGSVTCETKDLFAARPQVVAVDINDLGTIKLNLEITWYPFDV... | null | null | cell adhesion [GO:0007155]; cell differentiation [GO:0030154]; cellular response to chemokine [GO:1990869]; chemotaxis [GO:0006935]; muscle organ development [GO:0007517]; negative regulation of cell adhesion [GO:0007162]; negative regulation of establishment of T cell polarity [GO:1903904]; negative regulation of prot... | apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; filopodium [GO:0030175]; stereocilium [GO:0032420]; stereocilium membrane [GO:0060171] | 14-3-3 protein binding [GO:0071889] | PF15903; | 1.25.10.10; | RIPOR family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17825087}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9Y4F9}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q9Y4F9}. Apical cell membrane {ECO:0000250|UniProtKB:Q7TP54}. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q80U16}. Cell projection, stereocil... | null | null | null | null | null | FUNCTION: Acts as an inhibitor of the small GTPase RHOA and plays several roles in the regulation of myoblast and hair cell differentiation, lymphocyte T proliferation and neutrophil polarization. Plays a role in fetal mononuclear myoblast differentiation by promoting filopodia and myotube formation (PubMed:17825087). ... | Coturnix japonica (Japanese quail) (Coturnix coturnix japonica) |
A9ZPH9 | GMAS_METMY | MKSLEEAQKFLEDHHVKYVLAQFVDIHGVAKVKSVPASHLNDILTTGAGFAGGAIWGTGIAPNGPDYMAIGELSTLSLIPWQPGYARLVCDGHVNGKPYEFDTRVVLKQQIARLAEKGWTLYTGLEPEFSLLKKDEHGAVHPFDDSDTLQKPCYDYKGITRHSPFLEKLTESLVEVGLDIYQIDHEDANGQFEINYTYADCLKSADDYIMFKMAASEIANELGIICSFMPKPFSNRPGNGMHMHMSIGDGKKSLFQDDSDPSGLGLSKLAYHFLGGILAHAPALAAVCAPTVNSYKRLVVGRSLSGATWAPAYIAYGNNN... | 6.3.1.6; 6.3.4.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17284842}; | glutamine biosynthetic process [GO:0006542]; polyamine catabolic process [GO:0006598] | null | ATP binding [GO:0005524]; glutamate-ethylamine ligase activity [GO:0047942]; glutamate-methylamine ligase activity [GO:0047943]; glutamine synthetase activity [GO:0004356] | PF00120; | 3.10.20.70;3.30.590.10; | Glutamine synthetase family, Type 3 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + methylamine = ADP + H(+) + N(5)-methyl-L-glutamine + phosphate; Xref=Rhea:RHEA:17117, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58200, ChEBI:CHEBI:59338, ChEBI:CHEBI:456216; EC=6.3.4.12; Evidence={ECO:0000269|PubMed:17284842,... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.18 mM for methylamine {ECO:0000269|PubMed:17284842}; KM=0.57 mM for ethylamine {ECO:0000269|PubMed:17284842}; KM=3.9 mM for hydroxylamine {ECO:0000269|PubMed:17284842}; KM=84 mM for ammonia {ECO:0000269|PubMed:17284842}; KM=1.4 mM for glutamic acid (with methylam... | null | null | null | FUNCTION: Catalyzes the formation of N(5)-methyl-L-glutamine from glutamate and methylamine. In vitro, can also use ethylamine, hydroxylamine and ammonia, with 75%, 40% and 1% activity compared to methylamine, respectively. {ECO:0000269|PubMed:17284842, ECO:0000269|PubMed:18175924}. | Methylovorus mays |
A9ZSZ2 | AGO3_BOMMO | MADPGKGRGRSLALLQALKKSQMMDSPSQSESQSPESTPEQSTAPSTIASATPSTSGVSIGGRGRAAALMLAKMQQKPGSTTPAIFVPPSSTSAPTAGTGRGFKLLQNLQASQKASSQIASSQVTSSAQSDIKDLTEKMSETSVSAQASSVAKNKYFREVKDTPPVVKKGETGVPIEVTCNYIYLNFKENIVFEYEVKFEPDQDYKHLRFKLLNEHIEHFKEKTFDGTTLYVPHELPDAVRNLVSTNPYDQSKVNVSIIFRRTRRLSEMIHIYNVMFKCIMKDLKLIRFGRQHYNEHAAIQIPQHKLEVWPGYVTAVDEY... | 3.1.26.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A8D8P8}; | cell differentiation [GO:0030154]; meiotic cell cycle [GO:0051321]; regulatory ncRNA-mediated gene silencing [GO:0031047]; spermatogenesis [GO:0007283] | P granule [GO:0043186] | metal ion binding [GO:0046872]; piRNA binding [GO:0034584]; RNA endonuclease activity [GO:0004521] | PF02170;PF02171; | 3.40.50.2300;2.170.260.10;3.30.420.10; | Argonaute family, Piwi subfamily | PTM: Arginine methylation is required for the interaction with Tudor domain-containing protein Papi/TDRKH. {ECO:0000269|PubMed:23970546}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25558067}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. {ECO:0000269|PubMed:25558067}. | null | null | null | null | null | FUNCTION: Endoribonuclease that plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity (PubMed:19460866). Plays an essential role in meiotic differentiation of spermatocytes, germ cell differentiation and in self-r... | Bombyx mori (Silk moth) |
B0B9A0 | CDUB1_CHLT2 | MLSPTNSTSKTAPVPPRDSSKPVLISEEPRNQLLQKVARTALAVLLVVVTLGLILLFYSFSDLQSFPWCCQTHPSTKEQPTISIPVPLPSPPLAVPRPSTPPPPVISRPSTPSAPKPSTPPPLLPKAPKPVKTQEDLLPLVPEQVFVEMYEDMARRQTIEALVPAWDSDIIFKCLCYFHTLYPGLIPLETFPPATIFNFKQKIISILEDKKAVLRGEPIKGPLPICCSKENYRRHLQRTTLLPVFMWYHPTPKTLSDTMQTMKQLAIKGSVGASHWLLVIVDIQARRLVYFDSLYNYVMPPENMKKELQSFAQQLDQVYP... | 3.4.22.- | null | protein deneddylation [GO:0000338]; protein desumoylation [GO:0016926]; protein deubiquitination [GO:0016579]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; host cell [GO:0043657]; membrane [GO:0016020] | cysteine-type deubiquitinase activity [GO:0004843]; deNEDDylase activity [GO:0019784]; deSUMOylase activity [GO:0016929] | PF02902; | null | Peptidase C48 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18503636}. Host cell {ECO:0000269|PubMed:18503636}. Membrane {ECO:0000269|PubMed:18503636}; Single-pass membrane protein {ECO:0000269|PubMed:18503636}. Note=Secreted, and delivered into the host cell. Located predominantly on the plasma membrane and to a lesser extent ... | null | null | null | null | null | FUNCTION: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protease possesses deubiquitinating and deneddylating activities (By similarity). Impairs ubiquitination and degradation of NF-kappa-B inhibitor alpha (NFKBIA), thereby preventing NF-kappa-B activatio... | Chlamydia trachomatis serovar L2 (strain ATCC VR-902B / DSM 19102 / 434/Bu) |
B0BF33 | PKP2_DANRE | MLKPHPEHKEQPQDSFTPSGDSTPDASMAEERDFMRSVLPVYDSFHPEDSSLALPLANKLTLADAHRLNRLQQQVQLTLSRKKRKPKPADSSLAESQSSCQISSSSSLGSLHLKRTFSVNHEATRSLRMVDRSQWPSMEPPLFHRGYGSFRYTPKRAGLCLGSNSLTLPSAPTTSHFQMNKLPLRYAHSEVLRNPRFAGLSAATQIPSSPVYENPHTDDTDDVFLPSTSVERGRMESEKHTLQQTLCKQREGGFVALEQSENVSWQSRVRKPSLEFVAGRRPSQTGSLISMEEQSGSLGRIEKLEVKQHAVTTLTKKGKP... | null | null | cell-cell adhesion [GO:0098609]; cell-cell junction assembly [GO:0007043]; cell-cell signaling involved in cardiac conduction [GO:0086019]; desmosome organization [GO:0002934]; heart development [GO:0007507]; heart looping [GO:0001947]; intermediate filament bundle assembly [GO:0045110]; protein localization to plasma ... | adherens junction [GO:0005912]; cytoplasm [GO:0005737]; desmosome [GO:0030057]; intercalated disc [GO:0014704]; intermediate filament [GO:0005882]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | alpha-catenin binding [GO:0045294]; cadherin binding [GO:0045296]; intermediate filament binding [GO:0019215]; molecular adaptor activity [GO:0060090]; protein kinase C binding [GO:0005080] | PF00514; | 1.25.10.10; | Beta-catenin family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99959}. Cell junction, desmosome {ECO:0000250|UniProtKB:Q99959}. Cell junction {ECO:0000250|UniProtKB:Q99959}. Cytoplasm {ECO:0000250|UniProtKB:Q99959}. | null | null | null | null | null | FUNCTION: Required for development of the heart, potentially via cell-cell adhesion and modulation of expression of cardiac precursor genes (PubMed:23124967). Plays a role in desmosome cell-cell junctions and their intracellular connectivity (PubMed:23124967). {ECO:0000269|PubMed:23124967}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B0BK71 | MSP1_MYCSO | MKLFSASVFAAIIASHYASATAHIRAPNVKPRRTNSLLTAPPQQPPLPSAQQAASASSSAGLNLTDIQGDILIGMKKNKELFFFFSITDAATFKAKLGSDILELITSTNQLLAVATQPITAVNVAFSSTGLKALGITDDLKDPVFEAGMLSNAVSDLSDPGTGNWVPGFVGTSVHGVFLLASDTIDNVNTELANIQTILNGSITEIHRLQGEARPGDQQGHEHFGFMDGISNPAVDGFTPPAEIRPGQALIPPGIMLLGEANDTFQNDRPPWAKDGSFLVFRQMQQRAPEFNKFLQDHALNMPNMTSEQGADLLGARIVG... | 1.11.1.19; 1.11.1.7 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P31545, ECO:0000269|PubMed:18038130}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently per monomer. {ECO:0000250|UniProtKB:P31545, ECO:0000269|PubMed:18038130}; | carotene catabolic process [GO:0016121] | cytosol [GO:0005829]; extracellular region [GO:0005576] | heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601] | PF21105;PF20628; | null | DyP-type peroxidase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18038130}. | CATALYTIC ACTIVITY: Reaction=2 H2O2 + Reactive Blue 5 = 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H(+) + 2 H2O + phthalate; Xref=Rhea:RHEA:28086, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:17563, ChEBI:CHEBI:63950, ChEBI:CHEBI:63955, ChEBI:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 uM for H(2)O(2) {ECO:0000269|PubMed:23111597}; | null | null | null | FUNCTION: Manganese-independent peroxidase that is able to convert a large number of compounds, but its physiological substrate is not known (PubMed:23111597). In addition to classic peroxidase substrates (e.g. 2,6-dimethoxyphenol), oxidizes dyes such as Reactive Blue 5 (PubMed:23111597). Also degrades beta-carotene (P... | Mycetinis scorodonius (Garlic mushroom) (Marasmius scorodonius) |
B0BK72 | MSP2_MYCSO | MRLTYLPLFAGIAIQSASALPDFFKSSVLKPRRTNSLLINPDAQPDLPTAQQASTAAASVGLNLTDIQGDILIGMKKNKEMFFFFSIADATAFKSHLDSAILPLITSTQQLLTVATQPTTAVNLAFSQTGLNALGLASQGLGDSLFASGQFSGAESLGDPGTSNWVQAFAGTGIHGVFLLASDTIDNVNAELSQIQSILGTSITEAYRLQGEARPDDQQGHEHFGFMDGISNPAIDGFSTALPGQAVLSPGLFLLAEDGDGSSSSRPSWAKDGSLLAFRQLQQRVPEFNKFLADNAALTQGNADLLGARMMGRWKSGAPV... | 1.11.1.- | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255, ECO:0000269|PubMed:18038130}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently per monomer. {ECO:0000255, ECO:0000269|PubMed:18038130}; | carotene catabolic process [GO:0016121] | cytosol [GO:0005829] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601] | PF21105;PF20628; | null | DyP-type peroxidase family | null | null | null | null | null | null | null | FUNCTION: Peroxidase capable of degrading beta-carotene. {ECO:0000269|PubMed:18038130}. | Mycetinis scorodonius (Garlic mushroom) (Marasmius scorodonius) |
B0BLU1 | RN168_XENTR | MAKVQKLPLPWSECICPICQEILLEPVTLPCKHTLCNPCFQMTVEKASLCCPFCRKRVSTWARQHSRTRTLVNKELWEVIQKQYPKQCQRRASGQESDDLSDELTSCPVPVLCKPGEIRQEYEAEVSKIEAERTAQEEAERKASEDYIQKLLAEEEAEENLHAEASQREIEEQLKRDEELARLLSGDMDLSNASCTSVSPVTSKKVVSKSSKIVKSKQRVSGDIERFLSPKPRRALAAFGINESRNSDTSGSCILLDEDEDEIPDLSPQCPSTSLIQERDVELPMPYLPNCYKLESDAASQQDSCSERNDICNGTYSCSD... | 2.3.2.27 | null | DNA damage response [GO:0006974]; DNA repair-dependent chromatin remodeling [GO:0140861]; double-strand break repair [GO:0006302]; isotype switching [GO:0045190]; negative regulation of transcription elongation by RNA polymerase II [GO:0034244]; positive regulation of DNA repair [GO:0045739]; protein K63-linked ubiquit... | nucleus [GO:0005634]; site of double-strand break [GO:0035861]; ubiquitin ligase complex [GO:0000151] | chromatin binding [GO:0003682]; histone binding [GO:0042393]; K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; metal ion binding [GO:0046872]; nucleosome binding [GO:0031491]; ubiquitin binding [GO:0043130]; ubiquitin-protein transferase activity [GO:0004842] | PF00097; | 3.30.40.10; | RNF168 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03066}. Note=Localizes to double-strand breaks (DSBs) sites of DNA damage. {ECO:0000255|HAMAP-Rule:MF_03066}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000255|HAMAP-Rule:MF_03066}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|HAMAP-Rule:MF_03066}. | null | null | FUNCTION: E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with ube2n/ubc13 to amplify the rnf8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and ubiquitinates histone H2A and... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
B0BLW3 | LGR4_XENTR | MGCPGWPLALFALLLASCSGGPSGVSSPAPCPAPCACDLDGGADCSGKGLVTVPDGLSVFTHSLDLSMNNITKLPEGAFKGFPYLEELRLAGNDLSIIHPMALSGLKELKVLTLQNNQLKTVPSESLKGLVSLQSLRLDANHIVTVPEDSFEGLVQLRHLWLDDNSLTEVPIRPLSNLPSLQALTLALNKISHIPDYAFSNLSSLVVLHLHNNKIRTLGPHCFHGLDNLEALDLNYNNLIDFPDSIRSLPNLKELGFHSNSITIIPDGAFVKNPLLRTIHLYDNPLSFVGNSAFQNLSDLHFLIIRGASNVQWFPNLTGT... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; bone mineralization [GO:0030282]; bone remodeling [GO:0046849]; hormone-mediated signaling pathway [GO:0009755]; negative regulation of cytokine production [GO:0001818]; negative regulation of toll-like receptor signaling pathway [G... | plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; protein-hormone receptor activity [GO:0016500]; transmembrane signaling receptor activity [GO:0004888] | PF00001;PF13855; | 1.20.1070.10;3.80.10.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BXB1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BXB1}. | null | null | null | null | null | FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and is involved in the formation of various organs. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering t... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
B0BMY1 | LAAT1_RAT | MVWRTLVASNFSTCPNGSIQWIWDVFGECAQDGWDEASVALGLVSIFCFAASTFPQYIKACKTGNMDQALSLWFLLGWIGGDSCNLIGSFLADQLPLQTYTAVYYVLADLLMLTLYFHYKFKKQPSLLSAPINSVLLFILGTVCITPLLSSTDPVAVPREGFRGRTLLSVEPGNKPFTKKEVVGFVIGSASSVLYLLSRLPQIRTNFVRQSTQGISYSLFALVMLGNTLYGLSVLLKNPEVGQSEGSYLLHHLPWLVGSLGVLLLDTIISIQFLVYRSHDADAASEREPLLPS | null | null | intracellular amino acid homeostasis [GO:0080144]; L-arginine transmembrane transport [GO:1903826]; lysine transport [GO:0015819] | lysosomal membrane [GO:0005765]; organelle membrane [GO:0031090] | basic amino acid transmembrane transporter activity [GO:0015174]; L-arginine transmembrane transporter activity [GO:0061459]; L-lysine transmembrane transporter activity [GO:0015189] | PF04193; | 1.20.1280.290; | Laat-1 family | null | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:23169667}; Multi-pass membrane protein {ECO:0000269|PubMed:23169667}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.36 mM for arginine {ECO:0000269|PubMed:23169667}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is acidic with no activity detected at a pH higher that 7.0. {ECO:0000269|PubMed:23169667}; | null | FUNCTION: Amino acid transporter that specifically mediates the pH-dependent export of the cationic amino acids arginine, histidine and lysine from lysosomes. {ECO:0000269|PubMed:23169667}. | Rattus norvegicus (Rat) |
B0BND0 | ENPP6_RAT | MAGKLWTFLLLFGFSWVWPASAHRKLLVLLLDGFRSDYISEDALASLPGFREIVNRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPRTNKSFDIGVNRDSLMPLWWNGSEPLWITLMKARRKVYMYYWPGCEVEILGVRPTYCLEYKNVPTDINFANAVSDALDSLKSGRADLAAIYHERIDVEGHHYGPSSPQRKDALKAVDTVLKYMTQWIQERGLQNDLNVILFSDHGMTDIFWMDKVIELSKYISLDDLQQVKDQGPVVSLWPVPEKHSEIYHKLRTVEHMTVYEKEAIPNRFYYKKGKFVSPLT... | 3.1.4.-; 3.1.4.38 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q8BGN3}; | choline metabolic process [GO:0019695]; lipid catabolic process [GO:0016042]; lipid metabolic process [GO:0006629] | extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | glycerophosphocholine cholinephosphodiesterase activity [GO:0047390]; glycerophosphodiester phosphodiesterase activity [GO:0008889]; metal ion binding [GO:0046872]; phosphoric diester hydrolase activity [GO:0008081] | PF01663; | 3.30.1360.180;3.40.720.10; | Nucleotide pyrophosphatase/phosphodiesterase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=H2O + sn-glycerol 3-phosphocholine = glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:19545, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:17754, ChEBI:CHEBI:295975; EC=3.1.4.38; Evidence={ECO:0000250|UniProtKB:Q8BGN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:... | null | null | null | null | FUNCTION: Choline-specific glycerophosphodiesterase that hydrolyzes glycerophosphocholine (GPC) and lysophosphatidylcholine (LPC) and contributes to supplying choline to the cells. Has a preference for LPC with short (12:0 and 14:0) or polyunsaturated (18:2 and 20:4) fatty acids. In vitro, hydrolyzes only choline-conta... | Rattus norvegicus (Rat) |
B0BNF1 | SEPT8_RAT | MAATDLERISNAEPEPRSLSLGGHVGFDSLPDQLVSKSVTQGFSFNILCVGETGIGKSTLMNTFFNTTFETEEASHHEECVRLRPQTYDLQESNVHLKLTIVDAVGFGDQINKDDSYRPIVDYIDTQFENYLQEELKIRRSLFDYHDTRIHVCLYFITPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTISKSELHKFKIKIMGELVSNGVQIYQFPTDDEAVAEINAVMNAHLPFAVVGSTEEVKVGNKLVRARQYPWGVVQVENENHCDFVKLREMLIRVNMEDLREQTHSRHYELYRRCKLEEMGFQDSDGDSQPF... | null | null | cytoskeleton-dependent cytokinesis [GO:0061640]; regulation of intracellular protein transport [GO:0033157]; regulation of protein stability [GO:0031647]; regulation of SNARE complex assembly [GO:0035542] | axon [GO:0030424]; cell division site [GO:0032153]; microtubule cytoskeleton [GO:0015630]; myelin sheath [GO:0043209]; presynapse [GO:0098793]; septin complex [GO:0031105]; septin ring [GO:0005940]; synaptic vesicle membrane [GO:0030672] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; molecular adaptor activity [GO:0060090]; SNARE binding [GO:0000149] | PF00735; | 3.40.50.300; | TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Septin GTPase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19196426}. Cytoplasm, cytoskeleton {ECO:0000250}. Synapse {ECO:0000269|PubMed:19196426}. Cell projection, axon {ECO:0000269|PubMed:19196426}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000305|PubMed:19196426}. Presynapse {ECO:0000269|PubMe... | null | null | null | null | null | FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in platelet secretion (By similarity). Seems to participate in the process of SNARE complex formation in synaptic vesicles (PubMed:19196426). {ECO:0000250|UniProtKB:Q92599, ECO:0000269|PubMed:19196426}. | Rattus norvegicus (Rat) |
B0BNF9 | HAOX1_RAT | MLPRLVCISDYEQHARTVLQKSVYDYYKSGANDQETLADNIRAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALRWMQLYIYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNRFKLPPQLRMKNFETNDLAFSPKGNFGDNSGLAEYVAQAIDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGARAVFVGRPIIWG... | 1.1.3.15; 1.2.3.5 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:Q9UJM8}; | fatty acid alpha-oxidation [GO:0001561]; glycine biosynthetic process [GO:0006545]; glycolate catabolic process [GO:0046296]; response to oxidative stress [GO:0006979] | peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777] | (S)-2-hydroxy-acid oxidase activity [GO:0003973]; FMN binding [GO:0010181]; glyoxylate oxidase activity [GO:0047969] | PF01070; | 3.20.20.70; | FMN-dependent alpha-hydroxy acid dehydrogenase family | null | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000305|PubMed:10777549}. | CATALYTIC ACTIVITY: Reaction=a (2S)-2-hydroxycarboxylate + O2 = a 2-oxocarboxylate + H2O2; Xref=Rhea:RHEA:16789, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:35179, ChEBI:CHEBI:58123; EC=1.1.3.15; Evidence={ECO:0000250|UniProtKB:Q9UJM8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16790; Evidence={ECO:000... | null | PATHWAY: Amino-acid biosynthesis; glycine biosynthesis. {ECO:0000250|UniProtKB:Q9UJM8}. | null | null | FUNCTION: Broad substrate specificity (S)-2-hydroxy-acid oxidase that preferentially oxidizes glycolate. The glyoxylate produced by the oxidation of glycolate can then be utilized by alanine-glyoxylate aminotransferase for the peroxisomal synthesis of glycine; this pathway appears to be an important step for the detoxi... | Rattus norvegicus (Rat) |
B0BNK7 | LRFN3_RAT | MAVLPLLLCLLPLAPASSPPQPATSSPCPRRCRCQTQSLPLSVLCPGAGLLFVPPSLDRRAAELRLADNFIAAVRRRDLANMTGLLHLSLSRNTIRHVAAGAFADLRALRALHLDGNRLTSLGEGQLRGLVNLRHLILSNNQLAALAAGALDDCAETLEDLDLSYNNLEQLPWEALGRLGNVNTLGLDHNLLASVPAGAFSRLHKLARLDMTSNRLTTIPPDPLFSRLPLLARPRGSPASALVLAFGGNPLHCNCELVWLRRLAREDDLEACASPPALGGRYFWAVGEEEFVCEPPVVTHRSPPLAVPAGRPAALRCRAV... | null | null | regulation of presynapse assembly [GO:1905606]; regulation of synaptic membrane adhesion [GO:0099179]; synaptic membrane adhesion [GO:0099560] | axon [GO:0030424]; cell surface [GO:0009986]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; postsynaptic density membrane [GO:0098839]; postsynaptic specialization membrane [GO:0099634]; presynaptic active zone membrane [GO:0048787] | null | PF00041;PF07679;PF13855; | 2.60.40.10;3.80.10.10; | LRFN family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BLY3}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18227064}; Single-pass type I membrane protein {ECO:0000269|PubMed:18227064}. Cell projection, axon {ECO:0000269|PubMed:18227064}. Cell projection, dendrite {ECO:0000269|PubMed:18227064}. Synapse {ECO:0000269|PubMed:18227064}. Presynaptic cell membrane {ECO:000026... | null | null | null | null | null | FUNCTION: Cell adhesion molecule that mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Promotes neurite outgrowth in hippocampal neurons (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
B0BNM1 | NNRE_RAT | MSGLRTLLGLGLLVAGSRLPRIASRQSVCRAGPIWWGTQHRSSETMASAAVKYLSQEEAQAVDEELFNEYQFSVDQLMELAGLSCATAIAKAYPPTSMSKSPPTVLVICGPGNNGGDGLVCARHLKLFGYQPTIYYPKRPNKPLFTGLVTQCQKMDIPFLGEMPPEPMMVDELYELVVDAIFGFSFKGDVREPFHSILSVLSGLTVPIASIDIPSGWDVEKGNPSGIQPDLLISLTAPKKSATQFTGRYHYLGGRFVPPALEKKYQLNLPAYPDTECVYRLQ | 5.1.99.6 | COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP-Rule:MF_03159}; Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03159}; | lipid transport [GO:0006869]; membrane raft distribution [GO:0031580]; negative regulation of angiogenesis [GO:0016525]; nicotinamide nucleotide metabolic process [GO:0046496]; regulation of cholesterol efflux [GO:0010874]; sprouting angiogenesis [GO:0002040] | cell body [GO:0044297]; cilium [GO:0005929]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; mitochondrion [GO:0005739] | identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; NADHX epimerase activity [GO:0052856]; NADPHX epimerase activity [GO:0052857]; nucleotide binding [GO:0000166] | PF03853; | 3.40.50.10260; | NnrE/AIBP family | PTM: Undergoes physiological phosphorylation during sperm capacitation, downstream to PKA activation. {ECO:0000255|HAMAP-Rule:MF_03159}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03159}. Secreted {ECO:0000255|HAMAP-Rule:MF_03159}. Note=In sperm, secretion gradually increases during capacitation. {ECO:0000255|HAMAP-Rule:MF_03159}. | CATALYTIC ACTIVITY: Reaction=(6R)-NADHX = (6S)-NADHX; Xref=Rhea:RHEA:32215, ChEBI:CHEBI:64074, ChEBI:CHEBI:64075; EC=5.1.99.6; Evidence={ECO:0000250|UniProtKB:Q8NCW5}; CATALYTIC ACTIVITY: Reaction=(6R)-NADPHX = (6S)-NADPHX; Xref=Rhea:RHEA:32227, ChEBI:CHEBI:64076, ChEBI:CHEBI:64077; EC=5.1.99.6; Evidence={ECO:0000250|U... | null | null | null | null | FUNCTION: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. Accelerates cholesterol efflux from endothe... | Rattus norvegicus (Rat) |
B0CM99 | HMGB1_CALJA | MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEEDEEDEEDEEEEEDEEDEDEEEDDDDE | null | null | adaptive immune response [GO:0002250]; autophagy [GO:0006914]; chemotaxis [GO:0006935]; DNA geometric change [GO:0032392]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; positive regulation of response to external stimulus [GO:0032103]; ... | chromosome [GO:0005694]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endosome [GO:0005768]; extracellular region [GO:0005576]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | bubble DNA binding [GO:0000405]; DNA binding, bending [GO:0008301]; four-way junction DNA binding [GO:0000400]; non-sequence-specific DNA binding, bending [GO:0044378]; supercoiled DNA binding [GO:0097100] | PF00505;PF09011; | 1.10.30.10; | HMGB family | PTM: Phosphorylated at serine residues. Phosphorylation in both NLS regions is required for cytoplasmic translocation followed by secretion. {ECO:0000250|UniProtKB:P09429}.; PTM: Acetylated on multiple sites upon stimulation with LPS (By similarity). Acetylation on lysine residues in the nuclear localization signals (N... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09429}. Chromosome {ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}. Cytoplasm {ECO:0000250|UniProtKB:P09429}. Secreted {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}. Cell membrane {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P6315... | null | null | null | null | null | FUNCTION: Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stabi... | Callithrix jacchus (White-tufted-ear marmoset) |
B0D6H2 | ARO1_LACBS | MANADVLKVSILGKESIHCGFHLIPYIAQTVLSNLPSSTYVLVTDTNVANFHLTAFEKEFEQRISSLPTSSTKPRFLSLVIPPGETSKSREGKANIEDFLLLHRCTRDSVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGAFWQPEYIFIDAAFLETLPSREFSNGMAEVVKTAAIWNEAEFISLESRSADIFAAIQTPSADYAGRSKQTRSIAQELLLSVIVGSISVKAHIVTIDERETGLRNLVNFGHTIGHAIEAVLTPTILHGECVSVGMILEGEISRQMGILSQVGVG... | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:000476... | PF01761;PF01487;PF00275;PF18317;PF01488;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver) (Laccaria laccata var. bicolor) |
B0EXJ8 | HTOMT_CATRO | MDVQSEEFRGAQAQIWSQSCSFITSASLKCAVKLGIPDTIDNHGKPITLSELTNALVPPVHPSKAPFIYRLMRVLAKNGFCSEEQLDGETEPLYSLTPSSRILLKKEPLNLRGIVLTMADPVQLKAWESLSDWYQNEDDSSTAFETAHGKNFWGYSSEHMEHAEFFNEAMASDSQLISKLLIGEYKFLFEGLASLVDIGGGTGTIAKAIAKNFPQLKCTVFDLPHVVANLESKENVEFVAGDMFEKIPSANAIFLKWILHDWNDEDCVKILKSCKKAIPAKGGKVIIIDMVMYSDKKDDHLVKTQTSMDMAMLVNFAAKE... | 2.1.1.94 | null | alkaloid biosynthetic process [GO:0009821]; aromatic compound biosynthetic process [GO:0019438]; methylation [GO:0032259] | cytoplasm [GO:0005737] | 11-O-demethyl-17-O-deacetylvindoline O-methyltransferase activity [GO:0030766]; O-methyltransferase activity [GO:0008171]; protein homodimerization activity [GO:0042803] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family, COMT subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21047699}. | CATALYTIC ACTIVITY: Reaction=16-hydroxytabersonine + S-adenosyl-L-methionine = 16-methoxytabersonine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:20992, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58239, ChEBI:CHEBI:58930, ChEBI:CHEBI:59789; EC=2.1.1.94; Evidence={ECO:0000269|PubMed:18053006}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.6 uM for 16-hydroxytabersonine {ECO:0000269|PubMed:18053006}; KM=21.7 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:18053006}; Vmax=0.58 mmol/sec/mg enzyme toward 16-hydroxytabersonine {ECO:0000269|PubMed:18053006}; Vmax=0.79 mmol/sec/mg enzyme toward S-aden... | PATHWAY: Alkaloid biosynthesis; vindoline biosynthesis. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:18053006}; | null | FUNCTION: 16-O-methyltransferase involved in the biosynthesis of vindoline. Highly specific for 16-hydroxytabersonine. No activity with tabersonine, 3-hydroxytyramine, 4-hydroxytyramine, 5-hydroxytryptamine (5HT), 2,3-dihydro-3-hydroxytabersonine, lochnericine, hoerhammericine, 16-hydroxy-2,3-dihydro-3-hydroxytabersoni... | Catharanthus roseus (Madagascar periwinkle) (Vinca rosea) |
B0F0H3 | MKRN2_XENLA | MSPKQVTCRYFLHGVCREGSRCLFSHDLATSKPSTVCRFFLRGQCAYGTRCRYDHVKPCNGTVFIPPQEMSPVLSPPPLFPAQEAAVPPTIPAPQRREKKTLVLRDRDLCGASVDPALQPGCITESQGSEGEAKPHSYLEAICTGLDESQDPASYPGAPQQLCPFAQAGECHCGDSCPYLHGDACEICGLQVLHPHDQEQRRDHEKLCMENFELDMERAFAVQASEGRVCSICMERVYEKQSPAQRRFRILSDCNHTYCLTCIRQWRCARQFDNPVIKSCPECRVISEFVIPSAYWVEDQSKKDELIEAFKQGMGKKLCK... | 2.3.2.27 | null | axis specification [GO:0009798]; cell differentiation [GO:0030154]; DNA-templated transcription [GO:0006351]; embryo development ending in birth or egg hatching [GO:0009792]; negative regulation of inflammatory response to antigenic stimulus [GO:0002862]; negative regulation of neurogenesis [GO:0050768]; negative regul... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630] | PF00642;PF14608;PF18044;PF13445; | 4.10.1000.10;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ERV1}. Nucleus {ECO:0000250|UniProtKB:Q9ERV1}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9ERV1}; | null | null | null | null | FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (By similarity). Inhibits neurogenesis and axis formation during embryonic development by modulating the phosphatidylinositol 3-kinase (PI3K) pathway (PubMed:18198183). Acts downstream of PI3K and akt1 to up-r... | Xenopus laevis (African clawed frog) |
B0F2B4 | NLGN4_MOUSE | MPAPVPALLCLALALASAQPSPPPPPPFPVVATNYGKLRGVRAALPGDVLGPVTQFLGVPYAAPPTGERRFQPPEPPSSWAGVRDATRFAPVCPQHLDERALLRDCLPAWFAANLDAIAAYVQDQSEDCLYLNLYVPGGANGKKMADDVTGNDHGDDQDSRDPGVGGAAAAAARKPVMVYIHGGSYMEGTANIVDGSVLASYGDVIVVTVNYRLGVLGFLSTGDQAAKGNYGLLDQIQALRWVEENAGAFGGDPDRVTVFGSGAGASCVSLLTLSHYSEGLFQKAIIQSGTALSSWAVNYQPARYARALGERVGCATPDP... | null | null | brainstem development [GO:0003360]; cerebellum development [GO:0021549]; chemical synaptic transmission [GO:0007268]; male courtship behavior [GO:0008049]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of excitatory postsynaptic potential [GO:0090394]; neuron cell-cell adhesion [GO:0007... | cell surface [GO:0009986]; dendrite [GO:0030425]; excitatory synapse [GO:0060076]; glycinergic synapse [GO:0098690]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; postsynaptic specialization membrane [GO:0099634]; presynapse [GO:0098793]; synapse [GO:0045202] | neurexin family protein binding [GO:0042043]; signaling receptor activity [GO:0038023] | PF00135; | 3.40.50.1820; | Type-B carboxylesterase/lipase family | null | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Postsynaptic cell membrane. Note=Detected at glycinergic postsynapses in retina. Detected on dendritic spines on cultured neurons. | null | null | null | null | null | FUNCTION: Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in the formation or maintenance of synaptic junctions via its interactions (via the extracellular domains) with neurexin family members. Plays a role in synaptic signal transmission. {ECO:00... | Mus musculus (Mouse) |
B0F481 | BIODA_ARATH | MIPVTATLIRHRLRHLRHRIRFKSTSVSPFHLPLNHPTYLIWSANTSLGKTLVSTGIAASFLLQQPSSSATKLLYLKPIQTGFPSDSDSRFVFSKLDSLSLRRQIPISISNSVLHSSLPAAKSLGLNVEVSESGMCSLNFRDEKTVTGAPELLCKTLYAWEAAISPHLAAERENATVEDSVVLQMIEKCLKEEMECGVKSEKSDLLCLVETAGGVASPGPSGTLQCDLYRPFRLPGILVGDGRLGGISGTIAAYESLKLRGYDIAAVVFEDHGLVNEVPLTSYLRNKVPVLVLPPVPKDPSDDLIEWFVESDGVFKALKE... | 2.6.1.62; 6.3.3.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22547782}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:22547782}; | biotin biosynthetic process [GO:0009102] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | adenosylmethionine-8-amino-7-oxononanoate transaminase activity [GO:0004015]; ATP binding [GO:0005524]; dethiobiotin synthase activity [GO:0004141]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170] | PF13500;PF00202; | 3.90.1150.10;3.40.50.300;3.40.640.10; | Dethiobiotin synthetase family; Class-III pyridoxal-phosphate-dependent aminotransferase family, BioA subfamily | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:22547782}. | CATALYTIC ACTIVITY: Reaction=(7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate; Xref=Rhea:RHEA:15805, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:149469, ChEBI:CHEBI:149473, ChEBI:CHEBI:456216; EC=6.3.3.3; Evidence={ECO:0000269|PubMe... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat is 0.072 min(-1) for 7,8-diamino-pelargonic acid aminotransferase + dethiobiotin synthetase activities, and 1.85 min(-1) for 7,8-diamino-pelargonic acid aminotransferase activity only (at pH 7.5 and 30 degrees Celsius). {ECO:0000269|PubMed:22547782}; | PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2. {ECO:0000269|PubMed:22547782}.; PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1. {ECO:0000269|PubMed:22547782}. | null | null | FUNCTION: Bifunctional enzyme that catalyzes two different reactions involved in the biotin biosynthesis. {ECO:0000269|PubMed:12644697, ECO:0000269|PubMed:17993549, ECO:0000269|PubMed:22547782, ECO:0000269|PubMed:23031218}.; FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 betw... | Arabidopsis thaliana (Mouse-ear cress) |
B0F9L4 | GOGC6_ARATH | MDLASRYKGVVGMVFGDNQSSNEDSYIQRLLDRISNGTLPDDRRTAIVELQSVVAESNAAQLAFGAAGFPVIVGILKDQRDDLEMVRGALETLLGALTPIDHARAQKTEVQAALMNSDLLSREAENITLLLSLLEEEDFYVRYYTLQILTALLMNSQNRLQEAILTTPRGITRLMDMLMDREVIRNEALLLLTHLTREAEEIQKIVVFEGAFEKIFSIIKEEGGSDGDVVVQDCLELLNNLLRSSSSNQILLRETMGFEPIISILKLRGITYKFTQQKTVNLLSALETINMLIMGRADTEPGKDSNKLANRTVLVQKKLL... | null | null | endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; Golgi vesicle docking [GO:0048211]; post-embryonic development [GO:0009791]; protein exit from endoplasmic reticulum [GO:0032527]; transcytosis [GO:0045056]; vesicle fusion with Golgi apparatus [GO:0048280] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795] | null | PF04871;PF04869; | 1.25.10.10; | null | null | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:18182439}. Golgi apparatus, Golgi stack {ECO:0000269|PubMed:20837504}. Note=Concentrates only on one side of the Golgi bodies. {ECO:0000269|PubMed:18182439}. | null | null | null | null | null | FUNCTION: Golgi matrix protein playing a role in tethering of vesicles to Golgi membranes and in maintaining the overall structure of the Golgi apparatus. Functions in the anterograde transport of storage protein precursors from the endoplasmic reticulum (ER) to the Golgi complex. {ECO:0000269|PubMed:20837504}. | Arabidopsis thaliana (Mouse-ear cress) |
B0F9W3 | GPER1_MICUN | MEEQTTSLVWIYVNSTEQLNTSYEYNTTYLIEDSDKYQSYVIGLFLSCLYTILLFPIGFIGNILILVVNLNHRGKMAIPDLYFVNLAVADLILVADSLIEVFNLNEKYYDYAVLCTFMSLFLQVNMYSSIFFLTWMSFDRYIALANSMSSSPLRTMQHAKLSCGLIWMASILATLLPFTIVQTQHRGEVHFCFANVFEIQWLEVTIGFLVPFSIIGLCYSLIGRILMRSQKHRGLWPRRQKALRMIVVVVLVFFICWLPENVFISIQLLQGTADPSQRTATTLRHDYPLTGHIVNLAAFSNSCLNPIIYSFLGETFRDKL... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cellular response to estradiol stimulus [GO:0071392]; cellular response to gonadotropin stimulus [GO:0071371]; intracellular steroid hormone... | axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; cytoplasmic vesicle membrane [GO:0030659]; cytoskeleton [GO:0005856]; dendritic spine membrane [GO:0032591]; early endosome [GO:0005769]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; mitochondrial membrane [GO:0031966]; nucleus [G... | G protein-coupled receptor activity [GO:0004930]; nuclear estrogen receptor activity [GO:0030284]; steroid binding [GO:0005496]; steroid hormone binding [GO:1990239] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:18420744}; Multi-pass membrane protein {ECO:0... | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=Binds 17-beta-estradiol (E2) in plasma membranes with high affinity and displays rapid kinetics of association and dissociation. {ECO:0000269|PubMed:18420744, ECO:0000269|PubMed:19931550}; | null | null | null | FUNCTION: Membrane G-protein coupled estrogen receptor that binds to 17-beta-estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Plays a role in the embryonic development of sensory and motor neurons. May induce apoptosis and reduce proliferation of... | Micropogonias undulatus (Atlantic croaker) |
B0FPE9 | NLRP3_MACMU | MKMASTRCKLARYLEDLEDVDLKKFKMHLEDYPPQKGCISLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYEKAKRDEPKWGSDNARVSNPTVICQEDSIEEEWMGLLEYLSRISICKKKKDYCKKYRKYVRSRFQCIEDRNARLGESVSLNKRYTRLRLIKEHRSQQEREHELLAIGKTKTWESPVSPIKMELLFDPDDEHSEPVHTVVFQGAAGIGKTILARKIMLDWASGTLYQDRFDYLFYIHCREVSLVTQRSLGDLIMSCCPDPNPPIRKIVSKPSRILFLMDGFDELQGAFDEHIGPLCT... | 3.6.4.- | null | detection of biotic stimulus [GO:0009595]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; negative regulation of acute inflammatory response [GO:0002674]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; NLRP3 inflammasome complex assembly [GO:0044546]; positive... | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; Golgi membrane [GO:0000139]; interphase microtubule organizing center [GO:0031021]; membrane [GO:0016020]; mitochondrion [GO:0005739]; NLRP3 inflammasome complex [GO:0072559]; nucleus [GO:0005634] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA-binding transcription factor binding [GO:0140297]; phosphatidylinositol phosphate binding [GO:1901981]; phosphatidylinositol-4-phosphate binding [GO:0070273]; sequence-specific DNA binding [GO:0043565]; signaling adaptor activ... | PF14484;PF13516;PF05729;PF17776;PF17779;PF02758; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | PTM: The disulfide bond in the pyrin domain might play a role in reactive oxygen species-mediated activation. {ECO:0000250|UniProtKB:Q96P20}.; PTM: Phosphorylation at Ser-198 by MAPK8/JNK1 increases inflammasome activation by promoting deubiquitination by BRCC3 and NLRP3 homooligomerization. Phosphorylation at Ser-805 ... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8R4B8}. Inflammasome {ECO:0000250|UniProtKB:Q8R4B8}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q8R4B8}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8R4B8}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8R4B8}. Mito... | 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; Evidence={ECO:0000250|UniProtKB:Q8R4B8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:Q8R4... | null | null | null | null | FUNCTION: Sensor component of the NLRP3 inflammasome, which mediates inflammasome activation in response to defects in membrane integrity, leading to secretion of inflammatory cytokines IL1B and IL18 and pyroptosis. In response to pathogens and other damage-associated signals that affect the integrity of membranes, ini... | Macaca mulatta (Rhesus macaque) |
B0FYY4 | ITB1_SHEEP | MNLQLIFWIGLISSVCCVFGQADENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCHPNDIENPRGSKDIKKNKNVTNRSKGTAEKLQPEDITQIQPQQLVLQLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTNEQNCTSPFSYKNVLSLTDKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENDMYTMSHYYDYPSIA... | null | null | cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; cellular response to low-density lipoprotein particle stimulus [GO:0071404]; integrin-mediated signaling pathway [GO:0007229]; muscle organ development [GO:0007517]; myoblast differentiation [GO:0045445]; myoblast fusion [GO:0007520]; negativ... | cell surface [GO:0009986]; focal adhesion [GO:0005925]; integrin alpha9-beta1 complex [GO:0034679]; lamellipodium [GO:0030027]; melanosome [GO:0042470]; membrane [GO:0016020]; recycling endosome [GO:0055037]; ruffle membrane [GO:0032587] | C-X3-C chemokine binding [GO:0019960]; collagen binding involved in cell-matrix adhesion [GO:0098639]; fibronectin binding [GO:0001968]; integrin binding involved in cell-matrix adhesion [GO:0098640]; laminin binding [GO:0043236]; metal ion binding [GO:0046872]; protein heterodimerization activity [GO:0046982] | PF07974;PF18372;PF08725;PF07965;PF00362;PF17205; | 4.10.1240.30;1.20.5.100;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410; | Integrin beta chain family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P05556}; Single-pass ty... | null | null | null | null | null | FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, a... | Ovis aries (Sheep) |
B0G0Y8 | PDE3_DICDI | MAPQQNIMKQLQQMQSSPYPSSSPSSTTVSQNNDNLNHNVHSLNNSSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSINEKNKINDNNNRGNSDDGNNNNSNNNSNNNNSNNNNRDDEEEEGDDEDNNNNNNSNNNKIRGYNDNNDINDIFSINFSSWSKSKDNLIENGVLIFEESGLYKELNLSKSSILNFLSIVASSYRNNPFHSFNHAIAVTQTIFLILLKTNLFNILSPIEKLSIIIASICHDLDHPALSNRFQINMKSSIAVLYNNKSVLENHHLSICLGILESKIGNELLSTLTVEEKKQFFRRVKI... | 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]; cGMP-mediated signaling [GO:0019934] | cytosol [GO:0005829] | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; cGMP binding [GO:0030553]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145] | PF00233; | 1.10.1300.10; | Cyclic nucleotide phosphodiesterase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12429832, ECO:0000269|PubMed:17040207}. | 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:0000269|PubMed:11171061}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958; Evidence={ECO:0000269|PubMed:11171061}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.22 uM for cGMP {ECO:0000269|PubMed:11171061}; Vmax=2 pmol/min/mg enzyme with cGMP as substrate {ECO:0000269|PubMed:11171061}; Note=cAMP/cGMP selectivity of 0.0015. {ECO:0000269|PubMed:11171061}; | null | null | null | FUNCTION: Phosphodiesterase specific for cGMP, which is not activated by cGMP. Involved in the degradation of intracellular cGMP. {ECO:0000269|PubMed:11171061, ECO:0000269|PubMed:12429832}. | Dictyostelium discoideum (Social amoeba) |
B0G126 | FYV1_DICDI | MAESFQQLGVGSKSNERSFFSKFFGTDDSQKDFGPLPEIEYSDEQRFNPYPAIYEKKNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSNGNGNRSNSSLNNSNNNNQVRRTHSPSVSNKSDESNTTNTNTNITTNTNITTNTNTNTNTNSTNNDTSSNVTQQQLLTNLGQSKIISALKTKFQRPLPPVDDKKFWMPDHSSAVCYECSEEFTTFKRRHHCRLCGQIFCWKCSQKTLTDGKGERVRVCNFCYRRYMAPDDLDMEGYHYDPITGTVISLITNNDDGTNLNNGNGLIKLDGSTHNMNVSLGNSGDNSSFVQSP... | 2.7.1.150; 2.7.11.1 | null | defense response to Gram-negative bacterium [GO:0050829]; phagosome acidification [GO:0090383]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phospholipid metabolic process [GO:0006644]; phosphorylation [GO:0016310]; protein localization to phagocytic vesicle [GO:1905161]; sorocarp spore cell differ... | early endosome membrane [GO:0031901]; endosome membrane [GO:0010008]; late endosome membrane [GO:0031902]; macropinosome [GO:0044354]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670] | 1-phosphatidylinositol-3-phosphate 5-kinase activity [GO:0000285]; 1-phosphatidylinositol-5-kinase activity [GO:0052810]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310] | PF00118;PF01363;PF01504; | 3.30.810.10;3.50.7.10;3.30.800.10;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q9Y2I7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z1T6}. Early endosome membrane {ECO:0000250|UniProtKB:Q9Y2I7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y2I7}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9Y2I7}; ... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:13609, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57923, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.150; Evid... | null | null | null | null | FUNCTION: Dual specificity kinase part of the PI(3,5)P2 regulatory complex which regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinosi... | Dictyostelium discoideum (Social amoeba) |
B0G168 | SRSA_DICDI | MIAKVFKSITPESYILLVNAGLISAYGVRIIFQSVKNDEGKVDEKAHIGIGHFFKKRGAQLVDGKNLTDILKEKKKKKKKKKKINISNKLIIFKISRQLYSKLKLK | null | null | aggregation involved in sorocarp development [GO:0031152]; cell aggregation [GO:0098743]; regulation of DNA-templated transcription [GO:0006355]; response to imidacloprid [GO:1902351]; response to starvation [GO:0042594]; socially cooperative development [GO:0099120]; sorocarp morphogenesis [GO:0031288]; sporulation re... | plasma membrane [GO:0005886] | null | null | null | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Involved in starvation response and aggregation stage of the life cycle. May be involved in fruiting body morphogenesis and spore formation. {ECO:0000269|PubMed:18673382}. | Dictyostelium discoideum (Social amoeba) |
B0I1T2 | MYO1G_HUMAN | MEDEEGPEYGKPDFVLLDQVTMEDFMRNLQLRFEKGRIYTYIGEVLVSVNPYQELPLYGPEAIARYQGRELYERPPHLYAVANAAYKAMKHRSRDTCIVISGESGAGKTEASKHIMQYIAAVTNPSQRAEVERVKDVLLKSTCVLEAFGNARTNRNHNSSRFGKYMDINFDFKGDPIGGHIHSYLLEKSRVLKQHVGERNFHAFYQLLRGSEDKQLHELHLERNPAVYNFTHQGAGLNMTVHSALDSDEQSHQAVTEAMRVIGFSPEEVESVHRILAAILHLGNIEFVETEEGGLQKEGLAVAEEALVDHVAELTATPRD... | null | null | actin filament organization [GO:0007015]; actin filament-based movement [GO:0030048]; cell gliding [GO:0071976]; cell-substrate adhesion [GO:0031589]; endocytosis [GO:0006897]; exocytosis [GO:0006887]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; T cell meandering migration [GO:0120117]; T... | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; filopodium [GO:0030175]; lamellipodium [GO:0030027]; leading edge membrane [GO:0031256]; membrane [GO:0016020]; microvillus [GO:0005902]; myosin complex [GO:0016459]; nucleoplasm [GO:0005654]; phagocytic cup [GO:0001891]; plasm... | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546] | PF00063;PF06017; | 1.10.10.820;1.20.5.4820;1.20.58.530;3.40.850.10;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19968988, ECO:0000269|PubMed:20071333}; Peripheral membrane protein {ECO:0000269|PubMed:19968988, ECO:0000269|PubMed:20071333}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q5SUA5}. Note=Recruited to Fc-gamma receptor (Fc-gamma-R) phagocytic cup. In T-ce... | null | null | null | null | null | FUNCTION: Unconventional myosin required during immune response for detection of rare antigen-presenting cells by regulating T-cell migration. Unconventional myosins are actin-based motor molecules with ATPase activity and serve in intracellular movements. Acts as a regulator of T-cell migration by generating membrane ... | Homo sapiens (Human) |
B0JJ82 | GLMU_MICAN | MVAVAILAAGKGTRMKSSLPKVLHPLGSRSLVERVLNVSESLHPQRKLVIIGYQGQQVRNTLQHLDDIEFVEQKEQLGTGHAIQQLIPHLEDFQGDLLVLNGDVPLLRPETLQNLLQIHQDHGNAATLLTANLPNPKGYGRVFCDGNNLVKQIVEERDCTDAQRQNHRINGGIYCFNWSKLAAILPNLTPNNDQGEYYLTDVVNFLDPVMAVDVEDFLEITGINDRKQLAAAYDILQTRVKDDWMAAGVTIIDPDSVTIEDTVTLSADVIIEPQTHLRGETIIASGCRIGPGSLIENSRIGSDVTVLFSVISDSQVDSGC... | 2.3.1.157; 2.7.7.23 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01631}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01631}; | cell morphogenesis [GO:0000902]; cell wall organization [GO:0071555]; lipid A biosynthetic process [GO:0009245]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048] | carboxysome [GO:0031470]; cytoplasm [GO:0005737] | glucosamine-1-phosphate N-acetyltransferase activity [GO:0019134]; magnesium ion binding [GO:0000287]; structural constituent of carboxysome shell [GO:0043886]; UDP-N-acetylglucosamine diphosphorylase activity [GO:0003977] | PF00132;PF12804; | 2.160.10.10; | N-acetylglucosamine-1-phosphate uridyltransferase family; Transferase hexapeptide repeat family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01631}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000255|HAMAP-Rule:MF_01631}; CATALYTIC ACTI... | null | PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. {ECO:0000255|HAMAP-Rule:MF_01631}.; PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acet... | null | null | FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is ... | Microcystis aeruginosa (strain NIES-843 / IAM M-2473) |
B0JZV4 | CBPC5_XENTR | MEVRCGGLLFSSKFDSGNLARVEKVEKPGAEGDAFSGSVSGGSVPTPDYEFNIWTKPDCAETEYENGNRSWFYFSVRFGAPGKLIKINIMNMNKQSKLYSQGMAPFVRTVPIRSRWERIRDRPTFEMVENQFILSFVHRFLDCRGSTTYFAFCFPFSYEESQELMAGLDDRFSDCKNITPGSFPDSIYYHRELLCHSLDGLRVDLLTISSCHGMTEEREPRLDKLFPDRSTPRPYRFTGKRVYFLSSRVHPGETPSSFVFNGFLEFILRQDDPRAQMLRRMFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLNPDFEL... | 3.4.17.-; 3.4.17.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00730}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730}; | C-terminal protein deglutamylation [GO:0035609]; defense response to virus [GO:0051607]; protein branching point deglutamylation [GO:0035611]; protein deglutamylation [GO:0035608]; protein side chain deglutamylation [GO:0035610]; proteolysis [GO:0006508] | cytosol [GO:0005829]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; nucleus [GO:0005634] | metallocarboxypeptidase activity [GO:0004181]; tubulin binding [GO:0015631]; zinc ion binding [GO:0008270] | PF18027;PF00246; | 2.60.40.3120;3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q09M02}. Nucleus {ECO:0000250|UniProtKB:Q09M02}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NDL9}. Midbody {ECO:0000250|UniProtKB:Q8NDL9}. | CATALYTIC ACTIVITY: Reaction=gamma-L-glutamyl-L-glutamyl-[protein] + H2O = L-glutamate + L-glutamyl-[protein]; Xref=Rhea:RHEA:60152, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15377, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:143622; Evidence={ECO:0000250|UniProtKB:Q09M02}; PhysiologicalDirection=le... | null | null | null | null | FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Cleaves alpha- and gamma-linked polyglutamate tu... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
B0K011 | OSR1_RAT | MGSKTLPAPVPIHPSLQLTNYSFLQAVNGLPTVPSDHLPNLYGFSALHAVHLHQWTLGYPAMHLPRSSFSKVPGAVSSLMDARFQLPAFPWFPHVIHPKPEITAGGSGAALKTKPRFDFANLALAATQEDPTKLGRGEGPGSPAGGLGALLDVTKLSPEKKPTRGRLPSKTKKEFVCKFCGRHFTKSYNLLIHERTHTDERPYTCDICHKAFRRQDHLRDHRYIHSKEKPFKCQECGKGFCQSRTLAVHKTLHSQVKELKTSKIKC | null | null | cell differentiation [GO:0030154]; cell proliferation involved in kidney development [GO:0072111]; cellular response to retinoic acid [GO:0071300]; chondrocyte differentiation [GO:0002062]; embryonic digit morphogenesis [GO:0042733]; embryonic forelimb morphogenesis [GO:0035115]; embryonic hindlimb morphogenesis [GO:00... | cell cortex [GO:0005938]; cytosol [GO:0005829]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific double-stranded DNA binding [GO:1990837] | PF00096; | 3.30.160.60; | Odd C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Transcription factor that plays a role in the regulation of embryonic heart and urogenital development. {ECO:0000250}. | Rattus norvegicus (Rat) |
B0K019 | BAG1_RAT | MADRGGARRPRGDQEPLGPRLRAPRSARETRQSESRAERGLPPSQRSSVRSAASGHDRSTRGAASGACKPRVKKKVRPRSSQSEKVAHSKELTRSKKLTRSKKVTGTQEATQVEEVTTIEEATQTEEITVAEEVTQTENMAQTEEMVQTEEMEPPTLSVVVTHSNERYDLLVTPQQGNSEPIVQDLAQLVEEATGVPLPFQKLIFKGKSLKEMETPLSALGMQNGCRVMLIGEKSNPEEEAELKKLKDLEVSVEKTANHLEELNKELSDIQQGFLAKELQAEALCRLDRKIKATIEQFMKILEEIDTMVLPENFKDSRLK... | null | null | apoptotic process [GO:0006915]; chaperone cofactor-dependent protein refolding [GO:0051085]; negative regulation of apoptotic process [GO:0043066]; negative regulation of motor neuron apoptotic process [GO:2000672]; negative regulation of protein phosphorylation [GO:0001933]; neuron differentiation [GO:0030182]; positi... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | adenyl-nucleotide exchange factor activity [GO:0000774]; protein-folding chaperone binding [GO:0051087]; ubiquitin protein ligase binding [GO:0031625] | PF02179;PF00240; | 1.20.58.120; | null | PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC... | Rattus norvegicus (Rat) |
B0K020 | CISD1_RAT | MGLSSDSPVRVEWIAAVTFAAGTAALGYLAYKKFYAKESRTKAMVNLQIQKDNPKVVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHIKHNEETGDNVGPLIIKKKET | 2.6.1.3 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250|UniProtKB:Q9NZ45}; Note=Binds 1 [2Fe-2S] cluster per subunit. The [2Fe-2S] cluster is redox-active and pH labile and is significantly less stable at pH 4.5 as compared with pH 7.0. {ECO:0000250|UniProtKB:Q9NZ45}; COFACTOR: Name=pyridoxal 5'... | protein maturation by [2Fe-2S] cluster transfer [GO:0106034]; regulation of autophagy [GO:0010506]; regulation of cellular respiration [GO:0043457] | cytoplasmic side of mitochondrial outer membrane [GO:0032473]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739] | 2 iron, 2 sulfur cluster binding [GO:0051537]; identical protein binding [GO:0042802]; L-cysteine transaminase activity [GO:0047801]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170] | PF10660;PF09360; | 3.40.5.90; | CISD protein family | PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000250|UniProtKB:Q9NZ45}. | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9NZ45}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:Q9NZ45}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-cysteine = 2-oxo-3-sulfanylpropanoate + L-glutamate; Xref=Rhea:RHEA:17441, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35235, ChEBI:CHEBI:57678; EC=2.6.1.3; Evidence={ECO:0000250|UniProtKB:Q9NZ45}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17442; Evidence... | null | null | null | null | FUNCTION: L-cysteine transaminase that catalyzes the reversible transfer of the amino group from L-cysteine to the alpha-keto acid 2-oxoglutarate to respectively form 2-oxo-3-sulfanylpropanoate and L-glutamate (By similarity). The catalytic cycle occurs in the presence of pyridoxal 5'-phosphate (PLP) cofactor that faci... | Rattus norvegicus (Rat) |
B0KW95 | CADH2_CALJA | MCRIAGAPRTLLPLLAALLQASVEASGEIALCKTGFPEDVYSAVLSKDVHEGQPLLNVKFSNCNGKRKVQYESSEPADFKVDEDGMVYAVRSFPLSSEHAKFLIYAQDKETQEKWQVAVKLSLKPTLPEESVKESTEVEEIVFPRQLGKHSGHLQRQKRDWVIPPINLPENSRGPFPQELVRIRSDRDKNLSLRYSVTGPGADQPPTGIFIINPISGQLSVTKPLDREQIARFHLRAHAVDINGNQVENPIDIVINVIDMNDNRPEFLHQVWNGTVPEGSKPGTYVMTVTAIDADDPNALNGMLRYRILSQAPSTPSPNM... | null | null | adherens junction organization [GO:0034332]; blood vessel morphogenesis [GO:0048514]; brain development [GO:0007420]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell morphogenesis [GO:0000902]; cell-cell adhesion [GO:0098609]; cell-cell adhesion mediated by cadherin [... | adherens junction [GO:0005912]; apical part of cell [GO:0045177]; catenin complex [GO:0016342]; cell junction [GO:0030054]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; desmosome [GO:0030057]; intercalated disc [GO:0014704]; lamellipodium [GO:0030027]; neuron projection [GO:004300... | cadherin binding [GO:0045296]; calcium ion binding [GO:0005509] | PF01049;PF00028;PF08758; | 2.60.40.60;4.10.900.10; | null | PTM: Cleaved by MMP24. Ectodomain cleavage leads to the generation of a soluble 90 kDa N-terminal soluble fragment and a 45 kDa membrane-bound C-terminal fragment 1 (CTF1), which is further cleaved by gamma-secretase into a 35 kDa (By similarity). Cleavage in neural stem cells by MMP24 affects CDH2-mediated anchorage o... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15116}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P15116}. Cell junction {ECO:0000250|UniProtKB:P19022}. Cell surface {ECO:0000250|UniProtKB:P15116}. Cell junction, desmosome {ECO:0000250|UniProtKB:P151... | null | null | null | null | null | FUNCTION: Calcium-dependent cell adhesion protein; preferentially mediates homotypic cell-cell adhesion by dimerization with a CDH2 chain from another cell. Cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem... | Callithrix jacchus (White-tufted-ear marmoset) |
B0KWU8 | BRCC3_CALJA | MAVQVVQAVQAVHLESDAFLVCLNHALSTEKEEVMGLCIGELNDDTRSDSKFAYTGTEMRTVAEKVDAVRIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAELTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSIQAQKSSESLHGPRDFWSSSKHISIEGQKEEERYERIEIPIHIVPHVTIGKVCLESAVELPKILCQEEQDAYRRIHSLTHLDSVTKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHLRELQQEKEELMQELSSLE | 3.4.19.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:E2AXC7, ECO:0000250|UniProtKB:P46736}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:E2AXC7}; | cell division [GO:0051301]; chromatin remodeling [GO:0006338]; DNA repair-dependent chromatin remodeling [GO:0140861]; double-strand break repair [GO:0006302]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; positive regulation of DNA repair [GO:0045739]; positive regulation of NLRP3 inflammasome complex assem... | BRCA1-A complex [GO:0070531]; BRISC complex [GO:0070552]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; spindle pole [GO:0000922] | cysteine-type deubiquitinase activity [GO:0004843]; metal ion binding [GO:0046872]; metal-dependent deubiquitinase activity [GO:0140492]; metallopeptidase activity [GO:0008237]; polyubiquitin modification-dependent protein binding [GO:0031593] | PF18110;PF01398; | 3.40.140.10; | Peptidase M67A family, BRCC36 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P46736}. Cytoplasm {ECO:0000250|UniProtKB:P46736}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P46736}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). Interaction with ABRAXAS2 retains BRCC3 in the cytoplasm. {ECO:0000250|UniPr... | null | null | null | null | null | FUNCTION: Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to targ... | Callithrix jacchus (White-tufted-ear marmoset) |
B0KYV5 | LIMA1_PIG | MESTPFNRQQWTSLSLRVTAKELSLVNKNKSSAIVEIFSKYQKAAEEANMEKRRSNTENLPQHFRRGNLTVLKKKWENPAPGVESLPESTRNSSAEVRHRGDPPPAEVASSSASGVEADQGVCPRPRFSSPPEVPYPNPRIKDTEHLKDHSAESKKMENCLAESRHEVGKPETSENAEASNKIEKYNVPLNRLKMMFERGEPAQTKILRAQSRSTGGRKISENSYSLDDLEIGPGQLSSSAFNTEKSESRRNLEFPRLSDTSIKDRMAKYQAAVSKQSSSTNYTNELKANGGEIKTHKLEQKENVPPGPEVCISHQDGEK... | null | null | actin filament bundle assembly [GO:0051017]; cell migration [GO:0016477]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; intestinal cholesterol absorption [GO:0030299]; ruffle organization [GO:0031529] | actin cytoskeleton [GO:0015629]; brush border membrane [GO:0031526]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]; ruffle [GO:0001726] | actin filament binding [GO:0051015]; metal ion binding [GO:0046872] | PF00412; | 2.10.110.10; | null | PTM: Phosphorylation of the C-terminal region by MAPK1/MAPK3 reduces its association with F-actin and contributes to actin filament reorganization and enhances cell motility. {ECO:0000250|UniProtKB:Q9ERG0}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UHB6}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9UHB6}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UHB6}. Cell membrane {ECO:0000250|UniProtKB:Q9ERG0}. Note=This cytoskeletal protein colocalizes with actin stress fibers and focal adhesion plaqu... | null | null | null | null | null | FUNCTION: Actin-binding protein involved in actin cytoskeleton regulation and dynamics. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments (By simil... | Sus scrofa (Pig) |
B0L3A2 | DESPR_HUMAN | MTMFKGSNEMKSRWNWGSITCIICFTCVGSQLSMSSSKASNFSGPLQLYQRELEIFIVLTDVPNYRLIKENSHLHTTIVDQGRTV | null | null | endothelin receptor signaling pathway [GO:0086100]; vascular endothelial growth factor signaling pathway [GO:0038084] | plasma membrane [GO:0005886] | endothelin receptor activity [GO:0004962]; vascular endothelial growth factor binding [GO:0038085] | null | null | null | PTM: N-glycosylated. {ECO:0000269|PubMed:27301377}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24465725, ECO:0000269|PubMed:27301377, ECO:0000269|PubMed:33853558}; Single-pass membrane protein {ECO:0000305|PubMed:27301377}. | null | null | null | null | null | FUNCTION: Dual receptor for both endothelin-1 and the signal sequence of vascular endothelial growth factor A (PubMed:17446437, PubMed:24465725). Does not act as a receptor for angiotensin-2 (PubMed:17446437). Does not bind the VEGFA mature protein (By similarity). May play a role in angiogenesis with a significant rol... | Homo sapiens (Human) |
B0LDU5 | PKS4_RUBID | MVTVEEVRKAQRAEGPATVLAIGTATPPNCVGQSTYPDYYFRITNSEHKIELKQKFQRMCDKSMIKKRYMYLTEEILKENPSMCEYMAPSLDARQDMVIVEIPKLGKEAATKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLIKLFGLRPSVKRLMMYQQGCFAGGTVLRLAKDLAENNRGARVLVVCSEITVVTFRGPSDTHLDCLVGQALFGDGVASIIVGADPLPEIEKPLFELVSAAQTILPDSEGAIEGHLREVGLTFHLLENVPALISKNIEKSLNETFKPLDIMDWNSLFWIAHPGGPAILDQVEAKLGLK... | 2.3.1.212; 2.3.1.74 | null | flavonoid biosynthetic process [GO:0009813]; polyketide biosynthetic process [GO:0030639] | null | chalcone synthase activity [GO:0102128]; naringenin-chalcone synthase activity [GO:0016210]; protein homodimerization activity [GO:0042803] | PF02797;PF00195; | 3.40.47.10; | Thiolase-like superfamily, Chalcone/stilbene synthases family | null | null | CATALYTIC ACTIVITY: Reaction=4-coumaroyl-CoA + H(+) + H2O + malonyl-CoA = 4-hydroxybenzalacetone + 2 CO2 + 2 CoA; Xref=Rhea:RHEA:34483, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57355, ChEBI:CHEBI:57384, ChEBI:CHEBI:68636; EC=2.3.1.212; Evidence={ECO:0000269|PubMed:12226219... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 uM for malonyl-CoA {ECO:0000269|PubMed:12226219}; KM=3 uM for p-coumaryl CoA {ECO:0000269|PubMed:12226219}; | PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is approximately 8.0. {ECO:0000269|PubMed:12226219}; | null | FUNCTION: Bifunctional polyketide synthase producing both 4-hydroxybenzalacetone and naringenin chalcone. Can use p-coumaryl-CoA and ferulyl-CoA as substrates. Catalyzes the initial key reaction step in the biosynthesis of phenylbutanoids. {ECO:0000269|PubMed:18068110}. | Rubus idaeus (Raspberry) |
B0LL23 | PLR_SINHE | MAKSRVLIVGGTGYLGRRMVKACLDQGHTTYVLHRQEVGVDIDKIQMLLSFKEQGAHLVEGSFNDHRSLVEAVKLVDVVICTISGVHIRSHQILLQLKLVEAIEEAGNVKRFLPSEFGMDPARMAHAMEPGRATFDEKMVVRKAIEDAKIPHTYASANCFAGYFLGGLCQFGKIIPSKESVILSGDGNVKGIYVDEYDIATYTIKTMDDPRTLNKTIYIRPPANILSQREVVEIWEKLIGKVLDKSSLSEEDFLALMKGLSHGHQAGLTHYYHVSYEGCLTNFEVEDGVDASKLYPQVNYTTVSEYLKRYL | 1.23.1.1; 1.23.1.2 | null | (+)-pinoresinol catabolic process [GO:1902125]; (-)-secoisolariciresinol biosynthetic process [GO:1902138]; aromatic compound biosynthetic process [GO:0019438]; phenylpropanoid biosynthetic process [GO:0009699]; response to jasmonic acid [GO:0009753]; response to UV [GO:0009411]; response to wounding [GO:0009611] | null | lariciresinol reductase activity [GO:0010284]; pinoresinol reductase activity [GO:0010283] | PF05368; | 3.40.50.720;3.90.25.10; | NmrA-type oxidoreductase family, Isoflavone reductase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(-)-secoisolariciresinol + NADP(+) = (+)-lariciresinol + H(+) + NADPH; Xref=Rhea:RHEA:34423, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65004, ChEBI:CHEBI:67246; EC=1.23.1.2; Evidence={ECO:0000269|PubMed:26359402}; PhysiologicalDirection=left-to-right; Xref=Rhea:RH... | null | PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:26359402}. | null | null | FUNCTION: Reductase involved in lignan biosynthesis (PubMed:26359402). Also involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family (PubMed:26359402). Catalyzes the enantioselective sequential conversion of (+)-pinoresinol into (+)-lariciresinol and of (+)-lariciresi... | Sinopodophyllum hexandrum (Himalayan may apple) (Podophyllum hexandrum) |
B0LPN4 | RYR2_RAT | MADAGEGEDEIQFLRTDDEVVLQCTATIHKEQQKLCLAAEGFGNRLCFLESTSNSKNVPPDLSICTFVLEQSLSVRALQEMLANTVEKSEGKFMMKTAQGGGHRTLLYGHAILLRHSYSGMYLCCLSTSRSSTDKLAFDVGLQEDTTGEACWWTIHPASKQRSEGEKVRVGDDLILVSVSSERYLHLSYGNSSWRVDAAFQQTLWSVAPISSGSEAAQGYLIGGDVLRLLHGHMDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLMEDKNLLLMDKEKADVKST... | null | null | calcium ion transmembrane import into cytosol [GO:0097553]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; calcium ion transport into cytosol [GO:0060402]; calcium-mediated signaling [GO:0019722]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cardiac ... | A band [GO:0031672]; calcium channel complex [GO:0034704]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; protein-containing complex [GO:0032991]; sarcolemma [GO:0042383]; sarcomere [GO:0030017]; sarcoplasmic reticulum [GO:0016529]; sarcopl... | calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-induced calcium release activity [GO:0048763]; calmodulin binding [GO:0005516]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; intracellularly gated calcium channel activity [GO:0015278]; organic cyclic compound bindi... | PF13499;PF08709;PF00520;PF02815;PF08454;PF06459;PF01365;PF21119;PF02026;PF00622; | 1.10.287.70;1.10.490.160;2.60.120.920;2.80.10.50;1.10.238.10;1.25.10.30; | Ryanodine receptor (TC 1.A.3.1) family, RYR2 subfamily | PTM: Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2798 and Ser-2804 increases the open probability of the calcium channel. Phosphorylation is increased in failing heart, leading to calcium leaks and increased cytoplasmic Ca(2+) levels (By similarity). {ECO:0000250}.; PTM: Phosphorylation at ... | SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q92736}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q92736}; | null | null | null | null | FUNCTION: Cytosolic calcium-activated calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytosol and thereby plays a key role in triggering cardiac muscle contraction. Aberrant channel activation can lead to cardiac arrhythmia. In cardiac myocytes, calcium release is triggered ... | Rattus norvegicus (Rat) |
B0LSW3 | LIS1_FELCA | MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTI... | null | null | acrosome assembly [GO:0001675]; actin cytoskeleton organization [GO:0030036]; adult locomotory behavior [GO:0008344]; ameboidal-type cell migration [GO:0001667]; auditory receptor cell development [GO:0060117]; brain morphogenesis [GO:0048854]; cell division [GO:0051301]; chemical synaptic transmission [GO:0007268]; co... | 1-alkyl-2-acetylglycerophosphocholine esterase complex [GO:0008247]; astral microtubule [GO:0000235]; axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; cell leading edge [GO:0031252]; centrosome [GO:0005813]; cytoplasmic microtubule [GO:0005881]; glutamatergic synapse [GO:0098978]; kinetochore [GO:0000776]; microt... | dynein complex binding [GO:0070840]; identical protein binding [GO:0042802]; microtubule plus-end binding [GO:0051010]; phosphoprotein binding [GO:0051219]; protein heterodimerization activity [GO:0046982] | PF08513;PF00400; | 1.20.960.30;2.130.10.10; | WD repeat LIS1/nudF family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03141}. Nucleus membrane {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to... | null | null | null | null | null | FUNCTION: Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic... | Felis catus (Cat) (Felis silvestris catus) |
B0LT89 | STK24_RAT | MAHSPVQSGLPGMQTLKADPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSALDLLEPGPLDEIQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELAKGEPPHSELHPMKVLFLIPKNNPPTLEGSYSRPLKEFVEACLNKEPSFRPTAKELLKHKFIIRNAKKTSYLTELIDRYKRWKAEQSHEDSSSEDSDVETDSQASGGS... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; | cellular response to oxidative stress [GO:0034599]; cellular response to starvation [GO:0009267]; execution phase of apoptosis [GO:0097194]; intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; negative regulation of cell migration [GO:0030336]; positive regulation of axon regeneration [G... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleolus [GO:0005730]; nucleus [GO:0005634] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF20929;PF00069; | 1.10.12.70;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | PTM: Proteolytically processed by caspases during apoptosis. Proteolytic cleavage results in kinase activation, nuclear translocation of the truncated form (MST3/N) and the induction of apoptosis (By similarity). {ECO:0000250}.; PTM: Oxidative stress induces phosphorylation. Activated by autophosphorylation at Thr-178 ... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Membrane {ECO:0000250}. Note=The truncated form (MST3/N) translocates to the nucleus. Colocalizes with STK38L in the membrane (By similarity). {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that acts on both serine and threonine residues and promotes apoptosis in response to stress stimuli and caspase activation. Mediates oxidative-stress-induced cell death by modulating phosphorylation of JNK1-JNK2 (MAPK8 and MAPK9), p38 (MAPK11, MAPK12, MAPK13 and MAPK14) during... | Rattus norvegicus (Rat) |
B0M3E8 | UGE1_PEA | MVASSQKILVTGGAGFIGTHTVVQLLNNGFNVSIIDNFDNSVMEAVERVREVVGSNLSQNLEFTLGDLRNKDDLEKLFSKSKFDAVIHFAGLKAVGESVENPRRYFDNNLVGTINLYEVMAKHNCKKMVFSSSATVYGQPEKIPCVEDFKLQAMNPYGRTKLFLEEIARDIQKAEPEWRIVLLRYFNPVGAHESGKLGEDPRGIPNNLMPYIQQVAVGRLPELNVYGHDYPTRDGSAIRDYIHVMDLADGHIAALRKLFTSENIGCTAYNLGTGRGSSVLEMVAAFEKASGKKIALKLCPRRPGDATEVYASTAKAEKEL... | 5.1.3.2; 5.1.3.5 | COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250|UniProtKB:Q14376}; | capsule polysaccharide biosynthetic process [GO:0045227]; cell wall organization [GO:0071555]; galactose catabolic process via UDP-galactose [GO:0033499]; UDP-L-arabinose biosynthetic process [GO:0033358] | cytosol [GO:0005829] | UDP-arabinose 4-epimerase activity [GO:0050373]; UDP-glucose 4-epimerase activity [GO:0003978] | PF16363; | 3.40.50.720;3.90.25.10; | NAD(P)-dependent epimerase/dehydratase family | null | null | CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose; Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914; EC=5.1.3.2; Evidence={ECO:0000269|PubMed:19754426}; CATALYTIC ACTIVITY: Reaction=UDP-beta-L-arabinopyranose = UDP-alpha-D-xylose; Xref=Rhea:RHEA:11320, ChEBI:CHEBI:57632, ChEBI:CHEBI:614... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.29 mM for UDP-galactose {ECO:0000269|PubMed:19754426}; KM=0.31 mM for UDP-glucose {ECO:0000269|PubMed:19754426}; KM=0.15 mM for UDP-xylose {ECO:0000269|PubMed:19754426}; KM=0.16 mM for UDP-arabinose {ECO:0000269|PubMed:19754426}; | PATHWAY: Carbohydrate metabolism; galactose metabolism. {ECO:0000305}.; PATHWAY: Nucleotide-sugar biosynthesis; UDP-L-arabinose biosynthesis; UDP-L-arabinose from UDP-alpha-D-xylose: step 1/1. {ECO:0000305}.; PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis. {ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5-9.0. {ECO:0000269|PubMed:19754426}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:19754426}; | FUNCTION: Catalyzes the interconversion between UDP-glucose and UDP-galactose and the interconversion between UDP-arabinose and UDP-xylose. {ECO:0000269|PubMed:19754426}. | Pisum sativum (Garden pea) (Lathyrus oleraceus) |
B0R0I6 | CHD8_DANRE | MADPIMDLFDDTPLFNLDSLPEDAFSQGSSDPVEEALKLALGQVDPPTDPIPDPGVPILSDVVTDPALIPTPVSVPLQNLQTQQLSQIPHEVSVASAPISIQPSLSVASNSSGAATVLLSSSLGVPVSGAQVTPQQQTQQITAVTQQAAGQHAPKIVILKGPQGQTQVLQGVTGATGSPGKVTLARVLTGTPLRPGMAVVSGGTVLNATSPAQGQVKVGTGVQRLVQTANGPMKQVLLTSVPQTQSQVQTQPVQVQIPVQTQLQSPSQPQQLQAQIQAQTQVALQTQAQTQTPTSPAAAGIRPQSVTLSAVPQQVRFVLG... | 3.6.4.12 | null | brain development [GO:0007420]; chromatin remodeling [GO:0006338]; digestive tract development [GO:0048565]; enteric nervous system development [GO:0048484]; forebrain development [GO:0030900]; head development [GO:0060322]; midbrain development [GO:0030901]; negative regulation of apoptotic process [GO:0043066]; negat... | chromatin [GO:0000785]; MLL1 complex [GO:0071339]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; beta-catenin binding [GO:0008013]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; histone binding [GO:0042393]; p53 binding [GO:0002039] | PF07533;PF00385;PF00271;PF00176; | 2.40.50.40;3.40.5.120;1.10.10.60;3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family, CHD8 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03071}. | 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=3.6.4.12; Evidence={ECO:0000255|HAMAP-Rule:MF_03071}; | null | null | null | null | FUNCTION: DNA helicase that acts as a chromatin remodeling factor and regulates transcription. Acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. Suppresses p53/tp53-mediated apoptosis by recruiting histone H1 and preventing p53/tp53 transactivation activity. ... | Danio rerio (Zebrafish) (Brachydanio rerio) |
B0R367 | MPCT_HALS3 | MNITQAYKRSLWWSMDMVGATGSVERKMLTAVGLQFLAAGGMAFLTVFTAGTVQLIGVGGMLALSVVAFYNTYLIAEADFVEPLVALEDAADDIAAGEFERADIPSSKRDDEIASLVASFDGMQSNLEVASRQADALARQAFDDPALDESVPGAFGESITEMADSLEAYTAELEDKTAELEHQQAELERQSEQLRALVDALSEATDAARAGDLTATVDAAALDVTDDHRAAVEDFNQLLETLADTISDIQSFSDAVLAVSRTTDERVDAVADRSAAVSESVTEIADGANQQTNQLNNIAAEMDTVSATVEEIAASANDVA... | null | null | chemotaxis [GO:0006935]; signal transduction [GO:0007165] | plasma membrane [GO:0005886] | lysozyme activity [GO:0003796]; transmembrane signaling receptor activity [GO:0004888] | PF00672;PF00015; | 1.10.8.500;1.10.287.950; | Methyl-accepting chemotaxis (MCP) protein family | PTM: Methylated by CheR. {ECO:0000269|PubMed:15752193, ECO:0000269|PubMed:18514223}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15752193}; Multi-pass membrane protein {ECO:0000305|PubMed:15752193}. | null | null | null | null | null | FUNCTION: Mediates bacteriorhodopsin- and halorhodopsin-dependent photoresponses by detecting membrane potential changes. Probably transduces the signal to the histidine kinase CheA. {ECO:0000269|PubMed:15752193}. | Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1) |
B0R6I4 | BAST_HALS3 | MSDIDRGLFERVLPARIRGSYAAKFNVLLLVVVIIVAAAGGYIHLQTQSTVGENTERRVSGIAEQQAATLHDWLTQKESTTTFLASNIGGDAVRTSDVKPQLERQLATLQQDVRAIHVVSTSQDTVVASTDDARSGTTLQAGDAPWLSTIEDGTTDVSVSDPYEVDDSPVVAMTAPTDKPGWVLVMTMSLAQHSQSFNSPIATGDVKVVNGDGVITLDNRNRALLEQYTDTAGNVPAAVATARSGQTVYNTEPERTGMDDGRYATAYTPVAGTDWVLTYHVPRGQAYALQSEVTQNLAGLVVVALVGLLLVGLTVGRRTS... | null | null | chemotaxis [GO:0006935]; signal transduction [GO:0007165] | plasma membrane [GO:0005886] | lysozyme activity [GO:0003796]; transmembrane signaling receptor activity [GO:0004888] | PF00672;PF00015; | 6.10.340.10;1.10.287.950;3.30.450.20; | Methyl-accepting chemotaxis (MCP) protein family | PTM: Methylated by CheR. {ECO:0000269|PubMed:10672186, ECO:0000269|PubMed:18514223}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10672186}; Multi-pass membrane protein {ECO:0000269|PubMed:10672186}. | null | null | null | null | null | FUNCTION: Mediates chemotaxis towards five attractant amino acids (leucine, isoleucine, valine, methionine and cysteine). Probably transduces the signal from the substrate-binding protein BasB to the histidine kinase CheA. {ECO:0000269|PubMed:10672186, ECO:0000269|PubMed:12006484}. | Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1) |
B0R8E4 | CSG_HALS3 | MTDTTGKLRAVLLTALMVGSVIGAGVAFTGGAAAANASDLNDYQRFNENTNYTYSTASEDGKTEGSVASGATIFQGEEDVTFRKLDNEKEVSPATLSRTGGSDEGVPLQMPIPEDQSTGSYDSNGPDNDEADFGVTVQSPSVTMLEVRNNADNDVTGGVLNTQQDESSIAVDYNYYAAEDLELTVEDEDGLDVTDEILAADQSGGAYEDGTGNNGPNTLRFDIDPNNVDAGDYTVSVEGVEDLDFGDATESASVTISSSNKASLNLAEDEVVQGANLKYTIENSPEGNYHAVTIDSSDFRDSSSGADAAKVMRSVGDTVD... | null | null | cell wall organization [GO:0071555] | extracellular region [GO:0005576]; plasma membrane [GO:0005886]; S-layer [GO:0030115] | null | PF18204; | null | Halobacterial S-layer protein family | PTM: N-linked glycan at Asn-36 consists of a glycosaminoglycan chain, constructed by a repeating sulfated pentasaccharide block composed of GlcNAc, GalNAc, Gal, GalA, 3-O-methyl-GalA, and sulfate in the molar ratio of 1:1:1:1:1:2; the other N-linked glycans contain Glc, GlcA and IdoA. {ECO:0000269|PubMed:3036870}.; PTM... | SUBCELLULAR LOCATION: Secreted, cell wall, S-layer {ECO:0000250|UniProtKB:P25062}. Cell membrane {ECO:0000250|UniProtKB:P25062}. | null | null | null | null | null | FUNCTION: S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell. {ECO:0000250|UniProtKB:P25062}. | Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1) |
B0RP51 | PFP_XANCB | MTNGNLLYAQSGGVTAVINATAAGVIGEARARKIKVLAARNGILGALREELIDTSKESAAAIAALAQTPGGAFGSCRYKLKSLEQDRAKYERLLEVLRAHDVRWFLYNGGNDSADTALKVSQLAKAFGYPLHCIGVPKTIDNDLAVTDTCPGFGSAAKYTAVSVREAALDVAAMADTSTKVFIYEAMGRHAGWLAAAAGLAGQGPDDAPQIILLPERAFDQAAFLAKVRQMVERVGWCVVVASEGIQDAQGKFVADAGGATDSFGHAQLGGVASFLAAQVKQELGYKVHWTLPDYLQRSARHLASKTDWEQAQAVGKAAV... | 2.7.1.90 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01978}; | fructose 6-phosphate metabolic process [GO:0006002] | cytoplasm [GO:0005737] | 6-phosphofructokinase activity [GO:0003872]; diphosphate-fructose-6-phosphate 1-phosphotransferase activity [GO:0047334]; metal ion binding [GO:0046872] | PF00365; | 3.40.50.450;3.40.50.460; | Phosphofructokinase type A (PFKA) family, PPi-dependent PFK group II subfamily, Clade 'B2' sub-subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01978}. | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613, ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90; Evidence={ECO:0000255|HAMAP-Rule:MF_01978, ECO:0000269|PubMed:24... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.5 mM for phosphate {ECO:0000269|PubMed:24508689}; KM=41 uM for diphosphate {ECO:0000269|PubMed:24508689}; KM=202 uM for fructose 6-phosphate {ECO:0000269|PubMed:24508689}; KM=24 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:24508689}; Vmax=58 umol/min/mg e... | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_01978}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8. {ECO:0000269|PubMed:24508689}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:24508689}; | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and glu... | Xanthomonas campestris pv. campestris (strain B100) |
B0S5G3 | CSTN2_DANRE | MKMRAITAMLLLVLSGQCGILAGKVNKHKPWIETSYHGVITENMDTVMLDPPLVALDKDAPVPYAGEICAFKIHGQEAPFEAEVLNRTSGEGVLRARGPIDCEQQKEYTFIIQAYDCGASPNGADWKKSHKAVVHIQVDDVNEFSPVFREPLYRATVTEGKIYDSILQVEAWDQDCSPQYSQICNYEIVTQDTPFAIDRNGNIRNTERLSFDKQQHYKIMVTAYDCGQKRAMESVPVHIDVKPVCKPGWQGWNKRVDYEPGTGSKQLFPKMHLETCDGPLSSVRAMVELQTSHIGKGCDRETYSEKSLQKLCGAASGSTD... | null | null | homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; positive regulation of synapse assembly [GO:0051965]; positive regulation of synaptic transmission [GO:0050806] | cell surface [GO:0009986]; dendrite [GO:0030425]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; postsynaptic membrane [GO:0045211] | amyloid-beta binding [GO:0001540]; calcium ion binding [GO:0005509]; kinesin binding [GO:0019894]; X11-like protein binding [GO:0042988] | PF00028;PF19699; | 2.60.120.200;2.60.40.60; | Calsyntenin family | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9ER65}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9ER65}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9ER65}; Single-pass type ... | null | null | null | null | null | FUNCTION: Postsynaptic adhesion molecule (PubMed:25463516). Promotes synapse development by acting as a cell adhesion molecule at the postsynaptic membrane, which associates with presynaptic neurexins (By similarity). {ECO:0000250|UniProtKB:Q99JH7, ECO:0000269|PubMed:25463516}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B0S5N4 | PLXA3_DANRE | MRSLWLLVFSFSVLTGTNMAFPMILSERPEVTGSFKVKDTSLTHLTVHRKTGEVFVGAINRVYKLSANLTETRSHQTGPVEDNAKCYPPPSVRACTQKLESTDNVNKLLLVDYAGNRLVACGSIWQGVCQFLRLEDLFKLGEPHHRKEHYLSGAKESDGMAGVVVGDDDGDLKKKKKGGSRLFIGAAIDGKSEYFPTLSSRKLVADEESVNMFSLVYQDEFVSSQIKIPSDTLSQYPAFDIYYVYGFSSRTYIYFLTLQLDTQLTQVDVTGEKFFTSKIVRMCSNDTEFYSYVEFPLGCTKDGVEYRLVQAAYKHRPGKI... | null | null | axon extension [GO:0048675]; branching morphogenesis of a nerve [GO:0048755]; cardiac chamber development [GO:0003205]; embryonic skeletal joint morphogenesis [GO:0060272]; motor neuron axon guidance [GO:0008045]; negative regulation of cell adhesion [GO:0007162]; positive regulation of axonogenesis [GO:0050772]; regul... | membrane [GO:0016020]; plasma membrane [GO:0005886]; semaphorin receptor complex [GO:0002116] | identical protein binding [GO:0042802]; semaphorin receptor activity [GO:0017154] | PF08337;PF20170;PF01437;PF01403;PF01833;PF18020;PF17960; | 2.60.40.10;2.130.10.10; | Plexin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Coreceptor for class 3 semaphorins. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance in the developing nervous system. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of th... | Danio rerio (Zebrafish) (Brachydanio rerio) |
B0S6J3 | SRGP2_DANRE | MTSPAKFRKDKEIIAEYETQVKEIRAQLVEQLKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRYTKDPQFKKEQNILSPVNCWNLLLAQVKRESRDHATLSDLYLNNIIPRFAQISEDSGRLFKKSKEVGLQLQEDLMKVLNELYTVMKTYHMYNMDSINAESKLKEAEKQEEKQMSRSVRHEEKQTPRSPDSLTNIKIEDKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNSCVFKYYIHDLSDLIDCCDLGYHASLNRALRTYLSAEFNVETSKHGGLETIENAAENLE... | null | null | actin filament severing [GO:0051014]; dendritic spine development [GO:0060996]; filopodium assembly [GO:0046847]; negative regulation of cell migration [GO:0030336]; negative regulation of neuron migration [GO:2001223]; neuron projection morphogenesis [GO:0048812]; podocyte development [GO:0072015]; positive regulation... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine head [GO:0044327]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211] | GTPase activator activity [GO:0005096]; protein homodimerization activity [GO:0042803]; small GTPase binding [GO:0031267] | PF00611;PF00620;PF00018; | 1.20.1270.60;1.10.555.10;2.30.30.40; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q91Z67}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q91Z67}. Postsynaptic density {ECO:0000250|UniProtKB:Q91Z67}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q91Z67}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O75044}. Cytoplasmic ... | null | null | null | null | null | FUNCTION: Postsynaptic RAC1 GTPase activating protein (GAP) that plays a key role in neuronal morphogenesis and migration mainly during development of the cerebral cortex. Regulates excitatory and inhibitory synapse maturation and density in cortical pyramidal neurons. Mechanistically, acts by binding and deforming mem... | Danio rerio (Zebrafish) (Brachydanio rerio) |
B0S6T2 | S15A2_DANRE | MGKMKDKDVDAEKYEKAQRSPKLCGTNYPVSIAFIVVNEFCERFSYYGMKAVLTLYFMNYLHWDKNLSTAIYHAFSGLCYFTPLLGALIADSWLGKFKTIIYLSIVYVIGHVVKSVGAIPDVGDSTVHIALSMVGLGLIALGTGGIKPCVAAFGGDQFDEDNIDERRKFFSIFYMSINAGSVLSTIITPILRGDVQCFGGDCYALAFGVPAALMVIALVVFISGSGLYKKSPPEGNVLVRVCKCIGFAISNRWTNSKKSPKRSHWLDWAEEKYSKRLIQEIKMVCRVLVLYIPLPMFWALFDQQGSRWTLQATRMNMDFG... | null | null | dipeptide import across plasma membrane [GO:0140206]; innate immune response [GO:0045087]; peptidoglycan transport [GO:0015835]; protein transport [GO:0015031]; regulation of nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0070424]; response to yeast [GO:0001878]; tripeptide imp... | apical plasma membrane [GO:0016324]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886] | dipeptide transmembrane transporter activity [GO:0071916]; peptide:proton symporter activity [GO:0015333]; tripeptide transmembrane transporter activity [GO:0042937] | PF00854; | 1.20.1250.20; | Major facilitator superfamily, Proton-dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q63424}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q16348}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000305|PubMed:16317081}; Multi-pass membrane protein {ECO:0000255}.... | CATALYTIC ACTIVITY: Reaction=a dipeptide(out) + 2 H(+)(out) = a dipeptide(in) + 2 H(+)(in); Xref=Rhea:RHEA:76179, ChEBI:CHEBI:15378, ChEBI:CHEBI:90799; Evidence={ECO:0000269|PubMed:16317081}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76180; Evidence={ECO:0000269|PubMed:16317081}; CATALYTIC ACTIVITY: Reaction... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=97 uM for Gly-L-Gln (at pH 5.5 and -160 mV) {ECO:0000269|PubMed:16317081}; KM=79 uM for Gly-L-Gln (at pH 6.5 and -160 mV) {ECO:0000269|PubMed:16317081}; KM=48 uM for Gly-L-Gln (at pH 7.5 and -160 mV) {ECO:0000269|PubMed:16317081}; KM=163 uM for Gly-L-Gln (at pH 8.5... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:16317081}; | null | FUNCTION: Proton-coupled amino-acid transporter that transports oligopeptides of 2 to 4 amino acids with a preference for dipeptides (PubMed:16317081). Transports neutral and anionic dipeptides with a proton to peptide stoichiometry of 2:1 or 3:1 (By similarity). {ECO:0000250|UniProtKB:Q63424, ECO:0000269|PubMed:163170... | Danio rerio (Zebrafish) (Brachydanio rerio) |
B0TLB9 | FADB_SHEHH | MIYQSPTIEVELLEDNIAHLCFKAQGSVNKFDRETIDSLNAALDSIKQDTSIKALMLSSAKDAFIVGADITEFLGLFAEEDAVLQSWLEQANVVFNKLEDLPFPTLSAINGFALGAGCETILATDFRIADTTARIGLPETKLGIIPGFGGTVRLPRVIGADNALEWITSGKDQRPDAALKVGAIDAVVAPEQLRPAALRMLKDAMAEKLDWQTRRAKKLAPLTLPKLEAMMSFATAKGMVFKIAGKHYPAPMAVISVIEQAAQCGRAEALQIEHQAFIKLAKTEVAQALIGIFLNDQLVKGKAKKAGKLAKKVNSAAVLG... | 1.1.1.35; 4.2.1.17; 5.1.2.3; 5.3.3.8 | null | fatty acid beta-oxidation [GO:0006635] | fatty acid beta-oxidation multienzyme complex [GO:0036125] | 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; 3-hydroxybutyryl-CoA epimerase activity [GO:0008692]; delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300]; NAD+ binding [GO:0070403] | PF00725;PF02737;PF00378; | 1.10.1040.50;3.40.50.720; | Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-... | null | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000255|HAMAP-Rule:MF_01621}. | null | null | FUNCTION: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. | Shewanella halifaxensis (strain HAW-EB4) |
B0V1P1 | MC4R_DANRE | MNTSHHHGLHHSFRNHSQGALPVGKPSHGDRGSASGCYEQLLISTEIFLTLGLVSLLENILVIAAIVKNKNLHSPMYFFICSLAVADLLVSVSNASETVVMALITGGNLTNRESIIKNMDNVFDSMICSSLLASIWSLLAIAVDRYITIFYALRYHNIMTQRRAGTIITCIWTFCTVSGVLFIVYSESTTVLICLISMFFTMLALMASLYVHMFLLARLHMKRIAALPGNGPIWQAANMKGAITITILLGVFVVCWAPFFLHLILMISCPRNPYCVCFMSHFNMYLILIMCNSVIDPLIYAFRSQEMRKTFKEICCCWYG... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; energy homeostasis [GO:0097009]; energy reserve metabolic process [GO:0006112]; negative regulation of feeding behavior [GO:2000252]; regulation of growth [GO:0040008]; regulation of metabolic process [GO:0019222] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | melanocortin receptor activity [GO:0004977]; melanocyte-stimulating hormone receptor activity [GO:0004980] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Receptor specific to the heptapeptide core common to adrenocorticotropic hormone and alpha-, beta-, and gamma-MSH. Plays a central role in energy homeostasis and somatic growth. This receptor is mediated by G proteins that stimulate adenylate cyclase (cAMP). {ECO:0000269|PubMed:23869017}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B0V2N1 | PTPRS_MOUSE | MAPTWSPSVVSVVGPVGLFLVLLARGCLAEEPPRFIREPKDQIGVSGGVASFVCQATGDPKPRVTWNKKGKKVNSQRFETIDFDESSGAVLRIQPLRTPRDENVYECVAQNSVGEITIHAKLTVLREDQLPPGFPNIDMGPQLKVVERTRTATMLCAASGNPDPEITWFKDFLPVDPSASNGRIKQLRSGALQIESSEETDQGKYECVATNSAGVRYSSPANLYVRVRRVAPRFSILPMSHEIMPGGNVNITCVAVGSPMPYVKWMQGAEDLTPEDDMPVGRNVLELTDVKDSANYTCVAMSSLGVIEAVAQITVKSLPK... | 3.1.3.48 | null | cerebellum development [GO:0021549]; cerebral cortex development [GO:0021987]; corpus callosum development [GO:0022038]; establishment of endothelial intestinal barrier [GO:0090557]; hippocampus development [GO:0021766]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of axon extension [G... | axon [GO:0030424]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynaptic membrane [GO:0042734]; receptor complex [GO:0043235]; Schaffer collateral - CA1 synapse [GO:0098685]; syna... | chondroitin sulfate binding [GO:0035374]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; protein tyrosine phosphatase activity [GO:0004725] | PF00041;PF07679;PF13927;PF00102; | 2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 2A subfamily | PTM: A cleavage occurs, separating the extracellular domain from the transmembrane segment. This process called 'ectodomain shedding' is thought to be involved in receptor desensitization, signal transduction and/or membrane localization (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26231120}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:21454754}. Perikaryon {ECO:0000269|PubMed:21454754}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q64605}. Synapse, ... | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMe... | null | null | null | null | FUNCTION: Cell surface receptor that binds to glycosaminoglycans, including chondroitin sulfate proteoglycans and heparan sulfate proteoglycans (PubMed:19833921, PubMed:21454754, PubMed:22406547). Binding to chondroitin sulfate and heparan sulfate proteoglycans has opposite effects on PTPRS oligomerization and regulati... | Mus musculus (Mouse) |
B0VXE8 | CDK14_CALJA | MSTRNCQGMDSVIKPLDTIPEDKKVRVQRTQSTFDPFEKPTNQVKRVHSENNACINFKTSSTGKESPKVRRHSSPSSPTSPKFGKADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYVHTDLCQYMDKHPGGLHPDNVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYSNEVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQDQLERIFLVLGTPNEDTWPGVHSLPHF... | 2.7.11.22 | null | cell division [GO:0051301]; G2/M transition of mitotic cell cycle [GO:0000086]; phosphorylation [GO:0016310]; regulation of canonical Wnt signaling pathway [GO:0060828]; Wnt signaling pathway [GO:0016055] | cytoplasmic cyclin-dependent protein kinase holoenzyme complex [GO:0000308]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Recruited to the cell membrane by CCNY. {ECO:0000250}. | 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; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase involved in the control of the eukaryotic cell cycle, whose activity is controlled by an associated cyclin. Acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by mediating the phosphorylation of LRP6 at 'Ser-1490', leading to the activation of the Wnt sig... | Callithrix jacchus (White-tufted-ear marmoset) |
B0XMC1 | ER10A_ASPFC | MAIQTTTGLAARLVAKRATFPASRRNFSASRSALKEIQEAYILSGARTPTAKFNGSFVSVSAPELGAVAIKSAVSKSGVPVEKITDVYMGNVLQGAVGQAPARQASMFAGLSPTVESMTVNKVCASGLKAVALAAQNIQLGLAEAQVAGGMENMSRVPYYLPRSTQLPPFGEIKLQDGLIQDGLWDVYNQFHMGICAEKTAKKYEISREEQDQYAIQSYQRAQAAWKENKFAEEIAPVTVKGKKGETVVERDEGYENLRIDKMATLKPAFLRDGTGTVTAGNASTMNDGASALVLGSKAIAREFAQGNRALARIVSTADA... | 2.3.1.9 | COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:Q4WCL5}; | fatty acid beta-oxidation [GO:0006635] | mitochondrion [GO:0005739] | acetyl-CoA C-acetyltransferase activity [GO:0003985]; metal ion binding [GO:0046872] | PF02803;PF00108; | 3.40.47.10; | Thiolase-like superfamily, Thiolase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:32005728}. | CATALYTIC ACTIVITY: Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9; Evidence={ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000269|PubMed:32005728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21037; Evidence={ECO:0000269|Pu... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=26 uM for CoA {ECO:0000269|PubMed:32005728}; KM=43 uM for acetoacetyl-CoA {ECO:0000269|PubMed:32005728}; KM=232 uM for acetyl-CoA {ECO:0000269|PubMed:32005728}; | PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3. {ECO:0000269|PubMed:32005728}. | null | null | FUNCTION: Mitochondrial acetyl-CoA acetyltransferase that catalyzes both the formation and degradation of acetoacetyl-CoA (PubMed:32005728). Has no overlapping function with erg10B and seems not to be involved in ergosterol biosynthesis (PubMed:32005728). Plays an important role in growth, morphogenesis and maintaining... | Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya fumigata) |
B0XRM8 | ARO1_ASPFC | MTGPTKISILGQESIVADFGLWRNYVAKDLISGCPSTTYVLITDTNIGSIYTPGFQKSFEEAAASVSPSPRLLIYNAPPGEVSKSRQTKADIEDWMLSQSPPCGRDTVVIALGGGVIGDLTGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPSRIYIDLEFLETLPVREFINGMAEVIKTAAISSEEEFTALEDNAETILSAVRREVKPGQRRFEGIEEILKARILASARHKAFVVSADEREGGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELARHLGILKGVAVARIVKCI... | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:000476... | PF01761;PF01487;PF00275;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya fumigata) |
B0XT72 | GEL1_ASPFC | MKASAVTAALAVGASTVLAAPSIKARDDVTPITVKGNAFFKGDERFYIRGVDYQPGGSSDLADPIADADGCKRDIAKFKELGLNTIRVYSVDNSKNHDECMNALADAGIYLVLDVNTPKYSINRAKPKESYNDVYLQYIFATVDAFAGYKNTLAFFSGNEVINDGPSSSAAPYVKAVTRDLRQYIRSRKYREIPVGYSAADIDTNRLQMAQYMNCGSDDERSDFFAFNDYSWCDPSSFKTSGWDQKVKNFTGYGLPLFLSEYGCNTNKRQFQEVSSLYSTDMTGVYSGGLVYEYSQEASNYGLVEISGNNVKELPDFDAL... | 2.4.1.- | null | fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process [GO:0071970]; fungal-type cell wall organization [GO:0031505] | plasma membrane [GO:0005886]; side of membrane [GO:0098552] | 1,3-beta-glucanosyltransferase activity [GO:0042124] | PF03198; | 3.20.20.80; | Glycosyl hydrolase 72 family | PTM: The GPI-like anchor contains a phosphoceramide lipid group. The anchor position has not been determined. | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5. Active from pH 2.5 to 6.0. {ECO:0000269|PubMed:8900166}; | null | FUNCTION: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall morphogen... | Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya fumigata) |
B0Y0P7 | UBA4_ASPFC | MENLEQTCASLRAQIAATEAQLAGLKRELEIAEQAAEVKAQSTTRTITAEDGKTNETREWPLLSEEYKRYGRQMIVPQLGLQGQLKLRAARVLIVGAGGLGCPAALYLAGAGVGTLGLVDGDTVENSNLHRQVLHSSKNVGTFKVDSAIEYLRELNPHPTYVPYRAHLTPQEAPGIFKDYDIVLDCTDNPATRYLISDTAVLLGKPLVSASALRTEGQLMVLNYPPRPVGDKSGGPCYRCVFPKPPPANSVVSCADGGILGPVVGTMGVLQALEAIKVITSPAVNPSASPPSLLIFSAYSTPLFRTIRLRARRANCAVCS... | 2.7.7.80; 2.8.1.11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049}; | cell budding [GO:0007114]; cellular response to oxidative stress [GO:0034599]; invasive growth in response to glucose limitation [GO:0001403]; Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; protein urmylation [GO:0032447]; regulation of pseudohyphal growth [GO:2000220]; tRNA wobble position uridine thiola... | cytosol [GO:0005829] | AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; molybdopterin-synthase adenylyltransferase activity [GO:0061605]; molybdopterin-synthase sulfurtransferase activity [GO:0061604]; sulfotransferase activity [GO:0008146]; thiosulfate sulfurtr... | PF00581;PF00899; | 3.40.50.720;3.40.250.10; | HesA/MoeB/ThiF family, UBA4 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}. | CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ... | null | PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.; PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}. | null | null | FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm... | Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya fumigata) |
B0Y3B5 | SKP1_ASPFC | MTTVTLTSSDGVDITVDRDVAERSILIKNMLEDLGESDEAIPIPNVNEVVLKKVIEWCTHHKNDPPSTGDDDDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKALLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEE | null | null | exit from mitosis [GO:0010458]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; kinetochore assembly [GO:0051382]; mitotic nuclear membrane biogenesis [GO:0101026]; negative regulation of cytoplasmic translation [GO:2000766]; negative regulation of mitotic metapha... | CBF3 complex [GO:0031518]; kinetochore [GO:0000776]; nuclear SCF ubiquitin ligase complex [GO:0043224]; RAVE complex [GO:0043291]; single-stranded DNA-dependent ATP-dependent DNA helicase complex [GO:0017117] | cullin family protein binding [GO:0097602]; DNA replication origin binding [GO:0003688]; ubiquitin protein ligase activity [GO:0061630] | PF01466;PF03931; | null | SKP1 family | null | null | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor (By ... | Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya fumigata) |
B0Y4X4 | MPKA_ASPFC | MSDLQGRKVFKVFNQDFIVDERYNVTKELGQGAYGIVCAATNVHTGEGVAIKKVTNVFSKKILAKRALREIKLLQHFRGHRNITCLYDMDIPRPDNFNETYLYEELMECDLAAIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGFSIDPEENAGYMTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGGRPFFKGRDYVDQLNQILHYLGTPNEETLSRIGSPRAQEYVRNLPFMPKIPFQRLFPNANPDALDLLDRMLAFDPASRISVEEALEHPYLHIWHDA... | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:17981060}; | negative regulation of glucose mediated signaling pathway [GO:1902660]; negative regulation of mitotic cytokinesis [GO:1902413]; phosphorylation [GO:0016310]; positive regulation of calcium ion import across plasma membrane [GO:1905665]; positive regulation of calcium-mediated signaling [GO:0050850] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Phosphorylated during cell wall stress by the upstream MAPKK mkk2 (PubMed:17981060). Iron starvation triggers phosphorylation and thus activation of mpkA (PubMed:21883519). Phosphorylation increases upon osmotic stress and cell wall damage and depends on mpkC and sakA (PubMed:26878695). {ECO:0000269|PubMed:1798106... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21883519}. Note=Accumulates in the nucleus under iron depletion conditions. {ECO:0000269|PubMed:21883519}. | 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=2.7.11.24; Evidence={ECO:0000305|PubMed:17981060}; Physiolo... | null | null | null | null | FUNCTION: Mitogen-activated kinase (MAPK), part of the cell wall integrity (CWI) signaling pathway composed by three protein kinases bck1, mkk2 and mpkA and responsible for the maintaining of cell-wall integrity balance (PubMed:17981060, PubMed:19715768). The CWI pathway regulates also the oxidative stress response, as... | Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya fumigata) |
B0YA65 | ER10B_ASPFC | MSSLPAVYIVSSARTPVGSFLGSLSSLTAPQLGAHAIKAALAKVDGLKPSDVQEVFFGNVISANVGQNPARQCALGAGLEESTICTTVNKVCASGLKAIILGAQTIMTGNADVVVAGGTESMSNAPHYLPNLRTGAKYGHQSLVDGIMKDGLTDAGKQELMGLQAEECAQDHGFSREQQDEYAIRTYEKAQAAQKAGLFDEEIAPIQLPGFRGKPDVTVTQDEEPKNLNPEKLRAIKPAFIPGSGTVTAPNSSPLNDGAAAVVLVSEAKLKELNLKPVAKILGWGDAAQQPSKFTTAPALAIPKALKHAGVGQDAIDAFE... | 2.3.1.9 | COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000269|Ref.5}; | ergosterol biosynthetic process [GO:0006696]; fatty acid beta-oxidation [GO:0006635] | cytosol [GO:0005829]; mitochondrion [GO:0005739] | acetyl-CoA C-acetyltransferase activity [GO:0003985]; metal ion binding [GO:0046872] | PF02803;PF00108; | 3.40.47.10; | Thiolase-like superfamily, Thiolase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:32005728}. | CATALYTIC ACTIVITY: Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9; Evidence={ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000269|Ref.5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21037; Evidence={ECO:0000269|Ref.5}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=42 uM for acetoacetyl-CoA (in law salt conditions) {ECO:0000269|Ref.5}; KM=8 uM for acetoacetyl-CoA (in the presence of 100 mM NaCl) {ECO:0000269|Ref.5}; KM=8 uM for acetoacetyl-CoA (in the presence of 100 mM KCl) {ECO:0000269|Ref.5}; | PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3. {ECO:0000269|Ref.5}. | null | null | FUNCTION: Acetyl-CoA acetyltransferase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (Probable) (PubMed:32005728). In this module, the cytoso... | Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya fumigata) |
B0YJ81 | HACD1_HUMAN | MGRLTEAAAAGSGSRAAGWAGSPPTLLPLSPTSPRCAATMASSDEDGTNGGASEAGEDREAPGERRRLGVLATAWLTFYDIAMTAGWLVLAIAMVRFYMEKGTHRGLYKSIQKTLKFFQTFALLEIVHCLIGIVPTSVIVTGVQVSSRIFMVWLITHSIKPIQNEESVVLFLVAWTVTEITRYSFYTFSLLDHLPYFIKWARYNFFIILYPVGVAGELLTIYAALPHVKKTGMFSIRLPNKYNVSFDYYYFLLITMASYIPLFPQLYFHMLRQRRKVLHGEVIVEKDD | 4.2.1.134 | null | cementum mineralization [GO:0071529]; fatty acid elongation [GO:0030497]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; positive regulation of cell-substrate adhesion [GO:0010811]; protein-containing complex assembly [GO:0065003]; sphingolipid biosynthetic process [GO:0030148]; very long-chain fatty acid... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | 3-hydroxyacyl-CoA dehydratase activity [GO:0018812]; enzyme binding [GO:0019899]; hydroxyapatite binding [GO:0046848]; very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase activity [GO:0102158] | PF04387; | null | Very long-chain fatty acids dehydratase HACD family | PTM: N-glycosylated. {ECO:0000269|PubMed:23933735}. | SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18554506}; Multi-pass membrane protein {ECO:0000269|PubMed:18554506}. | CATALYTIC ACTIVITY: Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:45812, ChEBI:CHEBI:15377, ChEBI:CHEBI:83728, ChEBI:CHEBI:85440; EC=4.2.1.134; Evidence={ECO:0000269|PubMed:18554506, ECO:0000269|PubMed:23933735}; PhysiologicalDirection=left-to-right; Xref=Rhe... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=33.6 uM for 3-hydroxypalmitoyl-CoA (at 37 degrees Celsius) {ECO:0000269|PubMed:18554506}; | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000269|PubMed:18554506}. | null | null | FUNCTION: [Isoform 1]: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-h... | Homo sapiens (Human) |
B0ZB55 | OMT1_HUMLU | MESLRGQEQIWQLMFSFVDSMALKCAIELRIADIIHSHGKPITLSQIASGIRSNSNSSISPNIPYLSRIMRFLVRKNIFTEHQEDNDEVISLYGLSDSSRWLLRDFKSSLAPMVLMQTHPLSMAVWHFLEDYVRNSSNTFEKAHGCNIWEFSSANPDFNKIFNNAMASIVPIYMGAVLSSYKDGLGCIKGTVVDVGGGTGGSISELMKYYPNIKGINFDLPHVIATAPALDGVTHISGDIFESIPSADAVLMKGVLHCFSDEKCVKVLRNCRKAITDKKNGKIIILEIVLDPTSNQIFDETRMVYDLLIPLFSGGKERTE... | 2.1.1.338 | null | melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259] | cytoplasm [GO:0005737] | acetylserotonin O-methyltransferase activity [GO:0017096]; protein dimerization activity [GO:0046983] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29760092}. | CATALYTIC ACTIVITY: Reaction=desmethylxanthohumol + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + xanthohumol; Xref=Rhea:RHEA:51696, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134289, ChEBI:CHEBI:134302; EC=2.1.1.338; Evidence={ECO:0000269|PubMed:18223037}; PhysiologicalDirectio... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18 uM for desmethylxanthohumol {ECO:0000269|PubMed:18223037}; KM=286 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:18223037}; Vmax=55 pmol/sec/mg enzyme toward desmethylxanthohumol {ECO:0000269|PubMed:18223037}; Vmax=56 pmol/sec/mg enzyme toward S-adenosyl-L-m... | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:30468448}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:18223037}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-37 degrees Celsius.; | FUNCTION: Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Catalyzes the biosynthesis of xanthohumol (PubMed:18223037). Methylates desmethylxanthohumol and xanthogalenol, but not caffeic acid, prenylfla... | Humulus lupulus (European hop) |
B0ZB56 | OMT2_HUMLU | MELARNDQTEAALRGEANVWKSINGIADFMVMKCALELRIPDIVHSHSAPITLAQIASSVPDSPSLNLSYLSRIMRLLVRRKIFSQHKSLDGEEVLYGPTHSSRLLLSKTTLPDQVTLAPFVAFMTHPYLSAPWSCLARCVKEGGNGFEMVHGGRQLWDLSPGNPEFNKVFNDGMASTARITTMAILSEYRDVFCGICSLVDVGGEFGGSISAIVKSHPHIKGINYDLPHVVATAPTYTGLVSHVGGNMFEWIPTAVAVFMKWILHDWADEDCVKILKNCRRAMPEKGGKIIIVDIVLEPEGNGLFDDAAVMLDIALMAL... | 2.1.1.154; 2.1.1.338; 2.1.1.339 | null | melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259] | cytoplasm [GO:0005737] | acetylserotonin O-methyltransferase activity [GO:0017096]; isoliquiritigenin 2'-O-methyltransferase activity [GO:0033802]; protein dimerization activity [GO:0046983] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B0ZB55}. | CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + xanthohumol = 4-O-methylxanthohumol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51704, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134289, ChEBI:CHEBI:139273; EC=2.1.1.339; Evidence={ECO:0000269|PubMed:18223037}; PhysiologicalDirecti... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=237 uM for chalconaringenin {ECO:0000269|PubMed:18223037}; KM=23 uM for desmethylxanthohumol {ECO:0000269|PubMed:18223037}; KM=31 uM for xanthohumol {ECO:0000269|PubMed:18223037}; KM=19 uM for resveratrol {ECO:0000269|PubMed:18223037}; KM=34 uM for S-adenosyl-L-met... | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:30468448}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:18223037}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 39 degrees Celsius. {ECO:0000269|PubMed:18223037}; | FUNCTION: Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). O-methyltransferase with a low substrate selectivity (PubMed:18223037). Methylates chalconaringenin, desmethylxanthohumol, xanthohumol, isoliqu... | Humulus lupulus (European hop) |
B1A612 | MENC_GEOKU | MAINIEYVILRHLQMELKAPFTTSFGTFQTKEFILVEVVDCDGVSGWGESVAFSVPWYSEETVKTNWHMLEEFLVPLLFSKPLRHPAELPERFAAIRQNNMAKAALEGAVWDLYAKRLGVPLCQALGGTKKEIEVGVSIGIQPTVDDLLQVIERYVAQGYRRIKVKIKPGWDVDVIRDVRRAFPDVPLMADANSAYTLADAKRLQALDEFGLMMIEQPLAADDLVDHARLQPLLKTPICLDESIRSYDDARKALDLGSCRIINIKIGRVGGLWEAKRIHDLCAERGVPVWCGGMLEAGVGRAHNIAITTLENFALPGDTA... | 4.2.1.113; 5.1.1.- | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000269|Ref.1}; Note=Shows highest activity in vitro with Co(2+), Mn(2+) and Ni(2+). {ECO:0000269|Ref.1}; | menaquinone biosynthetic process [GO:0009234] | null | isomerase activity [GO:0016853]; magnesium ion binding [GO:0000287]; O-succinylbenzoate synthase activity [GO:0043748] | PF13378;PF02746; | 3.20.20.120;3.30.390.10; | Mandelate racemase/muconate lactonizing enzyme family, MenC type 2 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate = 2-succinylbenzoate + H2O; Xref=Rhea:RHEA:10196, ChEBI:CHEBI:15377, ChEBI:CHEBI:18325, ChEBI:CHEBI:58689; EC=4.2.1.113; Evidence={ECO:0000255|HAMAP-Rule:MF_01933}; CATALYTIC ACTIVITY: Reaction=N(alpha)-acetyl-D-methionine = N(a... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.12 mM for N-succinyl-L-alanine {ECO:0000269|Ref.1}; KM=0.13 mM for N-succinyl-D-alanine {ECO:0000269|Ref.1}; KM=0.13 mM for N-succinyl-L-phenylalanine {ECO:0000269|Ref.1}; KM=0.04 mM for N-succinyl-D-phenylalanine {ECO:0000269|Ref.1}; KM=8 mM for N-acetyl-L-methi... | PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_01933}.; PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01933}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|Ref.1}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|Ref.1}; | FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (By similarity). Also acts as a N-succinylamino acid racemase (NSAR) that catalyzes the racemization of various N-succinylamino acids, including N-succinyl-alanine and N-succinyl-phenylalanine (Ref.1). Can catal... | Geobacillus kaustophilus |
B1A8Z2 | CIB1_SHEEP | MGGSGSRLSKELLAEYQDLTFLTKQEILLAHRRFCELLPQEHRSVEESLQARVSLEQILSLPELKANPFKERICKVFSTSPSRDSLSFEDFLDLLSVFSDTATPDIKSHYAFRIFDFDDDGTLNREDLSQLVNCLTGESEDTRLSASEMKQLIDNILEESDIDRDGTINLSEFQHVISRSPDFASSFKIVL | null | null | angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cell division [GO:0051301]; cellular response to growth factor stimulus [GO:0071363]; integrin-mediated signaling pathway [GO:0007229]; positive regulation of calcineurin-NF... | apical plasma membrane [GO:0016324]; centrosome [GO:0005813]; filopodium tip [GO:0032433]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; ruffle membrane [GO:0032587]; sarcolemma [GO:0042383] | calcium ion binding [GO:0005509]; magnesium ion binding [GO:0000287]; protein-membrane adaptor activity [GO:0043495] | PF13499; | 1.10.238.10; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q99828}; Lipid-anchor {ECO:0000250|UniProtKB:Q99828}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q99828}. Cell membrane {ECO:0000250|UniProtKB:Q99828}. Apical cell membrane {ECO:0000250|UniProtKB:Q99828}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB... | null | null | null | null | null | FUNCTION: Calcium-binding protein that plays a role in the regulation of numerous cellular processes, such as cell differentiation, cell division, cell proliferation, cell migration, thrombosis, angiogenesis, cardiac hypertrophy and apoptosis. Involved in bone marrow megakaryocyte differentiation by negatively regulati... | Ovis aries (Sheep) |
B1AK53 | ESPN_HUMAN | MALEQALQAARQGELDVLRSLHAAGLLGPSLRDPLDALPVHHAARAGKLHCLRFLVEEAALPAAARARNGATPAHDASATGHLACLQWLLSQGGCRVQDKDNSGATVLHLAARFGHPEVVNWLLHHGGGDPTAATDMGALPIHYAAAKGDFPSLRLLVEHYPEGVNAQTKNGATPLYLACQEGHLEVTQYLVQECGADPHARAHDGMTPLHAAAQMGHSPVIVWLVSCTDVSLSEQDKDGATAMHFAASRGHTKVLSWLLLHGGEISADLWGGTPLHDAAENGELECCQILVVNGAELDVRDRDGYTAADLSDFNGHSHC... | null | null | actin filament bundle assembly [GO:0051017]; microvillar actin bundle assembly [GO:0030034]; sensory perception of sound [GO:0007605] | brush border [GO:0005903]; cytoplasm [GO:0005737]; filamentous actin [GO:0031941]; microvillus [GO:0005902]; stereocilium [GO:0032420]; stereocilium tip [GO:0032426] | actin filament binding [GO:0051015]; SH3 domain binding [GO:0017124] | PF12796;PF02205; | 1.25.40.20; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9ET47}. Cell projection, stereocilium {ECO:0000269|PubMed:29572253}. Cell projection, microvillus {ECO:0000269|PubMed:29572253}. | null | null | null | null | null | FUNCTION: Multifunctional actin-bundling protein. Plays a major role in regulating the organization, dimension, dynamics and signaling capacities of the actin filament-rich microvilli in the mechanosensory and chemosensory cells (PubMed:29572253). Required for the assembly and stabilization of the stereociliary paralle... | Homo sapiens (Human) |
B1AL88 | NALF1_HUMAN | MTRGAWMCRQYDDGLKIWLAAPRENEKPFIDSERAQKWRLSLASLLFFTVLLSDHLWFCAEAKLTRARDKEHQQQQRQQQQQQQQQRQRQQQQQQRRQQEPSWPALLASMGESSPAAQAHRLLSASSSPTLPPSPGDGGGGGGKGNRGKDDRGKALFLGNSAKPVWRLETCYPQGASSGQCFTVENADAVCARNWSRGAAGGDGQEVRSKHPTPLWNLSDFYLSFCNSYTLWELFSGLSSPNTLNCSLDVVLKEGGEMTTCRQCVEAYQDYDHHAQEKYEEFESVLHKYLQSEEYSVKSCPEDCKIVYKAWLCSQYFEVT... | null | null | calcium ion import across plasma membrane [GO:0098703] | plasma membrane [GO:0005886] | stretch-activated, monoatomic cation-selective, calcium channel activity [GO:0015275] | null | null | NALF family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32494638}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Auxillary component of the NALCN sodium channel complex, a channel that regulates the resting membrane potential and controls neuronal excitability. {ECO:0000269|PubMed:32494638}. | Homo sapiens (Human) |
B1AQJ2 | UBP36_MOUSE | MPIVDKLKEALKPGRKDSAEDGDLGRLLAASAKKVLLQRIEFEPASKSFSYQLESLKSKYVLLSARAEGASRHRSGDELQARKPGTERVSGSGGDGVPAPQKVLFPVERLSLRWERVFRVGAGLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSCHQGGFCMLCLMQNHMVQAFANSGNAIKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKACLNGYAKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIALEIRQAANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRT... | 2.3.2.-; 3.4.19.12 | null | chromatin organization [GO:0006325]; negative regulation of macroautophagy [GO:0016242]; nucleolus organization [GO:0007000]; protein deubiquitination [GO:0016579]; protein stabilization [GO:0050821]; proteolysis [GO:0006508]; regulation of apoptotic process [GO:0042981]; regulation of protein stability [GO:0031647]; r... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; histone H2B deubiquitinase activity [GO:0140936]; K48-linked deubiquitinase activity [GO:1990380]; RNA binding [GO:0003723]; transferase activity [GO:0016740] | PF00443; | 3.90.70.10; | Peptidase C19 family | PTM: Polyubiquitinated by NEDD4L, no effect on USP36 protein levels. Both proteins interact with and regulate each other's ubiquitination levels. {ECO:0000250|UniProtKB:Q9P275}. | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9P275}. Cytoplasm {ECO:0000250|UniProtKB:Q9P275}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q9P275}; | null | null | null | null | FUNCTION: Deubiquitinase essential for the regulation of nucleolar structure and function. Required for cell and organism viability (PubMed:29273634). Plays an important role in ribosomal RNA processing and protein synthesis, which is mediated, at least in part, through deubiquitination of DHX33, NPM1 and FBL, regulati... | Mus musculus (Mouse) |
B1ARD8 | SLFN8_MOUSE | METHPSLAVKWSCPDLTIYAGEVTIGEEDRNKMDSKKRKLEKTRITEAACALLNSGGGLIAMQMTNKSEHPVEMGQDLEKSLRELIMSPNMQAFFETKQQEDQFYIFVKSWSCRPEDGSTKPRICSLGSSLYCRSITSKVAMDSREAFEFLKDKKACIKYRPTDDGAPPAKIPRAMCQNSLESNPAFEIFQSKKLEYGQCLLFSESTSIEFKQFSTKHVQAYMKNIIPEYISAFANTQGGYLFIGVDDKRIILGCPKDNVDRDSLKTVANETISKVPVFHFCSSKDKDKVSYETRVIDVFQEGNLYGYLCVIKVEPFCCA... | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q5U311}; Note=Can also use Mn(2+). {ECO:0000250|UniProtKB:Q5U311}; | defense response to virus [GO:0051607]; immune system process [GO:0002376]; rRNA catabolic process [GO:0016075]; tRNA catabolic process [GO:0016078] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; RNA endonuclease activity [GO:0004521]; tRNA binding [GO:0000049]; zinc ion binding [GO:0008270] | PF17057;PF09848;PF04326;PF21026;PF13538; | 3.40.50.300;3.30.950.30; | Schlafen family, Subgroup III subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q68D06}. | null | null | null | null | null | FUNCTION: Endoribonuclease that cleaves tRNAs and rRNAs (PubMed:29563550). Cleaves tRNAs 11 nucleotides from the 3'-terminus at the acceptor stem (PubMed:29563550). May be involved in immune system via regulation of inflammation (PubMed:29528433). {ECO:0000269|PubMed:29528433, ECO:0000269|PubMed:29563550}. | Mus musculus (Mouse) |
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