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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O95989 | NUDT3_HUMAN | MMKLKSNQTRTYDGDGYKKRAACLCFRSESEEEVLLVSSSRHPDRWIVPGGGMEPEEEPSVAAVREVCEEAGVKGTLGRLVGIFENQERKHRTYVYVLIVTEVLEDWEDSVNIGRKREWFKIEDAIKVLQYHKPVQASYFETLRQGYSANNGTPVVATTYSVSAQSSMSGIR | 3.6.1.10; 3.6.1.52; 3.6.1.59; 3.6.1.61; 3.6.1.62 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19585659, ECO:0000269|PubMed:34788624}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:34788624}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:34788624}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000269... | adenosine 5'-(hexahydrogen pentaphosphate) catabolic process [GO:1901911]; cell-cell signaling [GO:0007267]; diadenosine hexaphosphate catabolic process [GO:1901909]; diadenosine pentaphosphate catabolic process [GO:1901907]; diadenosine polyphosphate catabolic process [GO:0015961]; diphosphoinositol polyphosphate cata... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | 5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity [GO:0140932]; 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity [GO:0140933]; bis(5'-adenosyl)-hexaphosphatase activity [GO:0034431]; bis(5'-adenosyl)-pentaphosphatase activity [GO:0034432]; diphosphoinositol-polyphosphate diphosphata... | PF00293; | 3.90.79.10; | Nudix hydrolase family, DIPP subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:34788624}. Nucleus {ECO:0000269|PubMed:34788624}. | CATALYTIC ACTIVITY: Reaction=diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.; EC=3.6.1.52; Evidence={ECO:0000269|PubMed:10585413, ECO:0000269|PubMed:12370170, ECO:0000269|PubMed:34788624, ECO:0000269|PubMed:9822604}; CATALYTIC ACTIVITY: Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.9 uM for Ap6A {ECO:0000269|PubMed:10419486, ECO:0000269|PubMed:12370170}; KM=7.7 uM for Ap5A {ECO:0000269|PubMed:10419486}; KM=38 mM for 5-phosphoribose 1-diphosphate {ECO:0000269|PubMed:12370170}; KM=4.2 nM for PP-InsP5 {ECO:0000269|PubMed:12370170}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-7.5 for PP-InsP5 hydrolysis. Displays strong endopolyphosphatase activity at pH 6.8 and 7.4. {ECO:0000269|PubMed:34788624, ECO:0000269|PubMed:9822604}; | null | FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction (PubMed:10585413, PubMed:12370170, PubMed:9822604). InsP6 (inositol hexakisphosphate) is no... | Homo sapiens (Human) |
O95990 | F107A_HUMAN | MYSEIQRERADIGGLMARPEYREWNPELIKPKKLLNPVKASRSHQELHRELLMNHRRGLGVDSKPELQRVLEHRRRNQLIKKKKEELEAKRLQCPFEQELLRRQQRLNQLEKPPEKEEDHAPEFIKVRENLRRIATLTSEEREL | null | null | actin filament bundle assembly [GO:0051017]; actin filament polymerization [GO:0030041]; cell cycle [GO:0007049]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to nutrient levels [GO:0031669]; cognition [GO:0050890]; negative regulation of focal adhesion assembly [GO:0051895]; negative re... | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; neuron projection [GO:0043005]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; ruffle membrane [GO:0032587]; stress fiber [GO:0001725]; synapse [GO:0045202] | actin binding [GO:0003779] | PF06625; | null | FAM107 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10564580, ECO:0000269|PubMed:11256614, ECO:0000269|PubMed:20543869, ECO:0000269|PubMed:28604741}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:20543869, ECO:0000269|PubMed:28604741}. Cell junction, focal adhesion {ECO:0000269|PubMed:20543869}. Cell projecti... | null | null | null | null | null | FUNCTION: Stress-inducible actin-binding protein that plays a role in synaptic and cognitive functions by modulating actin filamentous (F-actin) dynamics. Mediates polymerization of globular actin to F-actin. Also binds to, stabilizes and bundles F-actin. Involved in synaptic function by regulating neurite outgrowth in... | Homo sapiens (Human) |
O95992 | CH25H_HUMAN | MSCHNCSDPQVLCSSGQLFLQPLWDHLRSWEALLQSPFFPVIFSITTYVGFCLPFVVLDILCSWVPALRRYKIHPDFSPSAQQLLPCLGQTLYQHVMFVFPVTLLHWARSPALLPHEAPELLLLLHHILFCLLLFDMEFFVWHLLHHKVPWLYRTFHKVHHQNSSSFALATQYMSVWELFSLGFFDMMNVTLLGCHPLTTLTFHVVNIWLSVEDHSGYNFPWSTHRLVPFGWYGGVVHHDLHHSHFNCNFAPYFTHWDKILGTLRTASVPAR | 1.14.99.38 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:Q9Z0F5}; | B cell chemotaxis [GO:0035754]; cholesterol metabolic process [GO:0008203]; lipid metabolic process [GO:0006629]; negative regulation of cholesterol metabolic process [GO:0090206]; negative regulation of fusion of virus membrane with host plasma membrane [GO:1903914]; response to type I interferon [GO:0034340]; sterol ... | cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789] | C-4 methylsterol oxidase activity [GO:0000254]; cholesterol 25-hydroxylase activity [GO:0001567]; iron ion binding [GO:0005506]; steroid hydroxylase activity [GO:0008395] | PF04116; | null | Sterol desaturase family | PTM: N-glycosylated. {ECO:0000269|PubMed:9852097}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z0F5}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Z0F5}. | CATALYTIC ACTIVITY: Reaction=AH2 + cholesterol + O2 = 25-hydroxycholesterol + A + H2O; Xref=Rhea:RHEA:21104, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:17499, ChEBI:CHEBI:42977; EC=1.14.99.38; Evidence={ECO:0000269|PubMed:33239446, ECO:0000269|PubMed:9852097}; PhysiologicalD... | null | null | null | null | FUNCTION: Catalyzes the formation of 25-hydroxycholesterol from cholesterol, leading to repress cholesterol biosynthetic enzymes (PubMed:9852097). Plays a key role in cell positioning and movement in lymphoid tissues: 25-hydroxycholesterol is an intermediate in biosynthesis of 7-alpha,25-dihydroxycholesterol (7-alpha,2... | Homo sapiens (Human) |
O95994 | AGR2_HUMAN | MEKIPVSAFLLLVALSYTLARDTTVKPGAKKDTKDSRPKLPQTLSRGWGDQLIWTQTYEEALYKSKTSNKPLMIIHHLDECPHSQALKKVFAENKEIQKLAEQFVLLNLVYETTDKHLSPDGQYVPRIMFVDPSLTVRADITGRYSNRLYAYEPADTALLLDNMKKALKLLKTEL | null | null | digestive tract morphogenesis [GO:0048546]; inflammatory response [GO:0006954]; lung goblet cell differentiation [GO:0060480]; mucus secretion [GO:0070254]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of developmental growth [GO:0048639]; positive regulation of epidermal growth fact... | endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | dystroglycan binding [GO:0002162]; epidermal growth factor receptor binding [GO:0005154]; identical protein binding [GO:0042802] | PF13899; | 3.40.30.10; | AGR family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15834940}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O88312}. | null | null | null | null | null | FUNCTION: Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells (By similarity). Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth. Promotes cell adhesion (PubMed:23274113). {ECO:0000250, ECO:0000269|PubMe... | Homo sapiens (Human) |
O95995 | DRC4_HUMAN | MAPKKKGKKGKAKGTPIVDGLAPEDMSKEQVEEHVSRIREELDREREERNYFQLERDKIHTFWEITRRQLEEKKAELRNKDREMEEAEERHQVEIKVYKQKVKHLLYEHQNNLTEMKAEGTVVMKLAQKEHRIQESVLRKDMRALKVELKEQELASEVVVKNLRLKHTEEITRMRNDFERQVREIEAKYDKKMKMLRDELDLRRKTELHEVEERKNGQIHTLMQRHEEAFTDIKNYYNDITLNNLALINSLKEQMEDMRKKEDHLEREMAEVSGQNKRLADPLQKAREEMSEMQKQLANYERDKQILLCTKARLKVREKE... | null | null | axoneme assembly [GO:0035082]; brain development [GO:0007420]; cilium movement involved in cell motility [GO:0060294]; determination of left/right symmetry [GO:0007368]; epithelial cilium movement involved in extracellular fluid movement [GO:0003351]; establishment of localization in cell [GO:0051649]; flagellated sper... | axoneme [GO:0005930]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytosol [GO:0005829]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; microtubule [GO:0005874]; motile cilium [GO:0031514]; plasma membrane [GO:0005886]; sperm flagellum [GO:0036126] | microtubule binding [GO:0008017]; small GTPase binding [GO:0031267] | PF13851; | null | DRC4 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q60779}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10969087}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q60779}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:16643277, ECO:0000269|PubMed:26387594}. Cytoplasm, cytoskeleton, cilium ba... | null | null | null | null | null | FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Plays an important role in the assembly of the N-DRC linker (By similarity). Plays dua... | Homo sapiens (Human) |
O95996 | APCL_HUMAN | MASSVAPYEQLVRQVEALKAENSHLRQELRDNSSHLSKLETETSGMKEVLKHLQGKLEQEARVLVSSGQTEVLEQLKALQMDITSLYNLKFQPPTLGPEPAARTPEGSPVHGSGPSKDSFGELSRATIRLLEELDRERCFLLNEIEKEEKEKLWYYSQLQGLSKRLDELPHVETQFSMQMDLIRQQLEFEAQHIRSLMEERFGTSDEMVQRAQIRASRLEQIDKELLEAQDRVQQTEPQALLAVKSVPVDEDPETEVPTHPEDGTPQPGNSKVEVVFWLLSMLATRDQEDTARTLLAMSSSPESCVAMRRSGCLPLLLQI... | null | null | activation of GTPase activity [GO:0090630]; cell fate specification [GO:0001708]; cell migration [GO:0016477]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of microtubule depolymerization [GO:0007026]; nervous system develop... | actin filament [GO:0005884]; beta-catenin destruction complex [GO:0030877]; catenin complex [GO:0016342]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; intercellular bridge [GO:0045171]; lamellipodium membrane [GO:0031258]; microtubule cytoskeleton [GO... | beta-catenin binding [GO:0008013]; gamma-catenin binding [GO:0045295]; microtubule binding [GO:0008017] | PF05956;PF16689;PF05923;PF18797;PF00514;PF16629;PF05924;PF11414; | 1.20.5.10;1.10.287.450;1.25.10.10; | Adenomatous polyposis coli (APC) family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:25753423}. Golgi apparatus {ECO:0000269|PubMed:11691822}. Cytoplasm {ECO:0000269|PubMed:11691822}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10646860}. Note=Associated with actin filaments... | null | null | null | null | null | FUNCTION: Stabilizes microtubules and may regulate actin fiber dynamics through the activation of Rho family GTPases (PubMed:25753423). May also function in Wnt signaling by promoting the rapid degradation of CTNNB1 (PubMed:10021369, PubMed:11691822, PubMed:9823329). {ECO:0000269|PubMed:10021369, ECO:0000269|PubMed:116... | Homo sapiens (Human) |
O95997 | PTTG1_HUMAN | MATLIYVDKENGEPGTRVVAKDGLKLGSGPSIKALDGRSQVSTPRFGKTFDAPPALPKATRKALGTVNRATEKSVKTKGPLKQKQPSFSAKKMTEKTVKAKSSVPASDDAYPEIEKFFPFNPLDFESFDLPEEHQIAHLPLSGVPLMILDEERELEKLFQLGPPSPVKMPSPPWESNLLQSPSSILSTLDVELPPVCCDIDI | null | null | cell division [GO:0051301]; chromosome organization [GO:0051276]; DNA repair [GO:0006281]; homologous chromosome segregation [GO:0045143]; spermatogenesis [GO:0007283] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | cysteine-type endopeptidase inhibitor activity [GO:0004869]; molecular function activator activity [GO:0140677]; SH3 domain binding [GO:0017124] | PF04856; | null | Securin family | PTM: Phosphorylated at Ser-165 by CDK1 during mitosis. {ECO:0000269|PubMed:10656688}.; PTM: Phosphorylated in vitro by ds-DNA kinase. {ECO:0000269|PubMed:10656688}.; PTM: Ubiquitinated through 'Lys-11' linkage of ubiquitin moieties by the anaphase promoting complex (APC) at the onset of anaphase, conducting to its degr... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. | null | null | null | null | null | FUNCTION: Regulatory protein, which plays a central role in chromosome stability, in the p53/TP53 pathway, and DNA repair. Probably acts by blocking the action of key proteins. During the mitosis, it blocks Separase/ESPL1 function, preventing the proteolysis of the cohesin complex and the subsequent segregation of the ... | Homo sapiens (Human) |
O95998 | I18BP_HUMAN | MTMRHNWTPDLSPLWVLLLCAHVVTLLVRATPVSQTTTAATASVRSTKDPCPSQPPVFPAAKQCPALEVTWPEVEVPLNGTLSLSCVACSRFPNFSILYWLGNGSFIEHLPGRLWEGSTSRERGSTGTQLCKALVLEQLTPALHSTNFSCVLVDPEQVVQRHVVLAQLWAGLRATLPPTQEALPSSHSSPQQQG | null | null | cellular response to hydrogen peroxide [GO:0070301]; cellular response to tumor necrosis factor [GO:0071356]; response to lipopolysaccharide [GO:0032496]; T-helper 1 type immune response [GO:0042088] | extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | interleukin-18 binding [GO:0042007]; receptor antagonist activity [GO:0048019] | null | 2.60.40.10; | null | PTM: N- and O-glycosylated. O-glycosylated with core 1-like and core 2-like glycans. O-glycan heterogeneity at Ser-53: HexHexNAc (major) and Hex2HexNAc2 (minor). N-glycan heterogeneity at Asn-103: Hex5HexNAc4 (minor), dHex1Hex5HexNAc4 (major) and Hex6HexNAc5 (minor); N-glycan at Asn-147: dHex1Hex5HexNAc4. {ECO:0000269|... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31213488}. | null | null | null | null | null | FUNCTION: Isoform A binds to IL-18 and inhibits its activity. Functions as an inhibitor of the early TH1 cytokine response. {ECO:0000269|PubMed:10023777, ECO:0000269|PubMed:10655506, ECO:0000269|PubMed:31213488}. | Homo sapiens (Human) |
O95999 | BCL10_HUMAN | MEPTAPSLTEEDLTEVKKDALENLRVYLCEKIIAERHFDHLRAKKILSREDTEEISCRTSSRKRAGKLLDYLQENPKGLDTLVESIRREKTQNFLIQKITDEVLKLRNIKLEHLKGLKCSSCEPFPDGATNNLSRSNSDESNFSEKLRASTVMYHPEGESSTTPFFSTNSSLNLPVLEVGRTENTIFSSTTLPRPGDPGAPPLPPDLQLEEEGTCANSSEMFLPLRSRTVSRQ | null | null | adaptive immune response [GO:0002250]; antifungal innate immune response [GO:0061760]; B cell apoptotic process [GO:0001783]; canonical NF-kappaB signal transduction [GO:0007249]; cellular defense response [GO:0006968]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to mechanical stimulus [GO:0... | CBM complex [GO:0032449]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; immunological synapse [GO:0001772]; lysosome [GO:0005764]; membrane raft [GO:0045121]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; polkadots [GO:0002096]; protein-containing complex [GO:... | CARD domain binding [GO:0050700]; general transcription initiation factor binding [GO:0140296]; identical protein binding [GO:0042802]; kinase activator activity [GO:0019209]; NF-kappaB binding [GO:0051059]; protease binding [GO:0002020]; protein kinase B binding [GO:0043422]; protein self-association [GO:0043621]; pro... | PF00619; | 1.10.533.10; | null | PTM: Phosphorylated. Phosphorylation results in dissociation from TRAF2 and binding to BIRC2/c-IAP2 (PubMed:11466612). Phosphorylated by IKBKB/IKKB (PubMed:17213322). {ECO:0000269|PubMed:11466612, ECO:0000269|PubMed:17213322}.; PTM: Ubiquitinated via both 'Lys-63'-linked and linear ('Met-1'-linked) polyubiquitin chains... | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:17287217}. Membrane raft {ECO:0000269|PubMed:17287217}. Note=Appears to have a perinuclear, compact and filamentous pattern of expression. Also found in the nucleus of several types of tumor cells. Colocalized with DPP4 in membrane rafts. {ECO:0000... | null | null | null | null | null | FUNCTION: Plays a key role in both adaptive and innate immune signaling by bridging CARD domain-containing proteins to immune activation (PubMed:10187770, PubMed:10364242, PubMed:10400625, PubMed:24074955, PubMed:25365219). Acts by channeling adaptive and innate immune signaling downstream of CARD domain-containing pro... | Homo sapiens (Human) |
O96000 | NDUBA_HUMAN | MPDSWDKDVYPEPPRRTPVQPNPIVYMMKAFDLIVDRPVTLVREFIERQHAKNRYYYYHRQYRRVPDITECKEEDIMCMYEAEMQWKRDYKVDQEIINIMQDRLKACQQREGQNYQQNCIKEVEQFTQVAKAYQDRYQDLGAYSSARKCLAKQRQRMLQERKAAKEAAAATS | null | null | aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776] | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747] | NADH dehydrogenase (ubiquinone) activity [GO:0008137] | PF10249; | null | Complex I NDUFB10 subunit family | PTM: The formation of intramolecular disulfide bonds is assisted by CHCHD4 and ensures folding, import into the mitochondrion and is required for the function in mitochondrial respiratory chain complex I assembly. {ECO:0000269|PubMed:28040730}. | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:28040730, ECO:0000305|PubMed:12611891}; Peripheral membrane protein {ECO:0000305}; Matrix side {ECO:0000305}. | null | null | null | null | null | FUNCTION: Accessory subunit that is involved in the functional assembly of the mitochondrial respiratory chain complex I. Complex I has an NADH dehydrogenase activity with ubiquinone as an immediate electron acceptor and mediates the transfer of electrons from NADH to the respiratory chain. {ECO:0000269|PubMed:27626371... | Homo sapiens (Human) |
O96004 | HAND1_HUMAN | MNLVGSYAHHHHHHHPHPAHPMLHEPFLFGPASRCHQERPYFQSWLLSPADAAPDFPAGGPPPAAAAAATAYGPDARPGQSPGRLEALGGRLGRRKGSGPKKERRRTESINSAFAELRECIPNVPADTKLSKIKTLRLATSYIAYLMDVLAKDAQSGDPEAFKAELKKADGGRESKRKRELQQHEGFPPALGPVEKRIKGRTGWPQQVWALELNQ | null | null | angiogenesis [GO:0001525]; blastocyst development [GO:0001824]; cardiac left ventricle formation [GO:0003218]; cardiac right ventricle formation [GO:0003219]; cardiac septum morphogenesis [GO:0060411]; cartilage morphogenesis [GO:0060536]; embryonic heart tube development [GO:0035050]; embryonic heart tube formation [G... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | bHLH transcription factor binding [GO:0043425]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; enzyme binding... | PF00010; | 4.10.280.10; | null | PTM: Phosphorylation by PLK4 disrupts the interaction with MDFIC and leads to translocation into the nucleoplasm, allowing dimerization and transcription factor activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Interaction with MDFIC sequesters it into the nucleolus, preventing the transcription factor activity. Phosphorylation by PLK4 disrupts the interaction with MDFIC and releases it from the nucleolus, leading to transcription... | null | null | null | null | null | FUNCTION: Transcription factor that plays an essential role in both trophoblast giant cell differentiation and in cardiac morphogenesis (By similarity). Binds the DNA sequence 5'-NRTCTG-3' (non-canonical E-box) (By similarity). Acts as a transcriptional repressor of SOX15 (By similarity). In the adult, could be require... | Homo sapiens (Human) |
O96005 | CLPT1_HUMAN | MAAAQEADGARSAVVAAGGGSSGQVTSNGSIGRDPPAETQPQNPPAQPAPNAWQVIKGVLFRIFIIWAISSWFRRGPAPQDQAGPGGAPRVASRNLFPKDTLMNLHVYISEHEHFTDFNATSALFWEQHDLVYGDWTSGENSDGCYEHFAELDIPQSVQQNGSIYIHVYFTKSGFHPDPRQKALYRRLATVHMSRMINKYKRRRFQKTKNLLTGETEADPEMIKRAEDYGPVEVISHWHPNITINIVDDHTPWVKGSVPPPLDQYVKFDAVSGDYYPIIYFNDYWNLQKDYYPINESLASLPLRVSFCPLSLWRWQLYAA... | null | null | cell differentiation [GO:0030154]; regulation of T cell differentiation in thymus [GO:0033081] | endomembrane system [GO:0012505]; external side of plasma membrane [GO:0009897]; membrane [GO:0016020]; plasma membrane [GO:0005886] | GABA receptor binding [GO:0050811] | PF05602; | null | CLPTM1 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Involved in GABAergic but not glutamatergic transmission. Binds and traps GABAA receptors in the endoplasmic reticulum (ER). Modulates postsynaptic GABAergic transmission, and therefore inhibitory neurotransmission, by reducing the plasma membrane expression of these receptors. Altered GABAergic signaling is ... | Homo sapiens (Human) |
O96006 | ZBED1_HUMAN | MENKSLESSQTDLKLVAHPRAKSKVWKYFGFDTNAEGCILQWKKIYCRICMAQIAYSGNTSNLSYHLEKNHPEEFCEFVKSNTEQMREAFATAFSKLKPESSQQPGQDALAVKAGHGYDSKKQQELTAAVLGLICEGLYPASIVDEPTFKVLLKTADPRYELPSRKYISTKAIPEKYGAVREVILKELAEATWCGISTDMWRSENQNRAYVTLAAHFLGLGAPNCLSMGSRCLKTFEVPEENTAETITRVLYEVFIEWGISAKVFGATTNYGKDIVKACSLLDVAVHMPCLGHTFNAGIQQAFQLPKLGALLSRCRKLVE... | 2.3.2.- | null | negative regulation by host of viral genome replication [GO:0044828]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein autosumoylation [GO:1990466]; protein sumoylation [GO:0016925]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [... | centrosome [GO:0005813]; chromatin [GO:0000785]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory ... | PF05699;PF02892; | null | null | PTM: Autosumoylated with SUMO1, SUMO2, and SUMO3. {ECO:0000269|PubMed:25210186, ECO:0000269|PubMed:27068747}. | SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000269|PubMed:25210186, ECO:0000269|PubMed:27068747}. Nucleus {ECO:0000269|PubMed:12663651, ECO:0000269|PubMed:17209048}. Note=In granular structures. {ECO:0000269|PubMed:12663651, ECO:0000269|PubMed:17209048}.; SUBCELLULAR LOCATION: Nucleus, PML body. Note=(Microbial infec... | null | null | PATHWAY: Protein modification; protein sumoylation. {ECO:0000269|PubMed:27068747}. | null | null | FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase which sumoylates CHD3/Mi2-alpha, causing its release from DNA (PubMed:27068747). This results in suppression of CHD3/Mi2-alpha transcription repression, increased recruitment of RNA polymerase II to gene promoters and positive regulation of t... | Homo sapiens (Human) |
O96007 | MOC2B_HUMAN | MSSLEISSSCFSLETKLPLSPPLVEDSAFEPSRKDMDEVEEKSKDVINFTAEKLSVDEVSQLVISPLCGAISLFVGTTRNNFEGKKVISLEYEAYLPMAENEVRKICSDIRQKWPVKHIAVFHRLGLVPVSEASIIIAVSSAHRAASLEAVSYAIDTLKAKVPIWKKEIYEESSTWKGNKECFWASNS | 2.8.1.12 | null | Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; molybdopterin cofactor biosynthetic process [GO:0032324] | cytosol [GO:0005829]; molybdopterin synthase complex [GO:0019008]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654] | molybdopterin synthase activity [GO:0030366] | PF02391; | 3.90.1170.40; | MoaE family, MOCS2B subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03052, ECO:0000269|PubMed:15073332}. | CATALYTIC ACTIVITY: Reaction=2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 4 H(+) + molybdopterin; Xref=Rhea:RHEA:26333, Rhea:RHEA-COMP:12160, Rhea:RHEA-COMP:12202, ChEBI:CHEBI... | null | PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03052}. | null | null | FUNCTION: Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group. {ECO:0000255|HAMAP-Rule:MF_03052, ECO:0000269|... | Homo sapiens (Human) |
O96008 | TOM40_HUMAN | MGNVLAASSPPAGPPPPPAPALVGLPPPPPSPPGFTLPPLGGSLGAGTSTSRSSERTPGAATASASGAAEDGACGCLPNPGTFEECHRKCKELFPIQMEGVKLTVNKGLSNHFQVNHTVALSTIGESNYHFGVTYVGTKQLSPTEAFPVLVGDMDNSGSLNAQVIHQLGPGLRSKMAIQTQQSKFVNWQVDGEYRGSDFTAAVTLGNPDVLVGSGILVAHYLQSITPCLALGGELVYHRRPGEEGTVMSLAGKYTLNNWLATVTLGQAGMHATYYHKASDQLQVGVEFEASTRMQDTSVSFGYQLDLPKANLLFKGSVDS... | null | null | monoatomic ion transport [GO:0006811]; protein import into mitochondrial matrix [GO:0030150]; protein insertion into mitochondrial outer membrane [GO:0045040]; protein targeting to mitochondrion [GO:0006626] | cytosol [GO:0005829]; membrane [GO:0016020]; mitochondria-associated endoplasmic reticulum membrane [GO:0044233]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; mitochondrial outer membrane translocase complex [GO:0005742]; mitochondrion [GO:0005739]; pore complex [GO:0046930]; TO... | porin activity [GO:0015288]; protein transmembrane transporter activity [GO:0008320] | PF01459; | 2.40.160.10; | Tom40 family | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:15644312, ECO:0000269|PubMed:31206022}; Multi-pass membrane protein {ECO:0000255}. Note=Associates with the mitochondria-associated ER membrane via interaction with BCAP31. {ECO:0000269|PubMed:31206022}. | null | null | null | null | null | FUNCTION: Channel-forming protein essential for import of protein precursors into mitochondria (PubMed:15644312, PubMed:31206022). Plays a role in the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) by forming a complex with BCAP31 and mediating the translocation of Complex I com... | Homo sapiens (Human) |
O96009 | NAPSA_HUMAN | MSPPPLLQPLLLLLPLLNVEPSGATLIRIPLHRVQPGRRILNLLRGWREPAELPKLGAPSPGDKPIFVPLSNYRDVQYFGEIGLGTPPQNFTVAFDTGSSNLWVPSRRCHFFSVPCWLHHRFDPKASSSFQANGTKFAIQYGTGRVDGILSEDKLTIGGIKGASVIFGEALWEPSLVFAFAHFDGILGLGFPILSVEGVRPPMDVLVEQGLLDKPVFSFYLNRDPEEPDGGELVLGGSDPAHYIPPLTFVPVTVPAYWQIHMERVKVGPGLTLCAKGCAAILDTGTSLITGPTEEIRALHAAIGGIPLLAGEYIILCSEI... | 3.4.23.- | null | membrane protein proteolysis [GO:0033619]; proteolysis [GO:0006508]; surfactant homeostasis [GO:0043129] | alveolar lamellar body [GO:0097208]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; lysosome [GO:0005764]; multivesicular body lumen [GO:0097486] | aspartic-type endopeptidase activity [GO:0004190]; endopeptidase activity [GO:0004175]; peptidase activity [GO:0008233] | PF00026; | 2.40.70.10; | Peptidase A1 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be involved in processing of pneumocyte surfactant precursors. | Homo sapiens (Human) |
O96011 | PX11B_HUMAN | MDAWVRFSAQSQARERLCRAAQYACSLLGHALQRHGASPELQKQIRQLESHLSLGRKLLRLGNSADALESAKRAVHLSDVVLRFCITVSHLNRALYFACDNVLWAGKSGLAPRVDQEKWAQRSFRYYLFSLIMNLSRDAYEIRLLMEQESSACSRRLKGSGGGVPGGSETGGLGGPGTPGGGLPQLALKLRLQVLLLARVLRGHPPLLLDVVRNACDLFIPLDKLGLWRCGPGIVGLCGLVSSILSILTLIYPWLRLKP | null | null | peroxisome fission [GO:0016559]; peroxisome organization [GO:0007031]; regulation of peroxisome size [GO:0044375]; signal transduction [GO:0007165] | cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; protein-containing complex [GO:0032991] | identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803] | PF05648; | null | Peroxin-11 family | null | SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:20826455, ECO:0000269|PubMed:9792670, ECO:0000269|PubMed:9826565}; Single-pass membrane protein {ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:9792670, ECO:0000269|PubMed:9826565}. | null | null | null | null | null | FUNCTION: Involved in peroxisomal proliferation (PubMed:9792670). May regulate peroxisome division by recruiting the dynamin-related GTPase DNM1L to the peroxisomal membrane (PubMed:12618434). Promotes membrane protrusion and elongation on the peroxisomal surface (PubMed:20826455). {ECO:0000269|PubMed:12618434, ECO:000... | Homo sapiens (Human) |
O96013 | PAK4_HUMAN | MFGKRKKRVEISAPSNFEHRVHTGFDQHEQKFTGLPRQWQSLIEESARRPKPLVDPACITSIQPGAPKTIVRGSKGAKDGALTLLLDEFENMSVTRSNSLRRDSPPPPARARQENGMPEEPATTARGGPGKAGSRGRFAGHSEAGGGSGDRRRAGPEKRPKSSREGSGGPQESSRDKRPLSGPDVGTPQPAGLASGAKLAAGRPFNTYPRADTDHPSRGAQGEPHDVAPNGPSAGGLAIPQSSSSSSRPPTRARGAPSPGVLGPHASEPQLAPPACTPAAPAVPGPPGPRSPQREPQRVSHEQFRAALQLVVDPGDPRSY... | 2.7.11.1 | null | apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cell migration [GO:0016477]; cellular response to organic cyclic compound [GO:0071407]; cytoskeleton organization [GO:0007010]; dendritic spine development [GO:0060996]; intracellular signal transduction [GO:0035556]; negative regulation of endothelial cell apopt... | adherens junction [GO:0005912]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794] | ATP binding [GO:0005524]; cadherin binding involved in cell-cell adhesion [GO:0098641]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00786;PF00069; | 3.90.810.10;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | PTM: Autophosphorylated on serine residues when activated by CDC42/p21 (Ref.32). Phosphorylated on tyrosine residues upon stimulation of FGFR2 (By similarity). Methylated by SETD6. {ECO:0000250|UniProtKB:Q8BTW9, ECO:0000269|PubMed:30189201, ECO:0000269|Ref.32}.; PTM: Polyubiquitinated, leading to its proteasomal degrad... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12356872}. Note=Seems to shuttle between cytoplasmic compartments depending on the activating effector. For example, can be found on the cell periphery after activation of growth-factor or integrin-mediated signaling pathways. {ECO:0000269|PubMed:12356872}. | 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 plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, growth, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational chang... | Homo sapiens (Human) |
O96014 | WNT11_HUMAN | MRARPQVCEALLFALALQTGVCYGIKWLALSKTPSALALNQTQHCKQLEGLVSAQVQLCRSNLELMHTVVHAAREVMKACRRAFADMRWNCSSIELAPNYLLDLERGTRESAFVYALSAAAISHAIARACTSGDLPGCSCGPVPGEPPGPGNRWGGCADNLSYGLLMGAKFSDAPMKVKKTGSQANKLMRLHNSEVGRQALRASLEMKCKCHGVSGSCSIRTCWKGLQELQDVAADLKTRYLSATKVVHRPMGTRKHLVPKDLDIRPVKDSELVYLQSSPDFCMKNEKVGSHGTQDRQCNKTSNGSDSCDLMCCGRGYNP... | null | null | adrenal gland development [GO:0030325]; artery morphogenesis [GO:0048844]; atrial septum development [GO:0003283]; bicellular tight junction assembly [GO:0070830]; bone mineralization [GO:0030282]; canonical Wnt signaling pathway [GO:0060070]; cell fate commitment [GO:0045165]; cellular response to mechanical stimulus ... | cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; frizzled binding [GO:0005109]; GTPase activator activity [GO:0005096]; protein kinase activator activity [GO:0030295] | PF00110; | 3.30.2460.20; | Wnt family | PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. | null | null | null | null | null | FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters. | Homo sapiens (Human) |
O96015 | DNAL4_HUMAN | MGETEGKKDEADYKRLQTFPLVRHSDMPEEMRVETMELCVTACEKFSNNNESAAKMIKETMDKKFGSSWHVVIGEGFGFEITHEVKNLLYLYFGGTLAVCVWKCS | null | null | microtubule-based movement [GO:0007018] | cilium [GO:0005929]; cytoplasm [GO:0005737]; dynein complex [GO:0030286]; microtubule [GO:0005874]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; microtubule motor activity [GO:0003777] | PF01221; | 3.30.740.10; | Dynein light chain family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}. | null | null | null | null | null | FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
O96017 | CHK2_HUMAN | MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEDQEPEDQEPEEPTPAPWARLWALQDGFANLECVNDNYWFGRDKSCEYCFDEPLLKRTDKYRTYSKKHFRIFREVGPKNSYIAYIEDHSGNGTFVNTELVGKGKRRPLNNNSEIALSLSRNKVFVFFDLTVDDQSVYPKALRDEYIMSKTLGSGACGEVKLAFERKTCKKVAIKIISKRKFAIGSAREADPALNVETEIEILKKLNHPCIIKIKNFFDAEDYYIVLELMEGGELFDKVVGNKRLK... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | cell division [GO:0051301]; cellular response to gamma radiation [GO:0071480]; DNA damage checkpoint signaling [GO:0000077]; DNA damage response [GO:0006974]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; DNA damage response, signal transduction by p53 class... | cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; ubiquitin protein ligase binding [GO:... | PF00498;PF00069; | 2.60.200.20;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CHK2 subfamily | PTM: Phosphorylated. Phosphorylated at Ser-73 by PLK3 in response to DNA damage, promoting phosphorylation at Thr-68 by ATM and the G2/M transition checkpoint. Phosphorylation at Thr-68 induces homodimerization. Autophosphorylates at Thr-383 and Thr-387 in the T-loop/activation segment upon dimerization to become fully... | SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Note=Isoform 10 is present throughout the cell.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus.; SUBCELLULAR LOCATION: [Isoform 7]: Nucleus.; SUBCELLULAR LOCATION: [Isoform 9]: Nucleus.; SUBCELLULAR LOCATION: [Isoform 12]: Nucleus.; SUBCELLULAR LOCATION: Nucleus, PML body. Nucle... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:37943659}; CATALYTIC... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest, activation of DNA repair and apoptosis in response to the presence of DNA double-strand breaks. May also negatively regulate cell cycle progression during unperturbed cell cycles. Following activation, phosphorylates ... | Homo sapiens (Human) |
O96018 | APBA3_HUMAN | MDFPTISRSPSGPPAMDLEGPRDILVPSEDLTPDSQWDPMPGGPGSLSRMELDESSLQELVQQFEALPGDLVGPSPGGAPCPLHIATGHGLASQEIADAHGLLSAEAGRDDLLGLLHCEECPPSQTGPEEPLEPAPRLLQPPEDPDEDSDSPEWVEGASAEQEGSRSSSSSPEPWLETVPLVTPEEPPAGAQSPETLASYPAPQEVPGPCDHEDLLDGVIFGARYLGSTQLVSERNPPTSTRMAQAREAMDRVKAPDGETQPMTEVDLFVSTKRIKVLTADSQEAMMDHALHTISYTADIGCVLVLMARRRLARRPAPQD... | null | null | chemical synaptic transmission [GO:0007268]; in utero embryonic development [GO:0001701]; negative regulation of catalytic activity [GO:0043086]; protein transport [GO:0015031]; regulation of gene expression [GO:0010468] | cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | amyloid-beta binding [GO:0001540]; enzyme binding [GO:0019899]; enzyme inhibitor activity [GO:0004857] | PF00595;PF00640; | 2.30.42.10;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:19726677}. | null | null | null | null | null | FUNCTION: May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta. May enhance the activity of HIF1A in macrophages by inhibiting the activity of HIF1AN. {ECO:0000269|PubMed:19726677}. | Homo sapiens (Human) |
O96019 | ACL6A_HUMAN | MSGGVYGGDEVGALVFDIGSYTVRAGYAGEDCPKVDFPTAIGMVVERDDGSTLMEIDGDKGKQGGPTYYIDTNALRVPRENMEAISPLKNGMVEDWDSFQAILDHTYKMHVKSEASLHPVLMSEAPWNTRAKREKLTELMFEHYNIPAFFLCKTAVLTAFANGRSTGLILDSGATHTTAIPVHDGYVLQQGIVKSPLAGDFITMQCRELFQEMNIELVPPYMIASKEAVREGSPANWKRKEKLPQVTRSWHNYMCNCVIQDFQASVLQVSDSTYDEQVAAQMPTVHYEFPNGYNCDFGAERLKIPEGLFDPSNVKGLSGN... | null | null | blastocyst formation [GO:0001825]; chromatin remodeling [GO:0006338]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; negative regulation of cell differentiation [GO:0045596]; nervous system development [GO:0007399]; neural retina development [GO:0003407]; positive regulation of cell differentiation [GO:004559... | brahma complex [GO:0035060]; chromatin [GO:0000785]; GBAF complex [GO:0140288]; Ino80 complex [GO:0031011]; kinetochore [GO:0000776]; npBAF complex [GO:0071564]; NuA4 histone acetyltransferase complex [GO:0035267]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]; pla... | chromatin binding [GO:0003682]; transcription coactivator activity [GO:0003713] | PF00022; | 3.30.420.40; | Actin family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18026119}. | null | null | null | null | null | FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome ... | Homo sapiens (Human) |
O96020 | CCNE2_HUMAN | MSRRSSRLQAKQQPQPSQTESPQEAQIIQAKKRKTTQDVKKRREEVTKKHQYEIRNCWPPVLSGGISPCIIIETPHKEIGTSDFSRFTNYRFKNLFINPSPLPDLSWGCSKEVWLNMLKKESRYVHDKHFEVLHSDLEPQMRSILLDWLLEVCEVYTLHRETFYLAQDFFDRFMLTQKDINKNMLQLIGITSLFIASKLEEIYAPKLQEFAYVTDGACSEEDILRMELIILKALKWELCPVTIISWLNLFLQVDALKDAPKVLLPQYSQETFIQIAQLLDLCILAIDSLEFQYRILTAAALCHFTSIEVVKKASGLEWDS... | null | null | cell division [GO:0051301]; DNA replication initiation [GO:0006270]; G1/S transition of mitotic cell cycle [GO:0000082]; homologous chromosome pairing at meiosis [GO:0007129]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; regulation of cyclin-dependent protein serine/threonine kinase activi... | centrosome [GO:0005813]; cyclin E1-CDK2 complex [GO:0097134]; cyclin E2-CDK2 complex [GO:0097135]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | cyclin-dependent protein serine/threonine kinase regulator activity [GO:0016538]; protein kinase binding [GO:0019901] | PF02984;PF00134; | 1.10.472.10; | Cyclin family, Cyclin E subfamily | PTM: Phosphorylation by CDK2 triggers its release from CDK2 and degradation via the ubiquitin proteasome pathway. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9840943}. | null | null | null | null | null | FUNCTION: Essential for the control of the cell cycle at the late G1 and early S phase. | Homo sapiens (Human) |
O96024 | B3GT4_HUMAN | MQLRLFRRLLLAALLLVIVWTLFGPSGLGEELLSLSLASLLPAPASPGPPLALPRLLIPNQEACSGPGAPPFLLILVCTAPENLNQRNAIRASWGGLREARGLRVQTLFLLGEPNAQHPVWGSQGSDLASESAAQGDILQAAFQDSYRNLTLKTLSGLNWAEKHCPMARYVLKTDDDVYVNVPELVSELVLRGGRWGQWERSTEPQREAEQEGGQVLHSEEVPLLYLGRVHWRVNPSRTPGGRHRVSEEQWPHTWGPFPPYASGTGYVLSASAVQLILKVASRAPLLPLEDVFVGVSARRGGLAPTQCVKLAGATHYPLD... | 2.4.1.62 | null | ganglioside biosynthetic process [GO:0001574]; glycosphingolipid biosynthetic process [GO:0006688]; oligosaccharide biosynthetic process [GO:0009312]; protein O-linked glycosylation [GO:0006493] | Golgi membrane [GO:0000139] | ganglioside galactosyltransferase activity [GO:0047915]; UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity [GO:0008499] | PF01762; | 3.90.550.50; | Glycosyltransferase 31 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Z0F0}; Single-pass type II membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a ganglioside GM2 (d18:1(4E)) + UDP-alpha-D-galactose = a ganglioside GM1 (d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:16773, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:71502, ChEBI:CHEBI:77709; EC=2.4.1.62; Evidence={ECO:0000269|PubMed:9582303}; PhysiologicalDirection... | null | PATHWAY: Protein modification; protein glycosylation. | null | null | FUNCTION: Involved in GM1/GD1B/GA1 ganglioside biosynthesis. {ECO:0000269|PubMed:9582303}. | Homo sapiens (Human) |
O96028 | NSD2_HUMAN | MEFSIKQSPLSVQSVVKCIKMKQAPEILGSANGKTPSCEVNRECSVFLSKAQLSSSLQEGVMQKFNGHDALPFIPADKLKDLTSRVFNGEPGAHDAKLRFESQEMKGIGTPPNTTPIKNGSPEIKLKITKTYMNGKPLFESSICGDSAADVSQSEENGQKPENKARRNRKRSIKYDSLLEQGLVEAALVSKISSPSDKKIPAKKESCPNTGRDKDHLLKYNVGDLVWSKVSGYPWWPCMVSADPLLHSYTKLKGQKKSARQYHVQFFGDAPERAWIFEKSLVAFEGEGQFEKLCQESAKQAPTKAEKIKLLKPISGKLRA... | 2.1.1.357 | null | atrial septum primum morphogenesis [GO:0003289]; atrial septum secundum morphogenesis [GO:0003290]; bone development [GO:0060348]; double-strand break repair [GO:0006302]; membranous septum morphogenesis [GO:0003149]; methylation [GO:0032259]; negative regulation of transcription by RNA polymerase II [GO:0000122]; posi... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; histone H3 methyltransferase activity [GO:0140938]; histone H3K36 dimethyltransferase activity [GO:0140954]; histone H3K36 methyltransferase activity [GO:0046975]; histone H3K36 trimethyltransferase activity [GO:0140955]; histone H4K20 methyltransferase activity [GO:0042799]; metal ion b... | PF17907;PF17982;PF00505;PF00628;PF00855;PF00856; | 2.30.30.140;1.10.30.10;2.170.270.10;3.30.40.10; | Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, SET2 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15677557, ECO:0000269|PubMed:16197452}. Chromosome {ECO:0000250|UniProtKB:Q8BVE8}. Note=In embryonic stem (ES) cells, localizes to small foci, probably corresponding to euchromatin (By similarity). In B-cells, localizes to Ig heavy chain switch region during class switc... | CATALYTIC ACTIVITY: Reaction=L-lysyl(36)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(36)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60312, Rhea:RHEA-COMP:9785, Rhea:RHEA-COMP:9786, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Eviden... | null | null | null | null | FUNCTION: Histone methyltransferase which specifically dimethylates nucleosomal histone H3 at 'Lys-36' (H3K36me2) (PubMed:19808676, PubMed:22099308, PubMed:27571355, PubMed:29728617, PubMed:33941880). Also monomethylates nucleosomal histone H3 at 'Lys-36' (H3K36me) in vitro (PubMed:22099308). Does not trimethylate nucl... | Homo sapiens (Human) |
O96033 | MOC2A_HUMAN | MVPLCQVEVLYFAKSAEITGVRSETISVPQEIKALQLWKEIETRHPGLADVRNQIIFAVRQEYVELGDQLLVLQPGDEIAVIPPISGG | null | null | Mo-molybdopterin cofactor biosynthetic process [GO:0006777] | cytosol [GO:0005829]; molybdopterin synthase complex [GO:0019008] | molybdopterin synthase activity [GO:0030366]; nucleotide binding [GO:0000166] | PF02597; | 3.10.20.30; | MoaD family, MOCS2A subfamily | PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) via the hesA/moeB/thiF part of MOCS3, then thiocarboxylated (-COSH) via the rhodanese domain of MOCS3. {ECO:0000255|HAMAP-Rule:MF_03051, ECO:0000269|PubMed:12732628, ECO:0000269|PubMed:15073332, ECO:0000269|PubMed:15910006, ECO:00... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03051, ECO:0000269|PubMed:15073332}. | null | null | PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03051}. | null | null | FUNCTION: Acts as a sulfur carrier required for molybdopterin biosynthesis. Component of the molybdopterin synthase complex that catalyzes the conversion of precursor Z into molybdopterin by mediating the incorporation of 2 sulfur atoms into precursor Z to generate a dithiolene group. In the complex, serves as sulfur d... | Homo sapiens (Human) |
O96390 | RACF1_DICDI | MQNIKCVVVGDGAVGKTCMLISYTTNGFPSEYIPTVFDNYCANLMLEGKPYSLGLWDTAGQEDYDRLRPLSYPHTDVFLICFSIISQASFENVTTKWFKEVNHHAPGVPIILVGTKQDIRNDNDSIKKLKEKNIELVPYEKGLEKAKEINAIYLEASALTQRGIKDVFDQCIRSVIYPNKLIKKPKKKSCTIM | null | null | actin filament organization [GO:0007015]; cortical cytoskeleton organization [GO:0030865]; engulfment of apoptotic cell [GO:0043652]; establishment or maintenance of cell polarity [GO:0007163]; mitotic cytokinesis [GO:0000281]; motor neuron axon guidance [GO:0008045]; regulation of actin cytoskeleton organization [GO:0... | cell cortex [GO:0005938]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytoskeleton [GO:0005856]; macropinosome [GO:0044354]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase binding [GO:0019901] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rho family | null | SUBCELLULAR LOCATION: Membrane; Lipid-anchor. | null | null | null | null | null | FUNCTION: Might act in concert and/or share functions with other members of the RHO family in the regulation of a subset of cytoskeletal rearrangements that are required for these processes. | Dictyostelium discoideum (Social amoeba) |
O96433 | CCNT_DROME | MSLLATPMPQAATASSSSSASAAASASGIPITANNNLPFEKDKIWYFSNDQLANSPSRRCGIKGDDELQYRQMTAYLIQEMGQRLQVSQLCINTAIVYMHRFYAFHSFTHFHRNSMASASLFLAAKVEEQPRKLEHVIRAANKCLPPTTEQNYAELAQELVFNENVLLQTLGFDVAIDHPHTHVVRTCQLVKACKDLAQTSYFLASNSLHLTSMCLQYRPTVVACFCIYLACKWSRWEIPQSTEGKHWFYYVDKTVSLDLLKQLTDEFIAIYEKSPARLKSKLNSIKAIAQGASNRTANSKDKPKEDWKITEMMKGYHSN... | null | null | DNA-templated transcription [GO:0006351]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; regulation of transcription by RNA polymerase II [GO:0006357]; response to heat [GO:0009408]; ventral cord development... | cyclin/CDK positive transcription elongation factor complex [GO:0008024]; nucleus [GO:0005634]; P-TEFb complex [GO:0070691]; polytene chromosome [GO:0005700]; polytene chromosome puff [GO:0005703]; super elongation complex [GO:0032783]; transcription elongation factor complex [GO:0008023] | cyclin-dependent protein serine/threonine kinase activator activity [GO:0061575]; cyclin-dependent protein serine/threonine kinase regulator activity [GO:0016538] | PF00134;PF21797; | 1.10.472.10; | Cyclin family, Cyclin C subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin T) complex, also called positive transcription elongation factor B (P-TEFb), which is proposed to facilitate the transition from abortive to production elongation by phosphorylating the CTD (carboxy-terminal domain) of the large subunit of RN... | Drosophila melanogaster (Fruit fly) |
O96553 | C1TC_DROME | MSAQYQRFLKVLEKWPAEKSKVGSGEWTAEPAIKMSGAKIISGTAVAKSIREELRNEVTAMSKQLADFVPGLRIVQVGGREDSNVYIRMKIKAATEIGIDAAHVQLPRSITEVELLDKINDLNEDPRVHGIIVQMPLDCDTPIDSHRITDAVSPEKDVDGLHTVNEGRLAIGDLGGFLPCTPWGCLELIRRSGVEIAGARAVVLGRSKIVGTPAAELLKWANATVTVCHSKTRNLEEITRSADILVVGIGVAEMVKGSWIKPGAVVIDCGINVKPDASKASGSKLVGDVDYAEALQVAGHLTPVPGGVGPMTVAMLMKNT... | 1.5.1.5; 3.5.4.9; 6.3.4.3 | null | amino acid biosynthetic process [GO:0008652]; histidine biosynthetic process [GO:0000105]; methionine biosynthetic process [GO:0009086]; purine nucleotide biosynthetic process [GO:0006164]; tetrahydrofolate interconversion [GO:0035999] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; formate-tetrahydrofolate ligase activity [GO:0004329]; methenyltetrahydrofolate cyclohydrolase activity [GO:0004477]; methylenetetrahydrofolate dehydrogenase (NADP+) activity [GO:0004488] | PF01268;PF00763;PF02882; | 1.10.8.770;3.10.410.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Tetrahydrofolate dehydrogenase/cyclohydrolase family; Formate--tetrahydrofolate ligase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812, ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.5; Evidence={ECO:0000250|UniProtKB:P11586}; CATALYTIC ACTIVITY: Reaction=(6R)-5,10-... | null | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. | null | null | null | Drosophila melanogaster (Fruit fly) |
O96621 | ARP2_DICDI | MDSNKVIVMDNGTGFVKCGFAGANFPTAIFPSMVGRPILRSEEKVENVEIKDIMVGDEAAKLRSMLQITYPLENGIIRNWDDITHVWDYALKEKLKVSDPTECKILLTEPPMNPVANRQKMIECMFEKYGFQAVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHIIPVYEGYSIPHLTRRLDVAGRDVTRYLIKLLLLRGYAFNRTADFETIRQIKEKLCYVAYDVQQEMKLASETTVLVENYTLPDGRVIKVGQERFQASEALFNPSLVDVEGGGVHEQLFDCITKADRDLQQGFYQHIVLSGGSSMYPGLPSRLEKEIR... | null | null | actin filament polymerization [GO:0030041]; aggregation involved in sorocarp development [GO:0031152]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; bleb assembly [GO:0032060]; chemotaxis to cAMP [GO:0043327]; exocytosis [GO:0006887]; hyperosmotic response [GO:0006972]; phagocytosis [GO:0006909]; response to m... | Arp2/3 protein complex [GO:0005885]; cell cortex [GO:0005938]; cytosol [GO:0005829]; polyphosphate kinase complex [GO:0009358]; pseudopodium [GO:0031143] | actin filament binding [GO:0051015]; ATP binding [GO:0005524] | PF00022; | 3.30.420.40; | Actin family, ARP2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11807934}. Cytoplasm, cytosol {ECO:0000269|PubMed:11425877}. Cytoplasm, cell cortex {ECO:0000269|PubMed:11425877}. Cell projection, pseudopodium {ECO:0000269|PubMed:11425877}. | null | null | null | null | null | FUNCTION: Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. The Arp2/3 comp... | Dictyostelium discoideum (Social amoeba) |
O96622 | ARPC1_DICDI | MSAFEIEHLASCITAHAWNADRSRVALCPNNNEVHIYAKQGTSWVVEHVLAEHDQLVTSIDWAPKTNRILTSSQDRNAYVWTFKDGQWKPVLVLLRINRAATHVKWSPQENKFAVATGAKLVCICFFEEEHDWWASNHIKKHKSTVLKVDWHPNNLLLATSSSDYKVRVFDAYIKKADGRSVTRPYGEVAFGEPVFEFDQCASWVHALKWSPSGSTLAYSSHDGVFAVANFSTNPPTIEKLRVRNLPLRDLLYITENSIAGVGYDCAPLLITNQNGWKYSGEMDKASEGGAAAGSETSARKLFQNKVDLGESKSADKKLT... | null | null | actin filament polymerization [GO:0030041]; actin nucleation [GO:0045010]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; exocytosis [GO:0006887]; phagocytosis [GO:0006909] | Arp2/3 protein complex [GO:0005885]; cell cortex [GO:0005938]; cell leading edge [GO:0031252]; cell projection [GO:0042995]; clathrin-coated pit [GO:0005905]; cortical actin cytoskeleton [GO:0030864]; cytosol [GO:0005829]; extracellular matrix [GO:0031012]; filopodium [GO:0030175]; phagocytic cup [GO:0001891]; phagocyt... | actin filament binding [GO:0051015] | PF00400; | 2.130.10.10; | WD repeat ARPC1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection. Cytoplasm, cytosol. Cytoplasm, cell cortex. Cell projection, pseudopodium. | null | null | null | null | null | FUNCTION: Functions as a component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. The Arp2/3 complex is inv... | Dictyostelium discoideum (Social amoeba) |
O96623 | ARPC2_DICDI | MLLLETHNRILYDEVISHFEGDRRVNNIFADFDGVKFNVQTSDDKSSLMVSVSLHAAADLLKNGGSALLKSVYGDMLQAKPEGGYDVTLVIQSSFSGNKEELAKKVSLLKRHLVAAPFLMVFEGIEAKKPLPEIIAINYRTDETFYLKPQGDNVIVIFDIAFKDADDVILSKIFLQSFVDVRKTISNVPSITFSQKDPPLELKGVKGVRAGQANHGFVSFVLFPAHIKKPQESADLIQTFRDYLHYHIKCAKGYMHTSMRNRVESLIQVLNRAKPEPVNTVKRTITGKFFKQN | null | null | actin filament depolymerization [GO:0030042]; actin filament polymerization [GO:0030041]; actin nucleation [GO:0045010]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; exocytosis [GO:0006887]; phagocytosis [GO:0006909] | Arp2/3 protein complex [GO:0005885]; cell cortex [GO:0005938]; cytosol [GO:0005829]; pseudopodium [GO:0031143] | actin filament binding [GO:0051015]; structural constituent of cytoskeleton [GO:0005200] | PF04045; | 3.30.1460.20; | ARPC2 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection. Cytoplasm, cytosol. Cytoplasm, cell cortex. Cell projection, pseudopodium. | null | null | null | null | null | FUNCTION: Functions as a component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. The Arp2/3 complex is inv... | Dictyostelium discoideum (Social amoeba) |
O96624 | ARPC3_DICDI | MVYHSQFNDESAGFRLVGNVPILPLKTTHKGPAPKGDANSVDIIDEALDLFKANILFRNFEVQGNGDRVLIYLTLYITKCLLKIAPMNKADAEKALFLIAQEQFSIPGESAFPLGGLVTVPNTRDAADTLRQYFTQLRLELGVRLCQRVYAVDPSKANKWWICFSKRKFLNKAL | null | null | actin filament polymerization [GO:0030041]; actin nucleation [GO:0045010]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; exocytosis [GO:0006887]; phagocytosis [GO:0006909]; regulation of actin filament polymerization [GO:0030833] | Arp2/3 protein complex [GO:0005885]; cell cortex [GO:0005938]; cytosol [GO:0005829]; pseudopodium [GO:0031143] | actin filament binding [GO:0051015] | PF04062; | 1.10.1760.10; | ARPC3 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytosol. Cytoplasm, cell cortex. Cell projection, pseudopodium. | null | null | null | null | null | FUNCTION: Functions as a component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. The Arp2/3 complex is inv... | Dictyostelium discoideum (Social amoeba) |
O96625 | ARPC4_DICDI | MSTAQVPYLNCIRNTLTASMCLQNFGSQIVERHNKPEVEVKTSKELVLNPVIIARNKNERVLIETSINSIRISVSIKKSDEVDVILAKKFVRFLQQRAENFIILRRKPVEGYDISFLVTNFHTENMFKHKLVDFIIQFMEDIDREISDLKLTLNARGRIVASEYLKNFA | null | null | actin filament polymerization [GO:0030041]; actin nucleation [GO:0045010]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; exocytosis [GO:0006887]; phagocytosis [GO:0006909] | Arp2/3 protein complex [GO:0005885]; cell cortex [GO:0005938]; cytosol [GO:0005829]; pathogen-containing vacuole [GO:0140220]; pseudopodium [GO:0031143] | actin filament binding [GO:0051015] | PF05856; | 3.30.1460.20; | ARPC4 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytosol. Cytoplasm, cell cortex. Cell projection, pseudopodium. | null | null | null | null | null | FUNCTION: Functions as a component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. The Arp2/3 complex is inv... | Dictyostelium discoideum (Social amoeba) |
O96626 | ARPC5_DICDI | MNYEDDNVESGQAGKSDAEYKADIANREKEVTKALNAGKPQDALNVALADPPIYTKTGAIKDQNATIVLNLLGSFKDKDVETSVETLNDDQLDILMKYVYRGLATGENSPIFFKWHECVLKKGGAGTIIRVISEKKTV | null | null | actin filament polymerization [GO:0030041]; actin nucleation [GO:0045010]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; cell migration [GO:0016477]; exocytosis [GO:0006887]; phagocytosis [GO:0006909]; regulation of actin filament polymerization [GO:0030833] | Arp2/3 protein complex [GO:0005885]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; pseudopodium [GO:0031143] | actin filament binding [GO:0051015] | PF04699; | 1.25.40.190; | ARPC5 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytosol. Cytoplasm, cell cortex. Cell projection, pseudopodium. | null | null | null | null | null | FUNCTION: Functions as a component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. The Arp2/3 complex is inv... | Dictyostelium discoideum (Social amoeba) |
O96690 | PDF_DROME | MARYTYLVALVLLAICCQWGYCGAMAMPDEERYVRKEYNRDLLDWFNNVGVGQFSPGQVATLCRYPLILENSLGPSVPIRKRNSELINSLLSLPKNMNDAGK | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; circadian rhythm [GO:0007623]; circadian sleep/wake cycle [GO:0042745]; eclosion rhythm [GO:0008062]; entrainment of circadian clock by photoperiod [GO:0043153]; gravitaxis [GO:0042332]; locomotor rhythm [GO:0045475]; mating behavio... | extracellular space [GO:0005615]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025] | neuropeptide hormone activity [GO:0005184]; signaling receptor binding [GO:0005102] | PF06324; | null | Arthropod PDH family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Neuropeptide PDF is the main transmitter regulating circadian locomotor rhythms. Required to maintain behavioral rhythms under constant conditions by coordinating pacemaker interactions in the circadian system (PubMed:10619432, PubMed:10777797, PubMed:15356209). Together with CCHa1, involved in regulating int... | Drosophila melanogaster (Fruit fly) |
O96693 | DXR_PLAFX | MKKYIYIYFFFITITINDLVINNTSKCVSIERRKNNAYINYGIGYNGPDNKITKSRRCKRIKLCKKDLIDIGAIKKPINVAIFGSTGSIGTNALNIIRECNKIENVFNVKALYVNKSVNELYEQAREFLPEYLCIHDKSVYEELKELVKNIKDYKPIILCGDEGMKEICSSNSIDKIVIGIDSFQGLYSTMYAIMNNKIVALANKESIVSAGFFLKKLLNIHKNAKIIPVDSEHSAIFQCLDNNKVLKTKCLQDNFSKINNINKIFLCSSGGPFQNLTMDELKNVTSENALKHPKWKMGKKITIDSATMMNKGLEVIETH... | 1.1.1.267 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22355528}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:22355528}; Note=Binds 1 divalent cation per subunit. Mg(2+) or Mn(2+). {ECO:0000269|PubMed:22355528}; | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process [GO:0051484] | apicoplast [GO:0020011] | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity [GO:0030604]; manganese ion binding [GO:0030145]; NADPH binding [GO:0070402] | PF08436;PF02670;PF13288; | 1.10.1740.10;3.40.50.720; | DXR family | null | SUBCELLULAR LOCATION: Plastid, apicoplast {ECO:0000269|PubMed:10477522}. | CATALYTIC ACTIVITY: Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792, ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267; Evidence={ECO:0000269|PubMed:10477522}; PhysiologicalDirection=ri... | null | PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. {ECO:0000305|PubMed:10477522}. | null | null | FUNCTION: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP). {ECO:0000269|PubMed:10477522}. | Plasmodium falciparum (isolate HB3) |
O96759 | ADAS_DICDI | MSGEKKEYPKEHIDLYQQIKWNGWGDTRKFLHQLKPSGTIAMTTPEVSSVPLPSLRGFIKKELTLPGEEDKPFVLDETPALQIENIHVDPPKQYPEFVRELKAFFLPDQLKDDKLARITHTFGKSLRDLIRVRIGQVKNAPDLIVLPHSHEEVERLVQLAHKYNVVIIPMGGGSNIVGAIEPVSNERFTVSIDMRRMNKVLWVDRREMTACIQVGIMGPELEKQLHKQGVSLGHDPDSFEFSTLGGWLATCSSGHQSDKYGDIEDMAVSFRTVTPTGTLELRNGARSGAGINYKHIILGSEGTLGIITEAVMKVHAVPQA... | 2.5.1.26 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:17562315}; | ether lipid biosynthetic process [GO:0008611] | peroxisome [GO:0005777] | alcohol binding [GO:0043178]; alkylglycerone-phosphate synthase activity [GO:0008609]; FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; identical protein binding [GO:0042802] | PF02913;PF01565; | 3.40.462.40;3.30.43.10; | FAD-binding oxidoreductase/transferase type 4 family | null | SUBCELLULAR LOCATION: Peroxisome. | CATALYTIC ACTIVITY: Reaction=a 1-acylglycerone 3-phosphate + a long chain fatty alcohol = 1-O-alkylglycerone 3-phosphate + a long-chain fatty acid + H(+); Xref=Rhea:RHEA:36171, ChEBI:CHEBI:15378, ChEBI:CHEBI:17135, ChEBI:CHEBI:57534, ChEBI:CHEBI:57560, ChEBI:CHEBI:73315; EC=2.5.1.26; Evidence={ECO:0000269|PubMed:175623... | null | PATHWAY: Glycerolipid metabolism; ether lipid biosynthesis. | null | null | FUNCTION: Catalyzes the exchange of an acyl for a long-chain alkyl group and the formation of the ether bond in the biosynthesis of ether phospholipids. {ECO:0000269|PubMed:17562315}. | Dictyostelium discoideum (Social amoeba) |
O96821 | CDK2H_PLAKH | MEKYHGLEKIGEGTYGVVYKAQNNYGETFALKKIRLEKEDEGIPSTAIREISILKELKHSNIVKLYDVIHTKKRLILVFEHLDQDLKKLLDVCDGGLESVTAKSFLLQLLSGIAYCHEHRVLHRDLKPQNLLINREGELKIADFGLARAFGIPVRKYTHEVVTLWYRAPDILMGSKKYSTPIDIWSVGCIFAEMVNGRPLFPGVSETDQLMRIFRILGTPNSANWPSVTELPKYDPDFIVYEPLPWETFLKGLDDTGIDLLSKMLRLDPNQRITAKEALQHAYFKESS | 2.7.11.22; 2.7.11.23 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P61075}; | axonogenesis [GO:0007409]; cell cycle [GO:0007049]; cell division [GO:0051301]; phosphorylation [GO:0016310]; synaptic vesicle transport [GO:0048489]; vesicle-mediated transport [GO:0016192] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04551}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; Evidence={ECO:0000250|UniProtKB:P61075}; CATALYT... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase (By similarity). Involved in the control of the cell cycle. Required for entry into S-phase and mitosis (By similarity). Probable component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II (By similarity). {ECO:0000250|UniProtKB:P04551, E... | Plasmodium knowlesi (strain H) |
O96838 | FYV1_DROME | MTSNNQNNSSSHQHLHSPSKLTEFARNFEDKPESLFGRVVNKIQNVYNQSYNTVNDISSGSSSSSSTQPVQVVGKSQFFSDSQTSTAEIADVETSSQSSVRPQPPTTLSIRTNSETRGTSTSSNTAAEDSETSDRVETLPLPTSEANQGRTVSNVLKHISNIVATKNNNDLRNYKDTELQRFWMPDSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPGMIIRCDGDLKVCNYCSKIVLTFLKSSSSEMGQDMQELQQHLSNKLEVQDSGSSLAKHPQMQRAPLPRKTSVGYQEERFSSHPTYTTLSIDDRKN... | 2.7.1.150 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; | autophagosome maturation [GO:0097352]; endosome to lysosome transport [GO:0008333]; intracellular signal transduction [GO:0035556]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphorylation [GO:0016310] | endosome [GO:0005768]; endosome membrane [GO:0010008]; vesicle membrane [GO:0012506] | 1-phosphatidylinositol-3-phosphate 5-kinase activity [GO:0000285]; 1-phosphatidylinositol-5-kinase activity [GO:0052810]; ATP binding [GO:0005524]; zinc ion binding [GO:0008270] | 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:0000269|PubMed:16837550}. Note=Mainly associated with membranes of the late endocytic pathway. | 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: Regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) or PtdIns(3,5)P2) (PubMed:16837550). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phos... | Drosophila melanogaster (Fruit fly) |
O96923 | GNRA_DICDI | MEEDNIVDSKEIENNVEDKKEETPSSSPSPSSSLQQQQEEGGVVKQAVSNLVSSSITLHDDAKLIQVTGKDEPFHFISVPMSVEFLNLEDVFIMQSDAYIFVWCSEQANIKKKAKAVQMAQKLKVEIGCQRAVQVLEIGEEHPTFLFCLGVPKGTKLNVTKEKNDIFQVDEDDEEQVLEPEFFLFKIFTGTDGKPSIKPMEEDEGINQEMLESSACFILDCEHEMYIWLGKGVKKSTKDTLIPVAKKIWTQYDRPEYYGKLKLQPIITWVFDGAESCLFKSKFSKWVEKAQPLQTSYLSLSSKKKEALNFDVSSMHQDKE... | null | null | actin filament severing [GO:0051014]; actin polymerization or depolymerization [GO:0008154]; barbed-end actin filament capping [GO:0051016]; phototaxis [GO:0042331] | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410] | actin filament binding [GO:0051015]; filamin binding [GO:0031005]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; small GTPase binding [GO:0031267] | PF00626; | 3.40.20.10; | Villin/gelsolin family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:9880334}. | null | null | null | null | null | FUNCTION: Involved in phototaxis. Required for coupling photodetection to the locomotory machinery of slugs. May be essential in the natural environment for the propagation of spores. {ECO:0000269|PubMed:9880334}. | Dictyostelium discoideum (Social amoeba) |
O96935 | AMPN_PLAF7 | MKLTKGCAYKYIIFTVLILANILYDNKKRCMIKKNLRISSCGIISRLLKSNSNYNSFNKNYNFTSAISELQFSNFWNLDILQKDIFSNIHNNKNKPQSYIIHKRLMSEKGDNNNNNHQNNNGNDNKKRLGSVVNNEENTCSDKRMKPFEEGHGITQVDKMNNNSDHLQQNGVMNLNSNNVENNNNNNSVVVKKNEPKIHYRKDYKPSGFIINNVTLNINIHDNETIVRSVLDMDISKHNVGEDLVFDGVGLKINEISINNKKLVEGEEYTYDNEFLTIFSKFVPKSKFAFSSEVIIHPETNYALTGLYKSKNIIVSQCEA... | 3.4.11.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:12166515, ECO:0000269|PubMed:19196988, ECO:0000269|PubMed:21366301}; Note=Binds 1 zinc ion per subunit (PubMed:12166515, PubMed:19196988, PubMed:21366301, PubMed:21844374, PubMed:23713488, PubMed:23897806, PubMed:25299353, PubMed:25645579, PubM... | proteolysis [GO:0006508] | chloroplast [GO:0009507]; cytoplasm [GO:0005737]; food vacuole [GO:0020020]; membrane [GO:0016020]; nucleus [GO:0005634]; symbiont-containing vacuole membrane [GO:0020005]; vacuolar lumen [GO:0005775] | aminopeptidase activity [GO:0004177]; dipeptidase activity [GO:0016805]; metalloaminopeptidase activity [GO:0070006]; zinc ion binding [GO:0008270] | PF11940;PF17432;PF01433;PF17900; | 2.60.40.1840;3.30.2010.30;1.10.390.10;1.25.50.10;2.60.40.1730; | Peptidase M1 family | PTM: The full length protein appears to be cleaved into a 120 kDa precursor. This precursor is then proteolytically cleaved at the N-terminus generating a 96 kDa form which is further processed at the C-terminus into 68 kDa and 35 kDa forms that remain associated. {ECO:0000269|PubMed:12166515, ECO:0000269|PubMed:205911... | SUBCELLULAR LOCATION: [Aminopeptidase N]: Parasitophorous vacuole membrane {ECO:0000269|PubMed:20591164}; Peripheral membrane protein {ECO:0000305}. Note=In trophozoites, partially localizes to the parasitophorous vacuole membrane. {ECO:0000269|PubMed:20591164}.; SUBCELLULAR LOCATION: [p120 form]: Nucleus {ECO:0000269|... | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=110 uM for Arg-betaNA (at pH 7.5 and 27 degrees Celsius) {ECO:0000269|PubMed:21659511}; KM=170 uM for Arg-betaNA (at pH 7.5 and 27 degrees Celsius, recombinant protein) {ECO:0000269|PubMed:21659511}; KM=1100 uM for Arg-betaNA (at pH 5.5 and 27 degrees Celsius, reco... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7 (PubMed:21659511). Active between 5-8.5 (PubMed:21659511). {ECO:0000269|PubMed:21659511}; pH dependence: Optimum pH is 7-7.5 (PubMed:19196988, PubMed:20591164, PubMed:33536500). Active from pH 5 to 9 (PubMed:19196988, PubMed:33536500). Has less than 20% of ... | null | FUNCTION: Displays aminopeptidase activity with a broad substrate specificity (PubMed:12166515, PubMed:19196988, PubMed:21659511, PubMed:21844374, PubMed:22359643, PubMed:23897806, PubMed:33536500, PubMed:34133730, PubMed:9879894). Preferentially, cleaves after Leu and Met, but cleaves also after Ala and Arg (PubMed:12... | Plasmodium falciparum (isolate 3D7) |
O97101 | CBFA_DICDI | MEELIKAPNSNFIIMSNQPYQTTSPEIVEDYIIKRGQPFVLTGTTQGWSRSNMFTLDFLSERYSEMELINSPRNNETHTDLQGWRMKDFISYLQVSPEERNPKHLYGKDIACPREWQEYLSHKLQPQYSYKSRFDLVSHLPDYLQPETLLVYIGSNGTYTPGHIDMCGSLSQNLMVSSDQDAFAWWFIVPTEYKDEALKFWGDKGGDVYNESRFIRPIDLLGAPFPIYVFKQRPGDFIFVPPDSVHQVVNCGPGISTKVAWNSISLKSLPISYFSSLPHTRRMAKPELFRIKAIAYYTLRKIMGDVENTNFNTIDVNDVI... | null | null | aggregation involved in sorocarp development [GO:0031152]; chromatin organization [GO:0006325]; negative regulation of gene expression [GO:0010629]; phagocytosis [GO:0006909]; pinocytosis [GO:0006907]; positive regulation of gene expression [GO:0010628]; positive regulation of translational termination [GO:0045905]; tr... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; sequence-specific DNA binding [GO:0043565] | PF02373;PF10497; | 2.60.120.650; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10491202, ECO:0000269|PubMed:11162086, ECO:0000269|PubMed:16607013, ECO:0000269|PubMed:19343174, ECO:0000269|PubMed:8898890}. | null | null | null | null | null | FUNCTION: Transcriptional regulator involved in phagocytosis and pinocytosis. Both activates and represses transcription. Regulates expression of acaA, carA, pkaC, csaA, cotB and lagC (PubMed:11162086, PubMed:15470262, PubMed:16607013, PubMed:19343174, PubMed:23355006, PubMed:26339297). Promotes amplification of the tR... | Dictyostelium discoideum (Social amoeba) |
O97143 | PLK4_DROME | MLSNRAFGETIEDYEVQHLLGKGGFATVYKARCLHTHQDVAIKMIDKKLIQGTGLTNRVRQEVEIHSRLKHPSVLQLYTFFQDANYVYLVLELAHNGELHRYMNHIARPFTETEAASILKQVVAGLLYLHSHNIMHRDISLSNLLLSREMHVKIADFGLATQLKRPDERHMTMCGTPNYISPEVVSRTSHGLPADVWSVGCMLYTLLVGRPPFETDAVQSTLNKVVMSEYIMPAHLSYEAQDLINKLLKKLPHERITLEAVLCHPFMLKCSNGGHSAPGALNVFSQSMESGDSGIITFASSDSRNSQQIRSVENSGPQQV... | 2.7.11.21 | null | centriole replication [GO:0007099]; centrosome cycle [GO:0007098]; male meiotic nuclear division [GO:0007140]; mitotic spindle organization [GO:0007052]; positive regulation of protein catabolic process [GO:0045732]; protein autophosphorylation [GO:0046777]; regulation of centriole replication [GO:0046599]; regulation ... | centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; nucleus [GO:0005634]; spindle pole [GO:0000922] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069;PF18190;PF18409; | 2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily | PTM: Ubiquitinated by the SCF-slmb ubiquitin ligase complex; leading to its degradation by the proteasome during interphase and regulating centriole number and ensuring the block to centriole reduplication. {ECO:0000269|PubMed:19084407, ECO:0000269|PubMed:19171756}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:16326102, ECO:0000269|PubMed:19171756, ECO:0000269|PubMed:20946984, ECO:0000269|PubMed:32965218}. Note=Colocalizes with Sas-4 and Patronin at the microtubule organizing center (PubMed:20946984). Coloc... | 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=2.7.11.21; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as Sas-6. When overexpressed, it is... | Drosophila melanogaster (Fruit fly) |
O97148 | MTH_DROME | MKTLLVLRISTVILVVLVIQKSYADILECDYFDTVDISAAQKLQNGSYLFEGLLVPAILTGEYDFRILPDDSKQKVARHIRGCVCKLKPCVRFCCPHDHIMDNGVCYDNMSDEELAELDPFLNVTLDDGSVSRRHFKNELIVQWDLPMPCDGMFYLDNREEQDKYTLFENGTFFRHFDRVTLRKREYCLQHLTFADGNATSIRIAPHNCLIVPSITGQTVVMISSLICMVLTIAVYLFVKKLQNLHGKCFICYMVCLFMGYLFLLLDLWQISISFCKPAGFLGYFFVMAAFFWLSVISLHLWNTFRGSSHKANRFLFEHR... | null | null | cell surface receptor signaling pathway [GO:0007166]; determination of adult lifespan [GO:0008340]; G protein-coupled receptor signaling pathway [GO:0007186]; response to heat [GO:0009408]; response to paraquat [GO:1901562]; response to reactive oxygen species [GO:0000302]; response to starvation [GO:0042594]; synaptic... | membrane [GO:0016020]; plasma membrane [GO:0005886]; presynapse [GO:0098793] | G protein-coupled peptide receptor activity [GO:0008528]; G protein-coupled receptor activity [GO:0004930]; peptide binding [GO:0042277] | PF00002;PF06652; | 2.30.160.11;2.170.180.11;1.20.1070.10; | G-protein coupled receptor 2 family, Mth subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12367510}; Multi-pass membrane protein {ECO:0000269|PubMed:12367510}. Note=Plasma membrane of presynaptic terminals and innervating axons. | null | null | null | null | null | FUNCTION: Involved in biological aging and stress response. Essential for adult survival. Required in the presynaptic motor neuron to up-regulate neurotransmitter exocytosis at larval glutamatergic neuromuscular junctions (NMJs). Regulates a step associated with docking and clustering of vesicles at release sites. SP/A... | Drosophila melanogaster (Fruit fly) |
O97159 | CHDM_DROME | MASEEENDDNFQEEEEAQEDNAPAAELSNDSDAPLKPNNDEDDDYDPEDSRRKKKGKKRKTRKGEEKGRKKKKRKKNESEEDSDFVQHDEEVEYPSTSKRGRKRKEEKQAAKEKESASSGMPSVEDVCSAFSVCNVEIEYSEEELQSLTTYKAFMHHVRPILQKENPKIAAPKLVMLVAAKWREFCESNPHIQQEGGAAGSGGSAGQARSVTGDEPEEPRSSRSSRNEKPDDIYEEAVEEEEEEEEEEKKPRRKRSGRGKKGRRPSGKVPTLKIKLLGKRKRDSSDEEQDASGASERDSDLEFERMLQKSDDSADEKEAP... | 3.6.4.12 | null | chromatin remodeling [GO:0006338]; chromosome condensation [GO:0030261]; chromosome organization [GO:0051276]; mitotic sister chromatid cohesion [GO:0007064]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nucleosome organization ... | chromatin [GO:0000785]; cytosol [GO:0005829]; euchromatin [GO:0000791]; nucleus [GO:0005634]; NuRD complex [GO:0016581]; polytene chromosome [GO:0005700] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393]; nucleosome array spacer activity [GO:0140750]; zinc ion binding [GO:0008270] | PF08074;PF06461;PF08073;PF00385;PF06465;PF00271;PF00628;PF00176; | 2.40.50.40;1.10.10.60;3.40.50.300;3.40.50.10810;3.30.40.10; | SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18250149}. Chromosome {ECO:0000269|PubMed:18250149}. Note=During embryogenesis, detected in nuclei before and after their migration to the membrane of the preblastoderm embryo (PubMed:18250149). Expression is diffuse in mitotic nuclei and is still detectable in nuclei a... | 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:0000269|PubMed:18250149}; | null | null | null | null | FUNCTION: Helicase which acts in nucleosome-remodeling by catalyzing ATP-dependent nucleosome mobilization (PubMed:18250149). Involved in regulating transcription (PubMed:18250149, PubMed:9836641). Plays a vital role in development (PubMed:9836641). Binds to a portion of Hunchback (HB) protein that is critical for repr... | Drosophila melanogaster (Fruit fly) |
O97240 | APEX_PLAF7 | MKITSLHFLIFHKNLNYVSSKVKAKKIFYQRALNNIYLCTIRTMIVDIAEIKKRDNHALDTQESQELVNKIKEIKNSDEQNNSNNNNNNSSSSNFCSNNNSPFSHKETKLMVKEEVPNSIVKNILNNNSCATSIINNKFYTQINNIIPVKPEAMKEENINVSTVNTENDISKEKKENSHYFCDEIKVMKKEYSKDDFVTDVKLEMNDKEEEEEEKQKIGQESTHINIKVEKDTFNECNNSNVNEKKRNRSVDIHNELSNKRILTEDVVVKCNIKNDVKIIVTWNMNSITVRYKNKKKWDEFMNFFNNLNADVLCFQEVRL... | 3.1.11.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|RuleBase:RU362131, ECO:0000269|PubMed:33743509}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|RuleBase:RU362131, ECO:0000269|PubMed:33743509}; Note=Probably binds two magnesium or manganese ions per subunit. {ECO:0000255|RuleBase:RU36213... | base-excision repair [GO:0006284]; DNA repair [GO:0006281]; nucleotide-excision repair [GO:0006289] | mitochondrion [GO:0005739]; nucleus [GO:0005634] | DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; double-stranded DNA 3'-5' DNA exonuclease activity [GO:0008311]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; phosphoric diester hydrolase activity [GO:0008081]; RNA exonuclease activity [GO:0004532] | PF03372; | 3.60.10.10; | DNA repair enzymes AP/ExoA family | PTM: May be proteolytically cleaved into a 64 kDa form. {ECO:0000269|PubMed:33743509}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:33743509}. | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.2; Evidence={ECO:0000269|PubMed:33743509}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.69 uM for DNA gapped template with 3'-OH at the gap (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:33743509}; Note=kcat is 0.169 sec(-1) with DNA gapped template with 3'-OH at the gap as substrate (at pH 7.5 and 37 degrees Celsius). {ECO:0000269|PubMed:33... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-8.5 for apurinic/apyrimidinic (AP) endonuclease activity (PubMed:33743509). Optimum pH is 8-8.5 for 3'-5' exonuclease activity (PubMed:33743509). Optimum pH is 8-8.5 for nucleotide incision repair (NIR) cleavage activity (PubMed:33743509). {ECO:0000269|PubM... | null | FUNCTION: Multifunctional protein that plays a central role in mitochondrial DNA base excision repair (BER) pathway induced by oxidative stress. Has apurinic/apyrimidinic (AP) endonuclease activity towards double-stranded DNA (dsDNA) (PubMed:33743509). Has nucleotide incision repair (NIR) activity; acts on dsDNA with o... | Plasmodium falciparum (isolate 3D7) |
O97302 | RH5IP_PLAF7 | MFRIFFTLLIIILIKKTSAIDLIEGIFYEKNEIDKLTFSLDHRVRDNLKTDLILNNNGENDYAYLNKYVYTILNRDSTEKIKTFFSHNKDMKSCDYFISKEYNSSDKTNQICYKKTFCGVVIPNSEEIKTNKITNDKLYCAHFNSTHIIIYYISQPLLLEPHVVYEETFFEKGKNDQINCQGMYISLRSVHVHTHNAILQQETLTYIKNLCDGKNNCKFDFDSIKYENKSLTHYLFFINIQYQCISPLNLQENEMCDVYNDDTHKATCKYGFNKIELLKNVCEENYRCTQDICSVNQFCDGENETCTCKTSLLPSAKNNC... | null | null | symbiont entry into host [GO:0044409] | cytoplasmic vesicle [GO:0031410]; extracellular region [GO:0005576]; host cell membrane [GO:0033644]; host cell plasma membrane [GO:0020002]; host extracellular space [GO:0043655]; membrane [GO:0016020]; microneme [GO:0020009]; microneme lumen [GO:0034494]; plasma membrane [GO:0005886]; protein-containing complex [GO:0... | null | null | 2.90.20.10; | null | PTM: Proteolytically cleaved into two chains of 125kDa and 65kDa which remain associated. The cleavage occurs at the schizont stage prior to the release of merozoites. {ECO:0000269|PubMed:21909261}.; PTM: Contains disulfide bonds. {ECO:0000269|PubMed:21909261}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21909261, ECO:0000269|PubMed:25583518}. Cytoplasmic vesicle, secretory vesicle, microneme lumen {ECO:0000269|PubMed:21909261, ECO:0000269|PubMed:25583518, ECO:0000269|PubMed:27374406, ECO:0000269|PubMed:27692771}. Cell membrane {ECO:0000269|PubMed:21909261, ECO:0000269... | null | null | null | null | null | FUNCTION: Essential for the invasion of host erythrocytes by blood stage merozoites (PubMed:21909261, PubMed:25583518, PubMed:27374406, PubMed:27692771). As part of the PfRH5 adhesion complex, facilitates the interaction of RH5 and human BSG required for the Ca(2+) release into the erythrocyte (PubMed:27374406). {ECO:0... | Plasmodium falciparum (isolate 3D7) |
O97336 | EPTP7_PLAF7 | MAKDSQKNLNVSNNNNVQCTMGRSSQNINKSDSKGKIKRCTYAYKILLCTIFIWICQCFYNKSYYVYKKDGRRNKGKKILGIRINKSLAEMDHTKYHPEYYDEVQENYDPYYGVNQYSDECESYKSEDDDSEEEYYNSTPRVTVLEPQTENSEDEENYEKTIVDELNELPNDKKALILSYIRNGNDNNMQLLPYANNNKQNTQENISRNKEFFRHFVDFIKGYKLFDSPVLNALLPFIFIAFVYCTITMLVGNVRYIIALYILAKILKMHYDYKHKENNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNKKSKKN | null | null | symbiont intracellular protein transport in host [GO:0030581]; vesicle-mediated transport [GO:0016192] | exon-exon junction complex [GO:0035145]; host cell [GO:0043657]; Maurer's cleft [GO:0020036]; membrane [GO:0016020]; vesicle [GO:0031982] | null | null | null | null | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:35930605}. Vesicle {ECO:0000269|PubMed:35930605}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Note=In the host erythrocyte cytoplasm, localizes to Maurer's clefts, chaperone-containing structures known as J-dots, and EMP1-containing electr... | null | null | null | null | null | FUNCTION: During the asexual blood stage, plays an essential role in the recruitment and/or formation of EMP1-containing vesicles at the Maurer's clefts and their subsequent transfer to the host erythrocyte cell membrane. {ECO:0000269|PubMed:35930605}. | Plasmodium falciparum (isolate 3D7) |
O97364 | SUB2_PLAFA | MLNIIYVVSLILIKFIFYKECNNNNNYYLSNIELYNYKLRKRNRILNNNINDRKSFLSDLEQNYKPLFDIYELSANFEKRRKELEKKTKGEENEIEKKKENDLEEKKENEIEKKKENDLEKEYNDVINLLELSLSSEYKELNADVSNNDNSGHEENNKHKLNKKNSSNYKNDKSLDELIKGAILKLKQNPNIKNKNMLDYDKIFKIIKEKLINKNLASNKIKGGDNEKLKEEKKQSDISTNVEVKKDIINDQLNKGIPTKIENKDDMINKESNKEDITNEGKSNSLNNLNTLNNDGNIITKVYDHYTIVTNSNDILNDIS... | 3.4.21.62 | null | membrane protein ectodomain proteolysis [GO:0006509]; peptide hormone processing [GO:0016486] | cytoplasmic vesicle [GO:0031410]; extracellular space [GO:0005615]; microneme membrane [GO:0033163]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802] | serine-type endopeptidase activity [GO:0004252] | PF00082;PF18513; | 3.30.70.2370;3.40.50.200; | Peptidase S8 family | PTM: Proteolytically cleaved at the N-terminus to generate a 74kDa intermediate which is further processed into a 72kDa form (PubMed:10551362, PubMed:16322767). The first maturation cleavage is autocatalytic, occurs in the ER and is necessary for the subsequent SUB2 trafficking to the microneme (By similarity). The sec... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10551362, ECO:0000269|PubMed:16322767}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, microneme membrane {ECO:0000269|PubMed:16322767}; Single-pass type I membrane protein {ECO:0000305}. Note=In mature schizonts, locali... | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.; EC=3.4.21.62; Evidence={ECO:0000305|PubMed:16322767}; | null | null | null | null | FUNCTION: Serine protease which plays an essential role in the shedding of AMA1, MSP1 and MSP7 from the surface of the invading merozoite; this step is essential for productive invasion and the release of the adhesion between the erythrocyte and the merozoite (PubMed:16322767). May cleave TRAMP/PTTRAMP, thereby sheddin... | Plasmodium falciparum |
O97366 | PPAF1_HOLDI | MKQVHFFILWFFVLNLYSIKAQAGCRTPNGENARCVPINNCKILYDSVLTSDPEVIRFLRASQCGYNGQPLVCCGSSASYQPPPTSASIRNRRPELLPNDCGYQVEADKILNGDDTVPEEFPWTAMIGYKNSSNFEQFACGGSLINNRYIVTAAHCVAGRVLRVVGALNKVRLGEWNTATDPDCYGAVRVCVPDKPIDLGIEETIQHPDYVDGSKDRYHDIALIRLNRQVEFTNYIRPVCLPQPNEEVQVGQRLTVVGWGRTETGQYSTIKQKLAVPVVHAEQCAKTFGAAGVRVRSSQLCAGGEKAKDSCGGDSGGPLL... | 3.4.21.- | null | innate immune response [GO:0045087]; proteolysis [GO:0006508] | extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; endopeptidase activity [GO:0004175]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252] | PF12032;PF00089; | 3.30.1640.30;2.40.10.10; | Peptidase S1 family, CLIP subfamily | PTM: Cleaved following the recognition of pathogen-derived products, probably by a lysyl endopeptidase. {ECO:0000269|PubMed:11012672, ECO:0000269|PubMed:16362048, ECO:0000269|PubMed:17287215, ECO:0000269|PubMed:9652393, ECO:0000269|PubMed:9839951}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:9652393, ECO:0000269|PubMed:9839951}. Note=Secreted in the hemolymph. {ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:9652393, ECO:0000269|PubMed:9839951}. | null | null | null | null | null | FUNCTION: Serine endopeptidase which, by cleaving prophenoloxidase PPO1 and PPO2, is required for the activation of the prophenoloxidase cascade probably following the recognition of pathogen-derived products. {ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:16362048, ECO:0000269|PubMed:17287215, ECO:0000269|PubMed:965... | Holotrichia diomphalia (Korean black chafer) |
O97394 | SDK_DROME | MLKSAASSLRRRRPKTTITATLAIEMPSQPKLASLLAVLVLLCYCDSCFFCYADANLQQQNSIVQQQQLQAPRFTTHPSSSGSIVSEGSTKILQCHALGYPQPTYRWLKDGVPVGDFSSSQFYRFHSTRREDAGSYQCIARNDAGSIFSEKSDVVVAYMGIFENTTEGRLTVISGHPAIFDMPPIESIPVPSVMWQSEDGPLNYDIKYAFTHANQLIILSADENDRKGYRAKAINTQLGKEESSAFVHLNVSGDPYIEVAPEIIVRPQDVKVKVGTGVVELQCIANARPLHELETLWLKDGLAVETAGVRHTLNDPWNRT... | null | null | cell-cell adhesion [GO:0098609]; compound eye cone cell differentiation [GO:0042675]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; negative regulation of photoreceptor cell differentiation [GO:0046533]; pigment cell differentiation [GO:0050931] | apical part of cell [GO:0045177]; perivitelline space [GO:0098595]; plasma membrane [GO:0005886] | cell adhesion receptor activity [GO:0004895] | PF00041;PF07679;PF13927; | 2.60.40.10; | Sidekick family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Participates in homotypic or heterotypic interactions in the eye during pattern formation to prevent extra cells from joining the precluster and differentiating as photoreceptor cells. {ECO:0000269|PubMed:9310325}. | Drosophila melanogaster (Fruit fly) |
O97422 | B3GI_DROME | MSEVRIRPRQVLILIIVFLVVLMMVHRNGKRTCQGPEYLQAMFVQGDTLPTIYAVTPTYPRPAQKAELTRLSHLFMLLPHLHWIIVEDTNATTPLVRNLLDRAGLEKRSTLLNIKTPSEFKLKGKDPNWIKPRGVEQRNLALAWLRNHVDVDRHSIVFFMDDDNSYSTELFAEMSKIERGRVGVWPVGLVGGLMVERPLLTEDGTKVTGFNAAWRPERPFPIDMAAFAISMDLFIRNPQATFSYEVQRGYQESEILRHLTTRDQLQPLANRCTDVLVWHTRTEKTKLAAEEALLKKGQRSDGGMEV | 2.4.1.135 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:12511570}; | carbohydrate metabolic process [GO:0005975]; chondroitin sulfate proteoglycan biosynthetic process [GO:0050650]; protein glycosylation [GO:0006486]; proteoglycan biosynthetic process [GO:0030166] | Golgi membrane [GO:0000139] | galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity [GO:0015018]; metal ion binding [GO:0046872] | PF03360; | null | Glycosyltransferase 43 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:24168, Rhea:RHEA-COMP:12571, Rhea:RHEA-COMP:12573, ChEB... | null | PATHWAY: Protein modification; protein glycosylation. | null | null | FUNCTION: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins. Shows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates. {ECO:0000269|PubMed:12511570}. | Drosophila melanogaster (Fruit fly) |
O97531 | KCNQ1_FELCA | RVSIYSARRPLLARTHIQGRVYNFLERPTGWKCFVYHFAVFLIVLVCLIFSVLSTIEQYVALATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGVWGRLRFARKPISIIDLIVVLASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGQVEFGSYADALWWGVVTVTTIGYGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLIQTAWRCYAAENPESSTWNIYVRKPTRSHTLLSPS... | null | null | inner ear development [GO:0048839]; intestinal absorption [GO:0050892]; membrane repolarization [GO:0086009]; membrane repolarization during ventricular cardiac muscle cell action potential [GO:0098915]; potassium ion export across plasma membrane [GO:0097623]; regulation of gastric acid secretion [GO:0060453]; renal a... | basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; membrane raft [GO:0045121]; monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO... | calmodulin binding [GO:0005516]; delayed rectifier potassium channel activity [GO:0005251]; outward rectifier potassium channel activity [GO:0015271]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; voltage-gated potassium channel activity [GO:0005249]; voltage-gated potassium channel activity involved in a... | PF00520;PF03520; | 1.10.287.70;6.10.140.1910;1.20.120.350; | Potassium channel family, KQT (TC 1.A.1.15) subfamily, Kv7.1/KCNQ1 sub-subfamily | PTM: Phosphorylated by PKA; increases delayed rectifier potassium channel activity of the KCNQ1-KCNE1 complex through a macromolecular complex that includes PKA, PP1, and the targeting protein AKAP9. {ECO:0000250|UniProtKB:P51787}.; PTM: Ubiquitinated by NEDD4L; promotes internalization. The ubiquitinylated form is int... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51787}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P51787}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P51787}. Early endosome {ECO:0000250|UniProtKB:P51787}. Membrane raft {ECO:0000250|UniProtKB:P51787}. Endoplasmic reticulum {ECO:0000250|Uni... | null | null | null | null | null | FUNCTION: Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity). Associates with KCNE beta subunits that modulates current kinetics (By similarity). Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selectiv... | Felis catus (Cat) (Felis silvestris catus) |
O97554 | PGH1_RABIT | MSRSSPSLRLPVLLLLLLLLLLPPPPPVLPADPGAPAPVNPCCYFPCQHQGVCVRVALDRYQCDCTRTGYSGPNCTVPDLWTWLRSSLRPSPTFVHYLLTHVRWFWEFVNATFIRDTLMRLVLTVRSNLIPSPPTYNLDYDYISWEAFSNVSYYTRVLPSVPKDCPTPMGTKGKKQLPDAQVLAHRFLLRRTFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDSLERQYHLRLFKDGKLKYQVLDGEVYPPSVEEAPVLMHYPRGVPPRSQMAVGQEVFGLLPGLMLYATLWLREHNRVCD... | 1.14.99.1 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000250}; | cyclooxygenase pathway [GO:0019371]; response to oxidative stress [GO:0006979] | endoplasmic reticulum membrane [GO:0005789]; neuron projection [GO:0043005] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]; peroxidase activity [GO:0004601]; prostaglandin-endoperoxide synthase activity [GO:0004666] | PF03098; | 1.10.640.10;2.10.25.10; | Prostaglandin G/H synthase family | null | SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + 2 O2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:23728, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:57405; EC=1.14.99.1; Evidence={ECO:0000250|UniProtKB:P23219}; PhysiologicalDirection=... | null | PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000250|UniProtKB:P23219}. | null | null | FUNCTION: Dual cyclooxygenase and peroxidase that plays an important role in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates... | Oryctolagus cuniculus (Rabbit) |
O97562 | UCP2_PIG | MVGFKATEVPPTATVKFLGAGTAACIADLITFPLDTAKVRLQIQGERRGPVQAAASAQYRGVLGTILTMVRNEGPRSLYNGLVAGLQRQMSFASVRIGLYDSVKHFYTKGSEHAGIGSRLLAGSTTGALAVAVAQPTDVVKVRFQAQARAGGGRRYRSTVDAYKTIAREEGLRGLWKGTSPNVARNAIVNCAELVTYDLIKDTLLKADLMTDDLPCHFTSAFGAGFCTTVIASPVDVVKTRYMNSAPGQYSSAGHCALTMLQKEGPRAFYKGFTPSFLRLGSWNVVMFVTYEQLKRALMAARASREAPF | null | null | adaptive thermogenesis [GO:1990845]; C4-dicarboxylate transport [GO:0015740]; cellular response to glucose stimulus [GO:0071333]; glutamine metabolic process [GO:0006541]; glycolytic process [GO:0006096]; macrophage differentiation [GO:0030225]; mitochondrial fission [GO:0000266]; mitochondrial transmembrane transport ... | mitochondrial inner membrane [GO:0005743] | antiporter activity [GO:0015297]; L-aspartate transmembrane transporter activity [GO:0015183]; malate transmembrane transporter activity [GO:0015140]; oxaloacetate transmembrane transporter activity [GO:0015131]; oxidative phosphorylation uncoupler activity [GO:0017077]; phosphate ion uniporter activity [GO:0140787]; p... | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P70406}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) + L-aspartate(out) + phosphate(in) = H(+)(out) + L-aspartate(in) + phosphate(out); Xref=Rhea:RHEA:73307, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:P55851}; CATALYTIC ACTIVITY: Reaction=H(+)(in) + oxaloacetate(out) + phosphate(in) = H(+... | null | null | null | null | FUNCTION: Antiporter that exports dicarboxylate intermediates of the Krebs cycle in exchange for phosphate plus a proton across the inner membrane of mitochondria, a process driven by mitochondrial motive force with an overall impact on glycolysis, glutaminolysis and glutathione-dependent redox balance. Continuous expo... | Sus scrofa (Pig) |
O97572 | RAB7A_RABIT | MTSRKKVLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVMVDDRLVTMQIWDTAGQERFQSLSVAFYRGADCCVLVFDVTAPNTFKTLDSWRLEFLIQASPRDPENFPFVVLGNKIDLENRQVATKRAQAWSYSKNNIPYFETSAKEAINVEQAFQTIARNALKQETEVELYNEFPEPMKLDKNDRAKTSAESCSC | 3.6.5.2 | null | early endosome to late endosome transport [GO:0045022]; endosome to lysosome transport [GO:0008333]; endosome to plasma membrane protein transport [GO:0099638]; lipid catabolic process [GO:0016042]; lipophagy [GO:0061724]; phagosome acidification [GO:0090383]; phagosome-lysosome fusion [GO:0090385] | autophagosome membrane [GO:0000421]; cytosol [GO:0005829]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lipid droplet [GO:0005811]; lysosomal membrane [GO:0005765]; melanosome membrane [GO:0033162]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; phagocytic vesicle [GO:0045335]; pha... | G protein activity [GO:0003925]; GTP binding [GO:0005525] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | PTM: Deubiquitination at Lys-191 and Lys-194 by USP32. {ECO:0000250|UniProtKB:P51149}. | SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {EC... | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P51149}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|Uni... | null | null | null | null | FUNCTION: Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins playing a key role in the regulation of endo-lysosomal trafficking. Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endo... | Oryctolagus cuniculus (Rabbit) |
O97583 | NDST2_BOVIN | MLKLWKVVRPARQLELHRLILLLIAFSLGSMGFLAYYVSTSPKAKEPLPLPLGDCSSSGAAGGPGPVRPPVPPRPPRPPETARTEPVVLVFVESAYSQLGQEIVAILESSRFRYSTELAPGRGDMPTLTDHTRGRYVLVIYENLLKYVNLDAWSRELLDRYCVEYGVGIIGFFRAHEHSLLSAQLKGFPLFLHSNLGLRDYQVNPTAPLLHLTRPSRLEPGPLPGDDWTIFQSNHRTYEPVLLGSLRPAEPPVPGPVARRARLPTVVQDLGVHDGIQRVLFGHGLSFWLHKLVFRDAGGYLTGKGLLWDLDRYILVDIDD... | 2.8.2.-; 2.8.2.8; 3.-.-.- | null | heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process [GO:0015014]; heparin biosynthetic process [GO:0030210] | Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139] | [heparan sulfate]-glucosamine N-sulfotransferase activity [GO:0015016]; deacetylase activity [GO:0019213] | PF12062;PF00685; | 3.40.50.300; | Sulfotransferase 1 family, NDST subfamily | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = adenosine 3',5'-bisphosphate + 2 H(+) + N-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n); Xref=Rhea:RHEA:21980, Rhea:RHEA-COMP:9830, Rhea:RHEA-COMP:14602, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI... | null | PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.; PATHWAY: Glycan metabolism; heparin biosynthesis. | null | null | FUNCTION: Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in hepari... | Bos taurus (Bovine) |
O97593 | SMC1A_BOVIN | MGFLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQ... | null | null | cell division [GO:0051301]; DNA repair [GO:0006281]; meiotic cell cycle [GO:0051321]; response to DNA damage checkpoint signaling [GO:0072423]; response to radiation [GO:0009314]; sister chromatid cohesion [GO:0007062] | kinetochore [GO:0000776]; meiotic cohesin complex [GO:0030893]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; chromatin binding [GO:0003682]; DNA binding [GO:0003677] | PF06470;PF02463; | 1.20.1060.20;3.30.70.1620;3.40.50.300; | SMC family, SMC1 subfamily | PTM: Phosphorylated upon ionizing radiation or DNA methylation. Phosphorylation of Ser-957 and Ser-966 activates it and is required for S-phase checkpoint activation (By similarity). {ECO:0000250|UniProtKB:Q14683}.; PTM: Ubiquitinated by the DCX(DCAF15) complex, leading to its degradation. {ECO:0000250|UniProtKB:Q14683... | SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere. Note=Associates with chromatin. The phosphorylated form on Ser-957 and Ser-966 associates with chromatin during G1/S/G2 phases but not during M phase, suggesting that phosphorylation does not regulate cohesin function (By similarity). Before prophase it... | null | null | null | null | null | FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA repair. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, and works as a downstream effector in the ATM/NBS1 branch of S-phase checkpoint (By similarity). Central component of cohesin complex. The cohesin ... | Bos taurus (Bovine) |
O97594 | SMC3_BOVIN | MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVEIIFDNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNS... | null | null | cell division [GO:0051301]; DNA repair [GO:0006281]; meiotic cell cycle [GO:0051321]; mitotic sister chromatid cohesion [GO:0007064]; regulation of DNA replication [GO:0006275] | chromatin [GO:0000785]; chromosome, centromeric region [GO:0000775]; meiotic cohesin complex [GO:0030893]; mitotic spindle pole [GO:0097431]; nuclear matrix [GO:0016363] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cohesin loader activity [GO:0061775]; double-stranded DNA binding [GO:0003690]; dynein complex binding [GO:0070840] | PF06470;PF02463; | 1.10.287.1490;1.20.1060.20;3.30.70.1620;3.40.50.300; | SMC family, SMC3 subfamily | PTM: Phosphorylated at Ser-1082 in a SPO11-dependent manner. {ECO:0000250|UniProtKB:Q9CW03}.; PTM: Acetylation at Lys-105 and Lys-106 by ESCO1 is important for genome stability and S phase sister chromatid cohesion. Regulated by DSCC1, it is required for processive DNA synthesis, coupling sister chromatid cohesion esta... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9CW03}. Chromosome {ECO:0000250|UniProtKB:Q9CW03}. Chromosome, centromere {ECO:0000250|UniProtKB:Q9CW03}. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin prob... | null | null | null | null | null | FUNCTION: Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Co... | Bos taurus (Bovine) |
O97605 | CD40L_FELCA | MIETYSQTAPRSVAPGPPVSMKIFMYLLTVFLITQMIGSALFAVYLHRRLDKIEDERNLYEDFVFMKTLQKCNKGEGALSLLNCEEIKSRFEAFLKEIMLNKETKKEKNVAMQKGDQDPRVAAHVISEASSSTASVLQWAPKGYYTISSNLVTLENGKQLAVKRQGLYYIYAQVTFCSNREASSQAPFIASLCLHSPSGSERVLLRAANARSSSKPCGQQSIHLGGVFELHPGASVFVNVTDPSQVSHGTGFTSFGLLKL | null | null | B cell proliferation [GO:0042100]; immune response [GO:0006955]; inflammatory response [GO:0006954]; platelet activation [GO:0030168]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of interleukin-4 production [GO:0032753]; positive regulation of NF-kappaB transcription factor activi... | cell surface [GO:0009986]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | CD40 receptor binding [GO:0005174]; cytokine activity [GO:0005125]; protein serine/threonine kinase activator activity [GO:0043539]; tumor necrosis factor receptor binding [GO:0005164] | PF00229; | 2.60.120.40; | Tumor necrosis factor family | PTM: The soluble form derives from the membrane form by proteolytic processing. {ECO:0000250|UniProtKB:P29965}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P29965}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P29965}. Cell surface {ECO:0000250|UniProtKB:P29965}.; SUBCELLULAR LOCATION: [CD40 ligand, soluble form]: Secreted {ECO:0000250|UniProtKB:P29965}. Note=Release of soluble CD40L from platelets ... | null | null | null | null | null | FUNCTION: Cytokine that acts as a ligand to CD40/TNFRSF5 (By similarity). Costimulates T-cell proliferation and cytokine production (By similarity). Its cross-linking on T-cells generates a costimulatory signal which enhances the production of IL4 and IL10 in conjunction with the TCR/CD3 ligation and CD28 costimulation... | Felis catus (Cat) (Felis silvestris catus) |
O97626 | CD40L_CANLF | MIETYSQTAPRSVATGPPVSMKIFMYLLTVFLITQMIGSALFAVYLHRRLDKIEDERNLYEDFVFMKTLQKCNKGEGSLSLLNCEEIKSQFEAFLKEIMLNNEMKKEENIAMQKGDQDPRIAAHVISEASSNPASVLRWAPKGYYTISSNLVSLENGKQLAVKRQGLYYVYAQVTFCSNRAASSQAPFVASLCLHSPSGTERVLLRAASSRGSSKPCGQQSIHLGGVFELHPGASVFVNVTDPSQVSHGTGFTSFGLLKL | null | null | B cell proliferation [GO:0042100]; immune response [GO:0006955]; inflammatory response [GO:0006954]; platelet activation [GO:0030168]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of interleukin-4 production [GO:0032753]; positive regulation of NF-kappaB transcription factor activi... | cell surface [GO:0009986]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | CD40 receptor binding [GO:0005174]; cytokine activity [GO:0005125]; protein serine/threonine kinase activator activity [GO:0043539]; tumor necrosis factor receptor binding [GO:0005164] | PF00229; | 2.60.120.40; | Tumor necrosis factor family | PTM: The soluble form derives from the membrane form by proteolytic processing. {ECO:0000250|UniProtKB:P29965}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P29965}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P29965}. Cell surface {ECO:0000250|UniProtKB:P29965}.; SUBCELLULAR LOCATION: [CD40 ligand, soluble form]: Secreted {ECO:0000250|UniProtKB:P29965}. Note=Release of soluble CD40L from platelets ... | null | null | null | null | null | FUNCTION: Cytokine that acts as a ligand to CD40/TNFRSF5 (By similarity). Costimulates T-cell proliferation and cytokine production (By similarity). Its cross-linking on T-cells generates a costimulatory signal which enhances the production of IL4 and IL10 in conjunction with the TCR/CD3 ligation and CD28 costimulation... | Canis lupus familiaris (Dog) (Canis familiaris) |
O97627 | ARBK1_DIDVI | MADLEAVLADVSYLMAMEKSKATPAARASKKILLPEPSIRSVMQKYLEDRGEVTFEKIFSQKLGYLLFREFCLNHMEEAKPLVEFYDEIKKYEKLDSEEERTVKSREIFDLYIMKELLSCSHLFSKSATEHVQSRLLKKQVPTDLFQPYIEEICQRFRDDVFQKFIESEKFTRFCQWKNVELNIHLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNGGDLHYHLSQHGVFSESDMRFYAAEIILGLEHMHSRFVVYRDLKP... | 2.7.11.15 | null | desensitization of G protein-coupled receptor signaling pathway [GO:0002029]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of relaxation of smooth muscle [GO:1901081]; phosphorylation [GO:0016310]; regulation of the force of heart contraction [GO:0002026] | cell projection [GO:0042995]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; presynapse [GO:0098793] | ATP binding [GO:0005524]; beta-adrenergic receptor kinase activity [GO:0047696]; Edg-2 lysophosphatidic acid receptor binding [GO:0031755]; G protein-coupled receptor kinase activity [GO:0004703] | PF00169;PF00069;PF00615; | 2.30.29.30;1.10.167.10;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, GPRK subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P26817}. Cell membrane {ECO:0000250|UniProtKB:P21146}. Postsynapse {ECO:0000250|UniProtKB:P26817}. Presynapse {ECO:0000250|UniProtKB:P26817}. | CATALYTIC ACTIVITY: Reaction=[beta-adrenergic receptor] + ATP = [beta-adrenergic receptor]-phosphate + ADP + H(+); Xref=Rhea:RHEA:19429, Rhea:RHEA-COMP:11222, Rhea:RHEA-COMP:11223, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.15; Evidence={ECO:0000250|UniProt... | null | null | null | null | FUNCTION: Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors, probably inducing a desensitization of them (PubMed:9892019). Does not act on HTR1B/5-hydroxytryptamine 1B receptor (PubMed:9892019). Key regulator of LPAR1 signaling (By similarity). Competes with RALA... | Didelphis virginiana (North American opossum) (Didelphis marsupialis virginiana) |
O97666 | APJ_MACMU | MEEGGDFDNYYGADNQSECEYTDWKSSGALIPAIYMLVFLLGTTGNGLVLWTVFRSSREKRRSADIFIASLAVADLTFVVTLPLWATYTYRDYDWPFGTFSCKLSSYLIFVNMYASVFCLTGLSFDRYLAIVRPVANARLRLRVSGAVATAVLWVLAALLAMPVMVFRTTGDLENTTKVQCYMDYSMVATVSSDWAWEVGLGVSSTTVGFVVPFTIMLTCYFFIAQTIAGHFRKERIEGLRKRRRLLSIIVVLVVTFALCWMPYHLVKTLYMLGSLLHWPCDFDLFLMNVFPYCTCISYVNSCLNPFLYAFFDPRFRQAC... | null | null | blood vessel development [GO:0001568]; brain development [GO:0007420]; calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; coronary vasculature development [GO:0060976]; G protein-coupled receptor signaling pathway [GO:0007186]; gastrulation [GO:0007369]; heart development [GO:0007507]; immune respon... | external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | apelin receptor activity [GO:0060182]; C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35414}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P79960}. Note=After exposure to apelin (APLN) or apelin receptor early endogenous ligand (APELA), internalized from the cell surface into an endosomal recycling compartment, from where it is recycled t... | null | null | null | null | null | FUNCTION: Receptor for apelin receptor early endogenous ligand (APELA) and apelin (APLN) hormones coupled to G proteins that inhibit adenylate cyclase activity. Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for APELA hormone. May prom... | Macaca mulatta (Rhesus macaque) |
O97676 | SRBP1_PIG | MDEPPFTEAALEQALAEPCELDAALLTDIEDMLQLINNQDSDFPGLFDAPYAGVAGGTDPTSPDASSPGSPTPPPSTMSSPLEGFLGGARTPPPPPVSPTQPAPTPLKMYPSVPAFSPGPGIKEEPVPLTILQPPTPQPLSGALLPQSLPALAPPQLSPAPVLGYPSPPGSFSSATPPGSTSQTLPGLPLASLPGVLPVSVHTQVQSAAPQQLLTATATPVVSPGTTTVTSQIQQVPVLLQPHFIKADSLLLTTMKTDMGTPVKAAGIGSLAPGTAVQAAPLQTLVSGGTILATVPLVVDTDKLPINRLAAGGKALSSGQ... | null | null | cholesterol metabolic process [GO:0008203]; lipid biosynthetic process [GO:0008610]; positive regulation of triglyceride biosynthetic process [GO:0010867]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00010; | 4.10.280.10; | SREBP family | PTM: [Sterol regulatory element-binding protein 1]: Processed in the Golgi apparatus, releasing the protein from the membrane. At low cholesterol the SCAP-SREBP complex is recruited into COPII vesicles for export from the endoplasmic reticulum. In the Golgi, complex SREBPs are cleaved sequentially by site-1 (MBTPS1, S1... | SUBCELLULAR LOCATION: [Sterol regulatory element-binding protein 1]: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P36956}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9WTN3}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle mem... | null | null | null | null | null | FUNCTION: [Sterol regulatory element-binding protein 1]: Precursor of the transcription factor form (Processed sterol regulatory element-binding protein 1), which is embedded in the endoplasmic reticulum membrane (By similarity). Low sterol concentrations promote processing of this form, releasing the transcription fac... | Sus scrofa (Pig) |
O97703 | CD81_CHLAE | MGVEGCTKCIKYLLFVFNFVFWLAGGVILGVALWLRHDPQTTNLLYLELGDKPAPNTFYVGIYILIAVGAVMMFVGFLGCYGAIQESQCLLGTFFTCLVILFACEVAAGIWGFVNKDQIAKDVKQFYDQALQQAVVDDDANNAKAVVKTFHETLDCCGSSTLAALTTSVLKNNLCPSGSNIISNLLKKDCHQKIDELFSGKLYLIGIAAIVVAVIMIFEMILSMVLCCGIRNSSVY | null | null | CD4-positive, alpha-beta T cell costimulation [GO:0035783]; cellular response to low-density lipoprotein particle stimulus [GO:0071404]; humoral immune response mediated by circulating immunoglobulin [GO:0002455]; immunological synapse formation [GO:0001771]; macrophage fusion [GO:0034238]; myoblast fusion involved in ... | basolateral plasma membrane [GO:0016323]; immunological synapse [GO:0001772]; membrane [GO:0016020]; plasma membrane [GO:0005886]; tetraspanin-enriched microdomain [GO:0097197] | cholesterol binding [GO:0015485]; integrin binding [GO:0005178] | PF00335; | 1.10.1450.10; | Tetraspanin (TM4SF) family | PTM: Not glycosylated. {ECO:0000305}.; PTM: Likely constitutively palmitoylated at low levels. Protein palmitoylation is up-regulated upon coligation of BCR and CD9-C2R-CD81 complexes in lipid rafts. {ECO:0000250|UniProtKB:P60033}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35762}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P60033}; Multi-pass membrane protein {ECO:0000255}. Note=Associates with CLDN1 and the CLDN1-CD81 complex localizes to the basolateral cell membrane. {ECO:00002... | null | null | null | null | null | FUNCTION: Structural component of specialized membrane microdomains known as tetraspanin-enriched microdomains (TERMs), which act as platforms for receptor clustering and signaling. Essential for trafficking and compartmentalization of CD19 receptor on the surface of activated B cells. Upon initial encounter with micro... | Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops) |
O97711 | HYAS2_BOVIN | MHCERFLCILRIIGTTLFGVSLLLGITAAYIVGYQFIQTDNYYFSFGLYGAFLASHLIIQSLFAFLEHRKMKKSLETPIKLNKTVALCIAAYQEDPDYLRKCLQSVKRLTYPGIKVVMVIDGNSEDDLYMMDIFSEVMGRDKSATYIWKNNYHVKGPGETDESHKESSQHVTQLVLSNKSICTMQKWGGKREVMYTAFRALGRSVDYVQVCDSDTMLDPASSVEMVKVLEEDPMVGGVGGDVQILNKYDSWISFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFVEDWYNQEFMGSQCSFGDDRHLTNR... | 2.4.1.212 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | atrioventricular canal development [GO:0036302]; endocardial cushion to mesenchymal transition [GO:0090500]; extracellular matrix assembly [GO:0085029]; extracellular polysaccharide biosynthetic process [GO:0045226]; hyaluronan biosynthetic process [GO:0030213]; positive regulation of urine volume [GO:0035810]; renal w... | endoplasmic reticulum membrane [GO:0005789]; extracellular vesicle [GO:1903561]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; lysosome [GO:0005764]; plasma membrane [GO:0005886] | hyaluronan synthase activity [GO:0050501] | PF03142; | null | NodC/HAS family | PTM: Phosphorylation at Thr-328 is essential for hyaluronan synthase activity. {ECO:0000250|UniProtKB:Q92819}.; PTM: O-GlcNAcylation at Ser-221 increases the stability of HAS2 and plasma membrane localization. {ECO:0000250|UniProtKB:Q92819}.; PTM: Ubiquitination at Lys-190; this ubiquitination is essential for hyaluron... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q92819}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q92819}; Multi-pass membrane protein {ECO:0000255}. Vesicle {ECO:0000250|UniProtKB:Q92819}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q92819}; Multi-... | CATALYTIC ACTIVITY: Reaction=[hyaluronan](n) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N-acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP; Xref=Rhea:RHEA:20465, Rhea:RHEA-COMP:12583, Rhea:RHEA-COMP:12585, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:132153, ChEBI:CHEBI:132154; EC=2.4.1.... | null | PATHWAY: Glycan biosynthesis; hyaluronan biosynthesis. {ECO:0000250|UniProtKB:Q92819}. | null | null | FUNCTION: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation (By si... | Bos taurus (Bovine) |
O97716 | THA_PIG | MEQKPSKVECGSDPEENSARSPDGKRKRKNGQCSLKTSMSGYIPSYLDKDEQCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPTYSCKYDSCCVIDKITRNQCQLCRFKKCIAVGMAMDLVLDDSKRVAKRKLIEQNRERRRKEEMIRSLQQRPEPTPEEWDLIHVATEAHRSTNAQGSHWKQRRKFLPDDIGQSPIVSMPDGDKVDLEAFSEFTKIITPAITRVVDFAKKLPMFSELPCEDQIILLKGCCMEIMSLRAAVRYDPESDTLTLSGEMAVKREQLKNGGLGVVSDAIFELGKSLSAFNLDDTEVALLQ... | null | null | cell differentiation [GO:0030154]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; retinoic acid receptor signaling pathway [GO:0048384]; thyroid hormone mediated signaling pathway [GO:0002154] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; thyroid hormone binding [GO:0070324]; zinc ion binding [GO:0008270] | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | null | SUBCELLULAR LOCATION: Nucleus.; SUBCELLULAR LOCATION: [Isoform Alpha-2]: Cytoplasm {ECO:0000250|UniProtKB:P63058}. Nucleus {ECO:0000250|UniProtKB:P63058}. Note=When overexpressed found in the cytoplasm where it colocalizes with TACC1. {ECO:0000250|UniProtKB:P63058}. | null | null | null | null | null | FUNCTION: Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine. | Sus scrofa (Pig) |
O97741 | SCNNA_RABIT | MKGDKREEQGPGPETVAPQQPTEDEEALIEFHRSYRELFQFFCNNTTIHGAIRLVCSKHNRMKTAFWAVLWLCTFGMMYWQFGLLFGEYFSYPVNLNINLNSDKLVFPAVTVCTLNPYRYPEITEQLKELDSITQQTLLDLFKYNASTLEAQPRHRRDVHPPLPHPLQRLRVPPPRLEARRARSSASSVRDNSPEVGRKDWMIGFQLCNQNRSDCFYQRYSSGVDAVREWYRFHYINILSRLSDTSLSREQLGNFIFTCRFNQAFCGDGNYSHFHHPMYGNCYTFNDKNNSSLWMSSMPGINNGLSLTLRTEQNDFIPLL... | null | null | multicellular organismal-level water homeostasis [GO:0050891]; response to stimulus [GO:0050896]; sensory perception of taste [GO:0050909]; sodium ion homeostasis [GO:0055078]; sodium ion transmembrane transport [GO:0035725] | acrosomal vesicle [GO:0001669]; apical plasma membrane [GO:0016324]; ciliary membrane [GO:0060170]; cytoplasm [GO:0005737]; motile cilium [GO:0031514]; plasma membrane [GO:0005886]; sodium channel complex [GO:0034706]; sperm principal piece [GO:0097228] | ligand-gated sodium channel activity [GO:0015280] | PF00858; | 2.60.470.10;1.10.287.770; | Amiloride-sensitive sodium channel (TC 1.A.6) family, SCNN1A subfamily | PTM: Ubiquitinated; this targets individual subunits for endocytosis and proteasome-mediated degradation. {ECO:0000250|UniProtKB:P37089}.; PTM: ENaC cleavage by furin, and subsequently by prostasin (PRSS8), leads to a stepwise increase in the open probability of the channel as a result of release of the alpha and gamma... | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P37089}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P37089}. Cell projection, cilium {ECO:0000250|UniProtKB:P37088}. Cytoplasmic granule {ECO:0000250|UniProtKB:P37088}. Cytoplasm {ECO:0000250|UniProtKB:P37088}. Cytoplasmic vesicle, secretory vesi... | null | null | null | null | null | FUNCTION: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in... | Oryctolagus cuniculus (Rabbit) |
O97756 | SNAT_MACMU | MSTQSTHPPKPEAPRLPPAISSCQRRHTLPASEFRCLTPEDAVSAFEIEREAFISVLGVCPLYLDEIRHFLTLCPELSLGWFEEGCLVAFIIGSLWDKDRLMQESLTMHRPGGHIAHLHVLAVHCAFRQQGRGPILLWRYLHHLGSQPAVHRAALMCEDALVPFYERFGFHAMGPCAITVGSLSFTELHCSLQGHPFLRRNSGC | 2.3.1.87 | null | cellular response to cAMP [GO:0071320]; circadian rhythm [GO:0007623]; melatonin biosynthetic process [GO:0030187]; N-terminal protein amino acid acetylation [GO:0006474]; response to light stimulus [GO:0009416] | cytoplasm [GO:0005737]; perinuclear region of cytoplasm [GO:0048471] | aralkylamine N-acetyltransferase activity [GO:0004059] | PF00583; | 3.40.630.30; | Acetyltransferase family, AANAT subfamily | PTM: cAMP-dependent phosphorylation regulates AANAT activity by promoting interaction with 14-3-3 proteins. Phosphorylation levels exhibit night/day variations, with an increase during nighttime. {ECO:0000269|PubMed:12364461}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16613}. | CATALYTIC ACTIVITY: Reaction=a 2-arylethylamine + acetyl-CoA = an N-acetyl-2-arylethylamine + CoA + H(+); Xref=Rhea:RHEA:20497, ChEBI:CHEBI:15378, ChEBI:CHEBI:55469, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:77827; EC=2.3.1.87; Evidence={ECO:0000269|PubMed:12364461}; | null | PATHWAY: Aromatic compound metabolism; melatonin biosynthesis; melatonin from serotonin: step 1/2. | null | null | FUNCTION: Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin. {ECO:0000269|PubMed:12364461}. | Macaca mulatta (Rhesus macaque) |
O97758 | ZO1_CANLF | MSARAAAAKNTAMEETAIWEQHTVTLHRAPGFGFGIAISGGRDNPHFQSGETSIVISDVLKGGPAEGQLQENDRVAMVNGVSMDNVEHAFAVQQLRKSGKNAKITIRRKKKVQIPVSRPDPEPVSENEDSYDEEVHDPRSSRGGLVSRRSEKSWARDRSASRERSLSPRSDRRSVASSQPPKPTKVTLVKSRKNEEYGLRLASHIFVKEISQDSLAARDGNIQEGDVVLKINGTVTENMSLTDAKTLIERSKGKLKMVVQRDERATLLNVPDLSDSIHSANASERDDISEIQSLASDHSGRSHDRPPRHSRSRSPDQRSE... | null | null | bicellular tight junction assembly [GO:0070830]; cell-cell adhesion [GO:0098609]; cell-cell junction organization [GO:0045216]; cellular response to calcium ion [GO:0071277]; establishment of endothelial intestinal barrier [GO:0090557]; positive regulation of blood-brain barrier permeability [GO:1905605]; protein local... | bicellular tight junction [GO:0005923]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cytoplasmic vesicle [GO:0031410]; gap junction [GO:0005921]; plasma membrane [GO:0005886]; tight junction [GO:0070160] | calmodulin binding [GO:0005516]; cell adhesion molecule binding [GO:0050839] | PF00625;PF00595;PF07653;PF00791; | 2.30.42.10;2.60.220.30;3.40.50.300;2.30.30.40; | MAGUK family | PTM: Phosphorylated at tyrosine redidues in response to epidermal growth factor (EGF) (By similarity). This response is dependent on an intact actin microfilament system (By similarity). Dephosphorylated by PTPRJ (By similarity). {ECO:0000250|UniProtKB:Q07157}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9792688}; Peripheral membrane protein {ECO:0000269|PubMed:9792688}; Cytoplasmic side {ECO:0000269|PubMed:9792688}. Cell junction, tight junction {ECO:0000269|PubMed:9792688}. Cell junction {ECO:0000250|UniProtKB:P12830}. Cell junction, gap junction {ECO:0000250|Un... | null | null | null | null | null | FUNCTION: TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:10575001, PubMed:27802160, PubMed:9792688). The tight junction acts to limit movement of substances... | Canis lupus familiaris (Dog) (Canis familiaris) |
O97763 | NPC2_PIG | MHFLAAAFLLLTLSASALAEPVHFRDCGSGVGVIKEVNVNPCPTQPCQLHKGQSYSVNVTFTSNTQSKGSKAVVHGIVMGVPIPFPIPDPDGCKSGINCPIQKDQTYSYLNKLPVKAEYPSIKLVVEWKLQDDNDQCLFCWQIPVQIES | null | null | cholesterol efflux [GO:0033344]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; intracellular cholesterol transport [GO:0032367] | endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; lysosome [GO:0005764] | cholesterol binding [GO:0015485] | PF02221; | 2.60.40.770; | NPC2 family | PTM: N-glycosylated. Found in the epididymal fluid as a 19 kDa glycoprotein that is processed during its passage through the epididymis into a 16 kDa protein. {ECO:0000269|PubMed:10366780}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10366780}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P61916}. Lysosome {ECO:0000250|UniProtKB:P61916}. Note=Interaction with cell-surface M6PR mediates endocytosis and targeting to lysosomes. {ECO:0000250|UniProtKB:P61916}. | CATALYTIC ACTIVITY: Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747, ChEBI:CHEBI:16113; Evidence={ECO:0000250|UniProtKB:P79345}; | null | null | null | null | FUNCTION: Intracellular cholesterol transporter which acts in concert with NPC1 and plays an important role in the egress of cholesterol from the lysosomal compartment. Unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes is transferred by NPC2 to the cholesterol-bindin... | Sus scrofa (Pig) |
O97775 | ANDR_PANTR | MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLLLQQQQQQQQQQQQQQQQQQQQQQETSPRQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSAPECHPERGCVPEPGAAVAASKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSADLKDILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLGGTSTISDSAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYAPLLGVPPAVRPTPCAPLAECKGSLLDDSAGKSTEDTAEYSPFKGGYTKGLEGE... | null | null | androgen receptor signaling pathway [GO:0030521]; intracellular receptor signaling pathway [GO:0030522]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; male gonad development [GO:0008584]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of integrin ... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | androgen binding [GO:0005497]; beta-catenin binding [GO:0008013]; DNA-binding transcription factor activity [GO:0003700]; estrogen response element binding [GO:0034056]; nuclear receptor activity [GO:0004879]; steroid binding [GO:0005496]; transcription cis-regulatory region binding [GO:0000976]; zinc ion binding [GO:0... | PF02166;PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | PTM: Phosphorylated in prostate cancer cells in response to several growth factors including EGF. Phosphorylation is induced by c-Src kinase (CSK). Tyr-526 is one of the major phosphorylation sites and an increase in phosphorylation and Src kinase activity is associated with prostate cancer progression (By similarity).... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10275}. Cytoplasm {ECO:0000250|UniProtKB:P10275}. Note=Detected at the promoter of target genes. Predominantly cytoplasmic in unligated form but translocates to the nucleus upon ligand-binding. Can also translocate to the nucleus in unligated form in the presence of... | null | null | null | null | null | FUNCTION: Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NC... | Pan troglodytes (Chimpanzee) |
O97776 | ANDR_EULFC | MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGARLQQQQETSPPQQQQQQQGEDGSPQAQSRGPTGYLALDEEQQPSQQQSALECHPESGCVPEPGAAAAASKGLQQQPPAPSDEDDSAVPSTLSLLGPTFPGLSSCSADLKDILSEAGTMQLLQQQQQEAVSEGSSSGRAREAAGAPTSSKDSYLGGTSTISDSAKELCKAVSVSMGLGVETLEHLSPGEQLRGDCMYAPLLGGPPAVRPTPCAPLAECKGSLLDDSADKGTEEPAEYTPFKGSYTQGLEGESLGCSGSSEAGSSGTLEL... | null | null | androgen receptor signaling pathway [GO:0030521]; intracellular receptor signaling pathway [GO:0030522]; male gonad development [GO:0008584]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of integrin biosynthetic process [GO:0045720]; positive regulation of cell populati... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | androgen binding [GO:0005497]; beta-catenin binding [GO:0008013]; DNA-binding transcription factor activity [GO:0003700]; estrogen response element binding [GO:0034056]; nuclear receptor activity [GO:0004879]; steroid binding [GO:0005496]; transcription cis-regulatory region binding [GO:0000976]; zinc ion binding [GO:0... | PF02166;PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | PTM: Phosphorylated in prostate cancer cells in response to several growth factors including EGF. Phosphorylation is induced by c-Src kinase (CSK). Tyr-499 is one of the major phosphorylation sites and an increase in phosphorylation and Src kinase activity is associated with prostate cancer progression (By similarity).... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10275}. Cytoplasm {ECO:0000250|UniProtKB:P10275}. Note=Detected at the promoter of target genes. Predominantly cytoplasmic in unligated form but translocates to the nucleus upon ligand-binding. Can also translocate to the nucleus in unligated form in the presence of... | null | null | null | null | null | FUNCTION: Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NC... | Eulemur fulvus collaris (Collared brown lemur) (Eulemur collaris) |
O97799 | KIT_CANLF | MRGARGAWDFLCVLLLLLLLGVQTGSSQPSVSPGEPSLPSIHPAKSELIVSVGDELRLSCTDPGFVKWTFETLGQLNENTHNEWITEKAEAGHTGNYTCTNRDGLSRSIYVFVRDPAKLFLVDLPLYGKEGNDTLVRCPLTDPEVTNYSLRGCEGKPLPKDLTFVADPKAGITIRNVKREYHRLCLHCSADQKGRTVLSKKFTLKVRAAIRAVPVVSVSKTSSLLKEGEAFSVMCFIKDVSSFVDSMWIKENSQQTNAQTQSNSWHHGDFNFERQEKLIISSARVNDSGVFMCYANNTFGSANVTTTLEVVDKGFINIFP... | 2.7.10.1 | null | actin cytoskeleton organization [GO:0030036]; B cell differentiation [GO:0030183]; cell chemotaxis [GO:0060326]; cytokine-mediated signaling pathway [GO:0019221]; detection of mechanical stimulus involved in sensory perception of sound [GO:0050910]; digestive tract development [GO:0048565]; ectopic germ cell programmed... | cell-cell junction [GO:0005911]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; fibrillar center [GO:0001650]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; metal ion binding [GO:0046872]; protease binding [GO:0002020]; protein homodimerization activity [GO:0042803]; SH2 domain binding [GO:0042169]; stem cell factor receptor activity [GO:0005020]; transmembrane receptor protein tyr... | PF00047;PF07714; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily | PTM: Ubiquitinated by SOCS6. KIT is rapidly ubiquitinated after autophosphorylation induced by KITLG/SCF binding, leading to internalization and degradation. {ECO:0000250}.; PTM: Autophosphorylated on tyrosine residues. KITLG/SCF binding promotes autophosphorylation. Phosphorylated tyrosine residues are important for i... | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for the cytokine KITLG/SCF and plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. In response to KIT... | Canis lupus familiaris (Dog) (Canis familiaris) |
O97817 | AGRL2_BOVIN | MVSSGCRMRSLWFIIIISFLPNTEGFSRAALPFGLVRRELSCEGYSIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENTDCYLPDAFKIMTQRCNNRTQCIVVTGSDVFPDPCPGTYKYLEVQYECVPYMEQKVFVCPGTLKAIVDSPCIYEAEQKAGAWCKDPLQAADKIYFMPWTPYRTDTLIEYASLEDFQNSRQTTTYKLPNRVDGTGFVVYDGAVFFNKERTRNIVKYDLRTRIKSGEAIINYANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEQNNGMIVISQLNPYTLRFEATWETVYDKRAASNAFM... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cell surface receptor signaling pathway [GO:0007166]; signal transduction [GO:0007165] | extracellular space [GO:0005615]; membrane [GO:0016020] | carbohydrate binding [GO:0030246]; G protein-coupled receptor activity [GO:0004930] | PF00002;PF16489;PF02140;PF01825;PF02793;PF02354;PF02191; | 1.25.40.610;2.60.120.740;2.60.220.50;4.10.1240.10;1.20.1070.10; | G-protein coupled receptor 2 family, Adhesion G-protein coupled receptor (ADGR) subfamily | PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. {ECO:0000250}. | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Calcium-independent receptor of low affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor probably implicated in the regulation of exocytosis. {ECO:0000250|UniProtKB:O88923}. | Bos taurus (Bovine) |
O97827 | AGRL3_BOVIN | MWPSQLLVFMMLLAPIIHGGKHSERHPALASPLRHAERGPGGALPPRHLLQQPAAERATAHRGPGPRGATRGVRGPGAHGAQISAQAFSRAPIPMAVVRRELSCESYPIELRCPGTDVIMIESANYGRTDDKICDSDPAQMENIRCYLPDAYKIMSQRCNNRTQCAVVAGPDVFPDPCPGTYKYLEVQYECVPYKVEQKVFLCPGLLKGVYQSEHLFESDHQSGAWCKDPLQASDKIYYMPWTPYRTDTLTEYSSKDDFIAGRPTTTYKLPHRVDGTGFVVYDGALFFNKERTRNIVKFDLRTRIKSGEAIIANANYHDT... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cell surface receptor signaling pathway [GO:0007166]; cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; neuron migration [GO:0001764]; signal transduction [GO:0007165]; synapse assembly [GO:0007416] | axon [GO:0030424]; cell-cell junction [GO:0005911]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; G protein-coupled receptor activity [GO:0004930] | PF00002;PF16489;PF02140;PF01825;PF02793;PF02354;PF02191; | 1.25.40.610;2.60.120.740;2.60.220.50;4.10.1240.10;1.20.1070.10; | G-protein coupled receptor 2 family, LN-TM7 subfamily | PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. {ECO:0000250}.; PTM: O-glycosylated (major) and N-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q80TS3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q80TS3}. Cell projection, axon {ECO:0000250|UniProtKB:Q80TS3}. Cell junction {ECO:0000250|UniProtKB:Q80TS3}. | null | null | null | null | null | FUNCTION: Plays a role in cell-cell adhesion and neuron guidance via its interactions with FLRT2 and FLRT3 that are expressed at the surface of adjacent cells. Plays a role in the development of glutamatergic synapses in the cortex. Important in determining the connectivity rates between the principal neurons in the co... | Bos taurus (Bovine) |
O97831 | AGRL1_BOVIN | MARLAAVLWSLCVTAILVTSATQGLSRAGLPFGLMRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTYKYLEVQYDCVPYKVKQKVFVCPGTLQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTLRFEGTWETGYDKRSASNAFM... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cell surface receptor signaling pathway [GO:0007166]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; positive reg... | axon [GO:0030424]; extracellular space [GO:0005615]; growth cone [GO:0030426]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; synapse [GO:0045202] | carbohydrate binding [GO:0030246]; cell adhesion molecule binding [GO:0050839]; G protein-coupled receptor activity [GO:0004930]; latrotoxin receptor activity [GO:0016524] | PF00002;PF16489;PF02140;PF01825;PF02793;PF02354;PF02191; | 1.25.40.610;2.60.120.740;2.60.220.50;4.10.1240.10;1.20.1070.10; | G-protein coupled receptor 2 family, Adhesion G-protein coupled receptor (ADGR) subfamily | PTM: Autoproteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. This proteolytic processing takes place early in the biosynthetic pathway, either in the endoplasmic reticulum or in the early compartment of the Golgi apparatus. {ECO:0000250|UniProtKB:O88917}. | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell projection, axon {ECO:0000250|UniProtKB:O88917}. Cell projection, growth cone {ECO:0000250|UniProtKB:O88917}. Synapse {ECO:0000250|UniProtKB:O88917}. Presynaptic cell membrane {ECO:0000250|UniProtKB:O88917}. Synapse, synaptosome {ECO:0000250|UniProt... | null | null | null | null | null | FUNCTION: Calcium-independent receptor of high affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor for TENM2 that mediates heterophilic synaptic cell-cell contact and postsynaptic specialization. Re... | Bos taurus (Bovine) |
O97859 | NEUR3_BOVIN | MEEVTSCSFSSPLFQQEDKRGVTYRIPALIYVPPAHTFLAFAEKRSSSKDEDALHLVLRRGLRTGQSVQWEPLKSLMKATLPGHRTMNPCPVWERKSGYVYLFFICVQGHVTERQQIMSGRNPARLCFICSQDAGYSWSDVRDLTEEVIGPEVTHWATFAVGPGHGIQLQSGRLIIPAYAYYIPFWFFCFRLPYRARPHSLMIYSDDLGATWHHGRLIKPMVTVECEVAEVIGKAGHPVLYCSARTPNRHRAEALSIDHGECFQKPVLSHQLCEPPHGCQGSVVSFCPLEIPGGCQDLAGEDAPAIQQSPLLCSSVRPEP... | 3.2.1.18 | null | ganglioside catabolic process [GO:0006689]; oligosaccharide catabolic process [GO:0009313] | caveola [GO:0005901]; cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038] | exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; exo-alpha-sialidase activity [GO:0004308] | PF13088; | 2.120.10.10; | Glycosyl hydrolase 33 family | PTM: Palmitoylated; may regulate intracellular trafficking and anchorage to plasma membrane and endomembranes. {ECO:0000250|UniProtKB:Q9UQ49}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9988745}; Peripheral membrane protein {ECO:0000269|PubMed:9988745}. Membrane, caveola {ECO:0000250|UniProtKB:Q9UQ49}. Early endosome membrane {ECO:0000250|UniProtKB:Q9UQ49}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UQ49}. Recycling endosome membrane {E... | CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; Evidence={ECO:0000269|PubMed:9988745}; CATALYTIC ACTIVITY: Reaction=a gangli... | null | null | null | null | FUNCTION: Exo-alpha-sialidase that catalyzes the hydrolytic cleavage of the terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) of a glycan moiety in the catabolism of glycolipids, glycoproteins and oligosacharides. Displays high catalytic efficiency for gangliosides including alpha-(2->3)-sialylated GD1a and GM3 an... | Bos taurus (Bovine) |
O97921 | PTGDS_HORSE | MAASHTLWMGLVLLGVLGVLQTRAQAQPSLQPNFQQDKFLGRWFTSGLASNSSWFREKKKVLSMCTSVVAPTADGGFNLTSTFLRKDQCETRTLLLQPAGPPGCYSYTSPHWGMVHEVSVVETDYEEYALLYTHAESTKGLGGQDFRMATLYSRVQSPRPEVKEKFSTFAKAQGFTEDAIVFLPQTDKCMEEHN | 5.3.99.2 | null | gene expression [GO:0010467]; mast cell degranulation [GO:0043303]; negative regulation of male germ cell proliferation [GO:2000255]; prostaglandin biosynthetic process [GO:0001516]; regulation of circadian sleep/wake cycle, sleep [GO:0045187] | extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; nuclear membrane [GO:0031965]; perinuclear region of cytoplasm [GO:0048471]; rough endoplasmic reticulum [GO:0005791] | fatty acid binding [GO:0005504]; prostaglandin-D synthase activity [GO:0004667]; retinoid binding [GO:0005501] | PF00061; | 2.40.128.20; | Calycin superfamily, Lipocalin family | null | SUBCELLULAR LOCATION: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic ret... | CATALYTIC ACTIVITY: Reaction=prostaglandin H2 = prostaglandin D2; Xref=Rhea:RHEA:10600, ChEBI:CHEBI:57405, ChEBI:CHEBI:57406; EC=5.3.99.2; Evidence={ECO:0000250|UniProtKB:P41222}; | null | null | null | null | FUNCTION: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. B... | Equus caballus (Horse) |
O97939 | ENAM_PIG | MLLSCRHGASSPKLDNLVPSGKMKILLVFLGLLCYSAAMPMQMPRMPGFSSKSEEMMRYGHFNFMNAPHMAHLGTLYGNGMQLPQFFPQYQMPMWPQPPPNKKHPQKPSASKQQSKTDPAPESQKPNQPQPKTPTPKQPLNEPSPTPTQPEEETQTPQAFPPFGNGLFPYQQPLWHVPHRIPPGYGRPPTSNEEGGNPYFGFFGYHGFGGRPPYYSEEMFEQDFEKPKEKDPPKTETPATEPSVNTTVPETNSTQPNAPNPRGNDTSPTGTSGQGPNPRSNPTGQNGPAVNVSGQGVPRSQSPWGPRQTIIHENYPNPNI... | null | null | ameloblast differentiation [GO:0036305]; amelogenesis [GO:0097186]; biomineral tissue development [GO:0031214]; positive regulation of enamel mineralization [GO:0070175] | extracellular matrix [GO:0031012]; extracellular region [GO:0005576] | structural constituent of tooth enamel [GO:0030345] | PF15362; | null | null | PTM: Proteolytically cleaved into several smaller polypeptides. Cleavage of N-terminal region of enamelin occurs soon after secretion. {ECO:0000269|PubMed:9206327}.; PTM: Phosphorylated by FAM20C in vitro. {ECO:0000250|UniProtKB:Q9NRM1}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:9206327}. | null | null | null | null | null | FUNCTION: Involved in the mineralization and structural organization of enamel. Involved in the extension of enamel during the secretory stage of dental enamel formation. {ECO:0000269|PubMed:9206327}. | Sus scrofa (Pig) |
O97952 | ANDR_MACFA | MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLQQQQQQQQETSPRQQQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSAPECHPERGCVPEPGAAVAAGKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSTDLKDILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLGGTSTISDSAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYAPVLGVPPAVRPTPCAPLAECKGSLLDDSAGKSTEDTAEYSPFKGGYTKGLEGESLGCSGSAAAGSSG... | null | null | androgen receptor signaling pathway [GO:0030521]; intracellular receptor signaling pathway [GO:0030522]; male gonad development [GO:0008584]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of integrin biosynthetic process [GO:0045720]; positive regulation of cell populati... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | androgen binding [GO:0005497]; beta-catenin binding [GO:0008013]; DNA-binding transcription factor activity [GO:0003700]; estrogen response element binding [GO:0034056]; nuclear receptor activity [GO:0004879]; steroid binding [GO:0005496]; transcription cis-regulatory region binding [GO:0000976]; zinc ion binding [GO:0... | PF02166;PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | PTM: Phosphorylated in prostate cancer cells in response to several growth factors including EGF. Phosphorylation is induced by c-Src kinase (CSK). Tyr-510 is one of the major phosphorylation sites and an increase in phosphorylation and Src kinase activity is associated with prostate cancer progression (By similarity).... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10275}. Cytoplasm {ECO:0000250|UniProtKB:P10275}. Note=Detected at the promoter of target genes. Predominantly cytoplasmic in unligated form but translocates to the nucleus upon ligand-binding. Can also translocate to the nucleus in unligated form in the presence of... | null | null | null | null | null | FUNCTION: Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NC... | Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) |
O97960 | ANDR_PAPHA | MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLQQQQQQQQQETSPRQQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSAPECHPERGCVPEPGAAVAAGKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSADLKDILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLGGTSTISDSAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYAPVLGVPPAVRPTPCAPLAECKGSLLDDSAGKSTEDTAEYSPFKGGYTKGLEGESLGCSGSAAAGSSG... | null | null | androgen receptor signaling pathway [GO:0030521]; intracellular receptor signaling pathway [GO:0030522]; male gonad development [GO:0008584]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of integrin biosynthetic process [GO:0045720]; positive regulation of cell populati... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | androgen binding [GO:0005497]; beta-catenin binding [GO:0008013]; DNA-binding transcription factor activity [GO:0003700]; estrogen response element binding [GO:0034056]; nuclear receptor activity [GO:0004879]; steroid binding [GO:0005496]; transcription cis-regulatory region binding [GO:0000976]; zinc ion binding [GO:0... | PF02166;PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | PTM: Phosphorylated in prostate cancer cells in response to several growth factors including EGF. Phosphorylation is induced by c-Src kinase (CSK). Tyr-510 is one of the major phosphorylation sites and an increase in phosphorylation and Src kinase activity is associated with prostate cancer progression (By similarity).... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10275}. Cytoplasm {ECO:0000250|UniProtKB:P10275}. Note=Detected at the promoter of target genes. Predominantly cytoplasmic in unligated form but translocates to the nucleus upon ligand-binding. Can also translocate to the nucleus in unligated form in the presence of... | null | null | null | null | null | FUNCTION: Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NC... | Papio hamadryas (Hamadryas baboon) |
O97980 | HMHB1_HUMAN | MEEQPECREEKRGSLHVWKSELVEVEDDVYLRHSSSLTYRL | null | null | adaptive immune response [GO:0002250]; cellular response to tumor necrosis factor [GO:0071356]; positive regulation of type II interferon production [GO:0032729]; regulation of gene expression [GO:0010468] | null | null | null | null | null | null | null | null | null | null | null | null | FUNCTION: Precursor of the histocomplatibility antigen HB-1. More generally, minor histocomplatibility antigens (mHags) refer to immunogenic peptide which, when complexed with MHC, can generate an immune response after recognition by specific T-cells. The peptides are derived from polymorphic intracellular proteins, wh... | Homo sapiens (Human) |
P00002 | CYC_MACMU | MGDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGITWGEDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE | null | null | apoptotic process [GO:0006915]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122] | cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; respirasome [GO:0070469] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00034; | 1.10.760.10; | Cytochrome c family | PTM: Binds 1 heme c group covalently per subunit.; PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration. {ECO:0000250}. | SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane. | null | null | null | null | null | FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-trans... | Macaca mulatta (Rhesus macaque) |
P00004 | CYC_HORSE | MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE | null | null | apoptotic process [GO:0006915]; cytochrome c-heme linkage [GO:0018063]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cysteine-type endopeptida... | cytochrome complex [GO:0070069]; cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; respirasome [GO:0070469] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; metal ion binding [GO:0046872] | PF00034; | 1.10.760.10; | Cytochrome c family | PTM: Binds 1 heme c group covalently per subunit.; PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration. {ECO:0000250}. | SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane. | null | null | null | null | null | FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-trans... | Equus caballus (Horse) |
P00007 | CYC_HIPAM | MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQSPGFSYTDANKNKGITWGEETLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKQATNE | null | null | apoptotic process [GO:0006915]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122] | cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; respirasome [GO:0070469] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00034; | 1.10.760.10; | Cytochrome c family | PTM: Binds 1 heme c group covalently per subunit.; PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration. {ECO:0000250}. | SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane. | null | null | null | null | null | FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-trans... | Hippopotamus amphibius (Hippopotamus) |
P00008 | CYC_RABIT | MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAVGFSYTDANKNKGITWGEDTLMEYLENPKKYIPGTKMIFAGIKKKDERADLIAYLKKATNE | null | null | apoptotic process [GO:0006915]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122] | cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; respirasome [GO:0070469] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00034; | 1.10.760.10; | Cytochrome c family | PTM: Binds 1 heme c group covalently per subunit.; PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration. {ECO:0000250}. | SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane. | null | null | null | null | null | FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-trans... | Oryctolagus cuniculus (Rabbit) |
P00011 | CYC_CANLF | MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWGEETLMEYLENPKKYIPGTKMIFAGIKKTGERADLIAYLKKATKE | null | null | apoptotic process [GO:0006915]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122] | cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; respirasome [GO:0070469] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00034; | 1.10.760.10; | Cytochrome c family | PTM: Binds 1 heme c group covalently per subunit.; PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration. {ECO:0000250}. | SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane. | null | null | null | null | null | FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-trans... | Canis lupus familiaris (Dog) (Canis familiaris) |
P00012 | CYC_MIRLE | MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWGEETLMEYLENPKKYIPGTKMIFAGIKKTGERADLIAYLKIATKE | null | null | apoptotic process [GO:0006915]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122] | cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; respirasome [GO:0070469] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00034; | 1.10.760.10; | Cytochrome c family | PTM: Binds 1 heme c group covalently per subunit.; PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration. {ECO:0000250}. | SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane. | null | null | null | null | null | FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-trans... | Mirounga leonina (Southern elephant seal) (Phoca leonina) |
P00014 | CYC_MACGI | MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLNGIFGRKTGQAPGFTYTDANKNKGIIWGEDTLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE | null | null | apoptotic process [GO:0006915]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122] | cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; respirasome [GO:0070469] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00034; | 1.10.760.10; | Cytochrome c family | PTM: Binds 1 heme c group covalently per subunit.; PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration. {ECO:0000250}. | SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane. | null | null | null | null | null | FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-trans... | Macropus giganteus (Eastern gray kangaroo) |
P00015 | CYC2_MOUSE | MGDAEAGKKIFVQKCAQCHTVEKGGKHKTGPNLWGLFGRKTGQAPGFSYTDANKNKGVIWSEETLMEYLENPKKYIPGTKMIFAGIKKKSEREDLIKYLKQATSS | null | null | apoptotic process [GO:0006915]; hydrogen peroxide metabolic process [GO:0042743]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244] | mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; respirasome [GO:0070469] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00034; | 1.10.760.10; | Cytochrome c family | PTM: Binds 1 heme c group covalently per subunit.; PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration. {ECO:0000250}. | SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane. | null | null | null | null | null | FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-trans... | Mus musculus (Mouse) |
P00044 | CYC1_YEAST | MTEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKKNVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE | null | COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000269|PubMed:18390544}; Note=Binds 1 heme c group covalently per subunit. {ECO:0000269|PubMed:18390544}; | mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122] | mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; respirasome [GO:0070469] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00034; | 1.10.760.10; | Cytochrome c family | PTM: Methylation may enhance its transport into mitochondria. Methylation occurs in fungi, plants, and some protozoa, but not in animals. The precise role of methylation at Lys-79 is unknown, but it seems to preclude pro-apoptotic activity, possibly by lowering affinity for APAF1. {ECO:0000269|PubMed:10791961, ECO:0000... | SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:9866716}. | null | null | null | null | null | FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of ubiquinol-cytochrome c oxidoreductase. Cytochrome c then transfers this electron to the dinuclear copper A center (CU(A)) of the COX2 subunit of cytochrome oxid... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P00045 | CYC7_YEAST | MAKESTGFKPGSAKKGATLFKTRCQQCHTIEEGGPNKVGPNLHGIFGRHSGQVKGYSYTDANINKNVKWDEDSMSEYLTNPKKYIPGTKMAFAGLKKEKDRNDLITYMTKAAK | null | COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000269|PubMed:18390544}; Note=Binds 1 heme c group covalently per subunit. {ECO:0000269|PubMed:18390544}; | mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122] | mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; respirasome [GO:0070469] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00034; | 1.10.760.10; | Cytochrome c family | null | SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:8636074}. | null | null | null | null | null | FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of ubiquinol-cytochrome c oxidoreductase. Cytochrome c then transfers this electron to the dinuclear copper A center (CU(A)) of the COX2 subunit of cytochrome oxid... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P00125 | CY1_BOVIN | MAAAAATLRGAMVGPRGAGLPGARARGLLCGARPGQLPLRTPQAVSLSSKSGLSRGRKVILSALGMLAAGGAGLAVALHSAVSASDLELHPPSYPWSHRGLLSSLDHTSIRRGFQVYKQVCSSCHSMDYVAYRHLVGVCYTEDEAKALAEEVEVQDGPNEDGEMFMRPGKLSDYFPKPYPNPEAARAANNGALPPDLSYIVRARHGGEDYVFSLLTGYCEPPTGVSLREGLYFNPYFPGQAIGMAPPIYNEVLEFDDGTPATMSQVAKDVCTFLRWAAEPEHDHRKRMGLKMLLMMGLLLPLVYAMKRHKWSVLKSRKLA... | 7.1.1.8 | COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000269|PubMed:9651245}; Note=Binds 1 heme c group covalently per subunit. {ECO:0000269|PubMed:9651245}; | mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122] | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; ubiquinol-cytochrome-c reductase activity [GO:0008121] | PF02167; | 1.10.760.10;1.20.5.100; | Cytochrome c family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P07143}; Single-pass membrane protein {ECO:0000250|UniProtKB:P07143}. | CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000... | null | null | null | null | FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... | Bos taurus (Bovine) |
P00127 | QCR6_YEAST | MGMLELVGEYWEQLKITVVPVVAAAEDDDNEQHEEKAAEGEEKEEENGDEDEDEDEDEDDDDDDDEDEEEEEEVTDQLEDLREHFKNTEEGKALVHHYEECAERVKIQQQQPGYADLEHKEDCVEEFFHLQHYLDTATAPRLFDKLK | null | null | aerobic respiration [GO:0009060]; cellular respiration [GO:0045333]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; proton transmembrane transport [GO:1902600] | mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739]; nuclear periphery [GO:0034399] | null | PF02320; | 1.10.287.20; | UQCRH/QCR6 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:30598554}; Peripheral membrane protein {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Intermembrane side {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}. | null | null | null | null | null | FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P00128 | QCR7_YEAST | MPQSFTSIARIGDYILKSPVLSKLCVPVANQFINLAGYKKLGLKFDDLIAEENPIMQTALRRLPEDESYARAYRIIRAHQTELTHHLLPRNEWIKAQEDVPYLLPYILEAEAAAKEKDELDNIEVSK | null | null | aerobic respiration [GO:0009060]; cellular respiration [GO:0045333]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; mitochondrial respiratory chain complex III assembly [GO:0034551]; proton transmembrane transport [GO:1902600] | matrix side of mitochondrial inner membrane [GO:0099617]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739] | null | PF02271; | 1.10.1090.10; | UQCRB/QCR7 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Peripheral membrane protein {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Matrix side {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}. | null | null | null | null | null | FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P00156 | CYB_HUMAN | MTPMRKTNPLMKLINHSFIDLPTPSNISAWWNFGSLLGACLILQITTGLFLAMHYSPDASTAFSSIAHITRDVNYGWIIRYLHANGASMFFICLFLHIGRGLYYGSFLYSETWNIGIILLLATMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVQWIWGGYSVDSPTLTRFFTFHFILPFIIAALATLHLLFLHETGSNNPLGITSHSDKITFHPYYTIKDALGLLLFLLSLMTLTLFSPDLLGDPDNYTLANPLNTPPHIKPEWYFLFAYTILRSVPNKLGGVLALLLSILILAMIPILHMSKQQSMMFRPL... | null | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P00157}; Note=Binds 2 heme b groups non-covalently. {ECO:0000250|UniProtKB:P00157}; | animal organ regeneration [GO:0031100]; cellular respiration [GO:0045333]; electron transport coupled proton transport [GO:0015990]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; response to cadmium ion [GO:0046686]; response to calcium ion [GO:0051592]; response to cobalamin [GO:0033590]; r... | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739] | metal ion binding [GO:0046872]; protein-containing complex binding [GO:0044877]; ubiquinol-cytochrome-c reductase activity [GO:0008121] | PF00032;PF00033; | null | Cytochrome b family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00157}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00157}. | null | null | null | null | null | FUNCTION: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membra... | Homo sapiens (Human) |
P00157 | CYB_BOVIN | MTNIRKSHPLMKIVNNAFIDLPAPSNISSWWNFGSLLGICLILQILTGLFLAMHYTSDTTTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLYMHVGRGLYYGSYTFLETWNIGVILLLTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFAFHFILPFIIMAIAMVHLLFLHETGSNNPTGISSDVDKIPFHPYYTIKDILGALLLILALMLLVLFAPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAFSILILALIPLLHTSKQRSMMFRPL... | null | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:12269811, ECO:0000269|PubMed:15312779, ECO:0000269|PubMed:16024040, ECO:0000269|PubMed:16924113, ECO:0000269|PubMed:9204897, ECO:0000269|PubMed:9651245}; Note=Binds 2 heme b groups non-covalently. {ECO:0000269|PubMed:12269811, ECO:0000269|PubMe... | mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; respiratory electron transport chain [GO:0022904] | membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex III [GO:0005750] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; ubiquinol-cytochrome-c reductase activity [GO:0008121]; ubiquinone binding [GO:0048039] | PF00032;PF00033; | null | Cytochrome b family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:1225597, ECO:0000305|PubMed:1327781, ECO:0000305|PubMed:189810}; Multi-pass membrane protein {ECO:0000269|PubMed:12269811, ECO:0000269|PubMed:15312779, ECO:0000269|PubMed:16024040, ECO:0000269|PubMed:16924113, ECO:0000269|PubMed:9204897, ECO:0000269... | null | null | null | null | null | FUNCTION: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membra... | Bos taurus (Bovine) |
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