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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P16882 | GHR_MOUSE | MDLCQVFLTLALAVTSSTFSGSEATPATLGKASPVLQRINPSLGTSSSGKPRFTKCRSPELETFSCYWTEGDNPDLKTPGSIQLYYAKRESQRQAARIAHEWTQEWKECPDYVSAGKNSCYFNSSYTSIWIPYCIKLTTNGDLLDQKCFTVDEIVQPDPPIGLNWTLLNISLTGIRGDIQVSWQPPPNADVLKGWIILEYEIQYKEVNESKWKVMGPIWLTYCPVYSLRMDKEHEVRVRSRQRSFEKYSEFSEVLRVIFPQTNILEACEEDIQFPWFLIIIFGIFGVAVMLFVVIFSKQQRIKMLILPPVPVPKIKGIDP... | null | null | cytokine-mediated signaling pathway [GO:0019221]; endocytosis [GO:0006897]; growth hormone receptor signaling pathway [GO:0060396]; hormone-mediated signaling pathway [GO:0009755]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0... | cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; growth hormone receptor complex [GO:0070195]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; growth hormone receptor activity [GO:0004903]; peptide hormone binding [GO:0017046]; protein kinase binding [GO:0019901]; protein phosphatase binding [GO:0019903]; SH2 domain binding [GO:0042169] | PF09067;PF12772; | 2.60.40.10; | Type I cytokine receptor family, Type 1 subfamily | PTM: On GH binding, phosphorylated on tyrosine residues in the cytoplasmic domain by JAK2. {ECO:0000250}.; PTM: On ligand binding, ubiquitinated on lysine residues in the cytoplasmic domain. This ubiquitination is not sufficient for GHR internalization (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Note=On growth hormone binding, GHR is ubiquitinated, internalized, down-regulated and transported into a degradative or non-degradative pathway. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.; SUBCELLULAR LOCATION: [Growth hormone-... | null | null | null | null | null | FUNCTION: Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. On ligand binding, couples to, and activates the JAK2/STAT5 pathway (By similarity). {ECO:0000250}.; FUNCTION: The soluble form (GHBP) acts as a reservoir of growth hormone in plasma and may be a modulator/inhibitor of G... | Mus musculus (Mouse) |
P16884 | NFH_RAT | MMSFGSADALLGAPFAPLHGGGSLHYALSRKAGAGGTRSAAGSSSGFHSWARTSVSSVSASPSRFRGAASSTDSLDTLSNGPEGCVAAVAARSEKEQLQALNDRFAGYIDKVRQLEAHNRTLEGEAAALRQQKGRAAMGELYEREVREMRGAVLRLGAARGHVRLEQEHLLEDIAHVRQRLDEEARQREEAEAAARALARFAQEAEAARVELQKKAQALQEECGYLRRHHQEEVGELLGQIQGCGAAQAQAQAEARDALKCDVTSALREIRAQLEGHTVQSTLQSEEWFRVRLDRLSEAAKVNTDAMRSAQEEITEYRRQ... | null | null | axon development [GO:0061564]; axon regeneration [GO:0031103]; cellular response to estradiol stimulus [GO:0071392]; cellular response to hydroperoxide [GO:0071447]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to oxidative stress [GO:0034599]; cerebral cortex development [GO:0021987]... | apical dendrite [GO:0097440]; axon [GO:0030424]; basal proximal dendrite [GO:0150017]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; intermediate filament [GO:0005882]; neurofibrillary tangle [GO:0097418]; neurofilament [GO:0005883]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; postsynaptic density [G... | protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877]; protein-macromolecule adaptor activity [GO:0030674]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of postsynaptic intermediate filament cytoskeleton [GO:0099184]; toxic substance binding [GO:0015643] | PF07142;PF00038; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: There are a number of repeats of the tripeptide K-S-P, NFH is phosphorylated on a number of the serines in this motif. It is thought that phosphorylation of NFH results in the formation of interfilament cross bridges that are important in the maintenance of axonal caliber.; PTM: Phosphorylation seems to play a maj... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P19246}. Cell projection, axon {ECO:0000250|UniProtKB:P19246}. | null | null | null | null | null | FUNCTION: Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. NEFH has an important function in mature axons that is not subserved by the two smaller NEF proteins. May additionally cooperate with the neuronal intermediate f... | Rattus norvegicus (Rat) |
P16885 | PLCG2_HUMAN | MSTTVNVDSLAEYEKSQIKRALELGTVMTVFSFRKSTPERRTVQVIMETRQVAWSKTADKIEGFLDIMEIKEIRPGKNSKDFERAKAVRQKEDCCFTILYGTQFVLSTLSLAADSKEDAVNWLSGLKILHQEAMNASTPTIIESWLRKQIYSVDQTRRNSISLRELKTILPLINFKVSSAKFLKDKFVEIGAHKDELSFEQFHLFYKKLMFEQQKSILDEFKKDSSVFILGNTDRPDASAVYLHDFQRFLIHEQQEHWAQDLNKVRERMTKFIDDTMRETAEPFLFVDEFLTYLFSRENSIWDEKYDAVDMQDMNNPLSH... | 3.1.4.11 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; | antifungal innate immune response [GO:0061760]; B cell differentiation [GO:0030183]; B cell receptor signaling pathway [GO:0050853]; calcium-mediated signaling [GO:0019722]; cell activation [GO:0001775]; cellular response to calcium ion [GO:0071277]; cellular response to lectin [GO:1990858]; cellular response to lipid ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular vesicle [GO:0097708]; membrane raft [GO:0045121]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587] | phosphatidylinositol phospholipase C activity [GO:0004435]; phospholipase C activity [GO:0004629]; phosphorylation-dependent protein binding [GO:0140031]; phosphotyrosine residue binding [GO:0001784]; protein kinase binding [GO:0019901]; protein tyrosine kinase binding [GO:1990782]; scaffold protein binding [GO:0097110... | PF00168;PF16457;PF00388;PF00387;PF00017;PF00018; | 2.60.40.150;3.20.20.190;2.30.29.30;3.30.505.10;2.30.30.40; | null | PTM: Phosphorylated on tyrosine residues by CSF1R (By similarity). Phosphorylated on tyrosine residues by BTK and SYK; upon ligand-induced activation of a variety of growth factor receptors and immune system receptors. Phosphorylation leads to increased phospholipase activity. {ECO:0000250|UniProtKB:Q8CIH5, ECO:0000269... | SUBCELLULAR LOCATION: Membrane raft {ECO:0000250|UniProtKB:Q8CIH5}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11; Evidence={EC... | null | null | null | null | FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling. {ECO:0000269|PubMed:23000145}. | Homo sapiens (Human) |
P16892 | FUS3_YEAST | MPKRIVYNISSDFQLKSLLGEGAYGVVCSATHKPTGEIVAIKKIEPFDKPLFALRTLREIKILKHFKHENIITIFNIQRPDSFENFNEVYIIQELMQTDLHRVISTQMLSDDHIQYFIYQTLRAVKVLHGSNVIHRDLKPSNLLINSNCDLKVCDFGLARIIDESAADNSEPTGQQSGMTEYVATRWYRAPEVMLTSAKYSRAMDVWSCGCILAELFLRRPIFPGRDYRHQLLLIFGIIGTPHSDNDLRCIESPRAREYIKSLPMYPAAPLEKMFPRVNPKGIDLLQRMLVFDPAKRITAKEALEHPYLQTYHDPNDEPE... | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | cell cycle [GO:0007049]; cell division [GO:0051301]; intracellular signal transduction [GO:0035556]; invasive growth in response to glucose limitation [GO:0001403]; negative regulation of MAPK cascade [GO:0043409]; pheromone response MAPK cascade [GO:0071507]; pheromone-dependent signal transduction involved in conjuga... | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; mating projection tip [GO:0043332]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; periplasmic space [GO:0042597] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; MAP kinase activity [GO:0004707]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Dually phosphorylated on Thr-180 and Tyr-182 by STE7 in response to pheromone induction, which activates the enzyme. Activated FUS3 initiates a feedback signal, down-regulating phosphorylation of both, FUS3 and KSS1. {ECO:0000269|PubMed:1628831}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11781566}. Cytoplasm {ECO:0000269|PubMed:11781566}. Periplasm {ECO:0000269|PubMed:11781566}. Note=FUS3 shuttles rapidly between the cytoplasm and the nucleus independent of pheromone treatment or FUS3 phosphorylation level. Activated FUS3 translocates rapidly to the nuc... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Together with closely related KSS1, FUS3 is the final kinase in the signal transduction cascade regulating activation/repression of the mating and filamentation pathways, induced by pheromone and nitrogen/carbon limitation, respectively. Phosphorylated FUS3 activates the mating but suppresses the filamentatio... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P16894 | GPA1_DICDI | MGNICGKPELGSPEEIKANQHINSLLKQARSKLEGEIKLLLLGAGESGKSTIAKQMKIIHLNGFNDEEKSSYKTIIYNNTVGSMRVLVNAAEELKIGISENNKEAASRISNDLGDHFNGVLTAELAQDIKALWADPGIQNTFQRSSEFQLNDSAAYYFDSIDRISQPLYLPSENDVLRSRTKTTGIIETVFEIQNSTFRMVDVGGQRSERKKWMHCFQEVTAVIFCVALSEYDLKLYEDDTTNRMQESLKLFKEICNTKWFANTAMILFLNKRDIFSEKITKTPITVCFKEYDGPQTYEGCSEFIKQQFINQNENPKKSI... | null | null | adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway [GO:0140582]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; cell differentiation [GO:0030154]; chemotaxis to cAMP [GO:0043327]; signal transduction [GO:0007165]; small GTPase-mediated signal transduc... | cytoplasm [GO:0005737]; heterotrimeric G-protein complex [GO:0005834] | G protein activity [GO:0003925]; G protein-coupled receptor binding [GO:0001664]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872] | PF00503; | 1.10.400.10;3.40.50.300; | G-alpha family | null | null | null | null | null | null | null | FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. | Dictyostelium discoideum (Social amoeba) |
P16901 | POL_OMVVS | SNITAGKQQEGATCGAVRAPYVVTEAPPKIDIKVGTNWKKVLVDTGADRTIVRYHDNSGIPTGRIKLQGIGGIIEGEKWDKVVIQYKEKRIEGTIVVLPSSPVEVLGRDNMAKLDIGIIMANLEEKKIPITQVKLKEGCKGPHIAQWPLTQEKLEGLKEIVDKLEKEGKVGRAPPHWTCNTPIFCIKKKSGKWRMLIDFRELNKQTEDLAEAQLGLPHPGGLQKKKHVTILDIGDAYFTIPLYEPYRPYTCFTMLSPNNLGPCTRYYWKVLPQGWKLSPSVYQFTMQEILRDWIAKHPMIQFGIYMDDIYIGSDLDIMKH... | 2.7.7.-; 2.7.7.49; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.-; 3.6.1.23 | null | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; nucleotide metabolic process [GO:0009117]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; viral genome integration into host DNA [GO:0044826] | null | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; dUTP diphosphatase activity [GO:0004170]; exoribonuclease H activity [GO:0004533]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; zinc ion binding [GO:0008270] | PF00692;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815; | 1.10.10.200;2.70.40.10;3.30.70.270;2.40.70.10;3.10.10.10;2.30.30.10;3.30.420.10; | Retroviral Pol polyprotein family | PTM: Cleavage sites that yield the mature proteins remain to be determined. | null | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end... | null | null | null | null | FUNCTION: During replicative cycle of retroviruses, the reverse-transcribed viral DNA is integrated into the host chromosome by the viral integrase enzyme. RNase H activity is associated with the reverse transcriptase. | Ovine maedi visna related virus (strain South Africa) (SA-OMVV) (Ovine lentivirus) |
P16905 | KAPR1_DROME | MSYMMAKTLEEQSLRECEHYIQTHGIQRVLKDCIVQLCVCRPENPVQFLRQYFQKLEREQVKLDASRQVISPDDCEDLSPMPQTAAPPVRRRGGISAEPVTEEDATNYVKKVVPKDYKTMNALSKAIAKNVLFAHLDESERSDIFDAMFPVNHIAGENIIQQGDEGDNFYVIDVGEVDVFVNSELVTTISEGGSFGELALIYGTPRAATVRAKTDVKLWGIDRDSYRRILMGSTIRKRKMYEEFLSRVSILESLDKWERLTVADSLETCSFDDGETIVKQGAAGDDFYIILEGCAVVLQQRSEGEDPAEVGRLGSSDYFG... | null | null | actin filament organization [GO:0007015]; cAMP-mediated signaling [GO:0019933]; molting cycle, chitin-based cuticle [GO:0007591]; negative regulation of smoothened signaling pathway [GO:0045879]; neuromuscular synaptic transmission [GO:0007274]; olfactory learning [GO:0008355]; oocyte microtubule cytoskeleton polarizat... | cAMP-dependent protein kinase complex [GO:0005952]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; synapse [GO:0045202] | cAMP binding [GO:0030552]; cAMP-dependent protein kinase inhibitor activity [GO:0004862]; cAMP-dependent protein kinase regulator activity [GO:0008603]; protein kinase A catalytic subunit binding [GO:0034236] | PF00027;PF02197; | 1.20.890.10;2.60.120.10; | CAMP-dependent kinase regulatory chain family | PTM: The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain but is not phosphorylated. The physiological significance of phosphorylations by other kinases is unclear. | null | null | null | null | null | null | null | Drosophila melanogaster (Fruit fly) |
P16912 | KAPC3_DROME | MDLWHIFLERILVACRVSASVFANFGCGLYSSWKLICGDHDSASGLRAGLATPTQRGKATGDNGTTGTPARTIGKPQARIATAMSTATCARFCTPLSSGTAGSTSKLTTGNGSGNTMTSAYKIPSNNSTTANDSSNTETTFTFKLGRSNGRSSSNVASSESSDPLESDYSEEDPEQEQQRPDPATNSRSSSTATTTTTSSADHDNDVDEEDEEDDENEGEGNGRDADDATHDSSESIEEDDGNETDDEEDDDESEESSSVQTAKGVRKYHLDDYQIIKTVGTGTFGRVCLCRDRISEKYCAMKILAMTEVIRLKQIEHVK... | 2.7.11.1 | null | imaginal disc-derived wing morphogenesis [GO:0007476]; protein phosphorylation [GO:0006468]; signal transduction [GO:0007165] | cAMP-dependent protein kinase complex [GO:0005952]; cytosol [GO:0005829] | ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, cAMP subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Does not have an essential role in development. {ECO:0000269|PubMed:8601490}. | Drosophila melanogaster (Fruit fly) |
P16913 | PG187_VACCW | MNFQGLVLTDNCKNQWVVGPLIGKGGFGSIYTTNDNNYVVKIEPKANGSLFTEQAFYTRVLKPSVIEEWKKSHNIKHVGLITCKAFGLYKSINVEYRFLVINRLGADLDAVIRANNNRLPKRSVMLIGIEILNTIQFMHEQGYSHGDIKASNIVLDQIDKNKLYLVDYGLVSKFMSNGEHVPFIRNPNKMDNGTLEFTPIDSHKGYVVSRRGDLETLGYCMIRWLGGILPWTKISETKNCALVSATKQKYVNNTATLLMTSLQYAPRELLQYITMVNSLTYFEEPNYDEFRHILMQGVYY | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:1602551}; | phosphorylation [GO:0016310]; signal transduction [GO:0007165]; virion assembly [GO:0019068] | cytoplasm [GO:0005737]; host cell cytoplasm [GO:0030430]; virion component [GO:0044423] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, Poxviruses subfamily | PTM: Autophosphorylated. | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:1448924}. Host cytoplasm {ECO:0000269|PubMed:1448924}. Note=Localizes in cytoplasmic viral factories and is a minor component of the virion. {ECO:0000269|PubMed:1448924}. | 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:1602551}; CATALYTIC ... | null | null | null | null | FUNCTION: Essential serine/threonine-protein kinase that plays different role in the viral life cycle (PubMed:1560522, PubMed:1602551). Phosphorylates the host small ribosomal protein RACK1 thereby customizing the ribosomes to a state optimal for viral mRNAs (which contain poly-A leaders) but not for host mRNAs (PubMed... | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) |
P16914 | ELAV_DROME | MDFIMANTGAGGGVDTQAQLMQSAAAAAAVAATNAAAAPVQNAAAVAAAAQLQQQQVQQAILQVQQQQTQQAVAAAAAAVTQQLQQQQQAVVAQQAVVQQQQQQAAAVVQQAAVQQAVVPQPQQAQPNTNGNAGSGSQNGSNGSTETRTNLIVNYLPQTMTEDEIRSLFSSVGEIESVKLIRDKSQVYIDPLNPQAPSKGQSLGYGFVNYVRPQDAEQAVNVLNGLRLQNKTIKVSFARPSSDAIKGANLYVSGLPKTMTQQELEAIFAPFGAIITSRILQNAGNDTQTKGVGFIRFDKREEATRAIIALNGTTPSSCTD... | null | null | central nervous system development [GO:0007417]; embryo development ending in birth or egg hatching [GO:0009792]; germ cell development [GO:0007281]; negative regulation of mRNA 3'-end processing [GO:0031441]; negative regulation of oskar mRNA translation [GO:0007319]; nervous system development [GO:0007399] | Cajal body [GO:0015030]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904] | mRNA binding [GO:0003729]; mRNA regulatory element binding translation repressor activity [GO:0000900]; poly(U) RNA binding [GO:0008266]; RNA binding [GO:0003723] | PF00076; | 3.30.70.330; | RRM elav family | null | null | null | null | null | null | null | FUNCTION: Required for the proper development and maintenance of neurons presumably by affecting RNA metabolism. {ECO:0000269|PubMed:3144044}. | Drosophila melanogaster (Fruit fly) |
P16926 | MREC_ECOLI | MKPIFSRGPSLQIRLILAVLVALGIIIADSRLGTFSQIRTYMDTAVSPFYFVSNAPRELLDGVSQTLASRDQLELENRALRQELLLKNSELLMLGQYKQENARLRELLGSPLRQDEQKMVTQVISTVNDPYSDQVVIDKGSVNGVYEGQPVISDKGVVGQVVAVAKLTSRVLLICDATHALPIQVLRNDIRVIAAGNGCTDDLQLEHLPANTDIRVGDVLVTSGLGGRFPEGYPVAVVSSVKLDTQRAYTVIQARPTAGLQRLRYLLLLWGADRNGANPMTPEEVHRVANERLMQMMPQVLPSPDAMGPKLPEPATGIAQ... | null | null | establishment or maintenance of cell polarity regulating cell shape [GO:0071963]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360] | plasma membrane [GO:0005886] | protein self-association [GO:0043621] | PF04085; | 2.40.10.340;2.40.10.350; | MreC family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15612918}; Single-pass membrane protein {ECO:0000269|PubMed:15612918}. | null | null | null | null | null | FUNCTION: Involved in formation and maintenance of cell shape. Responsible for formation of rod shape. May also contribute to regulation of formation of penicillin-binding proteins. {ECO:0000269|PubMed:15612918, ECO:0000269|PubMed:2687239}. | Escherichia coli (strain K12) |
P16930 | FAAA_HUMAN | MSFIPVAEDSDFPIHNLPYGVFSTRGDPRPRIGVAIGDQILDLSIIKHLFTGPVLSKHQDVFNQPTLNSFMGLGQAAWKEARVFLQNLLSVSQARLRDDTELRKCAFISQASATMHLPATIGDYTDFYSSRQHATNVGIMFRDKENALMPNWLHLPVGYHGRASSVVVSGTPIRRPMGQMKPDDSKPPVYGACKLLDMELEMAFFVGPGNRLGEPIPISKAHEHIFGMVLMNDWSARDIQKWEYVPLGPFLGKSFGTTVSPWVVPMDALMPFAVPNPKQDPRPLPYLCHDEPYTFDINLSVNLKGEGMSQAATICKSNFK... | 3.7.1.2 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P35505}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P35505}; | arginine catabolic process [GO:0006527]; homogentisate catabolic process [GO:1902000]; L-phenylalanine catabolic process [GO:0006559]; lipid metabolic process [GO:0006629]; tyrosine catabolic process [GO:0006572] | cytosol [GO:0005829]; extracellular exosome [GO:0070062] | fumarylacetoacetase activity [GO:0004334]; metal ion binding [GO:0046872] | PF01557;PF09298; | 2.30.30.230;3.90.850.10; | FAH family | null | null | CATALYTIC ACTIVITY: Reaction=4-fumarylacetoacetate + H2O = acetoacetate + fumarate + H(+); Xref=Rhea:RHEA:10244, ChEBI:CHEBI:13705, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18034, ChEBI:CHEBI:29806; EC=3.7.1.2; Evidence={ECO:0000250|UniProtKB:P35505}; | null | PATHWAY: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 6/6. | null | null | null | Homo sapiens (Human) |
P16949 | STMN1_HUMAN | MASSDIQVKELEKRASGQAFELILSPRSKESVPEFPLSPPKKKDLSLEEIQKKLEAAEERRKSHEAEVLKQLAEKREHEKEVLQKAIEENNNFSKMAEEKLTHKMEANKENREAQMAAKLERLREKDKHIEEVRKNKESKDPADETEAD | null | null | axonogenesis [GO:0007409]; establishment of skin barrier [GO:0061436]; hepatocyte growth factor receptor signaling pathway [GO:0048012]; intracellular signal transduction [GO:0035556]; microtubule depolymerization [GO:0007019]; mitotic cytokinesis [GO:0000281]; mitotic spindle organization [GO:0007052]; negative regula... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; microtubule [GO:0005874]; neuron projection [GO:0043005] | tubulin binding [GO:0015631] | PF00836; | 6.10.280.30; | Stathmin family | PTM: Many different phosphorylated forms are observed depending on specific combinations among the sites which can be phosphorylated. MAPK is responsible for the phosphorylation of stathmin in response to NGF. Phosphorylation at Ser-16 seems to be required for neuron polarization (By similarity). Phosphorylation at Ser... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | null | null | null | null | null | FUNCTION: Involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. Phosphorylation at Ser-16 may be required for axon formation during neurogenesis. Involved in the control of the learned and innate fear (By similarity)... | Homo sapiens (Human) |
P16951 | ATF2_MOUSE | MSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARNDSVIVADQTPTPTRFLKNCEEVGLFNELASPFENEFKKASEDDIKKMPLDLSPLATPIIRSKIEEPSVVETTHQDSPLPHPESTTSDEKEVPLAQTAQPTSAIVRPASLQVPNVLLTSSDSSVIIQQAVPSPTSSTVITQAPSSNRPIVPVPGPFPLLLHLPNGQTMPVAIPASITSSNVHVPAAVPLVRPVTMVPSVPGIPGPSSPQPVQSEAKMRLKAALTQQHPPVTNGDTVKGHGSGLVRTQSEESRPQSLQQPATSTTETPASPAHTTPQTQN... | null | null | abducens nucleus development [GO:0021742]; adipose tissue development [GO:0060612]; amelogenesis [GO:0097186]; apoptotic process [GO:0006915]; apoptotic process involved in development [GO:1902742]; BMP signaling pathway [GO:0030509]; brainstem development [GO:0003360]; cellular lipid metabolic process [GO:0044255]; ce... | CCAAT-binding factor complex [GO:0016602]; cytoplasm [GO:0005737]; H4 histone acetyltransferase complex [GO:1902562]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861] | cAMP response element binding [GO:0035497]; cAMP response element binding protein binding [GO:0008140]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding tra... | PF00170; | 1.20.5.170;3.30.160.60; | BZIP family, ATF subfamily | PTM: Phosphorylation of Thr-51 by MAPK14 and MAPK11, and at Thr-53 by MAPK1/ERK2, MAPK3/ERK1, MAPK11, MAPK12 and MAPK14 in response to external stimulus like insulin causes increased transcriptional activity. Phosphorylated by PLK3 following hyperosmotic stress. Also phosphorylated and activated by JNK and CaMK4. ATM-m... | SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}. Note=Shuttles between the cytoplasm and the nucleus and heterodimerization with JUN is essential for the nuclear localization. Localization to the cytoplasm is observed under conditions of cellular stress and in disease ... | null | null | null | null | null | FUNCTION: Transcriptional activator which regulates the transcription of various genes, including those involved in anti-apoptosis, cell growth, and DNA damage response. Dependent on its binding partner, binds to CRE (cAMP response element) consensus sequences (5'-TGACGTCA-3') or to AP-1 (activator protein 1) consensus... | Mus musculus (Mouse) |
P16952 | SSPB_STRGN | MKNKKEVYGFRKSKVAKTLCGAVLGTALIAFADKAVFADEVTETTSTSTVEVATTGNPATNLPEAQGEMSQVAKESQAKAGSKESALPVEVSSADLDKAVADAKSAGVKVVQDETKDKGTATTATDNAQKQDEIKSDYAKQAEEIKTTTEAYKKEVAAHQAETDKINAENKAADDKYQKDLKSHQEEVEKINTANATAKAEYEAKLAQYQKDLATVKKANEDSQQDYQNKLSAYQTELARVQKANAEAKEAYEKAVKENTAKNEALKVENEAIKQRNETAKATYEAAMKQYEADLAAIKKANEDNDADYQAKLAAYQTEL... | null | null | null | extracellular region [GO:0005576] | metal ion binding [GO:0046872] | PF18652;PF17998;PF16364;PF08363;PF00746;PF06696; | 2.60.40.740;6.10.250.2200;2.60.530.10; | Antigen I/II family | null | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. | null | null | null | null | null | FUNCTION: May bind sialic acid residues of salivary agglutinin (SAG) in a calcium-dependent reaction. The interaction of SAG with its receptor in various oral streptococci modulate bacterial colonization of oral tissue and is associated with reduced levels of dental caries. | Streptococcus gordonii |
P16960 | RYR1_PIG | MGDGGEGEDEVQFLRTDDEVVLQCNATVLKEQLKLCLAAEGFGNRLCFLEPTSNAQNVPPDLAICCFVLEQSLSVRALQEMLANTVEAGVESSQGGGHRTLLYGHAILLRHAHSGMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTTHPASKQRSEGEKVRVGDDLILVSVSSERYLHLSTASGELQVDASFMQTLWNMNPICSGCEEGYVTGGHVLRLFHGHMDECLTISPADSDDQRRLVYYEGGSVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRYLALIEDQGLVVVDASKAHTKATSFCFRISK... | null | null | calcium ion transmembrane transport [GO:0070588]; cellular response to caffeine [GO:0071313]; cellular response to calcium ion [GO:0071277]; intracellular calcium ion homeostasis [GO:0006874]; muscle contraction [GO:0006936]; ossification involved in bone maturation [GO:0043931]; outflow tract morphogenesis [GO:0003151... | calcium channel complex [GO:0034704]; organelle membrane [GO:0031090]; ryanodine receptor complex [GO:1990425]; sarcolemma [GO:0042383]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum membrane [GO:0033017]; smooth endoplasmic reticulum [GO:0005790]; terminal cisterna [GO:0014802]; Z disc [GO:0030018] | ATP binding [GO:0005524]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; ryanodine-sensitive calcium-release channel activity [GO:0005219]; voltage-gated calcium channel activity [GO:0005245] | PF08709;PF00520;PF02815;PF08454;PF06459;PF01365;PF21119;PF02026;PF00622; | 1.10.287.70;1.10.490.160;2.60.120.920;2.80.10.50;6.20.350.10;1.25.10.30; | Ryanodine receptor (TC 1.A.3.1) family, RYR1 subfamily | PTM: Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2844 may increase channel activity. Repeated very high-level exercise increases phosphorylation at Ser-2844. {ECO:0000250|UniProtKB:P21817}.; PTM: Activated by reversible S-nitrosylation (By similarity). Repeated very high-level exercise incr... | SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:P11716}; Multi-pass membrane protein {ECO:0000255}. Note=The number of predicted transmembrane domains varies between orthologs. Both N-terminus and C-terminus are cytoplasmic. {ECO:0000250|UniProtKB:P11716}. | null | null | null | null | null | FUNCTION: Cytosolic calcium-activated calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytosol and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules (By similarity). Repeated very high-level exercise increases the open probability... | Sus scrofa (Pig) |
P16970 | ABCD3_RAT | MAAFSKYLTARNSSLAGAAFLLFCLLHKRRRALGLHGKKSGKPPLQNNEKEGKKERAVVDKVFLSRLSQILKIMVPRTFCKETGYLILIAVMLVSRTYCDVWMIQNGTLIESGIIGRSSKDFKRYLFNFIAAMPLISLVNNFLKYGLNELKLCFRVRLTRYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQGPASMMAYLLVSGLFLTRLRRPIGKMTIMEQKYEGEYRFVNSRLITNSEEIAFYNGNKREKQTIHSVFRKLVEHLHNFIFFRFSMGFIDSII... | 3.1.2.-; 7.6.2.- | null | bile acid and bile salt transport [GO:0015721]; bile acid biosynthetic process [GO:0006699]; fatty acid beta-oxidation [GO:0006635]; fatty acid biosynthetic process [GO:0006633]; lipid transport [GO:0006869]; long-chain fatty acid import into peroxisome [GO:0015910]; peroxisome organization [GO:0007031]; phytanic acid ... | mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777] | ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; fatty acyl-CoA hydrolase activity [GO:0047617]; long-chain fatty acid transporter activity [GO:0005324]; protein homodimerization activity [GO:00428... | PF06472;PF00005; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily, ABCD family, Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily | PTM: Ubiquitinated by PEX2 during pexophagy in response to starvation, leading to its degradation. {ECO:0000250|UniProtKB:P28288}. | SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:10207018}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a very long-chain fatty acyl-CoA + H2O = a very long-chain fatty acid + CoA + H(+); Xref=Rhea:RHEA:67072, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:58950, ChEBI:CHEBI:138261; Evidence={ECO:0000250|UniProtKB:P28288}; PhysiologicalDirection=left-to-right; Xref=Rhea:... | null | null | null | null | FUNCTION: Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that catalyzes the transport of long-chain fatty acids (LCFA)-CoA, dicarboxylic acids-CoA, long-branched-chain fatty acids-CoA and bile acids from the cytosol to the peroxisome lumen for beta-oxydation. Has fatty ac... | Rattus norvegicus (Rat) |
P16971 | RECA_BACSU | MSDRQAALDMALKQIEKQFGKGSIMKLGEKTDTRISTVPSGSLALDTALGIGGYPRGRIIEVYGPESSGKTTVALHAIAEVQQQGGQAAFIDAEHALDPVYAQKLGVNIEELLLSQPDTGEQALEIAEALVRSGAVDIVVVDSVAALVPKAEIEGDMGDSHVGLQARLMSQALRKLSGAINKSKTIAIFINQIREKVGVMFGNPETTPGGRALKFYSSVRLEVRRAEQLKQGNDVMGNKTKIKVVKNKVAPPFRTAEVDIMYGEGISKEGEIIDLGTELDIVQKSGSWYSYEEERLGQGRENAKQFLKENKDIMLMIQEQ... | null | null | DNA recombination [GO:0006310]; DNA repair [GO:0006281]; establishment of competence for transformation [GO:0030420]; SOS response [GO:0009432] | cytosol [GO:0005829]; nucleoid [GO:0009295] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent DNA damage sensor activity [GO:0140664]; damaged DNA binding [GO:0003684]; single-stranded DNA binding [GO:0003697] | PF00154;PF21096; | 3.40.50.300; | RecA family | null | SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:16061691}. Note=Protein is recruited to RC foci following DNA damage (PubMed:16061691). During competence a number of proteins (at least CoiA, ComFA, ComGA, DprA, RecA and SsbB) are thought to colocalize at the cell pole (PubMed:17630974). {ECO:0000269|PubMe... | null | null | null | null | null | FUNCTION: Multifunctional protein involved in homologous recombination, DNA repair and competence (PubMed:16061691, PubMed:16385024, PubMed:17803906, PubMed:18684995, PubMed:25138221). Can catalyze the hydrolysis of (d)ATP in the presence of single-stranded DNA; prefers dATP at least in vitro, catalyzes the dATP-depend... | Bacillus subtilis (strain 168) |
P16975 | SPRC_RAT | MRAWIFFLLCLAGRALAAPQTEAAEEMVAEETVVEETGLPVGANPVQVEMGEFEEGAEETVEEVVAENPCQNHHCKHGKVCELDESNTPMCVCQDPTSCPAPIGEFEKVCSNDNKTFDSSCHFFATKCTLEGTKKGHKLHLDYIGPCKYIAPCLDSELTEFPLRMRDWLKNVLVTLYERDEGNNLLTEKQKLRVKKIHENEKRLEAGDHPVELLARDFEKNYNMYIFPVHWQFGQLDQHPIDGYLSHTELAPLRAPLIPMEHCTTRFFETCDLDNDKYIALEEWAGCFGIKEQDINKDLVI | null | null | bone development [GO:0060348]; cellular response to growth factor stimulus [GO:0071363]; heart development [GO:0007507]; inner ear development [GO:0048839]; lung development [GO:0030324]; negative regulation of angiogenesis [GO:0016525]; negative regulation of endothelial cell proliferation [GO:0001937]; ossification [... | basement membrane [GO:0005604]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; nuclear matrix [GO:0016363]; platelet alpha granule [GO:0031091]; platelet alpha granule membrane [GO:0031092]; synapse [GO:0045202]... | calcium ion binding [GO:0005509]; collagen binding [GO:0005518]; extracellular matrix binding [GO:0050840] | PF09289;PF00050;PF10591; | 3.30.60.30;1.10.238.10; | SPARC family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:2322281}. Note=In or around the basement membrane. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-... | Rattus norvegicus (Rat) |
P16989 | YBOX3_HUMAN | MSEAGEATTTTTTTLPQAPTEAAAAAPQDPAPKSPVGSGAPQAAAPAPAAHVAGNPGGDAAPAATGTAAAASLATAAGSEDAEKKVLATKVLGTVKWFNVRNGYGFINRNDTKEDVFVHQTAIKKNNPRKYLRSVGDGETVEFDVVEGEKGAEAANVTGPDGVPVEGSRYAADRRRYRRGYYGRRRGPPRNYAGEEEEEGSGSSEGFDPPATDRQFSGARNQLRRPQYRPQYRQRRFPPYHVGQTFDRRSRVLPHPNRIQAGEIGEMKDGVPEGAQLQGPVHRNPTYRPRYRSRGPPRPRPAPAVGEAEDKENQQATSGP... | null | null | 3'-UTR-mediated mRNA stabilization [GO:0070935]; apoptotic process [GO:0006915]; cellular hyperosmotic response [GO:0071474]; cellular response to tumor necrosis factor [GO:0071356]; ectopic germ cell programmed cell death [GO:0035234]; fertilization [GO:0009566]; in utero embryonic development [GO:0001701]; male gonad... | bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; synapse [GO:0045202] | mRNA 3'-UTR binding [GO:0003730]; nucleic acid binding [GO:0003676]; polysome binding [GO:1905538]; RNA binding [GO:0003723]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; small GTPase binding [GO:0031267] | PF00313; | 2.40.50.140; | null | null | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. | null | null | null | null | null | FUNCTION: Binds to the GM-CSF promoter. Seems to act as a repressor. Binds also to full-length mRNA and to short RNA sequences containing the consensus site 5'-UCCAUCA-3'. May have a role in translation repression (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
P17010 | ZFX_HUMAN | MDEDGLELQQEPNSFFDATGADGTHMDGDQIVVEVQETVFVSDVVDSDITVHNFVPDDPDSVVIQDVIEDVVIEDVQCPDIMEEADVSETVIIPEQVLDSDVTEEVSLAHCTVPDDVLASDITSASMSMPEHVLTGDSIHVSDVGHVGHVGHVEHVVHDSVVEAEIVTDPLTTDVVSEEVLVADCASEAVIDANGIPVDQQDDDKGNCEDYLMISLDDAGKIEHDGSSGMTMDTESEIDPCKVDGTCPEVIKVYIFKADPGEDDLGGTVDIVESEPENDHGVELLDQNSSIRVPREKMVYMTVNDSQPEDEDLNVAEIAD... | null | null | fertilization [GO:0009566]; homeostasis of number of cells [GO:0048872]; multicellular organism growth [GO:0035264]; oocyte development [GO:0048599]; ovarian follicle development [GO:0001541]; parental behavior [GO:0060746]; positive regulation of transcription by RNA polymerase II [GO:0045944]; post-embryonic developm... | chromatin [GO:0000785]; chromosome [GO:0005694]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654] | chromatin insulator sequence binding [GO:0043035]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00096;PF13909;PF04704; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family, ZFX/ZFY subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Probable transcriptional activator. | Homo sapiens (Human) |
P17012 | ZFX_MOUSE | MDEDGLELQQQAPNSFFDATGAGATHMDGNQIVVEVQETVYVSDVVDSDITVHNYVPDDPDSVVIQDVIEDVVIEDVQCTDIMDEADVSETVIIPEQVLDSDVTEEVSLTHCTVPDDVLASDITSASISMPEHVLTSESIHVSDVGHVEHVVHDSVVEAEIVTDPLAADVVSEEVLVADCASEAVIDANGIPVNQQDEEKNNCEDYLMISLDDAGKIEHDGSSGLTMDNETEIDPCKVDGTCPEVIKVYIFKADPGEDDLGGTVDIVESEPENEHGVELLDPNNSIRVPREKMVYMAVNDSQQEEEELNVAEIADEVYME... | null | null | fertilization [GO:0009566]; germ cell development [GO:0007281]; homeostasis of number of cells [GO:0048872]; multicellular organism growth [GO:0035264]; oocyte development [GO:0048599]; ovarian follicle development [GO:0001541]; parental behavior [GO:0060746]; post-embryonic development [GO:0009791]; regulation of tran... | chromatin [GO:0000785]; chromosome [GO:0005694]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654] | chromatin insulator sequence binding [GO:0043035]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00096;PF04704; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family, ZFX/ZFY subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Probable transcriptional activator. | Mus musculus (Mouse) |
P17014 | ZNF12_HUMAN | MNKSLGPVSFKDVAVDFTQEEWQQLDPEQKITYRDVMLENYSNLVSVGYHIIKPDVISKLEQGEEPWIVEGEFLLQSYPDEVWQTDDLIERIQEEENKPSRQTVFIETLIEERGNVPGKTFDVETNPVPSRKIAYKNSLCDSCEKCLTSVSEYISSDGSYARMKADECSGCGKSLLHIKLEKTHPGDQAYEFNQNGEPYTLNEESLYQKIRILEKPFEYIECQKAFQKDTVFVNHMEEKPYKWNGSEIAFLQMSDLTVHQTSHMEMKPYECSECGKSFCKKSKFIIHQRTHTGEKPYECNQCGKSFCQKGTLTVHQRTHT... | null | null | negative regulation of DNA-templated transcription [GO:0045892]; regulation of transcription by RNA polymerase II [GO:0006357] | centrosome [GO:0005813]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837] | PF01352;PF00096; | 6.10.140.140;3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16806083}. | null | null | null | null | null | FUNCTION: Transcriptional repressor which suppresses activation protein 1 (AP-1)- and serum response element (SRE)-mediated transcriptional activity. {ECO:0000269|PubMed:16806083}. | Homo sapiens (Human) |
P17020 | ZNF16_HUMAN | MPSLRTRREEAEMELSVPGPSPWTPAAQARVRDAPAVTHPGSAACGTPCCSDTELEAICPHYQQPDCDTRTEDKEFLHKEDIHEDLESQAEISENYAGDVSQVPELGDLCDDVSERDWGVPEGRRLPQSLSQEGDFTPAAMGLLRGPLGEKDLDCNGFDSRFSLSPNLMACQEIPTEERPHPYDMGGQSFQHSVDLTGHEGVPTAESPLICNECGKTFQGNPDLIQRQIVHTGEASFMCDDCGKTFSQNSVLKNRHRSHMSEKAYQCSECGKAFRGHSDFSRHQSHHSSERPYMCNECGKAFSQNSSLKKHQKSHMSEKP... | null | null | cell cycle [GO:0007049]; cell division [GO:0051301]; cellular response to sodium dodecyl sulfate [GO:0072707]; negative regulation of apoptotic process [GO:0043066]; positive regulation of cell cycle phase transition [GO:1901989]; positive regulation of cell division [GO:0051781]; positive regulation of cell population... | nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00096; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16628192}. | null | null | null | null | null | FUNCTION: Acts as a transcriptional activator. Promotes cell proliferation by facilitating the cell cycle phase transition from the S to G2/M phase. Involved in both the hemin- and phorbol myristate acetate (PMA)-induced erythroid and megakaryocytic differentiation, respectively. Also plays a role as an inhibitor of ce... | Homo sapiens (Human) |
P17021 | ZNF17_HUMAN | MNLTEDYMVFEDVAIHFSQEEWGILNDVQRHLHSDVMLENFALLSSVGCWHGAKDEEAPSKQCVSVGVSQVTTLKPALSTQKAQPCETCSSLLKDILHLAEHDGTHPKRTAKLYLHQKEHLREKLTRSDEGRPSFVNDSVHLAKRNLTCMQGGKDFTGDSDLQQQALHSGWKPHRDTHGVEAFQSGQNNYSCTQCGKDFCHQHTLFEHQKIHTEERPYECSECGKLFRYNSDLIKHQRNHTGERPYKCSECGKAFSLKYNVVQHQKIHTGERPYECSECGKAFLRKSHLLQHQRIHTRPRPYVCSECGKAFLTQAHLVGH... | null | null | regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF01352;PF00096; | 6.10.140.140;3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be involved in transcriptional regulation. | Homo sapiens (Human) |
P17022 | ZNF18_HUMAN | MPVDLGQALGLLPSLAKAEDSQFSESDAALQEELSSPETARQLFRQFRYQVMSGPHETLKQLRKLCFQWLQPEVHTKEQILEILMLEQFLTILPGEIQMWVRKQCPGSGEEAVTLVESLKGDPQRLWQWISIQVLGQDILSEKMESPSCQVGEVEPHLEVVPQELGLENSSSGPGELLSHIVKEESDTEAELALAASQPARLEERLIRDQDLGASLLPAAPQEQWRQLDSTQKEQYWDLMLETYGKMVSGAGISHPKSDLTNSIEFGEELAGIYLHVNEKIPRPTCIGDRQENDKENLNLENHRDQELLHASCQASGEVP... | null | null | regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF01352;PF02023;PF00096; | 6.10.140.140;3.30.160.60;1.10.4020.10; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}. | null | null | null | null | null | FUNCTION: May be involved in transcriptional regulation. | Homo sapiens (Human) |
P17023 | ZNF19_HUMAN | MAAMPLKAQYQEMVTFEDVAVHFTKTEWTGLSPAQRALYRSVMLENFGNLTALGYPVPKPALISLLERGDMAWGLEAQDDPPAERTKNVCKDVETNIDSESTLIQGISEERDGMMSHGQLKSVPQRTDFPETRNVEKHQDIPTVKNIQGKVPRIPCARKPFICEECGKSFSYFSYYARHQRIHTGEKPFECSECGKAFNGNSSLIRHQRIHTGERPYQCEECGRAFNDNANLIRHQRIHSGDRPYYCTECGNSFTSSSEFVIHQRIHTGEKPYECNECGKAFVGNSPLLRHQKIHTGEKPYECNECGKSFGRTSHLSQHQ... | null | null | regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF01352;PF00096; | 6.10.140.140;3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be involved in transcriptional regulation. | Homo sapiens (Human) |
P17024 | ZNF20_HUMAN | MMFQDSVAFEDVAVSFTQEEWALLDPSQKNLYRDVMQETFKNLTSVGKTWKVQNIEDEYKNPRRNLSLMREKLCESKESHHCGESFNQIADDMLNRKTLPGITPCESSVCGEVGTGHSSLNTHIRADTGHKSSEYQEYGENPYRNKECKKAFSYLDSFQSHDKACTKEKPYDGKECTETFISHSCIQRHRVMHSGDGPYKCKFCGKAFYFLNLCLIHERIHTGVKPYKCKQCGKAFTRSTTLPVHERTHTGVNADECKECGNAFSFPSEIRRHKRSHTGEKPYECKQCGKVFISFSSIQYHKMTHTGEKPYECKQCGKAF... | null | null | regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF01352;PF00096;PF13894;PF13912; | 6.10.140.140;3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be involved in transcriptional regulation. | Homo sapiens (Human) |
P17027 | ZNF23_HUMAN | MLENYGNVASLGFPLLKPAVISQLEGGSELGGSSPLAAGTGLQGLQTDIQTDNDLTKEMYEGKENVSFELQRDFSQETDFSEASLLEKQQEVHSAGNIKKEKSNTIDGTVKDETSPVEECFFSQSSNSYQCHTITGEQPSGCTGLGKSISFDTKLVKHEIINSEERPFKCEELVEPFRCDSQLIQHQENNTEEKPYQCSECGKAFSINEKLIWHQRLHSGEKPFKCVECGKSFSYSSHYITHQTIHSGEKPYQCKMCGKAFSVNGSLSRHQRIHTGEKPYQCKECGNGFSCSSAYITHQRVHTGEKPYECNDCGKAFNVN... | null | null | regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837] | PF00096; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be involved in transcriptional regulation. May have a role in embryonic development. | Homo sapiens (Human) |
P17028 | ZNF24_HUMAN | MSAQSVEEDSILIIPTPDEEEKILRVKLEEDPDGEEGSSIPWNHLPDPEIFRQRFRQFGYQDSPGPREAVSQLRELCRLWLRPETHTKEQILELVVLEQFVAILPKELQTWVRDHHPENGEEAVTVLEDLESELDDPGQPVSLRRRKREVLVEDMVSQEEAQGLPSSELDAVENQLKWASWELHSLRHCDDDGRTENGALAPKQELPSALESHEVPGTLNMGVPQIFKYGETCFPKGRFERKRNPSRKKQHICDECGKHFSQGSALILHQRIHSGEKPYGCVECGKAFSRSSILVQHQRVHTGEKPYKCLECGKAFSQNS... | null | null | myelination [GO:0042552]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:000... | PF02023;PF00096; | 3.30.160.60;1.10.4020.10; | Krueppel C2H2-type zinc-finger protein family | PTM: Sumoylated. {ECO:0000269|PubMed:15561718}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187, ECO:0000269|PubMed:24224020}. | null | null | null | null | null | FUNCTION: Transcription factor required for myelination of differentiated oligodendrocytes. Required for the conversion of oligodendrocytes from the premyelinating to the myelinating state. In the developing central nervous system (CNS), involved in the maintenance in the progenitor stage by promoting the cell cycle. S... | Homo sapiens (Human) |
P17036 | ZNF3_HUMAN | METQADLVSQEPQALLDSALPSKVPAFSDKDSLGDEMLAAALLKAKSQELVTFEDVAVYFIRKEWKRLEPAQRDLYRDVMLENYGNVFSLDRETRTENDQEISEDTRSHGVLLGRFQKDISQGLKFKEAYEREVSLKRPLGNSPGERLNRKMPDFGQVTVEEKLTPRGERSEKYNDFGNSFTVNSNLISHQRLPVGDRPHKCDECSKSFNRTSDLIQHQRIHTGEKPYECNECGKAFSQSSHLIQHQRIHTGEKPYECSDCGKTFSCSSALILHRRIHTGEKPYECNECGKTFSWSSTLTHHQRIHTGEKPYACNECGKA... | null | null | cell differentiation [GO:0030154]; leukocyte activation [GO:0045321]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:00... | PF01352;PF00096; | 6.10.140.140;3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Involved in cell differentiation and/or proliferation. | Homo sapiens (Human) |
P17040 | ZSC20_HUMAN | MAMALELQAQASPQPEPEELLIVKLEEDSWGSESKLWEKDRGSVSGPEASRQRFRQFQYRDAAGPHEAFSQLWALCCRWLRPEIRLKEQILELLVLEQFLTILPREVQTWVQARHPESGEEAVALVEDWHRETRTAGQSGLELHTEETRPLKTGEEAQSFQLQPVDPWPEGQSQKKGVKNTCPDLPNHLNAEVAPQPLKESAVLTPRVPTLPKMGSVGDWEVTAESQEALGPGKHAEKELCKDPPGDDCGNSVCLGVPVSKPSNTSEKEQGPEFWGLSLINSGKRSTADYSLDNEPAQALTWRDSRAWEEQYQWDVEDMK... | null | null | regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF13837;PF02023;PF00096; | 3.30.160.60;1.10.4020.10;1.10.10.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}. | null | null | null | null | null | FUNCTION: May be involved in transcriptional regulation. | Homo sapiens (Human) |
P17041 | ZNF32_HUMAN | MFGFPTATLLDCHGRYAQNVAFFNVMTEAHHKYDHSEATGSSSWDIQNSFRREKLEQKSPDSKTLQEDSPGVRQRVYECQECGKSFRQKGSLTLHERIHTGQKPFECTHCGKSFRAKGNLVTHQRIHTGEKPYQCKECGKSFSQRGSLAVHERLHTGQKPYECAICQRSFRNQSNLAVHRRVHSGEKPYRCDQCGKAFSQKGSLIVHIRVHTGLKPYACTQCRKSFHTRGNCILHGKIHTGETPYLCGQCGKSFTQRGSLAVHQRSCSQRLTL | null | null | regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837] | PF00096;PF13465; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be involved in transcriptional regulation. | Homo sapiens (Human) |
P17046 | LAMP2_RAT | MRLLSPVTGSKLVLLFLFLGAVRSDALKLNLTDSKGTCLYAEWEMNFTITYEALKVNETVTITVPDKVTYNGSSCGDDKNGAKIMIQYGSTLSWAVNFTKEASQYFINNITLSYNTNDTKTFPGAVPKGILTVIIPVGSQLPLGVIFKCSSVLTFNLSPVVQHYWGIHLQAFVQNGTVSKHEQVCKEDKTATTVAPIIHTTVPSPTTTLTPTSIPVPTPTVGNYTISNGNATCLLATMGLQLNITEEKVPFIFNINPAITNFTGSCQPQTAQLRLNNSQIKYLDFIFAVKNEKRFYLKEVNVNMYLANGSAFHVSNNNLS... | null | null | autophagosome maturation [GO:0097352]; autophagy [GO:0006914]; cellular response to starvation [GO:0009267]; chaperone-mediated autophagy [GO:0061684]; lysosomal lumen acidification [GO:0007042]; lysosomal protein catabolic process [GO:1905146]; muscle cell cellular homeostasis [GO:0046716]; protein stabilization [GO:0... | autolysosome [GO:0044754]; autophagosome membrane [GO:0000421]; chaperone-mediated autophagy translocation complex [GO:0061742]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal matrix [GO:1990836]; ly... | enzyme binding [GO:0019899]; ion channel inhibitor activity [GO:0008200]; protein domain specific binding [GO:0019904] | PF01299;PF21222; | 2.40.160.110; | LAMP family | PTM: Extensively N-glycosylated (PubMed:1794981, PubMed:18644871). Contains a minor proportion of O-linked glycans (PubMed:1794981). Contains sialylated glycans (PubMed:1794981). {ECO:0000269|PubMed:1794981, ECO:0000269|PubMed:18644871}. | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:11082038, ECO:0000269|PubMed:1794981, ECO:0000269|PubMed:18644871, ECO:0000269|PubMed:2590192, ECO:0000269|PubMed:8662539}; Single-pass type I membrane protein {ECO:0000269|PubMed:11082038}. Endosome membrane {ECO:0000250|UniProtKB:P13473}; Single-pass type I ... | null | null | null | null | null | FUNCTION: Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, lysosomal pH regulation and autophagy (PubMed:11082038, PubMed:8662539). Acts as an important regulator of lysosomal lumen pH regulation by acting as a direct inhibitor of the proton channel TMEM175, facilitating lysosomal a... | Rattus norvegicus (Rat) |
P17047 | LAMP2_MOUSE | MCLSPVKGAKLILIFLFLGAVQSNALIVNLTDSKGTCLYAEWEMNFTITYETTNQTNKTITIAVPDKATHDGSSCGDDRNSAKIMIQFGFAVSWAVNFTKEASHYSIHDIVLSYNTSDSTVFPGAVAKGVHTVKNPENFKVPLDVIFKCNSVLTYNLTPVVQKYWGIHLQAFVQNGTVSKNEQVCEEDQTPTTVAPIIHTTAPSTTTTLTPTSTPTPTPTPTPTVGNYSIRNGNTTCLLATMGLQLNITEEKVPFIFNINPATTNFTGSCQPQSAQLRLNNSQIKYLDFIFAVKNEKRFYLKEVNVYMYLANGSAFNISN... | null | null | autophagosome maturation [GO:0097352]; autophagy [GO:0006914]; cellular response to starvation [GO:0009267]; chaperone-mediated autophagy [GO:0061684]; lysosomal lumen acidification [GO:0007042]; lysosomal protein catabolic process [GO:1905146]; muscle cell cellular homeostasis [GO:0046716]; protein stabilization [GO:0... | autolysosome [GO:0044754]; autophagosome membrane [GO:0000421]; chaperone-mediated autophagy translocation complex [GO:0061742]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal matrix [GO:1990836]; lysosomal membrane [GO:0005765]; lys... | enzyme binding [GO:0019899]; ion channel inhibitor activity [GO:0008200]; protein domain specific binding [GO:0019904] | PF01299;PF21222; | 2.40.160.110; | LAMP family | PTM: Extensively N-glycosylated. Contains a minor proportion of O-linked glycans. {ECO:0000269|PubMed:2142158}. | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:11082038, ECO:0000269|PubMed:2142158}; Single-pass type I membrane protein {ECO:0000255|PROSITE-ProRule:PRU00740}. Endosome membrane {ECO:0000250|UniProtKB:P13473}; Single-pass type I membrane protein {ECO:0000255|PROSITE-ProRule:PRU00740}. Cytoplasmic vesicle... | null | null | null | null | null | FUNCTION: Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, lysosomal pH regulation and autophagy (PubMed:10972293). Acts as an important regulator of lysosomal lumen pH regulation by acting as a direct inhibitor of the proton channel TMEM175, facilitating lysosomal acidification for... | Mus musculus (Mouse) |
P17050 | NAGAB_HUMAN | MLLKTVLLLGHVAQVLMLDNGLLQTPPMGWLAWERFRCNINCDEDPKNCISEQLFMEMADRMAQDGWRDMGYTYLNIDDCWIGGRDASGRLMPDPKRFPHGIPFLADYVHSLGLKLGIYADMGNFTCMGYPGTTLDKVVQDAQTFAEWKVDMLKLDGCFSTPEERAQGYPKMAAALNATGRPIAFSCSWPAYEGGLPPRVNYSLLADICNLWRNYDDIQDSWWSVLSILNWFVEHQDILQPVAGPGHWNDPDMLLIGNFGLSLEQSRAQMALWTVLAAPLLMSTDLRTISAQNMDILQNPLMIKINQDPLGIQGRRIHKE... | 3.2.1.49 | null | carbohydrate catabolic process [GO:0016052]; glycolipid catabolic process [GO:0019377]; glycoside catabolic process [GO:0016139]; oligosaccharide metabolic process [GO:0009311] | cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; lysosome [GO:0005764] | alpha-galactosidase activity [GO:0004557]; alpha-N-acetylgalactosaminidase activity [GO:0008456]; protein homodimerization activity [GO:0042803] | PF16499;PF17450; | 3.20.20.70;2.60.40.1180; | Glycosyl hydrolase 27 family | null | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:9741689}. | CATALYTIC ACTIVITY: Reaction=Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids.; EC=3.2.1.49; Evidence={ECO:0000269|PubMed:19683538}; CATALYTIC ACTIVITY: Reaction=a neolactoside IV(3)-alpha... | null | null | null | null | FUNCTION: Removes terminal alpha-N-acetylgalactosamine residues from glycolipids and glycopeptides. Required for the breakdown of glycolipids. {ECO:0000269|PubMed:9741689}. | Homo sapiens (Human) |
P17064 | FCY2_YEAST | MLEEGNNVYEIQDLEKRSPVIGSSLENEKKVAASETFTATSEDDQQYIVESSEATKLSWFHKFFASLNAETKGVEPVTEDEKTDDSILNAASMWFSANMVIASYALGALGPMVFGLNFGQSVLVIIFFNIMGLIFVAFFSVFGAELGLRQMILSRYLVGNVTARIFSLINVIACVGWGIVNTSVSAQLLNMVNEGSGHVCPIWAGCLIIIGGTVLVTFFGYSVIHAYEKWSWVPNFAVFLVIIAQLSRSGKFKGGEWVGGATTAGSVLSFGSSIFGFAAGWTTYAADYTVYMPKSTNKYKIFFSLVAGLAFPLFFTMILG... | null | null | cytidine transport [GO:0015861]; cytosine transport [GO:0015856]; purine-containing compound transmembrane transport [GO:0072530] | cell periphery [GO:0071944]; fungal-type vacuole membrane [GO:0000329]; plasma membrane [GO:0005886] | cytidine transmembrane transporter activity [GO:0015212]; nucleobase transmembrane transporter activity [GO:0015205] | PF02133; | 1.10.4160.10; | Purine-cytosine permease (2.A.39) family | PTM: Not N-glycosylated. | SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: This permease has a broad specificity towards purines, and also transport cytosine and 5-methylcytosine but neither uracil nor thymine. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17065 | SEC2_YEAST | MDASEEAKRVSIQVTSLSTQLIESVDKQSHLEEQLNKSLKTIASQKAAIENYNQLKEDYNTLKRELSDRDDEVKRLREDIAKENELRTKAEEEADKLNKEVEDLTASLFDEANNMVADARKEKYAIEILNKRLTEQLREKDTLLDTLTLQLKNLKKVMHSLDNESTVTNNSNRYSTILSDSATSSSTSLNKVPTSYSLASQDIYSGIVYSPSISSIRYDISLYNEFLKFVAALPRCENIKATSTESKLIRRLVNDEIQPILKIDNASGIGWLVKKTLLSLIIDGLVVVEPLSGVNATYQIGYNSSSPAKQATSNMPKMFK... | null | null | autophagy [GO:0006914]; exocytosis [GO:0006887]; protein transport [GO:0015031] | cell tip [GO:0051286]; cellular bud neck [GO:0005935]; cellular bud tip [GO:0005934]; cytosol [GO:0005829]; Golgi to plasma membrane transport vesicle [GO:0070319]; mating projection tip [GO:0043332]; transport vesicle [GO:0030133] | guanyl-nucleotide exchange factor activity [GO:0005085]; identical protein binding [GO:0042802]; phosphatidylinositol-4-phosphate binding [GO:0070273] | PF06428; | 6.10.140.910; | SEC2 family | null | SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:10747090}. Bud tip {ECO:0000269|PubMed:10747090}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:10747090}. Note=Localizes to sites of polarized growth, namely to the bud neck and to the bud tip of growing buds, and associates with membranes. Colocalizes wi... | null | null | null | null | null | FUNCTION: Guanine nucleotide exchange factor for SEC4, catalyzing the dissociation of GDP from SEC4 and also potently promoting binding of GTP. Activation of SEC4 by SEC2 is needed for the directed transport of vesicles to sites of exocytosis. Binds the Rab GTPase YPT32, but does not have exchange activity on YPT32. {E... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17066 | HSP76_HUMAN | MQAPRELAVGIDLGTTYSCVGVFQQGRVEILANDQGNRTTPSYVAFTDTERLVGDAAKSQAALNPHNTVFDAKRLIGRKFADTTVQSDMKHWPFRVVSEGGKPKVRVCYRGEDKTFYPEEISSMVLSKMKETAEAYLGQPVKHAVITVPAYFNDSQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLDRRGAGERNVLIFDLGGGTFDVSVLSIDAGVFEVKATAGDTHLGGEDFDNRLVNHFMEEFRRKHGKDLSGNKRALRRLRTACERAKRTLSSSTQATLEIDSLFEGVDFYTSITRARFEELCSDLFRSTLEPVE... | null | null | cellular response to heat [GO:0034605]; chaperone cofactor-dependent protein refolding [GO:0051085]; protein refolding [GO:0042026]; response to unfolded protein [GO:0006986] | blood microparticle [GO:0072562]; centriole [GO:0005814]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; secretory granule lumen [GO:0034774] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; protein folding chaperone [GO:0044183]; ubiquitin protein ligase binding [GO:0031625]; unfolded protein binding [GO:0051082] | PF00012; | 1.20.1270.10;3.30.30.30;3.30.420.40; | Heat shock protein 70 family | null | null | null | null | null | null | null | FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in th... | Homo sapiens (Human) |
P17067 | CAHC_PEA | MSTSSINGFSLSSLSPAKTSTKRTTLRPFVSASLNTSSSSSSSTFPSLIQDKPVFASSSPIITPVLREEMGKGYDEAIEELQKLLREKTELKATAAEKVEQITAQLGTTSSSDGIPKSEASERIKTGFLHFKKEKYDKNPALYGELAKGQSPPFMVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVPPYDQAKYAGTGAAIEYAVLHLKVSNIVVIGHSACGGIKGLLSFPFDGTYSTDFIEEWVKIGLPAKAKVKAQHGDAPFAELCTHCEKEAVNASLGNLLTYPFVREGLVNKTLALKGGYYDFVKGSFELWGLEF... | 4.2.1.1 | null | carbon utilization [GO:0015976]; cellular response to carbon dioxide [GO:0071244]; cellular response to oxidative stress [GO:0034599] | chloroplast stroma [GO:0009570] | carbonate dehydratase activity [GO:0004089]; zinc ion binding [GO:0008270] | PF00484; | 3.40.1050.10; | Beta-class carbonic anhydrase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma. | CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; | null | null | null | null | FUNCTION: Reversible hydration of carbon dioxide. | Pisum sativum (Garden pea) (Lathyrus oleraceus) |
P17074 | RS19_RAT | MPGVTVKDVNQQEFVRALAAFLKKSGKLKVPEWVDTVKLAKHKELAPYDENWFYTRAASTARHLYLRGGAGVGSMTKIYGGRQRNGVRPSHFSRGSKSVARRVLQALEGLKMVEKDQDGGRKLTPQGQRDLDRIAGQVAAANKKH | null | null | antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; erythrocyte differentiation [GO:0030218]; maturation of SSU-rRNA [GO:0030490]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; monocyte chemotaxis [GO:0002548]; negative regulatio... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic ribosome [GO:0022626]; cytosolic small ribosomal subunit [GO:0022627]; nucleolus [GO:0005730]; postsynaptic density [GO:0014069]; ribosome [GO:0005840]; small ribosomal subunit [GO:0015935]; small-subunit processome [GO:0032040]; synapse [GO:0045202] | fibroblast growth factor binding [GO:0017134]; identical protein binding [GO:0042802]; protein kinase binding [GO:0019901]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]; translation initiation factor binding [GO:0031369] | PF01090; | 1.10.10.10; | Eukaryotic ribosomal protein eS19 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P39019}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P39019}. | null | null | null | null | null | FUNCTION: Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Required for pre-rRNA processing and maturation of 40S ribosomal subunits. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribo... | Rattus norvegicus (Rat) |
P17076 | RL8A_YEAST | MAPGKKVAPAPFGAKSTKSNKTRNPLTHSTPKNFGIGQAVQPKRNLSRYVKWPEYVRVQRQKKILSIRLKVPPTIAQFQYTLDRNTAAETFKLFNKYRPETAAEKKERLTKEAAAVAEGKSKQDASPKPYAVKYGLNHVVALIENKKAKLVLIANDVDPIELVVFLPALCKKMGVPYAIVKGKARLGTLVNQKTSAVAALTEVRAEDEAALAKLVSTIDANFADKYDEVKKHWGGGILGNKAQAKMDKRAKNSDSA | null | null | cytoplasmic translation [GO:0002181]; maturation of LSU-rRNA [GO:0000470] | cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF01248; | 3.30.1330.30; | Eukaryotic ribosomal protein eL8 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17081 | RHOQ_HUMAN | MAHGPGALMLKCVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVSVTVGGKQYLLGLYDTAGQEDYDRLRPLSYPMTDVFLICFSVVNPASFQNVKEEWVPELKEYAPNVPFLLIGTQIDLRDDPKTLARLNDMKEKPICVEQGQKLAKEIGACCYVECSALTQKGLKTVFDEAIIAILTPKKHTVKKRIGSRCINCCLIT | null | null | actin filament organization [GO:0007015]; cellular response to insulin stimulus [GO:0032869]; cortical actin cytoskeleton organization [GO:0030866]; endocytosis [GO:0006897]; establishment or maintenance of cell polarity [GO:0007163]; GTP metabolic process [GO:0046039]; insulin receptor signaling pathway [GO:0008286]; ... | actin filament [GO:0005884]; extracellular exosome [GO:0070062]; Golgi-associated vesicle membrane [GO:0030660]; membrane raft [GO:0045121]; plasma membrane [GO:0005886] | GBD domain binding [GO:0032427]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; profilin binding [GO:0005522]; protein kinase binding [GO:0019901] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rho family | PTM: May be post-translationally modified by both palmitoylation and polyisoprenylation. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15546864}. Cell membrane {ECO:0000269|PubMed:15546864}; Lipid-anchor {ECO:0000269|PubMed:15546864}. | null | null | null | null | null | FUNCTION: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. May play a role in CFTR trafficking to the plasma membra... | Homo sapiens (Human) |
P17086 | URE1_PROMH | MKTISRQAYADMFGPTTGDRLRLADTELFLEIEKDFTTYGEEVKFGGGKVIRDGMGQSQVVSAECVDVLITNAIILDYWGIVKADIGIKDGRIVGIGKAGNPDVQPNVDIVIGPGTEVVAGEGKIVTAGGIDTHIHFICPQQAQEGLVSGVTTFIGGGTGPVAGTNATTVTPGIWNMYRMLEAVDELPINVGLFGKGCVSQPEAIREQITAGAIGLKIHEDWGATPMAIHNCLNVADEMDVQVAIHSDTLNEGGFYEETVKAIAGRVIHVFHTEGAGGGHAPDVIKSVGEPNILPASTNPTMPYTINTVDEHLDMLMVCH... | 3.5.1.5 | COFACTOR: Name=Ni cation; Xref=ChEBI:CHEBI:25516; Evidence={ECO:0000255|HAMAP-Rule:MF_01953}; Note=Binds 2 nickel ions per subunit. {ECO:0000255|HAMAP-Rule:MF_01953}; | urea catabolic process [GO:0043419] | cytoplasm [GO:0005737] | nickel cation binding [GO:0016151]; urease activity [GO:0009039] | PF01979;PF00449; | 3.20.20.140;2.30.40.10; | Metallo-dependent hydrolases superfamily, Urease alpha subunit family | PTM: Carboxylation allows a single lysine to coordinate two nickel ions. {ECO:0000255|HAMAP-Rule:MF_01953}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01953}. | CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:7559355, ECO:0000269|PubMed:8500894}; | null | PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01953}. | null | null | null | Proteus mirabilis (strain HI4320) |
P17095 | HMGA1_MOUSE | MSESGSKSSQPLASKQEKDGTEKRGRGRPRKQPPVSPGTALVGSQKEPSEVPTPKRPRGRPKGSKNKGAAKTRKVTTAPGRKPRGRPKKLEKEEEEGISQESSEEEQ | null | null | autophagy [GO:0006914]; B cell differentiation [GO:0030183]; cell population proliferation [GO:0008283]; chromatin organization [GO:0006325]; erythrocyte differentiation [GO:0030218]; gene expression [GO:0010467]; glucose homeostasis [GO:0042593]; heart development [GO:0007507]; inflammatory cell apoptotic process [GO:... | cytoplasm [GO:0005737]; male germ cell nucleus [GO:0001673]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]; senescence-associated heterochromatin focus [GO:0035985]; SUMO ligase complex [GO:0106068] | chromatin binding [GO:0003682]; D-loop DNA binding [GO:0062037]; DNA binding [GO:0003677]; minor groove of adenine-thymine-rich DNA binding [GO:0003680]; nuclear receptor coactivator activity [GO:0030374]; nuclear retinoic acid receptor binding [GO:0042974]; nuclear retinoid X receptor binding [GO:0046965]; peroxisome ... | null | null | HMGA family | PTM: Isoforms HMG-I and HMG-Y can be phosphorylated by HIPK2. Phosphorylation may modulate DNA-binding affinity (By similarity). {ECO:0000250}.; PTM: Methylation at Arg-58 is mutually exclusive with methylation at Arg-60. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: HMG-I/Y bind preferentially to the minor groove of A+T rich regions in double-stranded DNA. It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximi... | Mus musculus (Mouse) |
P17096 | HMGA1_HUMAN | MSESSSKSSQPLASKQEKDGTEKRGRGRPRKQPPVSPGTALVGSQKEPSEVPTPKRPRGRPKGSKNKGAAKTRKTTTTPGRKPRGRPKKLEKEEEEGISQESSEEEQ | null | null | base-excision repair [GO:0006284]; DNA unwinding involved in DNA replication [GO:0006268]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-templated transcription [GO:0045892]; nucleosome disassembly [GO:0006337]; oncogene-induced cell senescence [GO:0090402]; positive regu... | cytosol [GO:0005829]; focal adhesion [GO:0005925]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]; senescence-associated heterochromatin focus [GO:0035985]; transcription regulator complex [GO:0005667] | 5'-deoxyribose-5-phosphate lyase activity [GO:0051575]; chromatin binding [GO:0003682]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA binding, bending [GO:0008301]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; enzyme binding [GO:0019899]; mino... | null | null | HMGA family | PTM: Constitutively phosphorylated on two or three sites. Hyperphosphorylated at early stages of apoptosis, followed by dephosphorylation and methylation, which coincides with chromatin condensation. Isoforms HMG-I and HMG-Y can be phosphorylated by HIPK2. Phosphorylation of HMG-I at Ser-36, Thr-53 and Thr-78 and of HM... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: HMG-I/Y bind preferentially to the minor groove of A+T rich regions in double-stranded DNA. It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximi... | Homo sapiens (Human) |
P17099 | HBEAG_HBVA4 | MQLFHLCLIISCTCPTVQASKLCLGWLWGMDIDPYKEFGATVELLSFLPSDFFPSVRDLLDTASALYREALESPEHCSPHHTALRQAILCWGELMTLATWVGNNLEDPASRDLVVNYVNTNMGLKIRQLLWFRISYLTFGRETVLEYLVSFGVWIRTPPAYRPPNAPILSTLPETTVVRRRDRGRSPRRRTPSPRRRRSQSPRRRRSQSRESQC | null | null | microtubule-dependent intracellular transport of viral material towards nucleus [GO:0075521]; symbiont entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732]; virus-mediated perturbation of host defense response [GO:0019049] | extracellular region [GO:0005576]; host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; T=4 icosahedral viral capsid [GO:0039619] | DNA binding [GO:0003677]; RNA binding [GO:0003723]; structural molecule activity [GO:0005198] | PF08290;PF00906; | 1.10.4090.10; | Orthohepadnavirus precore antigen family | PTM: Phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04076}.; PTM: Cleaved by host furin. {ECO:0000255|HAMAP-Rule:MF_04076}. | SUBCELLULAR LOCATION: Secreted {ECO:0000255|HAMAP-Rule:MF_04076}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04076}. | null | null | null | null | null | FUNCTION: May regulate immune response to the intracellular capsid in acting as a T-cell tolerogen, by having an immunoregulatory effect which prevents destruction of infected cells by cytotoxic T-cells. This immune regulation may predispose to chronicity during perinatal infections and prevent severe liver injury duri... | Hepatitis B virus genotype A2 subtype adw2 (isolate Germany/991/1990) (HBV-A) |
P17101 | HBSAG_HBVA4 | MGGWSSKPRKGMGTNLSVPNPLGFFPDHQLDPVFGANSNNPDWDFNPIKDHWPAANQVGVGAFGPGFTPPHGGVLGWSPQAQGMLTPVSTIPPPASANRQSGRQPTPISPPLRDSHPQAMQWNSTAFHQALQDPRVRGLYFPAGGSSSGTVNPAPNIASHISSISARTGDPVTNMENITSGFLGPLPVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGSPVCLGQNSRSPTSNHSPTSCPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLILGSTTTSTGPCKTCTTPAQGNSMFPSCCCTKPTDGN... | null | null | caveolin-mediated endocytosis of virus by host cell [GO:0075513]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062] | membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00695; | null | Orthohepadnavirus major surface antigen family | PTM: Isoform M is N-terminally acetylated by host at a ratio of 90%, and N-glycosylated by host at the pre-S2 region. {ECO:0000250|UniProtKB:P03138, ECO:0000255|HAMAP-Rule:MF_04075}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04075}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04075}. | null | null | null | null | null | FUNCTION: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specifici... | Hepatitis B virus genotype A2 subtype adw2 (isolate Germany/991/1990) (HBV-A) |
P17105 | IP3KA_RAT | MTLPGHPTGMARPRGAGPCSPGLERAPRRSVGELRLLFEARCAAVAAAAAAGEPRARGAKRRGGQVPNGLPRAAPAPVIPQLTVTSEEDVAPASPGPPDREGNWLPAAGSHLQQPRRLSTSSLSSTGSSSLLEDSEDDLLSDSESRSRGNVQLETSEDVGQKSHWQKIRTMVNLPVMSPFKKRYSWVQLAGHTGSFKAAGTSGLILKRSSEPEHYCLVRLMADVLRGCVPAFHGVVERDGESYLQLQDLLDGFDGPCVLDCKMGVRTYLEEELTKARERPKLRKDMYKKMLAVDPEAPTEEEHAQRAVTKPRYMQWREGI... | 2.7.1.127 | null | actin cytoskeleton organization [GO:0030036]; cellular response to calcium ion [GO:0071277]; dendritic spine maintenance [GO:0097062]; inositol metabolic process [GO:0006020]; inositol phosphate biosynthetic process [GO:0032958]; modification of postsynaptic actin cytoskeleton [GO:0098885]; phosphatidylinositol phospha... | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; nucleus [GO:0005634]; postsynaptic actin cytoskeleton [GO:0098871] | ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; inositol tetrakisphosphate kinase activity [GO:0051765]; inositol-1,4,5-trisphosphate 3-kinase activity [GO:0008440]; small GTPase binding [GO:0031267] | PF03770; | 3.30.470.160; | Inositol phosphokinase (IPK) family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P23677}. | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:11020, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57895, ChEBI:CHEBI:203600, ChEBI:CHEBI:456216; EC=2.7.1.127; Evidence={ECO:0000269|PubMed:7646431}; PhysiologicalDirect... | null | null | null | null | FUNCTION: Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate and participates to the regulation of calcium homeostasis. {ECO:0000269|PubMed:7646431}. | Rattus norvegicus (Rat) |
P17106 | CBF1_YEAST | MNSLANNNKLSTEDEEIHSARKRGYNEEQNYSEARKKQRDQGLLSQESNDGNIDSALLSEGATLKGTQSQYESGLTSNKDEKGSDDEDASVAEAAVAATVNYTDLIQGQEDSSDAHTSNQTNANGEHKDSLNGERAITPSNEGVKPNTSLEGMTSSPMESTQQSKNDMLIPLAEHDRGPEHQQDDEDNDDADIDLKKDISMQPGRRGRKPTTLATTDEWKKQRKDSHKEVERRRRENINTAINVLSDLLPVRESSKAAILACAAEYIQKLKETDEANIEKWTLQKLLSEQNASQLASANEKLQEELGNAYKEIEYMKRVL... | null | null | chromatin remodeling [GO:0006338]; chromosome segregation [GO:0007059]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of sulfur metabolic process [GO:0042762]; regulation of transcription by RNA polymerase II [G... | Cbf1-Met4-Met28 complex [GO:0089713]; chromosome, centromeric region [GO:0000775]; kinetochore [GO:0000776]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | centromeric DNA binding [GO:0019237]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; protein dimerization activity [GO:0046983]; RNA poly... | PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Mitochondrion {ECO:0000269|PubMed:14576278}. Chromosome, centromere {ECO:0000269|PubMed:2185892}. | null | null | null | null | null | FUNCTION: Required for chromosome stability and methionine prototrophy. It is involved in chromosomal segregation. Binds to a highly conserved DNA sequence (5'-RTCACRTG-3'), called CDEI, found in centromeres and in several promoters. DNA-binding activity is enhanced by MET28. Required as an auxiliary factor for transcr... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17108 | IL2_RAT | MYSMQLASCVALTLVLLVNSAPTSSPAKETQQHLEQLLLDLQVLLRGIDNYKNLKLPMMLTFKFYLPKQATELKHLQCLENELGALQRVLDLTQSKSFHLEDAGNFISNIRVTVVKLKGSENKFECQFDDEPATVVEFLRRWIAICQSIISTMTQ | null | null | activated T cell proliferation [GO:0050798]; adaptive immune response [GO:0002250]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; G protein-coupled receptor signaling pathway [GO:0007186]; gene expression [GO:0010467]; interleukin-2-mediated signaling pathway [GO:0038110]; leukocyte activatio... | extracellular space [GO:0005615] | carbohydrate binding [GO:0030246]; cytokine activity [GO:0005125]; glycosphingolipid binding [GO:0043208]; growth factor activity [GO:0008083]; interleukin-2 receptor binding [GO:0005134]; kappa-type opioid receptor binding [GO:0031851] | PF00715; | 1.20.1250.10; | IL-2 family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Cytokine produced by activated CD4-positive helper T-cells and to a lesser extend activated CD8-positive T-cells and natural killer (NK) cells that plays pivotal roles in the immune response and tolerance. Binds to a receptor complex composed of either the high-affinity trimeric IL-2R (IL2RA/CD25, IL2RB/CD122... | Rattus norvegicus (Rat) |
P17109 | MEND_ECOLI | MSVSAFNRRWAAVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVAVIVTSGTAVANLYPALIEAGLTGEKLILLTADRPPELIDCGANQAIRQPGMFASHPTHSISLPRPTQDIPARWLVSTIDHALGTLHAGGVHINCPFAEPLYGEMDDTGLSWQQRLGDWWQDDKPWLREAPRLESEKQRDWFFWRQKRGVVVAGRMSAEEGKKVALWAQTLGWPLIGDVLSQTGQPLPCADLWLGNAKATSELQQAQIVVQLGSSLTGKRLLQWQASCEPEEYWIVDDIEGRLDPAH... | 2.2.1.9 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01659}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_01659}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000255|HAMAP-Rule:MF_01659}; Note=Binds 1 thiamine pyrophosphate per sub... | menaquinone biosynthetic process [GO:0009234] | null | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity [GO:0070204]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; protein homodimerization activity [GO:0042803]; thiamine pyrophosphate binding [GO:0030976] | PF02775;PF16582;PF02776; | 3.40.50.970;3.40.50.1220; | TPP enzyme family, MenD subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2; Xref=Rhea:RHEA:25593, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29780, ChEBI:CHEBI:58818; EC=2.2.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01659, ECO:000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=53 nM for isochorismate (at 22.5 degrees Celsius and pH 7.8) {ECO:0000269|PubMed:14621995, ECO:0000269|PubMed:17760421}; KM=1.5 uM for 2-oxoglutarate (at 22.5 degrees Celsius and pH 7.8) {ECO:0000269|PubMed:14621995, ECO:0000269|PubMed:17760421}; KM=2.4 uM for thia... | PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_01659}.; PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01659}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8. {ECO:0000269|PubMed:14621995, ECO:0000269|PubMed:17760421}; | null | FUNCTION: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). {ECO:0000255|HAMAP-Rule:MF_01659, E... | Escherichia coli (strain K12) |
P17115 | GUTQ_ECOLI | MSEALLNAGRQTLMLELQEASRLPERLGDDFVRAANIILHCEGKVVVSGIGKSGHIGKKIAATLASTGTPAFFVHPAEALHGDLGMIESRDVMLFISYSGGAKELDLIIPRLEDKSIALLAMTGKPTSPLGLAAKAVLDISVEREACPMHLAPTSSTVNTLMMGDALAMAVMQARGFNEEDFARSHPAGALGARLLNKVHHLMRRDDAIPQVALTASVMDAMLELSRTGLGLVAVCDAQQQVQGVFTDGDLRRWLVGGGALTTPVNEAMTVGGTTLQSQSRAIDAKEILMKRKITAAPVVDENGKLTGAINLQDFYQAGI... | 5.3.1.13 | null | keto-3-deoxy-D-manno-octulosonic acid biosynthetic process [GO:0019294]; protein homotetramerization [GO:0051289]; single-species biofilm formation [GO:0044010] | null | arabinose-5-phosphate isomerase activity [GO:0019146]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF00571;PF01380; | 3.10.580.10; | SIS family, GutQ/KpsF subfamily | null | null | CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:23104, ChEBI:CHEBI:57693, ChEBI:CHEBI:58121; EC=5.3.1.13; Evidence={ECO:0000269|PubMed:16199563}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23105; Evidence={ECO:0000269|PubMed:16199563}; PhysiologicalDirection=right... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.64 mM for Ru5P (at pH 8.25 and at 37 degrees Celsius) {ECO:0000269|PubMed:16199563}; KM=1.2 mM for A5P (at pH 8.25 and at 37 degrees Celsius) {ECO:0000269|PubMed:16199563}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.25. {ECO:0000269|PubMed:16199563}; | null | FUNCTION: Catalyzes the reversible aldol-ketol isomerization between D-ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P). It appears that the physiological function of G-API may be to synthesize the regulatory molecule A5P, which in turn participates in the induction of the gut operon through an unknown mec... | Escherichia coli (strain K12) |
P17117 | NFSA_ECOLI | MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR | 1.-.-.- | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:11034992, ECO:0000269|PubMed:8755878}; Note=Binds 1 FMN per monomer. {ECO:0000269|PubMed:11034992}; | null | cytosol [GO:0005829] | chromate reductase activity [GO:0034567]; FMN binding [GO:0010181]; NAD(P)H dehydrogenase (quinone) activity [GO:0003955]; protein homodimerization activity [GO:0042803] | PF00881; | 3.40.109.10; | Flavin oxidoreductase frp family | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11 uM for NADPH {ECO:0000269|PubMed:8755878}; KM=5.5 uM for nitrofurazone {ECO:0000269|PubMed:8755878}; | null | null | null | FUNCTION: Catalyzes the reduction of nitroaromatic compounds using NADPH. Has a broad electron acceptor specificity. Reduces nitrofurazone by a ping-pong bi-bi mechanism possibly to generate a two-electron transfer product. Major oxygen-insensitive nitroreductase in E.coli. {ECO:0000269|PubMed:8755878}. | Escherichia coli (strain K12) |
P17119 | KAR3_YEAST | MESLPRTPTKGRSTQHLSTPSPKNDILAMNGHKRRNTTTPPPKHTLLKPQRTDIHRHSLASQSRISMSPNRELLKNYKGTANLIYGNQKSNSGVTSFYKENVNELNRTQAILFEKKATLDLLKDELTETKEKINAVNLKFETLREEKIKIEQQLNLKNNELISIKEEFLSKKQFMNEGHEIHLKQLAASNKKELKQMENEYKTKIEKLKFMKIKQFENERASLLDKIEEVRNKITMNPSTLQEMLNDVEQKHMLEKEEWLTEYQSQWKKDIELNNKHMQEIESIKKEIENTLKPELAEKKKLLTEKRNAYEAIKVKVKEK... | 5.6.1.4 | null | cell division [GO:0051301]; karyogamy involved in conjugation with cellular fusion [GO:0000742]; meiotic cell cycle [GO:0051321]; microtubule bundle formation involved in mitotic spindle midzone assembly [GO:1903562]; mitotic cell cycle [GO:0000278]; mitotic sister chromatid cohesion [GO:0007064]; nuclear migration inv... | chromosome [GO:0005694]; cytoplasmic microtubule [GO:0005881]; microtubule [GO:0005874]; nucleus [GO:0005634]; spindle pole [GO:0000922]; spindle pole body [GO:0005816] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; minus-end-directed microtubule motor activity [GO:0008569] | PF00225; | 3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, NCD subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:10087265, ECO:0000269|PubMed:11729143, ECO:0000269|PubMed:25313961}. Nucleus {ECO:0000269|PubMed:11729143, ECO:0000269|PubMed:17620411}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11729143, ECO:0000269|P... | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:11387196, ECO:0000269|PubMed:17382884, ECO:0000269|PubMed:22734002, ECO:0000269|PubMed:9859995}; Physiologic... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12.2 uM for MgATP {ECO:0000269|PubMed:17382884}; KM=18.6 uM for MgATP in complex with CIK1 {ECO:0000269|PubMed:17382884}; KM=15 uM for MgATP in complex with VIK1 {ECO:0000269|PubMed:17382884}; Note=kcat is 0.49 sec(-1) with MgATP as substrate (PubMed:17382884). kca... | null | null | null | FUNCTION: Minus end-directed microtubule (MT) motor involved in spindle midzone assembly, poleward transport of newly captured kinetochores along the lateral side of MTs, karyogamy (nuclear fusion) during mating, and with an essential function in meiosis I (PubMed:11387196, PubMed:11729143, PubMed:17382884, PubMed:1762... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17120 | BIMC_EMENI | MAGPQRATSGLPTRRTTTRQPTRRAGSAIPERQTSTASPAVSTKTAAISRTRTLKSPGEPASVLAKRKERDIEREINEDTSIHVVVRCRGRNEREVKENSGVVLQTEGVKGKTVELSMGPNAVSNKTYTFDKVFSAAADQITVYEDVVLPIVTEMLAGYNCTIFAYGQTGTGKTYTMSGDMTDTLGILSDNAGIIPRVLYSLFAKLADTESTVKCSFIELYNEELRDLLSAEENPKLKIYDNEQKKGHMSTLVQGMEETYIDSATAGIKLLQQGSHKRQVAATKCNDLSSRSHTVFTITVNIKRTTESGEEYVCPGKLNL... | null | null | cell division [GO:0051301]; initial mitotic spindle pole body separation [GO:0000073]; microtubule-based movement [GO:0007018]; mitotic spindle assembly [GO:0090307]; mitotic spindle disassembly [GO:0051228]; spindle elongation [GO:0051231] | cytoplasm [GO:0005737]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; spindle microtubule [GO:0005876] | ATP binding [GO:0005524]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; minus-end-directed microtubule motor activity [GO:0008569]; molecular adaptor activity [GO:0060090]; plus-end-directed microtubule motor activity [GO:0008574] | PF00225;PF13931; | 3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, BimC subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. | null | null | null | null | null | FUNCTION: Important role in mitotic dividing cells. Microtubule motor required for spindle body separation. | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
P17124 | HRH2_CANLF | MISNGTGSSFCLDSPPCRITVSVVLTVLILITIAGNVVVCLAVGLNRRLRSLTNCFIVSLAITDLLLGLLVLPFSAFYQLSCRWSFGKVFCNIYTSLDVMLCTASILNLFMISLDRYCAVTDPLRYPVLITPVRVAVSLVLIWVISITLSFLSIHLGWNSRNETSSFNHTIPKCKVQVNLVYGLVDGLVTFYLPLLVMCITYYRIFKIARDQAKRIHHMGSWKAATIGEHKATVTLAAVMGAFIICWFPYFTVFVYRGLKGDDAINEAFEAVVLWLGYANSALNPILYATLNRDFRTAYQQLFRCRPASHNAQETSLRSN... | null | null | chemical synaptic transmission [GO:0007268]; G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger [GO:0007187]; gastric acid secretion [GO:0001696]; positive regulation of vasoconstriction [GO:0045907] | dendrite [GO:0030425]; plasma membrane [GO:0005886]; synapse [GO:0045202] | G protein-coupled serotonin receptor activity [GO:0004993]; histamine receptor activity [GO:0004969]; neurotransmitter receptor activity [GO:0030594] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: The H2 subclass of histamine receptors mediates gastric acid secretion. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. | Canis lupus familiaris (Dog) (Canis familiaris) |
P17125 | TGFB3_MOUSE | MHLQRALVVLALLNLATISLSLSTCTTLDFGHIKKKRVEAIRGQILSKLRLTSPPEPSVMTHVPYQVLALYNSTRELLEEMHGEREEGCTQETSESEYYAKEIHKFDMIQGLAEHNELAVCPKGITSKVFRFNVSSVEKNGTNLFRAEFRVLRVPNPSSKRTEQRIELFQILRPDEHIAKQRYIGGKNLPTRGTAEWLSFDVTDTVREWLLRRESNLGLEISIHCPCHTFQPNGDILENVHEVMEIKFKGVDNEDDHGRGDLGRLKKQKDHHNPHLILMMIPPHRLDSPGQGSQRKKRALDTNYCFRNLEENCCVRPLYI... | null | null | animal organ morphogenesis [GO:0009887]; cell population proliferation [GO:0008283]; cell-cell junction organization [GO:0045216]; cellular response to growth factor stimulus [GO:0071363]; detection of hypoxia [GO:0070483]; embryonic neurocranium morphogenesis [GO:0048702]; epithelial cell proliferation [GO:0050673]; f... | cell surface [GO:0009986]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; secretory granule [GO:0030141]; T-tubule [GO:0030315] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; protein-containing complex binding [GO:0044877]; transforming growth factor beta binding [GO:0050431]; type I transforming growth factor beta receptor binding [GO:0034713]; type II transforming growth factor bet... | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | PTM: Transforming growth factor beta-3 proprotein: The precursor proprotein is cleaved in the Golgi apparatus to form Transforming growth factor beta-3 (TGF-beta-3) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-3 inactive. {ECO:0000250|UniProtKB:P01137}.; PTM: Methy... | SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-3]: Secreted {ECO:0000250|UniProtKB:P01137}. | null | null | null | null | null | FUNCTION: Transforming growth factor beta-3 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-3 (TGF-beta-3) chains, which constitute the regulatory and active subunit of TGF-beta-3, respectively. {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202}.; FUNCTION: [L... | Mus musculus (Mouse) |
P17133 | RU17_DROME | MTQYLPPNLLALFAAREPIPFMPPVDKLPHEKKSRGYLGVAKFMADFEDPKDTPLPKTVETRQERLERRRREKAEQVAYKLEREIALWDPTEIKNATEDPFRTLFIARINYDTSESKLRREFEFYGPIKKIVLIHDQESGKPKGYAFIEYEHERDMHAAYKHADGKKIDSKRVLVDVERARTVKGWLPRRLGGGLGGTRRGGNDVNIKHSGREDNERERERYRLEREREDREGPGRGGGSNGLDARPGRGFGAERRRSRSRERRDRERDRGRGAVASNGRSRSRSRERRKRRAGSRERYDEFDRRDRRDRERERDRDRER... | null | null | mRNA splicing, via spliceosome [GO:0000398]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; oogenesis [GO:0048477]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of RNA splicing [GO:0043484]; spermatogenesis [GO:0007283] | catalytic step 2 spliceosome [GO:0071013]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; precatalytic spliceosome [GO:0071011]; spliceosomal complex [GO:0005681]; U1 snRNP [GO:0005685]; U2-type prespliceosome [GO:0071004] | mRNA binding [GO:0003729]; RNA binding [GO:0003723]; U1 snRNA binding [GO:0030619] | PF00076;PF12220; | 3.30.70.330; | null | null | SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q62376}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q62376}. | null | null | null | null | null | FUNCTION: Mediates the splicing of pre-mRNA by binding to the stem loop I region of U1-snRNA (PubMed:15611175). Required during oogenesis for nurse cell chromatin dispersal (PubMed:24244416). {ECO:0000269|PubMed:15611175, ECO:0000269|PubMed:24244416}. | Drosophila melanogaster (Fruit fly) |
P17136 | RSMB_RAT | MTVGKSSKMLQHIDYRMRCILQDGRIFIGTFKAFDKHMNLILCDCDEFRKIKPKNSKQAEREEKRVLGLVLLRGENLVSMTVEGPPPKDTGIARVPLAGAAGGPGIGRAAGRGIPAGVPMPQAPAGLAGPVRGVGGPSQQVMTPQGRGTVAAAAAAATASIAGAPTQYPPGRGGPPPPMGRGAPPPGMMGPPPGMRPPMGPPMGIPPGRGTPMGMPPPGMRPPPPGMRGLL | null | null | mRNA splicing, via spliceosome [GO:0000398]; spliceosomal snRNP assembly [GO:0000387] | catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; histone pre-mRNA 3'end processing complex [GO:0071204]; methylosome [GO:0034709]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SMN-Sm protein complex [GO:0034719]; spliceosomal complex [GO:0005681]; telomerase holoenzyme complex... | histone pre-mRNA DCP binding [GO:0071208]; RNA binding [GO:0003723]; telomerase RNA binding [GO:0070034]; U1 snRNP binding [GO:1990446]; U2 snRNP binding [GO:1990447] | PF01423; | 2.30.30.100; | SnRNP SmB/SmN family | PTM: Methylated by PRMT5 (By similarity). Arg-108 and Arg-112 are dimethylated, probably to asymmetric dimethylarginine (By similarity). {ECO:0000250|UniProtKB:P14678, ECO:0000250|UniProtKB:P27048}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P14678}. Nucleus {ECO:0000250|UniProtKB:P14678}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000250|UniProtKB:P14678}. | null | null | null | null | null | FUNCTION: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (By similarity). Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes (By similarity). As a c... | Rattus norvegicus (Rat) |
P17139 | CO4A1_CAEEL | MSRLSLLGLTAAVVLLSSFCQDRIHVDAAAACKGCAPPCVCPGTKGERGNPGFGGEPGHPGAPGQDGPEGAPGAPGMFGAEGDFGDMGSKGARGDRGLPGSPGHPGLQGLDGLPGLKGEEGIPGCNGTDGFPGMPGLAGPPGQSGQNGNPGRPGLSGPPGEGGVNSQGRKGVKGESGRSGVPGLPGNSGYPGLKGAKGDPGPYGLPGFPGVSGLKGRMGVRTSGVKGEKGLPGPPGPPGQPGSYPWASKPIEMEVLQGPVGPAGVKGEKGRDGPVGPPGMLGLDGPPGYPGLKGQKGDLGDAGQRGKRGKDGVPGNYGEK... | null | null | embryo development ending in birth or egg hatching [GO:0009792]; extracellular matrix organization [GO:0030198]; muscle organ development [GO:0007517]; nematode larval development [GO:0002119]; positive regulation of axon regeneration [GO:0048680]; positive regulation of protein secretion [GO:0050714]; response to sero... | basement membrane [GO:0005604]; collagen trimer [GO:0005581]; extracellular space [GO:0005615] | extracellular matrix structural constituent [GO:0005201]; extracellular matrix structural constituent conferring tensile strength [GO:0030020] | PF01413;PF01391; | 2.170.240.10; | Type IV collagen family | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.; PTM: Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known typ... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. | null | null | null | null | null | FUNCTION: Collagen type IV is specific for basement membranes (Probable). Required to restrict presynaptic growth at the neuromuscular junctions (NMJ) in late larval stage and in adult motor neurons (PubMed:25080592). May play a role in axon regeneration in embryos following injury in D-type motor neurons (PubMed:27984... | Caenorhabditis elegans |
P17140 | CO4A2_CAEEL | MKQRAALGPVLRLAILALLAVSYVQSQATCRDCSNRGCFCVGEKGSMGAPGPQGPPGTQGIRGFPGPEGLAGPKGLKGAQGPPGPVGIKGDRGAVGVPGFPGNDGGNGRPGEPGPPGAPGWDGCNGTDGAPGIPGRPGPPGMPGFPGPPGMDGLKGEPAIGYAGAPGEKGDGGMPGMPGLPGPSGRDGYPGEKGDRGDTGNAGPRGPPGEAGSPGNPGIGSIGPKGDPGDLGSVGPPGPPGPREFTGSGSIVGPRGNPGEKGDKGEPGEGGQRGYPGNGGLSGQPGLPGMKGEKGLSGPAGPRGKEGRPGNAGPPGFKGD... | null | null | cellular component organization [GO:0016043]; embryo development ending in birth or egg hatching [GO:0009792]; extracellular matrix organization [GO:0030198]; gonad morphogenesis [GO:0035262]; protein localization [GO:0008104]; regulation of distal tip cell migration [GO:1903354] | basement membrane [GO:0005604]; collagen type IV trimer [GO:0005587]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615] | extracellular matrix structural constituent [GO:0005201]; extracellular matrix structural constituent conferring tensile strength [GO:0030020] | PF01413;PF01391; | 2.170.240.10; | Type IV collagen family | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000255|PROSITE-ProRule:PRU00736}.; PTM: Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000255|PROSITE-ProRule:PRU00736, ECO:0000269|PubMed:19104038}. | null | null | null | null | null | FUNCTION: Collagen type IV is specific for basement membranes (Probable). Together with fbl-1 and downstream of metalloprotease mig-17, recruits nidogen nid-1 to the gonad basement membrane thereby probably inducing basement membrane remodeling required for the directional migration of distal tip cells (PubMed:19104038... | Caenorhabditis elegans |
P17151 | EP84_HCMVA | MDLPTTVVRKYWTFANPNRILHQSVNQTFDVRQFVFDTARLVNCVDGDGKVLHLNKGWLCATIMQHGEASAGAKTQQGFMSIDITGDGELQEHLFVRGGIVFNKSVSSVVGSSGPNESALLTMISENGNLQVTYVRHYLKNHGESSSGGGGCGAASTASAVCVSSLGGSGGTRDGPSAEEQQRRRQEQRHEERRKKSSSSAGGGGGGGAGGGGGGGGSGGQHSSDSANGLLRDPRLMNRQKERRPPPSSENDGSPPLREAKRQKTTAQHEGHGGGGKNETEQQSGGAGGGGGGGSGRMSLPLDTSEAVAFLNYSSSSSAV... | null | null | bidirectional double-stranded viral DNA replication [GO:0039686] | host cell nucleus [GO:0042025]; virion component [GO:0044423] | null | PF03064; | null | Herpesviridae U79/UL112 family | PTM: The isoforms p34, p43, p50 and p84 are cleaved by host calpain-1/CAPN1 and calpain-2/CAPN2 to generate p20, p26 and p28. | SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:16501081, ECO:0000269|PubMed:2824853}. Virion {ECO:0000269|PubMed:2824853}. Note=Found in subnuclear structures known as promyelocytic leukemia oncogenic domains (PODs) or nuclear domain 10 (ND10) during the early stages of viral infection (PubMed:16501081).; SUBCE... | null | null | null | null | null | FUNCTION: Promotes efficient viral DNA replication. Recruits the DNA polymerase processivity factor to pre-replication foci. {ECO:0000269|PubMed:16501081}. | Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5) |
P17152 | TMM11_HUMAN | MAAWGRRRLGPGSSGGSARERVSLSATDCYIVHEIYNGENAQDQFEYELEQALEAQYKYIVIEPTRIGDETARWITVGNCLHKTAVLAGTACLFTPLALPLDYSHYISLPAGVLSLACCTLYGISWQFDPCCKYQVEYDAYKLSRLPLHTLTSSTPVVLVRKDDLHRKRLHNTIALAALVYCVKKIYELYAV | null | null | inner mitochondrial membrane organization [GO:0007007]; mitochondrion organization [GO:0007005] | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | null | PF14972; | null | TMEM11 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:21274005}; Multi-pass membrane protein {ECO:0000269|PubMed:21274005}. | null | null | null | null | null | FUNCTION: Plays a role in mitochondrial morphogenesis. {ECO:0000269|PubMed:21274005}. | Homo sapiens (Human) |
P17153 | ANXA5_CHICK | MAKYTRGTVTAFSPFDARADAEALRKAMKGMGTDEETILKILTSRNNAQRQEIASAFKTLFGRDLVDDLKSELTGKFETLMVSLMRPARIFDAHALKHAIKGAGTNEKVLTEILASRTPAEVQNIKQVYMQEYEANLEDKITGETSGHFQRLLVVLLQANRDPDGRVDEALVEKDAQVLFRAGELKWGTDEETFITILGTRSVSHLRRVFDKYMTISGFQIEETIDRETSGDLEKLLLAVVKCIRSVPAYFAETLYYSMKGAGTDDDTLIRVMVSRSEIDLLDIRHEFRKNFAKSLYQMIQKDTSGDYRKALLLLCGGDD... | null | null | calcium ion homeostasis [GO:0055074]; negative regulation of coagulation [GO:0050819] | calcium channel complex [GO:0034704]; cytoplasm [GO:0005737]; sarcolemma [GO:0042383]; vesicle [GO:0031982] | calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; phosphatidylserine binding [GO:0001786] | PF00191; | 1.10.220.10; | Annexin family | null | null | null | null | null | null | null | FUNCTION: Collagen-binding protein. | Gallus gallus (Chicken) |
P17156 | HSP72_MOUSE | MSARGPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQSDMKHWPFRVVSEGGKPKVQVEYKGEMKTFFPEEISSMVLTKMKEIAEAYLGGKVQSAVITVPAYFNDSQRQATKDAGTITGLNVLRIINEPTAAAIAYGLDKKGCAGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHLAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPV... | null | null | chaperone cofactor-dependent protein refolding [GO:0051085]; male meiosis I [GO:0007141]; male meiotic nuclear division [GO:0007140]; negative regulation of inclusion body assembly [GO:0090084]; positive regulation of ATP-dependent activity [GO:0032781]; positive regulation of ATPase-coupled calcium transmembrane trans... | CatSper complex [GO:0036128]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; male germ cell nucleus [GO:0001673]; meiotic spindle [GO:0072687]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; synaptonemal com... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; disordered domain specific binding [GO:0097718]; enzyme binding [GO:0019899]; glycolipid binding [GO:0051861]; heat shock protein binding [GO:0031072]; protein folding chaperone [GO:0044183]; protein-fo... | PF00012; | 1.20.1270.10;3.30.30.30;3.30.420.40; | Heat shock protein 70 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:24557841}. Note=Colocalizes with SHCBP1L at spindle during the meiosis process (PubMed:24557841). {ECO:0000269|PubMed:24557841}. | null | null | null | null | null | FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in th... | Mus musculus (Mouse) |
P17157 | PHO85_YEAST | MSSSSQFKQLEKLGNGTYATVYKGLNKTTGVYVALKEVKLDSEEGTPSTAIREISLMKELKHENIVRLYDVIHTENKLTLVFEFMDNDLKKYMDSRTVGNTPRGLELNLVKYFQWQLLQGLAFCHENKILHRDLKPQNLLINKRGQLKLGDFGLARAFGIPVNTFSSEVVTLWYRAPDVLMGSRTYSTSIDIWSCGCILAEMITGKPLFPGTNDEEQLKLIFDIMGTPNESLWPSVTKLPKYNPNIQQRPPRDLRQVLQPHTKEPLDGNLMDFLHGLLQLNPDMRLSAKQALHHPWFAEYYHHAS | 2.7.11.22 | null | cell cycle G1/S phase transition [GO:0044843]; DNA damage response [GO:0006974]; establishment or maintenance of cytoskeleton polarity [GO:0030952]; fungal-type cell wall organization [GO:0031505]; G1/S transition of mitotic cell cycle [GO:0000082]; lipid homeostasis [GO:0055088]; long-chain fatty acid metabolic proces... | cellular bud neck [GO:0005935]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; Pho85-Pho80 CDK-cyclin complex [GO:1990860] | ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | PTM: Phosphorylation of Tyr-18 seems to be important to discriminate between the different cyclin partners for binding. {ECO:0000269|PubMed:10620010}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12455686}. Nucleus {ECO:0000269|PubMed:12455686}. Note=Predominantly localizes to the nucleus. {ECO:0000269|PubMed:12455686}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; Evidence={ECO:0000269|PubMed:10490639, ECO:00002... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 uM for substrate protein GSY2 (when associated with cyclin PCL10) {ECO:0000269|PubMed:10490639}; Vmax=11.5 umol/min/mg enzyme {ECO:0000269|PubMed:10490639}; | null | null | null | FUNCTION: Cyclin-dependent protein kinase (CDK) catalytic subunit that regulates multiple cell cycle and metabolic processes in response to nutrient availability. Associates with different cyclins, that control kinase activity, substrate specificity and subcellular location of the kinase. Regulates metabolic processes ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17164 | FUCO_RAT | MWDLKSEWWAVGFGLLLLLAASAQAGGLAPHHYTPDWPSLDSRPLPRWFDEAKFGLFVHWGVYSVPAWGSEWFWWHWQGEQSSAYVRFMKENYPPGFSYADFAPQFTARFFHPEEWADLFQAAGAKYVVLTAKHHEGFTNWPSAVSWNWNSKDVGPHRDLVGELGAAVRKRNIRYGLYHSLFEWFHPLYLLDKKNGLKTQHFVSTKTMPELYDLVNRYKPDLIWSDGEWECPDSYWNSTEFLAWLYNESPVKDQVVVNDRWGQNCSCRHGGYYNCEDKYRPHSLPDHKWEMCTSVDKASWGYRRDMSMSTIVDENEIIEE... | 3.2.1.51 | null | fucose metabolic process [GO:0006004]; glycoside catabolic process [GO:0016139]; lipid metabolic process [GO:0006629] | lysosome [GO:0005764] | alpha-L-fucosidase activity [GO:0004560]; carbohydrate binding [GO:0030246]; fucosidase activity [GO:0015928] | PF01120;PF16757; | 3.20.20.80;2.60.40.1180; | Glycosyl hydrolase 29 family | null | SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P04066}. | CATALYTIC ACTIVITY: Reaction=an alpha-L-fucoside + H2O = an alcohol + L-fucose; Xref=Rhea:RHEA:12288, ChEBI:CHEBI:2181, ChEBI:CHEBI:15377, ChEBI:CHEBI:28349, ChEBI:CHEBI:30879; EC=3.2.1.51; Evidence={ECO:0000255|PROSITE-ProRule:PRU10054}; CATALYTIC ACTIVITY: Reaction=a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:1(4E)) + ... | null | null | null | null | FUNCTION: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. | Rattus norvegicus (Rat) |
P17169 | GLMS_ECOLI | MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDAEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGEPSEVNAHPHVSEHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYGTVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESNLQYDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRISHGQVDLSELGPNADELLSKVEHIQILACGTSYNSGMVSRYWFESLAG... | 2.6.1.16 | null | carbohydrate metabolic process [GO:0005975]; fructose 6-phosphate metabolic process [GO:0006002]; glutamine metabolic process [GO:0006541]; protein N-linked glycosylation [GO:0006487]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048]; UDP-N-acetylglucosamine metabolic process [GO:0006047] | cytosol [GO:0005829] | carbohydrate derivative binding [GO:0097367]; glutamine-fructose-6-phosphate transaminase (isomerizing) activity [GO:0004360] | PF13522;PF01380; | 3.60.20.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; | null | null | null | null | FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. | Escherichia coli (strain K12) |
P17174 | AATC_HUMAN | MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQKIANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFLARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLENAPEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWAIRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPPAQGARIVASTLSNPELFEEW... | 2.6.1.1; 2.6.1.3 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | 2-oxoglutarate metabolic process [GO:0006103]; aspartate biosynthetic process [GO:0006532]; aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; cellular response to insulin stimulus [GO:0032869]; fatty acid homeostasis [GO:0055089]; gluconeogenesis [GO:0006094]; glutamate catabolic proce... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634] | L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-cysteine transaminase activity [GO:0047801]; phosphatidylserine decarboxylase activity [GO:0004609]; pyridoxal phosphate binding [GO:0030170] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-I pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1974457}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000269|PubMed:21900944}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21825; Evidence={ECO:0000250|... | null | null | null | null | FUNCTION: Biosynthesis of L-glutamate from L-aspartate or L-cysteine (PubMed:21900944). Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involv... | Homo sapiens (Human) |
P17177 | CP27A_RABIT | MAALGCARLRWALLGPRVAGCGLCPQGARAKAAIPTALPADEAAQAPGAGPGDRRRRRSLEELPRLGQLRFFYQAFVQGYLLHLHKLQVLNKARYGPMWVSYLGPQLFVNLASAPLVETVMRQEGKYPVRNDMQLWKEHRDHQDLAYGVFTTDGHDWYQLRQALNQRLLKPAEAALYTDALNEVIDSFVVRLDQLRAESASGDQVPDMADLLYHFALEAICYILFEKRIGCLEASIPKDTENFIRSVGLMFQNSVYVTFLPKWTRPLLPFWKRYLDGWDTIFSFGKNLIDQKLQEVVAQLQSAGSDGVQVSGYLHSLLTS... | 1.14.15.15 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:2722778}; | bile acid biosynthetic process [GO:0006699]; C21-steroid hormone biosynthetic process [GO:0006700]; calcitriol biosynthetic process from calciol [GO:0036378]; cellular response to peptide hormone stimulus [GO:0071375]; cholesterol catabolic process [GO:0006707]; cortisol metabolic process [GO:0034650]; glucocorticoid b... | mitochondrial inner membrane [GO:0005743] | 3-alpha,7-alpha,12-alpha-trihydroxycholestan-26-al 26-oxidoreductase activity [GO:0047103]; cholestanetetraol 26-dehydrogenase activity [GO:0047748]; cholestanetriol 26-monooxygenase activity [GO:0047749]; cholesterol 26-hydroxylase activity [GO:0031073]; cholesterol 7-alpha-monooxygenase activity [GO:0008123]; cholest... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P17178}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17178}. Note=Post-translationally targeted to mitochondria. All three of the receptor proteins in the TOM complex, TOMM70, TOMM20 and TOMM22 are required for the translocation across th... | CATALYTIC ACTIVITY: Reaction=5beta-cholestane-3alpha,7alpha,12alpha-triol + 5 H(+) + 3 O2 + 6 reduced [adrenodoxin] = (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + 4 H2O + 6 oxidized [adrenodoxin]; Xref=Rhea:RHEA:34631, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, C... | null | PATHWAY: Hormone biosynthesis; cholecalciferol biosynthesis. {ECO:0000250|UniProtKB:Q02318}.; PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000250|UniProtKB:Q02318}.; PATHWAY: Lipid metabolism; bile acid biosynthesis. {ECO:0000269|PubMed:2722778}. | null | null | FUNCTION: Cytochrome P450 monooxygenase that catalyzes regio- and stereospecific hydroxylation of cholesterol and its derivatives. Hydroxylates (with R stereochemistry) the terminal methyl group of cholesterol side-chain in a three step reaction to yield at first a C26 alcohol, then a C26 aldehyde and finally a C26 aci... | Oryctolagus cuniculus (Rabbit) |
P17178 | CP27A_RAT | MAVLSRMRLRWALLDTRVMGHGLCPQGARAKAAIPAALRDHESTEGPGTGQDRPRLRSLAELPGPGTLRFLFQLFLRGYVLHLHELQALNKAKYGPMWTTTFGTRTNVNLASAPLLEQVMRQEGKYPIRDSMEQWKEHRDHKGLSYGIFITQGQQWYHLRHSLNQRMLKPAEAALYTDALNEVISDFIARLDQVRTESASGDQVPDVAHLLYHLALEAICYILFEKRVGCLEPSIPEDTATFIRSVGLMFKNSVYVTFLPKWSRPLLPFWKRYMNNWDNIFSFGEKMIHQKVQEIEAQLQAAGPDGVQVSGYLHFLLTKE... | 1.14.15.15 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P17177}; | bile acid biosynthetic process [GO:0006699]; C21-steroid hormone biosynthetic process [GO:0006700]; calcitriol biosynthetic process from calciol [GO:0036378]; cellular response to peptide hormone stimulus [GO:0071375]; cholesterol catabolic process [GO:0006707]; cholesterol metabolic process [GO:0008203]; cortisol meta... | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | 3-alpha,7-alpha,12-alpha-trihydroxycholestan-26-al 26-oxidoreductase activity [GO:0047103]; cholestanetetraol 26-dehydrogenase activity [GO:0047748]; cholestanetriol 26-monooxygenase activity [GO:0047749]; cholesterol 26-hydroxylase activity [GO:0031073]; cholesterol 7-alpha-monooxygenase activity [GO:0008123]; cholest... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:19401463}; Peripheral membrane protein {ECO:0000305|PubMed:19401463}. Note=Post-translationally targeted to mitochondria. All three of the receptor proteins in the TOM complex, TOMM70, TOMM20 and TOMM22 are required for the translocation across the ... | CATALYTIC ACTIVITY: Reaction=5beta-cholestane-3alpha,7alpha,12alpha-triol + 5 H(+) + 3 O2 + 6 reduced [adrenodoxin] = (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + 4 H2O + 6 oxidized [adrenodoxin]; Xref=Rhea:RHEA:34631, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, C... | null | PATHWAY: Hormone biosynthesis; cholecalciferol biosynthesis. {ECO:0000250|UniProtKB:Q02318}.; PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000250|UniProtKB:Q02318}.; PATHWAY: Lipid metabolism; bile acid biosynthesis. {ECO:0000250|UniProtKB:Q02318}. | null | null | FUNCTION: Cytochrome P450 monooxygenase that catalyzes regio- and stereospecific hydroxylation of cholesterol and its derivatives. Hydroxylates (with R stereochemistry) the terminal methyl group of cholesterol side-chain in a three step reaction to yield at first a C26 alcohol, then a C26 aldehyde and finally a C26 aci... | Rattus norvegicus (Rat) |
P17181 | INAR1_HUMAN | MMVVLLGATTLVLVAVAPWVLSAAAGGKNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNITSTKCNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWLHAFLKRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSE... | null | null | cellular response to interferon-alpha [GO:0035457]; cellular response to interferon-beta [GO:0035458]; cellular response to virus [GO:0098586]; positive regulation of cellular respiration [GO:1901857]; receptor signaling pathway via JAK-STAT [GO:0007259]; response to lipopolysaccharide [GO:0032496]; response to virus [... | late endosome [GO:0005770]; lysosome [GO:0005764]; plasma membrane [GO:0005886] | cytokine binding [GO:0019955]; JAK pathway signal transduction adaptor activity [GO:0008269]; type I interferon binding [GO:0019962]; type I interferon receptor activity [GO:0004905] | PF09294;PF01108; | 2.60.40.10; | Type II cytokine receptor family | PTM: Ubiquitinated, leading to its internalization and degradation (PubMed:14532120, PubMed:15337770). Polyubiquitinated via 'Lys-48'-linked and 'Lys-63'-linked ubiquitin chains, leading to receptor internalization and lysosomal degradation (PubMed:18056411). The 'Lys-63'-linked ubiquitin chains are cleaved off by the ... | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:14532120, ECO:0000269|PubMed:18056411, ECO:0000269|PubMed:2153461, ECO:0000269|PubMed:35442418, ECO:0000305|PubMed:7665574}; Single-pass type I membrane protein {ECO:0000305}. Late endosome {ECO:0000269|PubMed:18056411, ECO:0000305|PubMed:14532120}. L... | null | null | null | null | null | FUNCTION: Together with IFNAR2, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa) (PubMed:10049744, PubMed:14532120, PubMed:15337770, PubMed:2153461, PubMed:21854986, PubMed:24075985, PubMed:31270247, PubMed:33252644, PubMed:35442418, PubMed:7813427). ... | Homo sapiens (Human) |
P17182 | ENOA_MOUSE | MSILRIHAREIFDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRDNDKTRFMGKGVSQAVEHINKTIAPALVSKKVNVVEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCKAGAVEKGVPLYRHIADLAGNPEVILPVPAFNVINGGSHAGNKLAMQEFMILPVGASSFREAMRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEALELLKTAIAKAGYTDQVVIGMDVAASEFYRSGKYDLDFKSPDDPSRYITPDQLADLYKSFVQNYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDL... | 4.2.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P06733}; Note=Binds two Mg(2+) per subunit. Required for catalysis and for stabilizing the dimer. {ECO:0000250|UniProtKB:P06733}; | canonical glycolysis [GO:0061621]; cellular response to interleukin-7 [GO:0098761]; gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glycolytic process [GO:0006096]; in utero embryonic development [GO:0001701] | cell cortex [GO:0005938]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; growth cone [GO:0030426]; membrane raft [GO:0045121]; myelin sheath [GO:0043209]; phosphopyruvate hydratase complex [GO:0000015]; plasma membrane [GO:0005886]; synaptic membrane [GO:0097060] | enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; RNA binding [GO:0003723] | PF00113;PF03952; | 3.20.20.120;3.30.390.10; | Enolase family | PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: Lysine 2-hydroxyisobutyrylation (Khib) by p300/EP300 activates the phosphopyruvate hydratase activity. {ECO:0000250|UniProtKB:P06733}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form (By similarity). ENO1 is localized to the M-band. {ECO:0000250, ECO:0000269|PubMed:11229603}. | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000250|UniProtKB:P06733}; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. | null | null | FUNCTION: Glycolytic enzyme the catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate. In addition to glycolysis, involved in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability... | Mus musculus (Mouse) |
P17183 | ENOG_MOUSE | MSIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRDGDKQRYLGKGVLKAVDHINSRIAPALISSGISVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAERDLPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKMVIGMDVAASEFYRDGKYDLDFKSPADPSRYITGDQLGALYQDFVRNYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDL... | 4.2.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Mg(2+) is required for catalysis and for stabilizing the dimer.; | canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096] | cell cortex [GO:0005938]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; growth cone [GO:0030426]; membrane raft [GO:0045121]; myelin sheath [GO:0043209]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; phosphopyruvate hydratase complex [GO:0000015]; photoreceptor inner segment [GO:0001917]; synaptic memb... | enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]; protein-containing complex binding [GO:0044877] | PF00113;PF03952; | 3.20.20.120;3.30.390.10; | Enolase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. | null | null | FUNCTION: Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
P17194 | HBSAG_HPBDB | MGQQPAKSMDVRRIEGGELLLNQLAGRMIPKGTVTWSGKFPTIDHLLDHVQTMEEVNTMQQQGAWPAGAGRRLGLTNPTPHETPQPQWTPEEDQKAREAFRRYQEERPPETTTIAPTSPTPWKLQPGDDPLLENKSLLETHPLYQNPEPAVPVIKTPPLKKKKMPGTFGGILAGLIGLLVSFFLLIKILEILRRLDWWWISLSSPKGKMQCAFQDTGAQISPHYVGSCPWGCPGFLWTYLRLFIIFLLILLVAAGLLYLTDNMSIILGKLQWESVSALFSSISSLLPSDQKSLVALIFGLLLIWMTSSSATQTLVTLTQL... | null | null | membrane fusion involved in viral entry into host cell [GO:0039663]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00695; | null | Avihepadnavirus major surface antigen family | PTM: Myristoylation contributes importantly to DHBV infectivity. It is most likely required for an early step of the life cycle involving the entry or uncoating of virus particles.; PTM: Phosphorylated on pre-S domain for about 50% of L proteins, the L chains with internal pre-S region (Li-HBsAg). | SUBCELLULAR LOCATION: Virion membrane. | null | null | null | null | null | FUNCTION: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specifici... | Duck hepatitis B virus (isolate brown Shanghai duck S5) (DHBV) |
P17195 | HBSAG_HPBDW | MGQQPAKSMDVRRIEGGELLLNQLAGRMIPKGTVTWSGKFPTIDHLLDHVQTMEEVNTLQQQGAWPAGAGRRLGLTNPAPQEPPQPQWTPEEDQKAREAFRRYQEERPPETTTIPPTSPTPWKLQPGDDPLLENKSLLETHPLYQNPEPAVPVIKTPPLRKKKMAGTFGGILAGLIGLLVGFFLLIKILEILRRLDWWWISLSSPKGKMQCAFQDTGAQISPHYAGFCPWGCPGFLWTYLRLFIIFLLILLVAAGLLYLTDNMSIILGKLQWESVSALFSSISSLLPSDQKSLVALMFGLLLIWMTSSSATQTLVTLTQL... | null | null | membrane fusion involved in viral entry into host cell [GO:0039663]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00695; | null | Avihepadnavirus major surface antigen family | PTM: Myristoylation contributes importantly to DHBV infectivity. It is most likely required for an early step of the life cycle involving the entry or uncoating of virus particles.; PTM: Phosphorylated on pre-S domain for about 50% of L proteins, the L chains with internal pre-S region (Li-HBsAg). | SUBCELLULAR LOCATION: Virion membrane. | null | null | null | null | null | FUNCTION: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specifici... | Duck hepatitis B virus (isolate white Shanghai duck S31) (DHBV) |
P17202 | BADH_SPIOL | MAFPIPARQLFIDGEWREPIKKNRIPVINPSTEEIIGDIPAATAEDVEVAVVAARRAFRRNNWSATSGAHRATYLRAIAAKITEKKDHFVKLETIDSGKPFDEAVLDIDDVASCFEYFAGQAEALDGKQKAPVTLPMERFKSHVLRQPLGVVGLISPWNYPLLMATWKIAPALAAGCTAVLKPSELASVTCLEFGEVCNEVGLPPGVLNILTGLGPDAGAPLVSHPDVDKIAFTGSSATGSKVMASAAQLVKPVTLELGGKSPIVVFEDVDIDKVVEWTIFGCFWTNGQICSATSRLLVHESIAAEFVDKLVKWTKNIKI... | 1.2.1.-; 1.2.1.19; 1.2.1.47; 1.2.1.8 | null | cellular aldehyde metabolic process [GO:0006081]; cellular detoxification of aldehyde [GO:0110095]; glycine betaine biosynthetic process from choline [GO:0019285] | null | 4-trimethylammoniobutyraldehyde dehydrogenase activity [GO:0047105]; aminobutyraldehyde dehydrogenase activity [GO:0019145]; betaine-aldehyde dehydrogenase activity [GO:0008802]; potassium ion binding [GO:0030955]; protein homodimerization activity [GO:0042803] | PF00171; | null | Aldehyde dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264, ChEBI:CHEBI:59888; EC=1.2.1.19; Evidence={ECO:0000269|PubMed:22345508}; PhysiologicalDirection=left-to-right... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=69 uM for betaine aldehyde {ECO:0000269|PubMed:22345508}; KM=5.5 uM for 4-aminobutanal {ECO:0000269|PubMed:22345508}; KM=2.6 uM for 3-aminopropanal {ECO:0000269|PubMed:22345508}; KM=3.6 uM for 4-(trimethylamino)butanal {ECO:0000269|PubMed:22345508}; Vmax=5 umol/min... | PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. {ECO:0000305}. | null | null | FUNCTION: Dehydrogenase innvolved in glycine betaine biosynthesis (PubMed:22345508, PubMed:2320587, PubMed:24884441). Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of betaine aldehyde to glycine betaine (PubMed:22345508, PubMed:2488444... | Spinacia oleracea (Spinach) |
P17208 | PO4F1_MOUSE | MMSMNSKQPHFAMHPTLPEHKYPSLHSSSEAIRRACLPTPPLQSNLFASLDETLLARAEALAAVDIAVSQGKSHPFKPDATYHTMNSVPCTSTSTVPLAHHHHHHHHHQALEPGDLLDHISSPSLALMAGAGGAGAAGGGGGAHDGPGGGGGPGGGGGPGGGGPGGGGGGGGPGGGGGGPGGGLLGGSAHPHPHMHGLGHLSHPAAAAAMNMPSGLPHPGLVAAAAHHGAAAAAAAAAAGQVAAASAAAAVVGAAGLASICDSDTDPRELEAFAERFKQRRIKLGVTQADVGSALANLKIPGVGSLSQSTICRFESLTLS... | null | null | cell migration in hindbrain [GO:0021535]; cellular response to cytokine stimulus [GO:0071345]; cellular response to estradiol stimulus [GO:0071392]; central nervous system neuron differentiation [GO:0021953]; habenula development [GO:0021986]; heart development [GO:0007507]; innervation [GO:0060384]; intrinsic apoptoti... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; neuron projection [GO:0043005]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor... | PF00046;PF00157; | 1.10.10.60;1.10.260.40; | POU transcription factor family, Class-4 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17668438}. Cytoplasm {ECO:0000269|PubMed:17668438}. | null | null | null | null | null | FUNCTION: Multifunctional transcription factor with different regions mediating its different effects (PubMed:10640682, PubMed:8621561, PubMed:9694219, PubMed:9722627). Acts by binding (via its C-terminal domain) to sequences related to the consensus octamer motif 5'-ATGCAAAT-3' in the regulatory regions of its target ... | Mus musculus (Mouse) |
P17210 | KINH_DROME | MSAEREIPAEDSIKVVCRFRPLNDSEEKAGSKFVVKFPNNVEENCISIAGKVYLFDKVFKPNASQEKVYNEAAKSIVTDVLAGYNGTIFAYGQTSSGKTHTMEGVIGDSVKQGIIPRIVNDIFNHIYAMEVNLEFHIKVSYYEIYMDKIRDLLDVSKVNLSVHEDKNRVPYVKGATERFVSSPEDVFEVIEEGKSNRHIAVTNMNEHSSRSHSVFLINVKQENLENQKKLSGKLYLVDLAGSEKVSKTGAEGTVLDEAKNINKSLSALGNVISALADGNKTHIPYRDSKLTRILQESLGGNARTTIVICCSPASFNESET... | null | null | actin filament bundle organization [GO:0061572]; anterograde axonal transport of mitochondrion [GO:0098957]; anterograde dendritic transport [GO:0098937]; anterograde dendritic transport of neurotransmitter receptor complex [GO:0098971]; axo-dendritic transport [GO:0008088]; axon guidance [GO:0007411]; axonogenesis [GO... | actin cap [GO:0030478]; axon cytoplasm [GO:1904115]; cytoplasm [GO:0005737]; dendrite cytoplasm [GO:0032839]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; microtubule plus-end [GO:0035371] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cytoskeletal motor activity [GO:0003774]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; plus-end-directed microtubule motor activity [GO:0008574]; tropomyosin binding [GO:0005523] | PF00225; | 3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Kinesin subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. | null | null | null | null | null | FUNCTION: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Milt and Miro form an essential protein complex that links Khc to mitochondria for light chain-independent, anterograde transport of mitochondria. {ECO:0000269|PubMed:16717129, ECO:0000269|PubMed:2522352}. | Drosophila melanogaster (Fruit fly) |
P17213 | BPI_HUMAN | MRENMARGPCNAPRWASLMVLVAIGTAVTAAVNPGVVVRISQKGLDYASQQGTAALQKELKRIKIPDYSDSFKIKHLGKGHYSFYSMDIREFQLPSSQISMVPNVGLKFSISNANIKISGKWKAQKRFLKMSGNFDLSIEGMSISADLKLGSNPTSGKPTITCSSCSSHINSVHVHISKSKVGWLIQLFHKKIESALRNKMNSQVCEKVTNSVSSELQPYFQTLPVMTKIDSVAGINYGLVAPPATTAETLDVQMKGEFYSENHHNPPPFAPPVMEFPAAHDRMVYLGLSDYFFNTAGLVYQEAGVLKMTLRDDMIPKES... | null | null | defense response to Gram-negative bacterium [GO:0050829]; innate immune response [GO:0045087]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of interleukin-8 production [GO:0032717]; negative regulation of macrophage activat... | azurophil granule lumen [GO:0035578]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; specific granule lumen [GO:0035580] | lipopolysaccharide binding [GO:0001530] | PF01273;PF02886; | null | BPI/LBP/Plunc superfamily, BPI/LBP family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8812832}. Cytoplasmic granule membrane {ECO:0000269|PubMed:2722846}. Note=Membrane-associated in polymorphonuclear Leukocytes (PMN) granules. {ECO:0000269|PubMed:2722846}. | null | null | null | null | null | FUNCTION: The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity ag... | Homo sapiens (Human) |
P17214 | EST1_YEAST | MDNEEVNEECMRLFFKNARAHLDKHLTSRLTCDENAYITFRCFLDGIHRKSTRFLEELLLKQENMYHNNNYERINDSVIPLVLKLLWLQIHEPTLQWFEHWFHDIMRLSNRRKFRVFRIFQKKMIQFFKITHRYYYDIIEHLCAKYDMNSVISNALFAKLNLMQYTDGLSTHEKIILNTSNPLTFSIVISLQRCVINLGSTHFYKTLLNKPSNKPKSVEGFEKSIRYLNIASLYLPAVGDTYFQRAKIYLITGKFSLYFFELVRGALVRIPSKCALNNLKDFILTPDFPERRRLMKKLAILVSKDLKGEKSFFEGQIVLQ... | null | null | G-quadruplex DNA formation [GO:0071919]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; regulation of telomere maintenance via telomerase [GO:0032210]; telomere maintenance [GO:0000723]; telomere maintenance via telomerase [GO:0007004] | chromosome, telomeric region [GO:0000781]; nucleolus [GO:0005730]; nucleus [GO:0005634]; telomerase holoenzyme complex [GO:0005697] | RNA binding [GO:0003723]; single-stranded DNA binding [GO:0003697]; telomerase RNA binding [GO:0070034]; telomeric DNA binding [GO:0042162] | PF10374;PF10373; | 1.25.40.10; | EST1 family | null | SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere {ECO:0000305}. | null | null | null | null | null | FUNCTION: Directly involved in telomere replication. Associates with telomerase and during its interaction with CDC13, telomerase activity is promoted. {ECO:0000269|PubMed:11390652, ECO:0000269|PubMed:17245108}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17220 | PSA2_RAT | MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVRDYLAAIA | null | null | proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; response to virus [GO:0009615] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; P-body [GO:0000932]; proteasome complex [GO:0000502]; proteasome core complex [GO:0005839]; proteasome core complex, alpha-subunit complex [GO:0019773] | null | PF00227;PF10584; | 3.60.20.10; | Peptidase T1A family | PTM: Phosphorylated on tyrosine residues; which may be important for nuclear import. {ECO:0000269|PubMed:8794741}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8794741}. Nucleus {ECO:0000269|PubMed:8794741}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9 (By similarity). Colocalizes with TRIM5 in cytoplasmic bodies (... | null | null | null | null | null | FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus p... | Rattus norvegicus (Rat) |
P17221 | FEM1_CAEEL | MTPNGHHFRTVIYNAAAVGNLQRIKVFTINSRNDRQWIIDCFNSDQDGRYPLVIAARNGHANVVEYLLEIGADPSVRGVVEFDNENIQGTPPLWAASAAGHIEIVKLLIEKANADVNQATNTRSTPLRGACYDGHLDIVKYLLEKGADPHIPNRHGHTCLMIASYRNKVGIVEELLKTGIDVNKKTERGNTALHDAAESGNVEVVKILLKHGSVLMKDIQGVDPLMGAALSGFLDVLNVLADQMPSGIHKRDALKLLGSTLLDKKMDAMSAMNCWKQSMEVPLHADDLRLVREMETFFEPQEVYEYQREAQNIAQVELLD... | null | null | cell differentiation [GO:0030154]; male germ-line sex determination [GO:0019100]; male sex determination [GO:0030238]; male somatic sex determination [GO:0019102]; masculinization of hermaphroditic germ-line [GO:0042006]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; proteasome-mediat... | Cul2-RING ubiquitin ligase complex [GO:0031462]; cytosol [GO:0005829]; nucleus [GO:0005634]; protein serine/threonine phosphatase complex [GO:0008287]; protein-containing complex [GO:0032991]; ubiquitin ligase complex [GO:0000151] | protein phosphatase binding [GO:0019903] | PF00023;PF12796; | 1.25.40.20;1.25.40.10; | Fem-1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:17609115, ECO:0000269|PubMed:28118078}. | null | null | FUNCTION: Substrate-recognition component of the cullin-RING-based CBC(fem-1) (Cul2-ElonginB-ElonginC) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degrada... | Caenorhabditis elegans |
P17225 | PTBP1_MOUSE | MDGIVPDIAVGTKRGSDELFSTCVSNGPFIMSSSASAANGNDSKKFKGDNRSAGVPSRVIHVRKLPSDVTEGEVISLGLPFGKVTNLLMLKGKNQAFIEMNTEEAANTMVNYYTSVAPVLRGQPIYIQFSNHKELKTDSSPNQARAQAALQAVNSVQSGNLALAASAAAVDAGMAMAGQSPVLRIIVENLFYPVTLDVLHQIFSKFGTVLKIITFTKNNQFQALLQYADPVSAQHAKLSLDGQNIYNACCTLRIDFSKLTSLNVKYNNDKSRDYTRPDLPSGDSQPSLDQTMAAAFGAPGIMSASPYAGAGFPPTFAIPQ... | null | null | 3'-UTR-mediated mRNA stabilization [GO:0070935]; gene expression [GO:0010467]; mRNA processing [GO:0006397]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; negative regulation of muscle cell differentiation [GO:0051148]; negative regulation of neuron differentiation [GO:0045665]; neurogenesis [GO:0... | neuron projection terminus [GO:0044306]; nucleus [GO:0005634] | mRNA binding [GO:0003729]; regulatory region RNA binding [GO:0001069]; RNA binding [GO:0003723]; sequence-specific DNA binding [GO:0043565]; single-stranded DNA binding [GO:0003697]; single-stranded DNA endodeoxyribonuclease activity [GO:0000014] | PF00076;PF13893;PF11835; | 3.30.70.330; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Plays a role in pre-mRNA splicing and in the regulation of alternative splicing events. Activates exon skipping of its own pre-mRNA during muscle cell differentiation. Binds to the polypyrimidine tract of introns. May promote RNA looping when bound to two separate polypyrimidine tracts in the same pre-mRNA. M... | Mus musculus (Mouse) |
P17244 | G3P_CRIGR | MVKVGVNGFGRIGRLVTRAAFTSGKVEVVAINDPFIDLNYMVYMFQYDSTHGKFKGTVKAENGKLVINGKAITIFQERDPANIKWGDAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNQDKYDNSLKIVSNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKPAKYEDIKKVVKQASEGPLKGILGYTEDQVVSCDFNSDSHSSTFDAGAGIALNDNFVKLISWYDNEFGYSN... | 1.2.1.12; 2.6.99.- | null | glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; innate immune response [GO:0045087]; microtubule cytoskeleton organization [GO:0000226]; neuron apoptotic process [GO:0051402]; peptidyl-cysteine S-trans-nitrosylation [GO:0035606]; positive regulation of canonical NF-kappaB signal transduction [G... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; GAIT complex [GO:0097452]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634] | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; microtubule binding [GO:0008017]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; peptidyl-cysteine S-nitrosylase activity [GO:0035605] | PF02800;PF00044; | 3.40.50.720; | Glyceraldehyde-3-phosphate dehydrogenase family | PTM: ISGylated. {ECO:0000250|UniProtKB:P04406}.; PTM: S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus S-nitrosylation of Cys-245 is induced by interferon-gamma and LDL(ox) implicating the iNOS-S100A8/9 transnitrosylase complex and seems to prevent interaction with ph... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P04797}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P04797}. Nucleus {ECO:0000250|UniProtKB:P04797}. Note=Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal. Colocalizes with C... | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000250|UniProtKB:P04406, ... | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. | null | null | FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
P17246 | TGFB1_RAT | MPPSGLRLLPLLLPLPWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESADPEPEPEADYYAKEVTRVLMVDRNNAIYDKTKDITHSIYMFFNTSDIREAVPEPPLLSRAELRLQRFKSTVEQHVELYQKYSNNSWRYLGNRLLTPTDTPEWLSFDVTGVVRQWLNQGDGIQGFRFSAHCSCDSKDNVLHVEINGISPKRRGDLGTIHDMNRPFLLLMATPLERAQHLHSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHAN... | null | null | adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains [GO:0002460]; animal organ regeneration [GO:0031100]; aortic valve morphogenesis [GO:0003180]; ATP biosynthetic process [GO:0006754]; branch elongation involved in mammary gland duct branching [GO:0... | axon [GO:0030424]; blood microparticle [GO:0072562]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; microvillus [GO:0005902]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; secretory g... | antigen binding [GO:0003823]; cytokine activity [GO:0005125]; deubiquitinase activator activity [GO:0035800]; enzyme binding [GO:0019899]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; protein serine/threonine kinase activator activity [GO:0043539]; protein-containing complex binding [GO:... | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | PTM: Transforming growth factor beta-1 proprotein: The precursor proprotein is cleaved in the Golgi apparatus by FURIN to form Transforming growth factor beta-1 (TGF-beta-1) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-1 inactive. {ECO:0000250|UniProtKB:P01137}.; P... | SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-1]: Secreted {ECO:0000250|UniProtKB:P01137}. | null | null | null | null | null | FUNCTION: Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively. {ECO:0000250|UniProtKB:P01137}.; FUNCTION: [Latency-associated peptide]: Re... | Rattus norvegicus (Rat) |
P17252 | KPCA_HUMAN | MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISP... | 2.7.11.13 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain. {ECO:0000250|UniProtKB:P05696}; | angiogenesis [GO:0001525]; apoptotic signaling pathway [GO:0097190]; cell adhesion [GO:0007155]; desmosome assembly [GO:0002159]; intracellular signal transduction [GO:0035556]; mitotic nuclear membrane disassembly [GO:0007077]; negative regulation of glial cell apoptotic process [GO:0034351]; peptidyl-serine phosphory... | alphav-beta3 integrin-PKCalpha complex [GO:0035866]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; perinuclear region of cyt... | ATP binding [GO:0005524]; calcium,diacylglycerol-dependent serine/threonine kinase activity [GO:0004698]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; enzyme binding [GO:0019899]; histone H3T6 kinase activity [GO:0035403]; integrin binding [GO:0005178]; protein kinase activity [GO:0004672]; p... | PF00130;PF00168;PF00069;PF00433; | 3.30.60.20;2.60.40.150;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23990668}. Cell membrane {ECO:0000269|PubMed:23990668}; Peripheral membrane protein {ECO:0000305|PubMed:23990668}. Mitochondrion membrane {ECO:0000269|PubMed:9738012}; Peripheral membrane protein {ECO:0000305|PubMed:9738012}. Nucleus {ECO:0000250|UniProtKB:P20444}. | 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=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, tumorigenesis, cardiac hypertrophy, angiogenesis, platelet function and inflammati... | Homo sapiens (Human) |
P17255 | VATA_YEAST | MAGAIENARKEIKRISLEDHAESEYGAIYSVSGPVVIAENMIGCAMYELVKVGHDNLVGEVIRIDGDKATIQVYEETAGLTVGDPVLRTGKPLSVELGPGLMETIYDGIQRPLKAIKEESQSIYIPRGIDTPALDRTIKWQFTPGKFQVGDHISGGDIYGSVFENSLISSHKILLPPRSRGTITWIAPAGEYTLDEKILEVEFDGKKSDFTLYHTWPVRVPRPVTEKLSADYPLLTGQRVLDALFPCVQGGTTCIPGAFGCGKTVISQSLSKYSNSDAIIYVGCFAKGTNVLMADGSIECIENIEVGNKVMGKDGRPREV... | 3.1.-.-; 7.1.2.2 | null | endosomal lumen acidification [GO:0048388]; Golgi lumen acidification [GO:0061795]; intein-mediated protein splicing [GO:0016539]; intron homing [GO:0006314]; protein metabolic process [GO:0019538]; proton transmembrane transport [GO:1902600]; vacuolar acidification [GO:0007035] | fungal-type vacuole membrane [GO:0000329]; Golgi membrane [GO:0000139]; phagocytic vesicle [GO:0045335]; proton-transporting V-type ATPase complex [GO:0033176]; vacuolar proton-transporting V-type ATPase complex [GO:0016471]; vacuolar proton-transporting V-type ATPase, V1 domain [GO:0000221] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; mRNA binding [GO:0003729]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]; proton-transporting ATPase activity, rotational mechanism [GO:0046961] | PF00006;PF02874;PF16886;PF05204;PF05203; | 2.40.30.20;2.40.50.100;3.10.28.10;3.40.50.300; | ATPase alpha/beta chains family | PTM: This protein undergoes a protein self splicing that involves a post-translational excision of the VDE intervening region (intein) followed by peptide ligation. | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:14562095}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Vacuole membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:2139027}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Membranes of var... | CATALYTIC ACTIVITY: Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate; Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2; Evidence={ECO:0000305|PubMed:18055462, ECO:0000305|PubMed:2139027}; | null | null | null | null | FUNCTION: Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:18055462, PubMed:2139027). V-ATPase is responsible for acidifying and maintaining the pH... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17256 | KIME_RAT | MLSEVLLVSAPGKVILHGEHAVVHGKVALAVALNLRTFLVLRPQSNGKVSLNLPNVGIKQVWDVATLQLLDTGFLEQGDVPAPTLEQLEKLKKVAGLPRDCVGNEGLSLLAFLYLYLAICRKQRTLPSLDIMVWSELPPGAGLGSSAAYSVCVAAALLTACEEVTNPLKDRGSIGSWPEEDLKSINKWAYEGERVIHGNPSGVDNSVSTWGGALRYQQGKMSSLKRLPALQILLTNTKVPRSTKALVAGVRSRLIKFPEIMAPLLTSIDAISLECERVLGEMAAAPVPEQYLVLEELMDMNQHHLNALGVGHASLDQLCQ... | 2.7.1.36 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11877411}; | cholesterol biosynthetic process [GO:0006695]; ergosterol biosynthetic process [GO:0006696]; isopentenyl diphosphate biosynthetic process, mevalonate pathway [GO:0019287]; isoprenoid biosynthetic process [GO:0008299]; isoprenoid metabolic process [GO:0006720]; negative regulation of inflammatory response [GO:0050728]; ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; peroxisome [GO:0005777] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; mevalonate kinase activity [GO:0004496]; mRNA binding [GO:0003729]; sequence-specific mRNA binding [GO:1990825] | PF08544;PF00288; | 3.30.230.10;3.30.70.890; | GHMP kinase family, Mevalonate kinase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14730012}. Peroxisome {ECO:0000269|PubMed:1312092}. | CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+); Xref=Rhea:RHEA:17065, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36464, ChEBI:CHEBI:58146, ChEBI:CHEBI:456216; EC=2.7.1.36; Evidence={ECO:0000269|PubMed:14680942}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=34.6 uM for (R,S)-mevalonate {ECO:0000269|PubMed:14680942}; KM=953 uM for ATP {ECO:0000269|PubMed:14680942}; Vmax=38.7 umol/min/mg enzyme with (R,S)-mevalonate as substrate {ECO:0000269|PubMed:14680942}; | PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3. {ECO:0000305}. | null | null | FUNCTION: Catalyzes the phosphorylation of mevalonate to mevalonate 5-phosphate, a key step in isoprenoid and cholesterol biosynthesis. {ECO:0000250|UniProtKB:Q03426}. | Rattus norvegicus (Rat) |
P17260 | KRE1_YEAST | MMRRTLLHSFATLLLSLSLWSAAVMAAVTTQVTVVTNVAGALVTETTIWDPATAAAAATTTAQTGFFTTVFTTTNDVGTTVTLTQTVNRATMLPTTTTSTSSTGKTTTTVPTATSSLSSGLYLSTVTTTNDLGTTVTLTQTFTHSSTSATSSASSSVSSSVSSSGSSSSVKTTTSTGSAVAETGTRPDPSTDFTEPPVSAVTSLSIDSYITITEGTTSTYTTTRAPTSMWVTVVRQGNTITVQTTFVQRFSSQYVTVASPSVGSIGMGTLTGTVGVIKSAIKKTVSHNEAQHLGMSSFTSILGGLLTVLIWFL | null | null | fungal-type cell wall organization [GO:0031505] | extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; fungal-type vacuole [GO:0000324]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | structural constituent of cell wall [GO:0005199] | PF17056; | null | KRE1 family | PTM: Extensively modified; probably through addition of O-linked mannose residues.; PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is co... | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. Secreted, cell wall. Note=Identified as GPI-anchored plasma membrane protein (GPI-PMP) as well as component of the cell wall. Concentrated at the surface of mother cells. | null | null | null | null | null | FUNCTION: Involved in a late stage of cell wall 1,6-beta-glucan synthesis and assembly. Has a structural, rather than enzymic, function within cell wall 1,6-beta-glucan assembly and architecture, possibly by being involved in covalently cross-linking 1,6-beta-glucans to other cell wall components such as 1,3-beta-gluca... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17275 | JUNB_HUMAN | MCTKMEQPFYHDDSYTATGYGRAPGGLSLHDYKLLKPSLAVNLADPYRSLKAPGARGPGPEGGGGGSYFSGQGSDTGASLKLASSELERLIVPNSNGVITTTPTPPGQYFYPRGGGSGGGAGGAGGGVTEEQEGFADGFVKALDDLHKMNHVTPPNVSLGATGGPPAGPGGVYAGPEPPPVYTNLSSYSPASASSGGAGAAVGTGSSYPTTTISYLPHAPPFAGGHPAQLGLGRGASTFKEEPQTVPEARSRDATPPVSPINMEDQERIKVERKRLRNRLAATKCRKRKLERIARLEDKVKTLKAENAGLSSTAGLLREQ... | null | null | cellular response to calcium ion [GO:0071277]; decidualization [GO:0046697]; embryonic process involved in female pregnancy [GO:0060136]; integrated stress response signaling [GO:0140467]; labyrinthine layer blood vessel development [GO:0060716]; osteoblast differentiation [GO:0001649]; osteoblast proliferation [GO:003... | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription factor AP-1 complex [GO:0035976]; transcription regulator complex [GO:0005667] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA b... | PF00170;PF03957; | 1.20.5.170; | BZIP family, Jun subfamily | PTM: Ubiquitinated by ITCH, leading to its degradation. {ECO:0000269|PubMed:16387660}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcription factor involved in regulating gene activity following the primary growth factor response. Binds to the DNA sequence 5'-TGA[GC]TCA-3'. Heterodimerizes with proteins of the FOS family to form an AP-1 transcription complex, thereby enhancing its DNA binding activity to an AP-1 consensus sequence an... | Homo sapiens (Human) |
P17276 | PH4H_DROME | MYQRQVSFDKPTRVEDSAYIVEGVDIKEARNTCLLFSPKDSSLSSGALANILAIFKKHDINLVHIESRSSLRVPGYEFFVEADGKSGALGKAIEDVKEQCSYFNIISRDYKDNATAVPWFPRRIRDLDRFANQILSYGSELDADHPGFTDPEYRKRRKYFADIAYNYKHGEPLPHVDYTKEEIETWGIIFRNLTKLYKTHACREYNHVFPLLVDNCGFREDNIPQLEDVSNFLRDCTGFTLRPVAGLLSSRDFLAGLAFRVFHSTQYIRHPSKPMYTPEPDVCHELMGHVPLFADPAFAQFSQEIGLASLGAPDDYIEKL... | 1.14.16.1; 1.14.16.4 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; | dopamine biosynthetic process [GO:0042416]; eye pigment biosynthetic process [GO:0006726]; germ-band extension [GO:0007377]; L-phenylalanine catabolic process [GO:0006559]; long-term memory [GO:0007616]; serotonin biosynthetic process from tryptophan [GO:0006587]; tyrosine biosynthetic process [GO:0006571] | null | iron ion binding [GO:0005506]; phenylalanine 4-monooxygenase activity [GO:0004505]; tryptophan 5-monooxygenase activity [GO:0004510] | PF00351; | 1.10.800.10; | Biopterin-dependent aromatic amino acid hydroxylase family | null | null | CATALYTIC ACTIVITY: Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine; Xref=Rhea:RHEA:20273, ChEBI:CHEBI:15379, ChEBI:CHEBI:15642, ChEBI:CHEBI:58095, ChEBI:CHEBI:58315, ChEBI:CHEBI:59560; EC=1.14.16.1; CATALYTIC ACTIVITY: ... | null | PATHWAY: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 1/6. | null | null | null | Drosophila melanogaster (Fruit fly) |
P17281 | ENV_SIVCZ | MKVMEKKKRDWNSLSIITIITIILLTPCLTSELWVTVYYGVPVWHDADPVLFCASDAKAHSTEAHNIWATQACVPTDPSPQEVFLPNVIESFNMWKNNMVDQMHEDIISLWDQSLKPCVKLTPLCVTLQCSKANFSQAKNLTNQTSSPPLEMKNCSFNVTTELRDKKKQVYSLFYVEDVVNLGNENNTYRIINCNTTAITQACPKTSFEPIPIHYCAPAGFAILKCNDKDFSGKGKCTNVSTVHCTHGIKPVVTTQLLINGSLAEGNITVRVENKSKNTDVWIVQLVEAVSLNCHRPGNNTRGEVQIGPGMTFYNIENVV... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Surface protein gp120]: Attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, whi... | Simian immunodeficiency virus (isolate CPZ GAB1) (SIV-cpz) (Chimpanzee immunodeficiency virus) |
P17282 | GAG_SIVCZ | MGARASVLTGGKLDRWEKVRLRPGGRKRYMMKHLVWASRELERFACDPGLMESKEGCTKLLQQLEPALKTGSEGLRSLFNTLAVLWCIHSDITVEDTQKALEQLKRHHGEQQSKTESNSGSREGGASQGASASAGISGNYPLVQNAQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGALPQDVNTMLNAVGGHQGAMQVLKEVINEEAAEWDRLHPTHAGPIAPGQLREPRGSDIAGTTSTLQEQIGWTTANPPIPVGDVYRRWVILGLNKVVRMYCPVSILDIRQGPKEPFRDYVDRFYKTLRAEQASQE... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Capsid protein p24 is phosphorylated. {ECO:0000250}.; PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: [Matrix protein p17]: Virion {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Host cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localizat... | null | null | null | null | null | FUNCTION: Matrix protein p17 targets Gag and Gag-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex. Implicated in the release from host cell mediated by Vpu (By similarity). {EC... | Simian immunodeficiency virus (isolate CPZ GAB1) (SIV-cpz) (Chimpanzee immunodeficiency virus) |
P17283 | POL_SIVCZ | MGARASVLTGGKLDRWEKVRLRPGGRKRYMMKHLVWASRELERFAKRHHGEQQSKTESNSGSREGGASQGASASAGISGNYPLVQNAQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGALPQDVNTMLNAVGGHQGAMQVLKEVINEEAAEWDRLHPTHAGPIAPGQLREPRGSDIAGTTSTLQEQIGWTTANPPIPVGDVYRRWVILGLNKVVRMYCPVSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTDTLLVQNANPDCKQILKALGPGATLEEMMTACQGVGGPSHKARVLAEAMSMVQ... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural mo... | PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. {ECO:0000255|P... | SUBCELLULAR LOCATION: [Matrix protein p17]: Virion {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Host cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localizat... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RN... | null | null | null | null | FUNCTION: Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shut off translation (By similarity). {ECO:000... | Simian immunodeficiency virus (isolate CPZ GAB1) (SIV-cpz) (Chimpanzee immunodeficiency virus) |
P17285 | TAT_SIVCZ | MDPIDPDLEPWKHPGSQPRTVCNNCYCKACCYHCIYCFTKKGLGISYGRKKRTTRRRTAPAGSKNNQDSIPKQPLSQSRGNKEGSEKSTKEVASKTEADQ | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970] | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Simian immunodeficiency virus (isolate CPZ GAB1) (SIV-cpz) (Chimpanzee immunodeficiency virus) |
P17289 | TY3H_BOVIN | MPTPNAASPQAKGFRRAVSELDAKQAEAIMSPRFVGRRQSLIQDARKEREKAEAAASSSESAEAAAWLERDGEAVLTLLFALPPTRPPALTRAIKVFETFEAHLHHLETRPAQPLRAGSPPLECFVRCEVPGPVVPALLSALRRVAEDVRAAGESKVLWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQAYRQRRKLIAEIAFQYKQGDPIPHVEYTAEETATWKEVYSTLRGLYPTHACREHLEAFELLERFCGYREDRIPQLEDVSRFLKERTGFQLRPAAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEP... | 1.14.16.2 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P04177}; | dopamine biosynthetic process from tyrosine [GO:0006585]; heart development [GO:0007507]; hyaloid vascular plexus regression [GO:1990384]; response to ethanol [GO:0045471]; response to hypoxia [GO:0001666] | axon [GO:0030424]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; synaptic vesicle [GO:0008021] | iron ion binding [GO:0005506]; tyrosine 3-monooxygenase activity [GO:0004511] | PF00351;PF21417;PF12549; | 3.30.70.260;1.10.800.10; | Biopterin-dependent aromatic amino acid hydroxylase family | PTM: Phosphorylated on Ser-19, Ser-31 and Ser-40 by several protein kinases with different site specificities. Phosphorylation at Ser-31 and Ser-40 leads to an increase of TH activity. Phosphorylation at Ser-40 activates the enzyme and also counteracts the feedback inhibition of TH by catecholamines (By similarity). Ph... | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P24529}. Nucleus {ECO:0000250|UniProtKB:P04177}. Cell projection, axon {ECO:0000250|UniProtKB:P24529}. Cytoplasm {ECO:0000250|UniProtKB:P04177}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:P04177}. Note=When p... | CATALYTIC ACTIVITY: Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-dopa; Xref=Rhea:RHEA:18201, ChEBI:CHEBI:15379, ChEBI:CHEBI:15642, ChEBI:CHEBI:57504, ChEBI:CHEBI:58315, ChEBI:CHEBI:59560; EC=1.14.16.2; Evidence={ECO:0000250|UniProt... | null | PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2. {ECO:0000250|UniProtKB:P07101}. | null | null | FUNCTION: Catalyzes the conversion of L-tyrosine to L-dihydroxyphenylalanine (L-Dopa), the rate-limiting step in the biosynthesis of cathecolamines, dopamine, noradrenaline, and adrenaline. Uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to L-Dopa (By similarity). In addition to tyrosine, is able to c... | Bos taurus (Bovine) |
P17293 | RS12_THETH | MPTINQLVRKGREKVRKKSKVPALKGAPFRRGVCTVVRTVTPKKPNSALRKVAKVRLTSGYEVTAYIPGEGHNLQEHSVVLIRGGRVKDLPGVRYHIVRGVYDAAGVKDRKKSRSKYGTKKPKEAAKTAAKK | null | null | response to antibiotic [GO:0046677]; translation [GO:0006412] | small ribosomal subunit [GO:0015935] | rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]; tRNA binding [GO:0000049] | PF00164; | 2.40.50.140; | Universal ribosomal protein uS12 family | null | null | null | null | null | null | null | FUNCTION: With S4 and S5 plays an important role in translational accuracy. {ECO:0000250}.; FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S s... | Thermus thermophilus |
P17301 | ITA2_HUMAN | MGPERTGAAPLPLLLVLALSQGILNCCLAYNVGLPEAKIFSGPSSEQFGYAVQQFINPKGNWLLVGSPWSGFPENRMGDVYKCPVDLSTATCEKLNLQTSTSIPNVTEMKTNMSLGLILTRNMGTGGFLTCGPLWAQQCGNQYYTTGVCSDISPDFQLSASFSPATQPCPSLIDVVVVCDESNSIYPWDAVKNFLEKFVQGLDIGPTKTQVGLIQYANNPRVVFNLNTYKTKEEMIVATSQTSQYGGDLTNTFGAIQYARKYAYSAASGGRRSATKVMVVVTDGESHDGSMLKAVIDQCNHDNILRFGIAVLGYLNRNAL... | null | null | animal organ morphogenesis [GO:0009887]; blood coagulation [GO:0007596]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; cell-substrate adhesion [GO:0031589]; cellular response to estradiol stimulus [GO:0071392]; cellular r... | axon terminus [GO:0043679]; basal part of cell [GO:0045178]; cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; focal adhesion [GO:0005925]; integrin alpha2-beta1 complex [GO:0034666]; integrin complex [GO:0008305]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | amyloid-beta binding [GO:0001540]; collagen binding [GO:0005518]; collagen binding involved in cell-matrix adhesion [GO:0098639]; collagen receptor activity [GO:0038064]; heparan sulfate proteoglycan binding [GO:0043395]; integrin binding [GO:0005178]; laminin binding [GO:0043236]; metal ion binding [GO:0046872]; prote... | PF01839;PF20805;PF20806;PF00092; | 1.20.5.930;2.130.10.130;2.60.40.1460;2.60.40.1510;2.60.40.1530;3.40.50.410; | Integrin alpha chain family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Integrin alpha-2/beta-1 is a receptor for laminin, collagen, collagen C-propeptides, fibronectin and E-cadherin. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. It is responsible for adhesion of platelets and other cells to collagens, modulation of collagen and collagenase gene expres... | Homo sapiens (Human) |
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