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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P14074 | PRO_HTL1C | MGQIFSRSASPIPRPPRGLAAHHWLNFLQAAYRLEPGPSSYDFHQLKKFLKIALETPVWICPINYSLLASLLPKGYPGRVNEILHILIQTQAQIPSRPAPPPPSSSTHDPPDSDPQIPPPYVEPTAPQVLPVMHPHGAPPNHRPWQMKDLQAIKQEVSQAAPGSPQFMQTIRLAVQQFDPTAKDLQDLLQYLCSSLVASLHHQQLDSLISEAETRGITGYNPLAGPLRVQANNPQQQGLRREYQQLWLAAFAALPGSAKDPSWASILQGLEEPYHAFVERLNIALDNGLPEGTPKDPILRSLAYSNANKECQKLLQARGH... | 3.4.23.- | null | proteolysis [GO:0006508]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral process [GO:0016032] | viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; nucleic acid binding [GO:0003676]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF02228;PF00607;PF19317;PF00077;PF00098; | 1.10.1200.30;2.40.70.10;1.10.185.10;1.10.375.10;4.10.60.10; | null | PTM: [Gag-Pro polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. The protease is autoproteolytically processed at its N- and C-termini. {ECO:0000250|UniProtKB:P10274}.; PTM: [Matrix protein p19]:... | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p15-pro]: Virion {ECO:0000250|UniProtKB:P03345}. | null | null | null | null | null | FUNCTION: [Gag-Pro polyprotein]: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.; FUNCTION: [Matrix protein p19]: Matrix protein. {ECO:0000250|UniProtKB:P033... | Human T-cell leukemia virus 1 (isolate Caribbea HS-35 subtype A) (HTLV-1) |
P14076 | GAG_HTL1C | MGQIFSRSASPIPRPPRGLAAHHWLNFLQAAYRLEPGPSSYDFHQLKKFLKIALETPVWICPINYSLLASLLPKGYPGRVNEILHILIQTQAQIPSRPAPPPPSSSTHDPPDSDPQIPPPYVEPTAPQVLPVMHPHGAPPNHRPWQMKDLQAIKQEVSQAAPGSPQFMQTIRLAVQQFDPTAKDLQDLLQYLCSSLVASLHHQQLDSLISEAETRGITGYNPLAGPLRVQANNPQQQGLRREYQQLWLAAFAALPGSAKDPSWASILQGLEEPYHAFVERLNIALDNGLPEGTPKDPILRSLAYSNANKECQKLLQARGH... | null | null | viral process [GO:0016032] | viral nucleocapsid [GO:0019013] | nucleic acid binding [GO:0003676]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF02228;PF00607;PF19317;PF00098; | 1.10.1200.30;1.10.185.10;1.10.375.10;4.10.60.10; | null | PTM: [Gag polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. {ECO:0000250|UniProtKB:P03345}.; PTM: [Matrix protein p19]: Phosphorylation of the matrix protein p19 by MAPK1 seems to play a role in... | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p15-gag]: Virion {ECO:0000250|UniProtKB:P03345}. | null | null | null | null | null | FUNCTION: [Gag polyprotein]: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.; FUNCTION: [Matrix protein p19]: Matrix protein. {ECO:0000250|UniProtKB:P03345}.... | Human T-cell leukemia virus 1 (isolate Caribbea HS-35 subtype A) (HTLV-1) |
P14077 | GAG_HTL1M | MGQIFSRSASPIPRPPRGLAAHHWLNFLQAAYRLEPGPSSYDFHQLKKFLKIALETPVWICPINYSLLASLLPKGYPGRVNEILHILIQTQAQIPSRPAPPPPSSPTHDPPDSDPQIPPPYVEPTAPQVLPVMHPHGAPPNHRPWQMKDLQAIKQEVSQAAPGSPQFMQTIRLAVQQFDPTAKDLQDLLQYLCSSLVASLHHQQLDSLISEAETRGITSYNPLAGPLRVQANNPQQQGLRREYQQLWLAAFAALPGSAKDPSWASILQGLEEPYHAFVERLNIALDNGLPEGTPKDPILRSLAYSNANKECQKLLQARGH... | null | null | viral process [GO:0016032] | viral nucleocapsid [GO:0019013] | nucleic acid binding [GO:0003676]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF02228;PF00607;PF19317;PF00098; | 1.10.1200.30;1.10.185.10;1.10.375.10;4.10.60.10; | null | PTM: [Gag polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. {ECO:0000250|UniProtKB:P03345}.; PTM: [Matrix protein p19]: Phosphorylation of the matrix protein p19 by MAPK1 seems to play a role in... | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p15-gag]: Virion {ECO:0000250|UniProtKB:P03345}. | null | null | null | null | null | FUNCTION: [Gag polyprotein]: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.; FUNCTION: [Matrix protein p19]: Matrix protein. {ECO:0000250|UniProtKB:P03345}.... | Human T-cell leukemia virus 1 (strain Japan MT-2 subtype A) (HTLV-1) |
P14078 | POL_HTL1C | MGQIFSRSASPIPRPPRGLAAHHWLNFLQAAYRLEPGPSSYDFHQLKKFLKIALETPVWICPINYSLLASLLPKGYPGRVNEILHILIQTQAQIPSRPAPPPPSSSTHDPPDSDPQIPPPYVEPTAPQVLPVMHPHGAPPNHRPWQMKDLQAIKQEVSQAAPGSPQFMQTIRLAVQQFDPTAKDLQDLLQYLCSSLVASLHHQQLDSLISEAETRGITGYNPLAGPLRVQANNPQQQGLRREYQQLWLAAFAALPGSAKDPSWASILQGLEEPYHAFVERLNIALDNGLPEGTPKDPILRSLAYSNANKECQKLLQARGH... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; Note=The RT polymerase active site binds 2 magnesium ions. {ECO:0000255|PROSITE-ProRule:PRU00405}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase ... | 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 nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural molecule activity [GO:0005198]; zinc ion bi... | PF02228;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF00098; | 1.10.1200.30;3.30.70.270;2.40.70.10;1.10.185.10;3.10.10.10;1.10.375.10;3.30.420.10;4.10.60.10; | null | PTM: [Matrix protein p19]: Phosphorylation of the matrix protein p19 by MAPK1 seems to play a role in budding. {ECO:0000250|UniProtKB:P03345}.; PTM: [Gag-Pro-Pol polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and i... | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p15-pro]: Virion {ECO:0000250|UniProtKB:P03345}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CH... | null | null | null | null | FUNCTION: [Gag-Pro-Pol polyprotein]: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.; FUNCTION: [Matrix protein p19]: Matrix protein. {ECO:0000250|UniProtKB:... | Human T-cell leukemia virus 1 (isolate Caribbea HS-35 subtype A) (HTLV-1) |
P14079 | TAX_HTL1C | MAHFPGFGQSLLFGYPVYVFGDCVQGDWCPISGGLCSARLHRHALLATCPEHQITWDPIDGRVIGSALQFLIPRLPSFPTQRTSKTLKVLTPPITHTTPNIPPSFLQAMRKYSPFRNGYMEPTLGQHLPTLSFPDPGLRPQNLYTLWGGSVVCMYLYQLSPPITWPLLPHVIFCHPGQLGAFLTNVPYKRIEKLLYKISLTTGALIILPEDCLPTTLFQPARAPVTLTAWQNGLLPFHSTLTTPGLIWTFTDGTPMISGPCPKDGQPSLVLQSSSFIFHKFQTKAYHPSFLLSHGLIQYSSFHNLHLLFEEYTNIPISLL... | null | null | cellular response to lipopolysaccharide [GO:0071222]; negative regulation of gene expression [GO:0010629]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of mRNA stability [GO:0043488]; symbiont-mediated perturbation of host cell cycle G0/G1 transition checkpoint [GO:0039646]; symbiont-medi... | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | DNA binding [GO:0003677]; metal ion binding [GO:0046872]; SH3 domain binding [GO:0017124] | PF02959; | null | Deltaretrovirus Tax protein family | PTM: Phosphorylation at Thr-48 results in the loss of NF-kappa-B activation function. Phosphorylation at Thr-215 results in loss of CREB and NF-B responsive promoters activation. Phosphorylation at Thr-184 and Ser-336 have no effect on these Tax functions. Phosphorylation of either Ser-300 or Ser-301 is necessary for l... | SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:14679154}. Host cytoplasm {ECO:0000269|PubMed:14679154}. Note=Shuttles from the host nucleus to the cytoplasm. Found predominantly in the nucleus, where it is equally distributed between the nucleoplasm and the nuclear matrix. {ECO:0000250|UniProtKB:P03409}. | null | null | null | null | null | FUNCTION: Transcriptional activator that governs the viral transcription from the 5'LTR via the recruitment of dimers of host phosphorylated CREB1. Together they bind cAMP response elements within the viral promoter and mediate high-level viral transcription. Increases host CREB1 O-GlcNAcylation to further increase 5'L... | Human T-cell leukemia virus 1 (isolate Caribbea HS-35 subtype A) (HTLV-1) |
P14081 | SELB_ECOLI | MIIATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYAYWPQPDGRVPGFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARVDEVERQVKEVLREYGFAEAKLFITAATEGRGMDALREHLLQLPEREHASQHSFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDSLWLTGVNKPMRVRALHAQNQPTETANAGQRIALNIAGDAEKEQINRGDWLLADVPPEPFTRVIVELQTHTPLTQWQPLHIHHAASHVTGRVSLLEDNLAELVFDTPLWLADNDR... | null | null | formation of translation preinitiation complex [GO:0001731]; selenocysteine incorporation [GO:0001514]; selenocysteine metabolic process [GO:0016259] | cytosol [GO:0005829] | GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; selenocysteine insertion sequence binding [GO:0035368]; translation elongation factor activity [GO:0003746]; translation initiation factor activity [GO:0003743]; tRNA binding [GO:0000049] | PF21214;PF00009;PF03144;PF21458;PF09106;PF09107; | 3.40.50.300;2.40.30.10;1.10.10.10; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, SelB subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP. | Escherichia coli (strain K12) |
P14082 | BDNF_PIG | MTILFLTMVISYFGCMKAAPMKEANVRGQGSLAYPGVRTHGTLESVNGPKAGSRGLTSSSSSSLADTFEHVIEELLDEDQKVRPNEENNKDADMYTSRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCDSISEWVTAADKKTAVDMSGGTVTVLEKVPVSKGQLKQYFYETKCNPMGYTKEGCRGIDKRHWNSQCRTTQSYVRALTMDSKKRIGWRFIRIDTSCVCTLTIKRGR | null | null | memory [GO:0007613]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of neuron apoptotic process [GO:0043524]; nerve development [GO:0021675]; nerve growth factor signaling pathway [GO:0038180]; neuron projection morphogenesis [GO:0048812]; peripheral nervous system development [GO:000742... | axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471]; synaptic vesicle [GO:0008021] | growth factor activity [GO:0008083]; nerve growth factor receptor binding [GO:0005163] | PF00243; | 2.10.90.10; | NGF-beta family | PTM: [BDNF precursor form]: N-glycosylated and glycosulfated, contrary to mature BDNF. {ECO:0000250|UniProtKB:P23560}.; PTM: Mature BDNF is produced by proteolytic removal of the propeptide, catalyzed by a FURIN family member. In addition, the precursor form is proteolytically cleaved within the propeptide, but this is... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P23560}.; SUBCELLULAR LOCATION: [BDNF precursor form]: Secreted {ECO:0000250|UniProtKB:P23560}. Note=A proportion of BDNF is secreted as immature precursor (proBDNF). {ECO:0000250|UniProtKB:P23560}. | null | null | null | null | null | FUNCTION: Important signaling molecule that activates signaling cascades downstream of NTRK2 (By similarity). During development, promotes the survival and differentiation of selected neuronal populations of the peripheral and central nervous systems. Participates in axonal growth, pathfinding and in the modulation of ... | Sus scrofa (Pig) |
P14083 | LOV_DROME | MLKDAHQKLIKHRQSTKLSMTDFACQAAPVKQPLPLELPLPLSVQLQLLAKTPTSDHAPMHSTPPTTPPTPPPLPLNMSQSASAVTEAATPENSLPATPPSEGALAVPSAPQDHYSLRWNNHQNHILRAFDALLKTKTLVDVTLVCAETSIRAHKMVLSACSPFFQRVFAETPCKHPVIVLKDFRGWVVQAIVDFMYRGEISVPQQRLQTLIQAGESLQVRGLVESSVPEHTPTPAASPDDFGMLDTSMLSSTFEDECPTMVRPSKGGKLLMPSARLFGNASSAIAALGLRRKREQESDRDLESDQELGGSSPMPRRKQA... | null | null | gravitaxis [GO:0042332]; larval feeding behavior [GO:0030536]; larval walking behavior [GO:0008346]; male courtship behavior [GO:0008049]; negative gravitaxis [GO:0048060]; oogenesis [GO:0048477]; regulation of transcription by RNA polymerase II [GO:0006357]; ventral midline development [GO:0007418] | nucleus [GO:0005634] | DNA binding [GO:0003677] | PF00651;PF05225; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00320}. | null | null | null | null | null | FUNCTION: Has a regulatory role during midline cell development. {ECO:0000269|PubMed:16631157}. | Drosophila melanogaster (Fruit fly) |
P14084 | SRC_AVISS | MGSSKSKPKDPSQRRRSLEPPDSTHHGGFPASQTPNKTAAPDTHRTPSRSFGTVATEPKLFGGFNTSDTVTSPQRAGALAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNPENPRGTFLVRESETTKGAYCLSVSDFDNARGLNVKHYKIRKLDSGGFYITSRTQFSSLQQLVAYYSKHADGLCHRLTNVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHE... | 2.7.10.2 | null | bone resorption [GO:0045453]; cell adhesion [GO:0007155]; epidermal growth factor receptor signaling pathway [GO:0007173]; innate immune response [GO:0045087]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; osteoclast... | extrinsic component of cytoplasmic side of plasma membrane [GO:0031234] | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; signaling receptor binding [GO:0005102] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: The phosphorylated form is termed pp60v-src. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: This phosphoprotein, required for both the initiation and the maintenance of neoplastic transformation, is a protein kinase that catalyzes the phosphorylation of tyrosine residues in vitro. | Avian sarcoma virus (strain S1) |
P14085 | SRC_AVIST | MGSSKSKPKDPSQRRRSLEPPDSTHHGGFPASQTPNKTAAPDTHRTPSRSFGTVATEPKLFGGFNTSDTVTSPQRAGALAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNPENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFSSLQQLVAYYSKHADGLCHRLTNVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHE... | 2.7.10.2 | null | bone resorption [GO:0045453]; cell adhesion [GO:0007155]; epidermal growth factor receptor signaling pathway [GO:0007173]; innate immune response [GO:0045087]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; osteoclast... | extrinsic component of cytoplasmic side of plasma membrane [GO:0031234] | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; signaling receptor binding [GO:0005102] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: The phosphorylated form is termed pp60v-src. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: This phosphoprotein, required for both the initiation and the maintenance of neoplastic transformation, is a protein kinase that catalyzes the phosphorylation of tyrosine residues in vitro. | Avian sarcoma virus (strain S2) |
P14087 | ANXA1_CAVCU | MSMVSEFLKQAYFIDNQEQDYVKTVKSSKGGPGSAVSPYPSFDASSDVAALHKAITVKGVDEATIIDILTKRNNAQRQQIKAAYLQEKGKPLDEALKKALTGHLEEVVLALLKTPAQLDADELRAAMKGLGTDEDTLIEILVSRKNREIKEINRVYRDELKRDLAKDITSDTSGDFQKALLSLAKGDRCEDLSVNDDLADSDARALYEAGERRKGTDVNVFITILTTRSYSHLRRVFQKYTKYSQHDMNKALDLELKGDIENCLTAIVKCATSTPAFFAEKLHLAMKGAGTRHKALIRIMVSRSEIDMNDIKVYYQKMYG... | null | null | actin cytoskeleton organization [GO:0030036]; adaptive immune response [GO:0002250]; alpha-beta T cell differentiation [GO:0046632]; arachidonic acid secretion [GO:0050482]; cell surface receptor signaling pathway [GO:0007166]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to hydrogen per... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; lateral plasma membrane [GO:0016328]; motile cilium [GO:0031514]; nucleus [GO:0005634]; phagocytic cup [GO:00... | cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; phospholipase A2 inhibitor activity [GO:0019834] | PF00191; | 1.10.220.10; | Annexin family | PTM: Phosphorylated by protein kinase C, EGFR and TRPM7. Phosphorylated in response to EGF treatment. {ECO:0000250|UniProtKB:P04083}.; PTM: Sumoylated. {ECO:0000250|UniProtKB:P10107}.; PTM: Proteolytically cleaved by cathepsin CTSG to release the active N-terminal peptide Ac2-26. {ECO:0000250|UniProtKB:P04083}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07150}. Cytoplasm {ECO:0000250|UniProtKB:P10107}. Cell projection, cilium {ECO:0000250|UniProtKB:P10107}. Basolateral cell membrane {ECO:0000250|UniProtKB:P51662}. Lateral cell membrane {ECO:0000250|UniProtKB:P10107}. Cell membrane {ECO:0000250|UniProtKB:P10107}; Pe... | null | null | null | null | null | FUNCTION: Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity. Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response. Contributes to the adaptive i... | Cavia cutleri (Guinea pig) |
P14091 | CATE_HUMAN | MKTLLLLLLVLLELGEAQGSLHRVPLRRHPSLKKKLRARSQLSEFWKSHNLDMIQFTESCSMDQSAKEPLINYLDMEYFGTISIGSPPQNFTVIFDTGSSNLWVPSVYCTSPACKTHSRFQPSQSSTYSQPGQSFSIQYGTGSLSGIIGADQVSVEGLTVVGQQFGESVTEPGQTFVDAEFDGILGLGYPSLAVGGVTPVFDNMMAQNLVDLPMFSVYMSSNPEGGAGSELIFGGYDHSHFSGSLNWVPVTKQAYWQIALDNIQVGGTVMFCSEGCQAIVDTGTSLITGPSDKIKQLQNAIGAAPVDGEYAVECANLNVM... | 3.4.23.34 | null | antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; protein autoprocessing [GO:0016540]; proteolysis [GO:0006508] | endosome [GO:0005768]; intracellular membrane-bounded organelle [GO:0043231] | aspartic-type endopeptidase activity [GO:0004190]; identical protein binding [GO:0042802]; peptidase activity [GO:0008233] | PF07966;PF00026; | 2.40.70.10; | Peptidase A1 family | PTM: Glycosylated. The nature of the carbohydrate chain varies between cell types. In fibroblasts, the proenzyme contains a high mannose-type oligosaccharide, while the mature enzyme contains a complex-type oligosaccharide. In erythrocyte membranes, both the proenzyme and mature enzyme contain a complex-type oligosacch... | SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:7983070}. Note=The proenzyme is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome. | CATALYTIC ACTIVITY: Reaction=Similar to cathepsin D, but slightly broader specificity.; EC=3.4.23.34; Evidence={ECO:0000269|PubMed:7789521, ECO:0000269|PubMed:8765029}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.06 mM for hemoglobin {ECO:0000269|PubMed:8346912}; KM=0.13 mM for Pro-Pro-Thr-Ile-Phe-Phe(4-NO2)-Arg-Leu {ECO:0000269|PubMed:8346912}; KM=0.04 mM for Lys-Pro-Ile-Glu-Phe-Phe(4-NO2)-Arg-Leu {ECO:0000269|PubMed:8346912}; | null | null | null | FUNCTION: May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain. {ECO:0000269|PubMed:87... | Homo sapiens (Human) |
P14094 | AT1B1_MOUSE | MARGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYGCLAGIFIGTIQVMLLTISELKPTYQDRVAPPGLTQIPQIQKTEISFRPNDPKSYEAYVLNIIRFLEKYKDSAQKDDMIFEDCGNVPSEPKERGDINHERGERKVCRFKLDWLGNCSGLNDDSYGYREGKPCIIIKLNRVLGFKPKPPKNESLETYPLMMKYNPNVLPVQCTGKRDEDKDKVGNIEYFGMGGYYGFPLQYYPYYGKLLQPKYLQPLLAVQFTNLTVDTEIRVECKAYGENIGYSEKDRFQGRFDVKIEIKS | null | null | ATP metabolic process [GO:0046034]; cardiac muscle contraction [GO:0060048]; cell adhesion [GO:0007155]; establishment or maintenance of transmembrane electrochemical gradient [GO:0010248]; intracellular calcium ion homeostasis [GO:0006874]; intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; caveola [GO:0005901]; intercalated disc [GO:0014704]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; myelin sheath [GO:0043209]; organelle membrane [GO:0031090]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; sodium:pot... | ATPase activator activity [GO:0001671]; ATPase binding [GO:0051117]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]; protein heterodimerization activity [GO:0046982]; protein kinase binding [GO:0019901]; protein-macromolecule adaptor activity [GO:0030674] | PF00287; | 1.20.5.170;2.60.40.1660; | X(+)/potassium ATPases subunit beta family | PTM: Glutathionylated (PubMed:21454534). N-glycosylated (By similarity). {ECO:0000250|UniProtKB:P07340, ECO:0000269|PubMed:21454534}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:P07340}; Single-pass type II membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000269|PubMed:23392350}. Note=Colocalizes with OBSCN at the intercalated disk an... | null | null | null | null | null | FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane.; ... | Mus musculus (Mouse) |
P14095 | GROA_RAT | MVSATRSLLCAALPVLATSRQATGAPVANELRCQCLQTVAGIHFKNIQSLKVMPPGPHCTQTEVIATLKNGREACLDPEAPMVQKIVQKMLKGVPK | null | null | antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cellular response to interleukin-17 [GO:0097398]; cellular response to lipopolysaccharide [GO:0071222]; chemokine-mediated signaling pathway [GO:0070098]; inflammatory response [GO:0006954]; neutrophil chemotaxis [GO:0030593]; positiv... | extracellular space [GO:0005615] | chemokine activity [GO:0008009]; CXCR chemokine receptor binding [GO:0045236]; growth factor activity [GO:0008083] | PF00048; | 2.40.50.40; | Intercrine alpha (chemokine CxC) family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Has chemotactic activity for neutrophils. Contributes to neutrophil activation during inflammation. | Rattus norvegicus (Rat) |
P14097 | CCL4_MOUSE | MKLCVSALSLLLLVAAFCAPGFSAPMGSDPPTSCCFSYTSRQLHRSFVMDYYETSSLCSKPAVVFLTKRGRQICANPSEPWVTEYMSDLELN | null | null | cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; cellular response to xenobiotic stimulus [GO:0071466]; chemokine-mediated signaling pathway [GO:0070098]; eosinophil chemotaxis [GO:0048245]; G protein-coupled ... | extracellular space [GO:0005615] | CCR chemokine receptor binding [GO:0048020]; chemokine activity [GO:0008009] | PF00048; | 2.40.50.40; | Intercrine beta (chemokine CC) family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Monokine with inflammatory and chemokinetic properties. | Mus musculus (Mouse) |
P14099 | PDE2A_BOVIN | MRRQPAASRDLFAQEPVPPGSGDGALQDALLSLGSVIDVAGLQQAVKEALSAVLPKVETVYTYLLDGESRLVCEEPPHELPQEGKVREAVISRKRLGCNGLGPSDLPGKPLARLVAPLAPDTQVLVIPLVDKEAGAVAAVILVHCGQLSDNEEWSLQAVEKHTLVALKRVQALQQRESSVAPEATQNPPEEAAGDQKGGVAYTNQDRKILQLCGELYDLDASSLQLKVLQYLQQETQASRCCLLLVSEDNLQLSCKVIGDKVLEEEISFPLTTGRLGQVVEDKKSIQLKDLTSEDMQQLQSMLGCEVQAMLCVPVISRAT... | 3.1.4.17 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:1654333}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions. {ECO:0000250|UniProtKB:O00408}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O00408}; Note=Binds 2 divalent m... | cAMP-mediated signaling [GO:0019933]; cellular response to cGMP [GO:0071321]; cellular response to granulocyte macrophage colony-stimulating factor stimulus [GO:0097011]; cellular response to macrophage colony-stimulating factor stimulus [GO:0036006]; cellular response to mechanical stimulus [GO:0071260]; cGMP cataboli... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial outer membrane [GO:0005741]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO... | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; cGMP binding [GO:0030553]; cGMP-stimulated cyclic-nucleotide phosphodiesterase activity [GO:0004118]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803] | PF01590;PF00233; | 3.30.450.40;1.10.1300.10; | Cyclic nucleotide phosphodiesterase family, PDE2 subfamily | null | SUBCELLULAR LOCATION: [Isoform PDE2A3]: Cell membrane {ECO:0000250|UniProtKB:Q01062}; Peripheral membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform PDE2A1]: Cytoplasm {ECO:0000250|UniProtKB:Q01062}.; SUBCELLULAR LOCATION: [Isoform PDE2A2]: Mitochondrion {ECO:0000250|UniProtKB:Q01062}. Mitochondrion inner m... | CATALYTIC ACTIVITY: Reaction=a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H(+); Xref=Rhea:RHEA:14653, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57867, ChEBI:CHEBI:58464; EC=3.1.4.17; Evidence={ECO:0000269|PubMed:1654333, ECO:0000269|PubMed:6276403}; PhysiologicalDirection=left-to-righ... | null | null | null | null | FUNCTION: cGMP-activated cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes (PubMed:1654333, PubMed:6276403). Has a higher efficiency with cGMP compared to cAMP (By similarity). Plays a role in cell grow... | Bos taurus (Bovine) |
P14100 | PDE1A_BOVIN | MGSTATETEELENTTFKYLIGEQTEKMWQRLKGILRCLVKQLEKGDVNVIDLKKNIEYAASVLEAVYIDETRRLLDTDDELSDIQSDSVPSEVRDWLASTFTRKMGMMKKKSEEKPRFRSIVHVVQAGIFVERMYRKSYHMVGLAYPEAVIVTLKDVDKWSFDVFALNEASGEHSLKFMIYELFTRYDLINRFKIPVSCLIAFAEALEVGYSKYKNPYHNLIHAADVTQTVHYIMLHTGIMHWLTELEILAMVFAAAIHDYEHTGTTNNFHIQTRSDVAILYNDRSVLENHHVSAAYRLMQEEEMNVLINLSKDDWRDLR... | 3.1.4.17 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q01064}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions. {ECO:0000250|UniProtKB:Q01064}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q01064}; Note=Binds 2 divalent... | cAMP-mediated signaling [GO:0019933] | neuronal cell body [GO:0043025] | 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; calmodulin binding [GO:0005516]; calmodulin-activated 3',5'-cyclic-GMP phosphodiesterase activity [GO:0048101]; calmodulin-activated dual specificity 3',5'-cyclic-GMP, 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004117]; metal ion binding [GO:0046872] | PF00233;PF08499; | 1.10.1300.10; | Cyclic nucleotide phosphodiesterase family, PDE1 subfamily | null | null | CATALYTIC ACTIVITY: [Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A]: Reaction=a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H(+); Xref=Rhea:RHEA:14653, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57867, ChEBI:CHEBI:58464; EC=3.1.4.17; Evidence... | null | null | null | null | FUNCTION: Calcium/calmodulin-dependent cyclic nucleotide phosphodiesterase with a dual specificity for the second messengers cGMP and cAMP, which are key regulators of many important physiological processes. Has a higher efficiency with cGMP compared to cAMP. {ECO:0000269|PubMed:8537356}. | Bos taurus (Bovine) |
P14105 | MYH9_CHICK | MAQRDADKYLYVDKNIINNPLTQADWAAKKLVWVPSEKSGFEAASLKEEVGDEAIVELAENGKKVKVNKDDIQKMNPPKFSKVEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQ... | null | null | actin cytoskeleton organization [GO:0030036]; actin filament-based movement [GO:0030048]; angiogenesis [GO:0001525]; blood vessel endothelial cell migration [GO:0043534]; cortical granule exocytosis [GO:0060471]; cytokinetic process [GO:0032506]; membrane protein ectodomain proteolysis [GO:0006509]; monocyte differenti... | actin cytoskeleton [GO:0015629]; actomyosin contractile ring [GO:0005826]; cell cortex [GO:0005938]; cell leading edge [GO:0031252]; cleavage furrow [GO:0032154]; cortical granule [GO:0060473]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]; nucleus [GO:000563... | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; integrin binding [GO:0005178]; microfilament motor activity [GO:0000146]; protein homodimerization activity [GO:0042803]; protein self-association [GO:0043621]; protein-membrane adaptor activity [GO:0043495] | PF00063;PF02736;PF01576; | 1.10.10.820;1.20.5.340;1.20.58.530;3.30.70.1590;6.10.250.2420;3.40.850.10;2.30.30.360;1.20.120.720;4.10.270.10; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8VDD5}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q8VDD5}. Cytoplasmic vesicle, secretory vesicle, Cortical granule {ECO:0000250|UniProtKB:Q8VDD5}. Note=Colocalizes with actin filaments at lamellipodia margins and at the leading edge of migrating... | null | null | null | null | null | FUNCTION: Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. {ECO:0000250|UniProtKB:P35579}. | Gallus gallus (Chicken) |
P14106 | C1QB_MOUSE | MKTQWGEVWTHLLLLLLGFLHVSWAQSSCTGPPGIPGIPGVPGVPGSDGQPGTPGIKGEKGLPGLAGDLGEFGEKGDPGIPGTPGKVGPKGPVGPKGTPGPSGPRGPKGDSGDYGATQKVAFSALRTINSPLRPNQVIRFEKVITNANENYEPRNGKFTCKVPGLYYFTYHASSRGNLCVNLVRGRDRDSMQKVVTFCDYAQNTFQVTTGGVVLKLEQEEVVHLQATDKNSLLGIEGANSIFTGFLLFPDMDA | null | null | complement activation, classical pathway [GO:0006958]; innate immune response [GO:0045087]; inner ear development [GO:0048839]; synapse pruning [GO:0098883] | collagen trimer [GO:0005581]; complement component C1 complex [GO:0005602]; complement component C1q complex [GO:0062167]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; postsynapse [GO:0098794]; synapse [GO:0045202] | identical protein binding [GO:0042802] | PF00386;PF01391; | 2.60.120.40; | null | PTM: Hydroxylated on lysine and proline residues. Hydroxylated lysine residues can be glycosylated. Mouse C1Q contains up to 64.0 hydroxylysine-galactosylglucose residues. Total percentage hydroxylysine residues glycosylated is 95.1%. Contains no hydroxylysine-monosaccharides. {ECO:0000269|PubMed:6286235}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc... | Mus musculus (Mouse) |
P14115 | RL27A_MOUSE | MPSRLRKTRKLRGHVSHGHGRIGKHRKHPGGRGNAGGMHHHRINFDKYHPGYFGKVGMRHYHLKRNQSFCPTVNLDKLWTLVSEQTRVNAAKNKTGVAPIIDVVRSGYYKVLGKGKLPKQPVIVKAKFFSRRAEEKIKGVGGACVLVA | null | null | cytoplasmic translation [GO:0002181]; translation [GO:0006412]; translation at postsynapse [GO:0140242]; translation at presynapse [GO:0140236] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; cytosolic ribosome [GO:0022626]; postsynapse [GO:0098794]; presynapse [GO:0098793]; ribosome [GO:0005840]; synapse [GO:0045202] | structural constituent of ribosome [GO:0003735] | PF00828; | 3.100.10.10;4.10.990.10; | Universal ribosomal protein uL15 family | PTM: Hydroxylated on His-39 by MINA. {ECO:0000250|UniProtKB:P46776}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:36517592}. | null | null | null | null | null | FUNCTION: Component of the large ribosomal subunit (PubMed:36517592). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:36517592). {ECO:0000269|PubMed:36517592}. | Mus musculus (Mouse) |
P14120 | RL30_YEAST | MAPVKSQESINQKLALVIKSGKYTLGYKSTVKSLRQGKSKLIIIAANTPVLRKSELEYYAMLSKTKVYYFQGGNNELGTAVGKLFRVGVVSILEAGDSDILTTLA | null | null | cytoplasmic translation [GO:0002181]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; rRNA processing [GO:0006364] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | pre-mRNA 5'-splice site binding [GO:0030627]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF01248; | 3.30.1330.30; | Eukaryotic ribosomal protein eL30 family | null | SUBCELLULAR LOCATION: Cytoplasm {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) |
P14126 | RL3_YEAST | MSHRKYEAPRHGHLGFLPRKRAASIRARVKAFPKDDRSKPVALTSFLGYKAGMTTIVRDLDRPGSKFHKREVVEAVTVVDTPPVVVVGVVGYVETPRGLRSLTTVWAEHLSDEVKRRFYKNWYKSKKKAFTKYSAKYAQDGAGIERELARIKKYASVVRVLVHTQIRKTPLAQKKAHLAEIQLNGGSISEKVDWAREHFEKTVAVDSVFEQNEMIDAIAVTKGHGFEGVTHRWGTKKLPRKTHRGLRKVACIGAWHPAHVMWSVARAGQRGYHSRTSINHKIYRVGKGDDEANGATSFDRTKKTITPMGGFVHYGEIKND... | null | null | cytoplasmic translation [GO:0002181]; maintenance of translational fidelity [GO:1990145]; ribosomal large subunit assembly [GO:0000027]; rRNA processing [GO:0006364]; translation [GO:0006412] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF00297; | 3.30.1430.10;4.10.960.10;2.40.30.10; | Universal ribosomal protein uL3 family | PTM: Methylation at His-243 by HPM1 is required for proper 60S subunit assembly and promotes translational elongation fidelity. {ECO:0000269|PubMed:24865971, ECO:0000269|PubMed:26826131}. | 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 (PubMed:22096102, PubMed:24865971). The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14131 | RS16_MOUSE | MPSKGPLQSVQVFGRKKTATAVAHCKRGNGLIKVNGRPLEMIEPRTLQYKLLEPVLLLGKERFAGVDIRVRVKGGGHVAQIYAIRQSISKALVAYYQKYVDEASKKEIKDILIQYDRTLLVADPRRCESKKFGGPGARARYQKSYR | null | null | cellular response to leukemia inhibitory factor [GO:1990830]; cytoplasmic translation [GO:0002181]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; ribosomal small subunit biogenesis [GO:0042274]; translation at postsynapse [GO:0140242]; translation at presynapse [... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; nucleolus [GO:0005730]; postsynapse [GO:0098794]; presynapse [GO:0098793]; ribosome [GO:0005840]; small ribosomal subunit [GO:0015935]; small-subunit processome [GO:0032040]; synapse [GO:0045202] | RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF00380; | 3.30.230.10; | Universal ribosomal protein uS9 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:36517592}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62249}. | 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 (PubMed:36517592). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome ... | Mus musculus (Mouse) |
P14136 | GFAP_HUMAN | MERRRITSAARRSYVSSGEMMVGGLAPGRRLGPGTRLSLARMPPPLPTRVDFSLAGALNAGFKETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNLAQDLATVRQKLQDETNLRLEAENNLAAYRQEADEATLARLDLERKIESLEEEIRFLRKIHEEEVRELQEQLARQQVHVELDVAKPDLTAALKEIRTQYEAMASSNMHEAEEWYRSKFADLTDAAARNAELLRQAKHEANDYRRQLQSLTCDLESLRGTNESLERQMREQEERHVRE... | null | null | astrocyte development [GO:0014002]; Bergmann glial cell differentiation [GO:0060020]; D-aspartate import across plasma membrane [GO:0070779]; extracellular matrix organization [GO:0030198]; gene expression [GO:0010467]; intermediate filament organization [GO:0045109]; intracellular protein transport [GO:0006886]; long-... | astrocyte end-foot [GO:0097450]; cell body [GO:0044297]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytoplasmic side of lysosomal membrane [GO:0098574]; cytosol [GO:0005829]; intermediate filament [GO:0005882]; intermediate filament cytoskeleton [GO:0045111] | identical protein binding [GO:0042802]; integrin binding [GO:0005178]; kinase binding [GO:0019900]; structural constituent of cytoskeleton [GO:0005200] | PF00038;PF04732; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: Phosphorylated by PKN1. {ECO:0000269|PubMed:12686604, ECO:0000269|PubMed:9099667, ECO:0000269|PubMed:9175763}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12058025}. Note=Associated with intermediate filaments. {ECO:0000269|PubMed:12058025}. | null | null | null | null | null | FUNCTION: GFAP, a class-III intermediate filament, is a cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells. | Homo sapiens (Human) |
P14137 | CP11A_RAT | MLAKGLCLRSVLVKSCQPFLSPVWQGPGLATGNGAGISSTNSPRSFNEIPSPGDNGWINLYHFLRENGTHRIHYHHMQNFQKYGPIYREKLGNMESVYILDPKDAATLFSCEGPNPERYLVPPWVAYHQYYQRPIGVLFKSSDAWRKDRIVLNQEVMAPDSIKNFVPLLEGVAQDFIKVLHRRIKQQNSGKFSGDISDDLFRFAFESITSVVFGERLGMLEEIVDPESQRFIDAVYQMFHTSVPMLNMPPDLFRLFRTKTWKDHAAAWDVIFSKADEYTQNFYWDLRQKRDFSKYPGVLYSLLGGNKLPFKNIQANITEM... | 1.14.15.6 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P05108}; | biphenyl metabolic process [GO:0018879]; C21-steroid hormone biosynthetic process [GO:0006700]; cellular response to antibiotic [GO:0071236]; cellular response to cadmium ion [GO:0071276]; cellular response to cAMP [GO:0071320]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to f... | mitochondrial crista [GO:0030061]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; perikaryon [GO:0043204] | cholesterol binding [GO:0015485]; cholesterol monooxygenase (side-chain-cleaving) activity [GO:0008386]; heme binding [GO:0020037]; iron ion binding [GO:0005506] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:21075169, ECO:0000269|PubMed:2170421, ECO:0000269|PubMed:3948785}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000269|PubMed:3948785}. | CATALYTIC ACTIVITY: Reaction=cholesterol + 6 H(+) + 3 O2 + 6 reduced [adrenodoxin] = 4-methylpentanal + 4 H2O + 6 oxidized [adrenodoxin] + pregnenolone; Xref=Rhea:RHEA:35739, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:16581, ChEBI:CH... | null | PATHWAY: Lipid metabolism; C21-steroid hormone metabolism. {ECO:0000250|UniProtKB:P05108}.; PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000250|UniProtKB:P05108}. | null | null | FUNCTION: A cytochrome P450 monooxygenase that catalyzes the side-chain hydroxylation and cleavage of cholesterol to pregnenolone, the precursor of most steroid hormones. Catalyzes three sequential oxidation reactions of cholesterol, namely the hydroxylation at C22 followed with the hydroxylation at C20 to yield 20R,22... | Rattus norvegicus (Rat) |
P14138 | EDN3_HUMAN | MEPGLWLLFGLTVTSAAGFVPCSQSGDAGRRGVSQAPTAARSEGDCEETVAGPGEETVAGPGEGTVAPTALQGPSPGSPGQEQAAEGAPEHHRSRRCTCFTYKDKECVYYCHLDIIWINTPEQTVPYGLSNYRGSFRGKRSAGPLPGNLQLSHRPHLRCACVGRYDKACLHFCTQTLDVSSNSRTAEKTDKEEEGKVEVKDQQSKQALDLHHPKLMPGSGLALAPSTCPRCLFQEGAP | null | null | axon extension [GO:0048675]; axon guidance [GO:0007411]; blood circulation [GO:0008015]; cell population proliferation [GO:0008283]; cell surface receptor signaling pathway [GO:0007166]; cell-cell signaling [GO:0007267]; establishment of localization in cell [GO:0051649]; intracellular calcium ion homeostasis [GO:00068... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | endothelin B receptor binding [GO:0031708]; hormone activity [GO:0005179]; signaling receptor binding [GO:0005102] | PF00322; | null | Endothelin/sarafotoxin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Endothelins are endothelium-derived vasoconstrictor peptides. | Homo sapiens (Human) |
P14141 | CAH3_RAT | MAKEWGYASHNGPEHWHELYPIAKGDNQSPIELHTKDIRHDPSLQPWSVSYDPGSAKTILNNGKTCRVVFDDTFDRSMLRGGPLSGPYRLRQFHLHWGSSDDHGSEHTVDGVKYAAELHLVHWNPKYNTFGEALKQPDGIAVVGIFLKIGREKGEFQILLDALDKIKTKGKEAPFNHFDPSCLFPACRDYWTYHGSFTTPPCEECIVWLLLKEPMTVSSDQMAKLRSLFASAENEPPVPLVGNWRPPQPIKGRVVRASFK | 4.2.1.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:11024467}; | one-carbon metabolic process [GO:0006730]; response to bacterium [GO:0009617]; response to ethanol [GO:0045471]; response to oxidative stress [GO:0006979] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | carbonate dehydratase activity [GO:0004089]; nickel cation binding [GO:0016151]; phosphatase activity [GO:0016791]; zinc ion binding [GO:0008270] | PF00194; | 3.10.200.10; | Alpha-carbonic anhydrase family | PTM: S-thiolated both by thiol-disulfide exchange with glutathione disulfide and by oxyradical-initiated S-thiolation with reduced glutathione. {ECO:0000269|PubMed:11024467}.; PTM: S-glutathionylated in hepatocytes under oxidative stress. {ECO:0000269|PubMed:11024467}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07451}. | 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; Evidence={ECO:0000250|UniProtKB:P07451}; | null | null | null | null | FUNCTION: Reversible hydration of carbon dioxide. {ECO:0000250|UniProtKB:P07451}. | Rattus norvegicus (Rat) |
P14142 | GLUT4_MOUSE | MPSGFQQIGSDDGEPPRQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNATWLGRQGPGGPDSIPQGTLTTLWALSVAIFSVGGMISSFLIGIISQWLGRKRAMLANNVLAVLGGALMGLANAAASYEILILGRFLIGAYSGLTSGLVPMYVGEIAPTHLRGALGTLNQLAIVIGILVAQVLGLESMLGTATLWPLLLALTVLPALLQLILLPFCPESPRYLYIIRNLEGPARKSLKRLTGWADVSDALAELKDEKRKLERERPMSLLQLLGSRTHRQPLIIAVVLQLSQQLSGINAVFYYSTSIFESAGVG... | null | null | amylopectin biosynthetic process [GO:0010021]; brown fat cell differentiation [GO:0050873]; cellular response to hypoxia [GO:0071456]; cellular response to insulin stimulus [GO:0032869]; cellular response to osmotic stress [GO:0071470]; cellular response to tumor necrosis factor [GO:0071356]; dehydroascorbic acid trans... | cell surface [GO:0009986]; clathrin-coated pit [GO:0005905]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; insulin-responsive compartment... | D-glucose transmembrane transporter activity [GO:0055056]; glucose transmembrane transporter activity [GO:0005355]; glucose uniporter activity [GO:0015304]; insulin-responsive glucose:proton symporter activity [GO:0005360] | PF00083; | 1.20.1250.20; | Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family, Glucose transporter subfamily | PTM: Sumoylated. {ECO:0000250|UniProtKB:P14672}.; PTM: Palmitoylated. Palmitoylation by ZDHHC7 controls the insulin-dependent translocation of GLUT4 to the plasma membrane. {ECO:0000250|UniProtKB:P14672}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21907143, ECO:0000269|PubMed:25586176, ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404, ECO:0000269|PubMed:27739494}; Multi-pass membrane protein {ECO:0000269|PubMed:21907143}. Endomembrane system {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}... | CATALYTIC ACTIVITY: Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376, ChEBI:CHEBI:4167; Evidence={ECO:0000250|UniProtKB:P19357}; | null | null | null | null | FUNCTION: Insulin-regulated facilitative glucose transporter, which plays a key role in removal of glucose from circulation (PubMed:26240143, PubMed:26629404). Response to insulin is regulated by its intracellular localization: in the absence of insulin, it is efficiently retained intracellularly within storage compart... | Mus musculus (Mouse) |
P14148 | RL7_MOUSE | MEAVPEKKKKVATVPGTLKKKVPAGPKTLKKKVPAVPETLKKKRRNFAELKVKRLRKKFALKTLRKARRKLIYEKAKHYHKEYRQMYRTEIRMARMARKAGNFYVPAEPKLAFVIRIRGINGVSPKVRKVLQLLRLRQIFNGTFVKLNKASINMLRIVEPYIAWGYPNLKSVNELIYKRGYGKINKKRIALTDNSLIARSLGKFGIICMEDLIHEIYTVGKRFKEANNFLWPFKLSSPRGGMKKKTTHFVEGGDAGNREDQINRLIRRMN | null | null | cytoplasmic translation [GO:0002181]; maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000463]; translation [GO:0006412]; translation at postsynapse [GO:0140242]; translation at presynapse [GO:0140236] | A band [GO:0031672]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; postsynapse [GO:0098794]; presynapse [GO:0098793]; ribonucleoprotein complex [GO:1990904]; ribosome [GO:0005840]; synapse [GO:0045202] | 5S rRNA binding [GO:0008097]; DNA binding [GO:0003677]; identical protein binding [GO:0042802]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF00327;PF08079; | 1.10.15.30;3.30.1390.20; | Universal ribosomal protein uL30 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:36517592}. | null | null | null | null | null | FUNCTION: Component of the large ribosomal subunit (PubMed:36517592). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:36517592). Binds to G-rich structures in 28S rRNA and in mRNAs (By similarity). Plays a regulatory role in the translation apparatus; inhi... | Mus musculus (Mouse) |
P14151 | LYAM1_HUMAN | MIFPWKCQSTQRDLWNIFKLWGWTMLCCDFLAHHGTDCWTYHYSEKPMNWQRARRFCRDNYTDLVAIQNKAEIEYLEKTLPFSRSYYWIGIRKIGGIWTWVGTNKSLTEEAENWGDGEPNNKKNKEDCVEIYIKRNKDAGKWNDDACHKLKAALCYTASCQPWSCSGHGECVEIINNYTCNCDVGYYGPQCQFVIQCEPLEAPELGTMDCTHPLGNFSFSSQCAFSCSEGTNLTGIEETTCGPFGNWSSPEPTCQVIQCEPLSAPDLGIMNCSHPLASFSFTSACTFICSEGTELIGKKKTICESSGIWSNPSPICQKLD... | null | null | calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell adhesion [GO:0007155]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; leukocyte cell-cell adhesion [GO:0007159]; leukocyte tethering or rolling [GO:0050901]; response to cytokin... | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; secretory granule membrane [GO:0030667] | calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; glycosphingolipid binding [GO:0043208]; heparin binding [GO:0008201]; oligosaccharide binding [GO:0070492]; protease binding [GO:0002020]; sialic acid binding [GO:0033691] | PF00008;PF00059;PF00084; | 2.10.70.10;2.10.25.10;3.10.100.10; | Selectin/LECAM family | PTM: N-glycosylated. {ECO:0000269|PubMed:2663882, ECO:0000269|PubMed:28011641, ECO:0000269|PubMed:28489325}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2509939, ECO:0000269|PubMed:2663882, ECO:0000269|PubMed:28011641}; Single-pass type I membrane protein {ECO:0000305|PubMed:2663882}. | null | null | null | null | null | FUNCTION: Calcium-dependent lectin that mediates cell adhesion by binding to glycoproteins on neighboring cells (PubMed:12403782, PubMed:28011641, PubMed:28489325). Mediates the adherence of lymphocytes to endothelial cells of high endothelial venules in peripheral lymph nodes. Promotes initial tethering and rolling of... | Homo sapiens (Human) |
P14152 | MDHC_MOUSE | MSEPIRVLVTGAAGQIAYSLLYSIGNGSVFGKDQPIILVLLDITPMMGVLDGVLMELQDCALPLLQDVIATDKEEIAFKDLDVAVLVGSMPRREGMERKDLLKANVKIFKSQGTALEKYAKKSVKVIVVGNPANTNCLTASKSAPSIPKENFSCLTRLDHNRAKSQIALKLGVTADDVKNVIIWGNHSSTQYPDVNHAKVKLQGKEVGVYEALKDDSWLKGEFITTVQQRGAAVIKARKLSSAMSAAKAIADHIRDIWFGTPEGEFVSMGVISDGNSYGVPDDLLYSFPVVIKNKTWKFVEGLPINDFSREKMDLTAKEL... | 1.1.1.37; 1.1.1.96 | null | gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; malate metabolic process [GO:0006108]; NAD metabolic process [GO:0019674]; NADH metabolic process [GO:0006734]; oxaloacetate metabolic process [GO:0006107]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209] | hydroxyphenylpyruvate reductase activity [GO:0047995]; L-malate dehydrogenase activity [GO:0030060]; malate dehydrogenase activity [GO:0016615]; NAD binding [GO:0051287] | PF02866;PF00056; | 3.90.110.10;3.40.50.720; | LDH/MDH superfamily, MDH type 2 family | PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: Acetylation at Lys-118 dramatically enhances enzymatic activity and promotes adipogenic differentiation. {ECO:0000250|UniProtKB:P40925}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P40925}. | CATALYTIC ACTIVITY: Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate; Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37; Evidence={ECO:0000250|UniProtKB:P40925}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21433; Evidence={... | null | null | null | null | FUNCTION: Catalyzes the reduction of aromatic alpha-keto acids in the presence of NADH. Plays essential roles in the malate-aspartate shuttle and the tricarboxylic acid cycle, important in mitochondrial NADH supply for oxidative phosphorylation. Catalyzes the reduction of 2-oxoglutarate to 2-hydroxyglutarate, leading t... | Mus musculus (Mouse) |
P14164 | ABF1_YEAST | MDKLVVNYYEYKHPIINKDLAIGAHGGKKFPTLGAWYDVINEYEFQTRCPIILKNSHRNKHFTFACHLKNCPFKVLLSYAGNAASSETSSPSANNNTNPPGTPDHIHHHSNNMNNEDNDNNNGSNNKVSNDSKLDFVTDDLEYHLANTHPDDTNDKVESRSNEVNGNNDDDADANNIFKQQGVTIKNDTEDDSINKASIDRGLDDESGPTHGNDSGNHRHNEEDDVHTQMTKNYSDVVNDEDINVAIANAVANVDSQSNNKHDGKDDDATNNNDGQDNNTNNDHNNNSNINNNNVGSHGISSHSPSSIRDTSMNLDVFNS... | null | null | chromatin remodeling [GO:0006338]; DNA-templated DNA replication [GO:0006261]; global genome nucleotide-excision repair [GO:0070911]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; silent mating-type cassette heterochromati... | nucleotide-excision repair factor 4 complex [GO:0000113]; nucleus [GO:0005634] | DNA replication origin binding [GO:0003688]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding, bending [GO:0044374] | PF04684; | null | BAF1 family | PTM: Extensively phosphorylated on Ser and Thr residues. {ECO:0000269|PubMed:2034654, ECO:0000269|PubMed:7608180}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15522095}. | null | null | null | null | null | FUNCTION: General regulatory factor (GRF) that contributes to transcriptional activation of a large number of genes, as well as to DNA replication, silencing and telomere structure. Involved in the transcription activation of a subset of ribosomal protein genes. Binds the ARS-elements found in many promoters. Binds to ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14173 | DDC_RAT | MDSREFRRRGKEMVDYIADYLDGIEGRPVYPDVEPGYLRALIPTTAPQEPETYEDIIRDIEKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMDWLGKMLELPEAFLAGRAGEGGGVIQGSASEATLVALLAARTKMIRQLQAASPELTQAALMEKLVAYTSDQAHSSVERAGLIGGVKIKAIPSDGNYSMRAAALREALERDKAAGLIPFFVVVTLGTTSCCSFDNLLEVGPICNQEGVWLHIDAAYAGSAFICPEFRYLLNGVEFADSFNFNPHKWLLVNFDCSAMWVKKRT... | 4.1.1.28 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:8889823}; | aminergic neurotransmitter loading into synaptic vesicle [GO:0015842]; amino acid metabolic process [GO:0006520]; carboxylic acid metabolic process [GO:0019752]; catecholamine biosynthetic process [GO:0042423]; catecholamine metabolic process [GO:0006584]; cellular response to alkaloid [GO:0071312]; cellular response t... | axon [GO:0030424]; cytoplasm [GO:0005737]; neuronal cell body [GO:0043025]; synaptic vesicle [GO:0008021] | 5-hydroxy-L-tryptophan decarboxylase activity [GO:0036467]; amino acid binding [GO:0016597]; aromatic-L-amino-acid decarboxylase activity [GO:0004058]; enzyme binding [GO:0019899]; L-dopa decarboxylase activity [GO:0036468]; protein domain specific binding [GO:0019904]; pyridoxal phosphate binding [GO:0030170] | PF00282; | 3.90.1150.10;1.20.1340.10;3.40.640.10; | Group II decarboxylase family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + L-dopa = CO2 + dopamine; Xref=Rhea:RHEA:12272, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57504, ChEBI:CHEBI:59905; EC=4.1.1.28; Evidence={ECO:0000269|PubMed:11358515, ECO:0000269|PubMed:8889823}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12273; Evidence={ECO:000026... | null | PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 2/2. {ECO:0000269|PubMed:11358515, ECO:0000269|PubMed:8889823}. | null | null | FUNCTION: Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine and L-5-hydroxytryptophan to serotonin. {ECO:0000269|PubMed:11358515, ECO:0000269|PubMed:8889823}. | Rattus norvegicus (Rat) |
P14174 | MIF_HUMAN | MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTFA | 5.3.2.1; 5.3.3.12 | null | carboxylic acid metabolic process [GO:0019752]; cell surface receptor signaling pathway [GO:0007166]; cellular senescence [GO:0090398]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; negative regulation of apoptotic p... | cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lumen [GO:1904813]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; secretory granule lumen [GO:0034774]; vesic... | chemoattractant activity [GO:0042056]; cytokine activity [GO:0005125]; cytokine receptor binding [GO:0005126]; dopachrome isomerase activity [GO:0004167]; identical protein binding [GO:0042802]; phenylpyruvate tautomerase activity [GO:0050178]; protease binding [GO:0002020] | PF01187; | 3.30.429.10; | MIF family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15908412, ECO:0000269|PubMed:19454686, ECO:0000269|PubMed:2552447, ECO:0000269|PubMed:8234256}. Cytoplasm {ECO:0000269|PubMed:11089976, ECO:0000269|PubMed:19454686}. Note=Does not have a cleavable signal sequence and is secreted via a specialized, non-classical pathway... | CATALYTIC ACTIVITY: Reaction=3-phenylpyruvate = enol-phenylpyruvate; Xref=Rhea:RHEA:17097, ChEBI:CHEBI:16815, ChEBI:CHEBI:18005; EC=5.3.2.1; Evidence={ECO:0000269|PubMed:11439086}; CATALYTIC ACTIVITY: Reaction=L-dopachrome = 5,6-dihydroxyindole-2-carboxylate; Xref=Rhea:RHEA:13041, ChEBI:CHEBI:16875, ChEBI:CHEBI:57509; ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=249 uM for phenylpyruvate {ECO:0000269|PubMed:11439086}; KM=168 uM for p-hydroxyphenylpyruvate {ECO:0000269|PubMed:11439086}; Vmax=2113 umol/min/mg enzyme toward phenylpyruvate {ECO:0000269|PubMed:11439086}; Vmax=524 umol/min/mg enzyme toward p-hydroxyphenylpyruvat... | null | null | null | FUNCTION: Pro-inflammatory cytokine involved in the innate immune response to bacterial pathogens (PubMed:15908412, PubMed:17443469, PubMed:23776208). The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense (PubMed:15908412, PubMed:17443469, P... | Homo sapiens (Human) |
P14175 | PROV_ECOLI | MAIKLEIKNLYKIFGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARRTPNGLIRKTPGFGPRSALKLLQDEDREYGYVIERGNKF... | null | null | amino acid import across plasma membrane [GO:0089718]; cellular response to osmotic stress [GO:0071470]; glycine betaine transport [GO:0031460]; glycine import across plasma membrane [GO:1903804]; hyperosmotic response [GO:0006972] | ATP-binding cassette (ABC) transporter complex [GO:0043190]; membrane [GO:0016020]; ProVWX complex [GO:1990222] | amine transmembrane transporter activity [GO:0005275]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; osmosensor activity [GO:0005034] | PF00005;PF00571; | 3.10.580.10;3.40.50.300; | ABC transporter superfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:16079137}; Peripheral membrane protein {ECO:0000269|PubMed:16079137}. | null | null | null | null | null | FUNCTION: Part of the ProU ABC transporter complex involved in glycine betaine and proline betaine uptake (PubMed:23249124, PubMed:3305496, PubMed:7898450). Probably responsible for energy coupling to the transport system (Probable). {ECO:0000269|PubMed:23249124, ECO:0000269|PubMed:3305496, ECO:0000269|PubMed:7898450, ... | Escherichia coli (strain K12) |
P14176 | PROW_ECOLI | MADQNNPWDTTPAADSAAQSADAWGTPTTAPTDGGGADWLTSTPAPNVEHFNILDPFHKTLIPLDSWVTEGIDWVVTHFRPVFQGVRVPVDYILNGFQQLLLGMPAPVAIIVFALIAWQISGVGMGVATLVSLIAIGAIGAWSQAMVTLALVLTALLFCIVIGLPLGIWLARSPRAAKIIRPLLDAMQTTPAFVYLVPIVMLFGIGNVPGVVVTIIFALPPIIRLTILGINQVPADLIEASRSFGASPRQMLFKVQLPLAMPTIMAGVNQTLMLALSMVVIASMIAVGGLGQMVLRGIGRLDMGLATVGGVGIVILAIIL... | null | null | amino acid import across plasma membrane [GO:0089718]; carnitine transmembrane transport [GO:1902603]; cellular response to osmotic stress [GO:0071470]; choline transport [GO:0015871]; glycine betaine transport [GO:0031460]; glycine import across plasma membrane [GO:1903804]; hyperosmotic response [GO:0006972] | ATP-binding cassette (ABC) transporter complex [GO:0043190]; membrane [GO:0016020]; plasma membrane [GO:0005886]; ProVWX complex [GO:1990222] | amine transmembrane transporter activity [GO:0005275]; carnitine transmembrane transporter activity [GO:0015226] | PF00528; | 1.10.3720.10; | Binding-protein-dependent transport system permease family, CysTW subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Part of the ProU ABC transporter complex involved in glycine betaine and proline betaine uptake (PubMed:23249124, PubMed:3305496, PubMed:7898450). Probably responsible for the translocation of the substrate across the membrane (Probable). {ECO:0000269|PubMed:23249124, ECO:0000269|PubMed:3305496, ECO:0000269|P... | Escherichia coli (strain K12) |
P14180 | CHS2_YEAST | MTRNPFMVEPSNGSPNRRGASNLSKFYANANSNSRWANPSEESLEDSYDQSNVFQGLPASPSRAALRYSPDRRHRTQFYRDSAHNSPVAPNRYAANLQESPKRAGEAVIHLSEGSNLYPRDNADLPVDPYHLSPQQQPSNNLFGSGRLYSQSSKYTMSTTSTTAPSLAEADDEKEKYLTSTTSYDDQSTIFSADTFNETKFELNHPTRQQYVRRANSESKRRMVSDLPPPSKKKALLKLDNPIPKGLLDTLPRRNSPEFTEMRYTACTVEPDDFLREGYTLRFAEMNRECQIAICITMYNEDKYSLARTIHSIMKNVAHL... | 2.4.1.16 | null | cell wall chitin biosynthetic process [GO:0006038]; cell wall organization [GO:0071555]; chitin biosynthetic process [GO:0006031]; mitotic actomyosin contractile ring contraction [GO:1902404] | cell periphery [GO:0071944]; cell septum [GO:0030428]; cellular bud neck [GO:0005935]; membrane [GO:0016020] | chitin synthase activity [GO:0004100] | PF01644;PF08407;PF13632; | null | Chitin synthase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595, ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223; EC=2.4.1.16; | null | null | null | null | FUNCTION: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer (Probable). Required for septum formation (Probable). {ECO:0000305, ECO:0000305|PubMed:2533436}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14193 | KPRS_BACSU | MSNQYGDKNLKIFSLNSNPELAKEIADIVGVQLGKCSVTRFSDGEVQINIEESIRGCDCYIIQSTSDPVNEHIMELLIMVDALKRASAKTINIVIPYYGYARQDRKARSREPITAKLFANLLETAGATRVIALDLHAPQIQGFFDIPIDHLMGVPILGEYFEGKNLEDIVIVSPDHGGVTRARKLADRLKAPIAIIDKRRPRPNVAEVMNIVGNIEGKTAILIDDIIDTAGTITLAANALVENGAKEVYACCTHPVLSGPAVERINNSTIKELVVTNSIKLPEEKKIERFKQLSVGPLLAEAIIRVHEQQSVSYLFS | 2.7.6.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:2169413, ECO:0000303|PubMed:28031352}; Note=Binds 2 Mg(2+) ions per subunit. Each Mg(2+) binds only one residue (His-136 and Asp-175, respectively) of this protein, however the magnesium ions also bind substrate... | 5-phosphoribose 1-diphosphate biosynthetic process [GO:0006015]; phosphorylation [GO:0016310]; purine nucleotide biosynthetic process [GO:0006164]; ribonucleoside monophosphate biosynthetic process [GO:0009156] | cytoplasm [GO:0005737]; ribose phosphate diphosphokinase complex [GO:0002189] | ATP binding [GO:0005524]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287]; ribose phosphate diphosphokinase activity [GO:0004749] | PF14572;PF13793; | 3.40.50.2020; | Ribose-phosphate pyrophosphokinase family, Class I subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}. | CATALYTIC ACTIVITY: Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:16008562, ECO:000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=191 uM for ATP (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:16008562}; KM=230 uM for Rib-5-P (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:16008562}; KM=480 uM for Rib-5-P (at pH 8.2 and 37 degrees Celsius) {ECO:0000269|PubMed:2169413}; KM=660 uM for... | PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000305|PubMed:16008562, ECO:0000305|PubMed:2169413}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-8.5. Activities at pH 7 and pH 9.5 are 35% and 85% of the maximal activity, respectively. {ECO:0000269|PubMed:2169413}; | null | FUNCTION: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P). {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:11790837, ECO:0000269|PubMed:16008562, ECO:0000269|PubMed:... | Bacillus subtilis (strain 168) |
P14199 | REF2P_DROME | MPEKLLKITYQGAGPQKKINAYLRMPSQNYTILRREIELYLFQERQLPKCDVRTFWIDADKDEIEIVNQNDYEIFLAKCESNMHVQVAPLAPVEEPKATKQEGSSANAEAPSVDDPSNFTIHDAVECDGCGLAPLIGFRYKCVQCSNYDLCQKCELAHKHPEHLMLRMPTNNGPGMVDAWFTGPGLGRRSGRRSRGHCPFQETNQADPAGEPARDSRRERRQARRHAGVLTQFVEMMTNLPLNTTTATAPAEPQKPKAAEQTESPPQAEPTVTAEKAAESEAKPTEPKKVNTDQSVPRTEDPVTTPRSTQPTTPVINLDN... | null | null | aggrephagy [GO:0035973]; endosome organization [GO:0007032]; mitochondrion organization [GO:0007005]; mitophagy [GO:0000423]; sperm mitochondrion organization [GO:0030382] | aggresome [GO:0016235]; amphisome [GO:0044753]; autophagosome [GO:0005776]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA binding [GO:0003677]; K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; protein kinase C binding [GO:0005080]; zinc ion binding [GO:0008270] | PF00564;PF16577;PF00569; | 3.30.60.90;1.10.8.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:22622177}. | null | null | null | null | null | FUNCTION: Required for selective autophagy activation by ubiquitinated proteins (PubMed:22622177). Implicated in sigma rhabdovirus multiplication and necessary for male fertility. Involved in activating transcription of Drs (PubMed:12446795, PubMed:2510997). {ECO:0000269|PubMed:12446795, ECO:0000269|PubMed:22622177, EC... | Drosophila melanogaster (Fruit fly) |
P14200 | MCH_RAT | MAKMSLSSYMLMLAFSLFSHGILLSASKSIRNVEDDIVFNTFRMGKAFQKEDTAERSVVAPSLEGYKNDESGFMKDDDDKTTKNTGSKQNLVTHGLPLSLAVKPYLALKGPAVFPAENGVQNTESTQEKREIGDEENSAKFPIGRRDFDMLRCMLGRVYRPCWQV | null | null | chemical synaptic transmission [GO:0007268]; drinking behavior [GO:0042756]; feeding behavior [GO:0007631]; lactation [GO:0007595]; learning or memory [GO:0007611]; negative regulation of blood pressure [GO:0045776]; negative regulation of synaptic transmission, dopaminergic [GO:0032227]; neuropeptide signaling pathway... | extracellular space [GO:0005615]; nucleus [GO:0005634]; synapse [GO:0045202] | melanin-concentrating hormone activity [GO:0030354]; type 1 melanin-concentrating hormone receptor binding [GO:0031777] | PF05824; | null | Melanin-concentrating hormone family | PTM: Pro-MCH is processed differentially in the brain and in peripheral organs producing two neuropeptides; NEI and MCH. A third peptide, NGE, may also be produced. Preferential processing in neurons by prohormone convertase 2 (PC2) generates NEI. MCH is generated in neurons of the lateral hypothalmic area by several p... | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: MCH inhibits ACTH secretion at the end of the light on period which corresponds to the peak of the circadian rhythm in ACTH. Inhibits also stress induced ACTH release during the light off period of the cycle. Involved as a neurotransmitter or neuromodulator in a broad array of neuronal functions. Stimulates s... | Rattus norvegicus (Rat) |
P14206 | RSSA_MOUSE | MSGALDVLQMKEEDVLKFLAAGTHLGGTNLDFQMEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVISSRNTGQRAVLKFAAATGATPIAGRFTPGTFTNQIQAAFREPRLLVVTDPRADHQPLTEASYVNLPTIALCNTDSPLRYVDIAIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPWEVMPDLYFYRDPEEIEKEEQAAAEKAVTKEEFQGEWTAPAPEFTAAQPEVADWSEGVQVPSVPIQQFPTEDWSAQPATEDWSAAPTAQATEWVGATTEWS | null | null | cell-cell adhesion [GO:0098609]; cytoplasmic translation [GO:0002181]; ribosomal small subunit assembly [GO:0000028] | 90S preribosome [GO:0030686]; basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; nucleus [GO:00056... | laminin binding [GO:0043236]; laminin receptor activity [GO:0005055]; structural constituent of ribosome [GO:0003735] | PF16122;PF00318; | null | Universal ribosomal protein uS2 family | PTM: Acylated. Acylation may be a prerequisite for conversion of the monomeric 37 kDa laminin receptor precursor (37LRP) to the mature dimeric 67 kDa laminin receptor (67LR), and may provide a mechanism for membrane association. {ECO:0000255|HAMAP-Rule:MF_03016}.; PTM: Cleaved by stromelysin-3 (ST3) at the cell surface... | SUBCELLULAR LOCATION: Cell membrane. Cytoplasm {ECO:0000269|PubMed:36517592}. Nucleus. Note=67LR is found at the surface of the plasma membrane, with its C-terminal laminin-binding domain accessible to extracellular ligands. 37LRP is found at the cell surface, in the cytoplasm and in the nucleus. Colocalizes with PPP1R... | null | null | null | null | null | FUNCTION: Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement mem... | Mus musculus (Mouse) |
P14207 | FOLR2_HUMAN | MVWKWMPLLLLLVCVATMCSAQDRTDLLNVCMDAKHHKTKPGPEDKLHDQCSPWKKNACCTASTSQELHKDTSRLYNFNWDHCGKMEPACKRHFIQDTCLYECSPNLGPWIQQVNQSWRKERFLDVPLCKEDCQRWWEDCHTSHTCKSNWHRGWDWTSGVNKCPAGALCRTFESYFPTPAALCEGLWSHSYKVSNYSRGSGRCIQMWFDSAQGNPNEEVARFYAAAMHVNAGEMLHGTGGLLLSLALMLQLWLLG | null | null | cell adhesion [GO:0007155]; folic acid transport [GO:0015884]; fusion of sperm to egg plasma membrane involved in single fertilization [GO:0007342]; inflammatory response [GO:0006954]; positive regulation of cell population proliferation [GO:0008284]; sperm-egg recognition [GO:0035036] | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; plasma membrane [GO:0005886] | folic acid binding [GO:0005542]; folic acid receptor activity [GO:0061714]; signaling receptor activity [GO:0038023] | PF03024; | null | Folate receptor family | PTM: N-glycosylated. {ECO:0000269|PubMed:23934049, ECO:0000269|PubMed:2605182}. | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate and folate analogs into the interior of cells. Has high affinity for folate and folic acid analogs at neutral pH. Exposure to slightly acidic pH after receptor endocytosis triggers a conformation change that s... | Homo sapiens (Human) |
P14209 | CD99_HUMAN | MARGAALALLLFGLLGVLVAAPDGGFDLSDALPDNENKKPTAIPKKPSAGDDFDLGDAVVDGENDDPRPPNPPKPMPNPNPNHPSSSGSFSDADLADGVSGGEGKGGSDGGGSHRKEGEEADAPGVIPGIVGAVVVAVAGAISSFIAYQKKKLCFKENAEQGEVDMESHRNANAEPAVQRTLLEK | null | null | homotypic cell-cell adhesion [GO:0034109]; positive regulation of neutrophil extravasation [GO:2000391]; T cell extravasation [GO:0072683] | cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886] | null | PF12301; | null | CD99 family | PTM: Extensively O-glycosylated. | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Involved in T-cell adhesion processes and in spontaneous rosette formation with erythrocytes. Plays a role in a late step of leukocyte extravasation helping leukocytes to overcome the endothelial basement membrane. Acts at the same site as, but independently of, PECAM1. Involved in T-cell adhesion processes (... | Homo sapiens (Human) |
P14210 | HGF_HUMAN | MWVTKLLPALLLQHVLLHLLLLPIAIPYAEGQRKRRNTIHEFKKSAKTTLIKIDPALKIKTKKVNTADQCANRCTRNKGLPFTCKAFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLYENKDYIRNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQCSEVECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQPRPWCYTLDPHTRWEYCAIKTCADNTMNDTDVPLETTECIQGQGEGYRGTVNTI... | null | null | cell chemotaxis [GO:0060326]; cell morphogenesis [GO:0000902]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; epithelial cell proliferation [GO:0050673]; epithelial to mesenchymal transition [GO:0001837]; hepatocyte growth factor receptor signaling pathway [GO:0048012]; liver development [GO:00018... | extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; platelet alpha granule lumen [GO:0031093] | chemoattractant activity [GO:0042056]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; signaling receptor binding [GO:0005102] | PF00051;PF00024;PF00089; | 3.50.4.10;2.40.20.10;2.40.10.10; | Peptidase S1 family, Plasminogen subfamily | PTM: The single-chain precursor undergoes proteolytic processing by TMPRSS13 resulting in an active two-chain form. {ECO:0000269|PubMed:20977675}. | null | null | null | null | null | null | FUNCTION: Potent mitogen for mature parenchymal hepatocyte cells, seems to be a hepatotrophic factor, and acts as a growth factor for a broad spectrum of tissues and cell types (PubMed:20624990). Activating ligand for the receptor tyrosine kinase MET by binding to it and promoting its dimerization (PubMed:15167892, Pub... | Homo sapiens (Human) |
P14211 | CALR_MOUSE | MLLSVPLLLGLLGLAAADPAIYFKEQFLDGDAWTNRWVESKHKSDFGKFVLSSGKFYGDLEKDKGLQTSQDARFYALSAKFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPSGLDQKDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDAAKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDANIYAYDSFAVLGLDLWQ... | null | null | cardiac muscle cell differentiation [GO:0055007]; cellular response to electrical stimulus [GO:0071257]; cellular response to lithium ion [GO:0071285]; cellular response to organic substance [GO:0071310]; cellular response to virus [GO:0098586]; cellular senescence [GO:0090398]; cortical actin cytoskeleton organization... | acrosomal vesicle [GO:0001669]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cortical granule [GO:0060473]; cytolytic granule [GO:0044194]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]... | calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; complement component C1q complex binding [GO:0001849]; hormone binding [GO:0042562]; integrin binding [GO:0005178]; iron ion binding [GO:0005506]; molecular sequestering activity [GO:0140313]; mRNA binding [GO:0003729]; nuclear androgen receptor bindi... | PF00262; | 2.60.120.200;2.10.250.10; | Calreticulin family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:8418194}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P27797}. Cytolytic granule {ECO:0000269|PubMed:8418194}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P27797}. Cell surface {ECO:0000250|UniProtKB:P27797}. Sarcoplasmic... | null | null | null | null | null | FUNCTION: Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (PubMed:20880849, PubMed:216527... | Mus musculus (Mouse) |
P14218 | DLDH_PSEFL | MSQKFDVVVIGAGPGGYVAAIRAAQLGLKTACIEKYIGKEGKVALGGTCLNVGCIPSKALLDSSYKYHEAKEAFKVHGIEAKGVTIDVPAMVARKANIVKNLTGGIATLFKANGVTSFEGHGKLLANKQVEVTGLDGKTQVLEAENVIIASGSRPVEIPPAPLSDDIIVDSTGALEFQAVPKKLGVIGAGVIGLELGSVWARLGAEVTVLEALDKFLPAADEQIAKEALKVLTKQGLNIRLGARVTASEVKKKQVTVTFTDANGEQKETFDKLIVAVGRRPVTTDLLAADSGVTLDERGFIYVDDHCKTSVPGVFAIGDV... | 1.8.1.4 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 1 FAD per subunit.; | null | cytoplasm [GO:0005737] | dihydrolipoyl dehydrogenase activity [GO:0004148]; flavin adenine dinucleotide binding [GO:0050660] | PF07992;PF02852; | 3.30.390.30;3.50.50.60; | Class-I pyridine nucleotide-disulfide oxidoreductase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4; | null | null | null | null | FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). | Pseudomonas fluorescens |
P14222 | PERF_HUMAN | MAARLLLLGILLLLLPLPVPAPCHTAARSECKRSHKFVPGAWLAGEGVDVTSLRRSGSFPVDTQRFLRPDGTCTLCENALQEGTLQRLPLALTNWRAQGSGCQRHVTRAKVSSTEAVARDAARSIRNDWKVGLDVTPKPTSNVHVSVAGSHSQAANFAAQKTHQDQYSFSTDTVECRFYSFHVVHTPPLHPDFKRALGDLPHHFNASTQPAYLRLISNYGTHFIRAVELGGRISALTALRTCELALEGLTDNEVEDCLTVEAQVNIGIHGSISAEAKACEEKKKKHKMTASFHQTYRERHSEVVGGHHTSINDLLFGIQA... | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; | apoptotic process [GO:0006915]; cellular defense response [GO:0006968]; defense response to tumor cell [GO:0002357]; defense response to virus [GO:0051607]; granzyme-mediated programmed cell death signaling pathway [GO:0140507]; immune response to tumor cell [GO:0002418]; immunological synapse formation [GO:0001771]; k... | cytolytic granule [GO:0044194]; cytolytic granule lumen [GO:1904856]; cytosol [GO:0005829]; endosome lumen [GO:0031904]; extracellular region [GO:0005576]; immunological synapse [GO:0001772]; membrane [GO:0016020]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; pore-forming activity [GO:0140911]; wide pore channel activity [GO:0022829] | PF00168;PF01823; | 2.60.40.150; | Complement C6/C7/C8/C9 family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:P10820}. | SUBCELLULAR LOCATION: Cytolytic granule {ECO:0000269|PubMed:20038786, ECO:0000269|PubMed:24088571}. Secreted. Cell membrane {ECO:0000269|PubMed:20889983, ECO:0000269|PubMed:21037563}; Multi-pass membrane protein {ECO:0000269|PubMed:20889983, ECO:0000269|PubMed:21037563}. Endosome lumen {ECO:0000269|PubMed:20038786}. No... | null | null | null | null | null | FUNCTION: Pore-forming protein that plays a key role in granzyme-mediated programmed cell death, and in defense against virus-infected or neoplastic cells (PubMed:20889983, PubMed:21037563, PubMed:24558045, PubMed:9058810, PubMed:9164947). Plays an important role in killing other cells that are recognized as non-self b... | Homo sapiens (Human) |
P14223 | ALF_PLAFA | MAHCTEYMNAPKKLPADVAEELATTAQKLVQAGKGILAADESTQTIKKRFDNIKLENTIENRASYRDLLFGTKGLGKFISGAILFEETLFQKNEAGVPMVNLLHNENIIPGIKVDKGLVNIPCTDEEKSTQGLDGLAERCKEYYKAGARFAKWRTVLVIDTAKGKPTDLSIHETAWGLARYASICQQNRLVPIVEPEILADGPHSIEVCAVVTQKVLSCVFKALQENGVLLEGALLKPNMVTAGYECTAKTTTQDVGFLTVRTLRRTVPPALPGVVFLSGGQSEEEASVNLNSINALGPHPWALTFSYGRALQASVLNTW... | 4.1.2.13 | null | fructose 1,6-bisphosphate metabolic process [GO:0030388]; glycolytic process [GO:0006096] | cytosol [GO:0005829]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | actin binding [GO:0003779]; fructose-bisphosphate aldolase activity [GO:0004332] | PF00274; | 3.20.20.70; | Class I fructose-bisphosphate aldolase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2190085}. Membrane {ECO:0000269|PubMed:2190085}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Host cell membrane {ECO:0000250|UniProtKB:Q27744}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence={ECO:0000305|PubMed:2190085}; | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. {ECO:0000305|PubMed:2190085}. | null | null | FUNCTION: Plays a key role in glycolysis by catalyzing the cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate (PubMed:2190085). Independently of its catalytic activity, connects the actin filaments, and thus the actomyosin motor, to cell surface adhesins of the thrombos... | Plasmodium falciparum |
P14231 | AT1B2_MOUSE | MVIQKEKKSCGQVVEEWKEFVWNPRTHQFMGRTGTSWAFILLFYLVFYGFLTAMFSLTMWVMLQTVSDHTPKYQDRLATPGLMIRPKTENLDVIVNISDTESWGQHVQKLNKFLEPYNDSIQAQKNDVCRPGRYYEQPDNGVLNYPKRACQFNRTQLGDCSGIGDPTHYGYSTGQPCVFIKMNRVINFYAGANQSMNVTCVGKRDEDAENLGHFVMFPANGSIDLMYFPYYGKKFHVNYTQPLVAVKFLNVTPNVEVNVECRINAANIATDDERDKFAGRVAFKLRINKT | null | null | cell-substrate adhesion [GO:0031589]; intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; lateral ventricle development [GO:0021670]; membrane repolarization [GO:0086009]; motor behavior [GO:0061744]; negative regulation of glial cell migration [GO:1903976]; neuronal... | apical plasma membrane [GO:0016324]; astrocyte end-foot [GO:0097450]; astrocyte projection [GO:0097449]; cell body membrane [GO:0044298]; cell periphery [GO:0071944]; cell projection membrane [GO:0031253]; cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; lateral plasma membrane [GO:0016328]; membr... | ATPase activator activity [GO:0001671]; ATPase binding [GO:0051117]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]; protein heterodimerization activity [GO:0046982]; protein-macromolecule adaptor activity [GO:0030674] | PF00287; | 1.20.5.170;2.60.40.1660; | X(+)/potassium ATPases subunit beta family | null | SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. | null | null | null | null | null | FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-2 subunit is not known.; FUNCTION: Mediates cell adhesion of neurons and astrocytes, and promotes neurite ... | Mus musculus (Mouse) |
P14234 | FGR_MOUSE | MGCVFCKKLEPASKEDVGLEGDFRSQTAEERYFPDPTQGRTSSVFPQPTSPAFLNTGNMRSISGTGVTIFVALYDYEARTGDDLTFTKGEKFHILNNTEYDWWEARSLSSGHRGYVPSNYVAPVDSIQAEEWYFGKISRKDAERQLLSSGNPQGAFLIRESETTKGAYSLSIRDWDQNRGDHIKHYKIRKLDTGGYYITTRAQFDSIQDLVRHYMEVNDGLCYLLTAPCTTTKPQTLGLAKDAWEIDRNSIALERRLGTGCFGDVWLGTWNCSTKVAVKTLKPGTMSPKAFLEEAQIMKLLRHDKLVQLYAVVSEEPIYI... | 2.7.10.2 | null | bone mineralization [GO:0030282]; cell differentiation [GO:0030154]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response [GO:0045087]; integrin-mediated signaling pathway [GO:0007229]; myoblast proliferation [GO:0051450]; negative regulation of natural killer cell activation [GO:0032815]; p... | aggresome [GO:0016235]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587] | ATP binding [GO:0005524]; Fc-gamma receptor I complex binding [GO:0034988]; immunoglobulin receptor binding [GO:0034987]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphotyrosine residue binding [GO:0001784]; protein kinase binding [GO:0019901]; protein tyrosine kinase activity [GO:0004713];... | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: Ubiquitinated. Becomes ubiquitinated in response to ITGB2 signaling; this does not lead to degradation (By similarity). {ECO:0000250}.; PTM: Phosphorylated. Autophosphorylated on tyrosine residues. Becomes phosphorylated in response to FCGR2 engagement, cell adhesion and signaling by ITGB2. Prior phosphorylation a... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15561106}; Lipid-anchor {ECO:0000305|PubMed:15561106}; Cytoplasmic side {ECO:0000305|PubMed:15561106}. Cell membrane {ECO:0000269|PubMed:15561106}; Peripheral membrane protein {ECO:0000269|PubMed:15561106}; Cytoplasmic side {ECO:0000269|PubMed:15561106}. Cell proj... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors devoid of kinase activity and contributes to the regulation of immune responses, including neutrophil, monocyte, macrophage and mast cell functions, cytoskeleton remodeling in response to extracellular stimuli, phagocytosi... | Mus musculus (Mouse) |
P14238 | FES_FELCA | MGFSSELCSPQGHGAVQQMQEAELRLLEGMRKWMAQRVKSDREYAGLLHHMSLQDGGGRGTGPYSPISQSWAEITSQTEGLSRLLRQHAEDLNSGPLSKLGLLIRERQQLRKTYSEQWQQLQQELTKTHNQDIEKLKSQYRALARDSAQARRKYQEASKDKDRDKAKDKYVRSLWKLFAHHNRYVLGVRAAQLHHHHHHQLMLPGLLQSLQDLHQEMACILKEILQEYLEISSLVQDEVVAIHLEMAAAVARIQPEAEYQGFLRQYGSTPDVPPCVTFDESLLEEGEPLEPGELQLNELTVESVQHTLTSVTDELTVATQ... | 2.7.10.2 | null | cell adhesion [GO:0007155]; chemotaxis [GO:0006935]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of microtubule polymerization [GO:0031116]; positive regulation of myeloid cell differentiation [GO:0045639]; positive regulation of neuron projection development [GO:0010976]; regulation of cell adh... | cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; microtubule cytoskeleton [GO:0015630] | ATP binding [GO:0005524]; immunoglobulin receptor binding [GO:0034987]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphatidylinositol binding [GO:0035091]; protein tyrosine kinase activity [GO:0004713] | PF00611;PF07714;PF00017; | 1.20.1270.60;1.10.287.160;3.30.505.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Fes/fps subfamily | PTM: Autophosphorylated on Tyr-711 in response to FGF2. Phosphorylated by LYN in response to FCER1 activation. Phosphorylated by HCK (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Note=Distr... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Tyrosine-protein kinase that acts downstream of cell surface receptors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, cell attachment and cell spreading. Plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Acts down-strea... | Felis catus (Cat) (Felis silvestris catus) |
P14240 | L_LYCVA | MDEIISELRELCLNYIEQDERLSRQKLNFLGQREPRMVLIEGLKLLSRCIEIDSADKSGCTHNHDDKSVETILVESGIVCPGLPLIIPDGYKLIDNSLILLECFVRSSPASFEKKFIEDTNKLACIREDLAVAGVTLVPIVDGRCDYDNSFMPEWANFKFRDLLFKLLEYSNQNEKVFEESEYFRLCESLKTTIDKRSGMDSMKILKDARSTHNDEIMRMCHEGINPNMSCDDVVFGINSLFSRFRRDLESGKLKRNFQKVNPEGLIKEFSELYENLADSDDILTLSREAVESCPLMRFITAETHGHERGSETSTEYERL... | 2.7.7.48; 3.1.-.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_04086}; Note=For endonuclease activity. Binds 2 Mn(2+) ions in the active site. The divalent metal ions are crucial for catalytic activity. {ECO:0000255|HAMAP-Rule:MF_04086}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0... | cap snatching [GO:0075526]; negative stranded viral RNA replication [GO:0039689]; RNA-templated viral transcription [GO:0039696] | host cell cytoplasm [GO:0030430]; virion component [GO:0044423] | hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; RNA-dependent RNA polymerase activity [GO:0003968] | PF06317;PF17296; | 3.30.70.2640;1.20.1440.300; | Bunyavirales RNA polymerase family | null | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04086}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04086}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|HAMAP-Rule:MF_04086}; | null | null | null | null | FUNCTION: RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate. During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving... | Lymphocytic choriomeningitis virus (strain Armstrong) (LCMV) |
P14242 | PMS1_YEAST | MTQIHQINDIDVHRITSGQVITDLTTAVKELVDNSIDANANQIEIIFKDYGLESIECSDNGDGIDPSNYEFLALKHYTSKIAKFQDVAKVQTLGFRGEALSSLCGIAKLSVITTTSPPKADKLEYDMVGHITSKTTTSRNKGTTVLVSQLFHNLPVRQKEFSKTFKRQFTKCLTVIQGYAIINAAIKFSVWNITPKGKKNLILSTMRNSSMRKNISSVFGAGGMRGLEEVDLVLDLNPFKNRMLGKYTDDPDFLDLDYKIRVKGYISQNSFGCGRNSKDRQFIYVNKRPVEYSTLLKCCNEVYKTFNNVQFPAVFLNLEL... | null | null | meiotic mismatch repair [GO:0000710]; mismatch repair [GO:0006298] | cytoplasm [GO:0005737]; MutLalpha complex [GO:0032389]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent DNA damage sensor activity [GO:0140664]; mismatched DNA binding [GO:0030983] | PF01119;PF13589;PF08676; | 3.30.230.10;3.30.565.10;3.30.1540.20;3.30.1370.100; | DNA mismatch repair MutL/HexB family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 mM for ATP {ECO:0000269|PubMed:11717305}; | null | null | null | FUNCTION: Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. Component of the MutLalpha heterodimer that forms a ternary complex with the MutS ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14246 | GTR2_MOUSE | MSEDKITGTLAFTVFTAVLSSFQFGYDIGVINAPQEVIISHYRHVLGVPLDDRKAAINYDVNGTDTPLTVTPAYTTPAPWDEEETEGSAHIVTMLWSLSVSSFAVGGMVASFFGGWLGDKLGRIKAMLAANSLSLTGALLMGCSKFGPAHALIIAGRSVSGLYCGLISGLVPMYIGEIAPTTLRGALGTLHQLALVTGILISQIAGLSFILGNQDHWHILLGLSAVPALLQCLLLLFCPESPRYLYIKLEEEVRAKKSLKRLRGTEDVTKDINEMKKEKEEASTEQKVSVIQLFTDANYRQPILVALMLHMAQQFSGING... | null | null | carbohydrate transport [GO:0008643]; carbohydrate utilization [GO:0009758]; cellular response to fatty acid [GO:0071398]; cellular response to organic cyclic compound [GO:0071407]; dehydroascorbic acid transport [GO:0070837]; fructose transmembrane transport [GO:0015755]; galactose transmembrane transport [GO:0015757];... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; brush border [GO:0005903]; brush border membrane [GO:0031526]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; endosome [GO:0005768]; membrane [GO:0016020]; plasma membrane [GO:0005886] | D-glucose transmembrane transporter activity [GO:0055056]; dehydroascorbic acid transmembrane transporter activity [GO:0033300]; fructose transmembrane transporter activity [GO:0005353]; galactose transmembrane transporter activity [GO:0005354]; glucose transmembrane transporter activity [GO:0005355]; insulin receptor ... | PF00083; | 1.20.1250.20; | Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family, Glucose transporter subfamily | PTM: N-glycosylated; required for stability and retention at the cell surface of pancreatic beta cells. {ECO:0000269|PubMed:16377570}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11168}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376, ChEBI:CHEBI:4167; Evidence={ECO:0000250|UniProtKB:P11168}; CATALYTIC ACTIVITY: Reaction=D-fructose(out) = D-fructose(in); Xref=Rhea:RHEA:60372, ChEBI:CHEBI:37721; Evidence={ECO:0000250|UniProtKB:P11168}; CATALYTIC ACTIVITY: Reaction=L-de... | null | null | null | null | FUNCTION: Facilitative hexose transporter that mediates the transport of glucose, fructose and galactose. Likely mediates the bidirectional transfer of glucose across the plasma membrane of hepatocytes and is responsible for uptake of glucose by the beta cells; may comprise part of the glucose-sensing mechanism of the ... | Mus musculus (Mouse) |
P14250 | GUN3_FIBSS | MQLKNFYPKMSVLGIATVMALTACGDENTQALFANNPVPGAENQVPVSSSDMSPTSSDAVIDPTSSSAAVVDPSTLPAEGPITMPEGLGTLVDDFEDGDNLSKIGDYWYTYNDNDNGGASIITTPLNEEENIIPGRVNNGSNYALQVNYTLDRGDYEYDPYVGWGVQVAPDEANGHFGGLTYWYKGGAHEVHIEITDVEDYDVHLAKFPASRTWKQAVVRFKDLVQGGWGKEIPFDAKHIMAISFQAKGNKSKLVTDSLFIDNIYLQDSSEVEKDQPDMEIKDPVIPVVEFTEAEITVTNPLQEKAMKYLNKGVNFTNWL... | 3.2.1.4 | null | cellulose catabolic process [GO:0030245] | cell surface [GO:0009986]; extracellular region [GO:0005576]; membrane [GO:0016020] | beta-glucosidase activity [GO:0008422]; cellulase activity [GO:0008810] | PF03425;PF00150; | 3.20.20.80; | Glycosyl hydrolase 5 (cellulase A) family | PTM: May be a lipoprotein and may be glycosylated. | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; | null | null | null | null | FUNCTION: Exhibits both endoglucanase and cellobiosidase activities. | Fibrobacter succinogenes (strain ATCC 19169 / S85) |
P14260 | HBB_CAIMO | MVHWTAEEKQLITGLWGKVNVADCGAEALARLLIVYPWTQRFFASFGNLSSPTAILGNPMVRAHGKKVLTSFGDAVKNLDNIKNTFAQLSELHCDKLHVDPENFRLLGDILIIVLAAHFTKDFTPDCQAAWQKLVRVVAHALARKYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. | Cairina moschata (Muscovy duck) |
P14263 | CP51_CANTR | MAIVDTAIDGINYFLSLSLTQQITILVVFPFIYNIAWQLLYSLRKDRVPMVFYWIPWFGSAASYGMQPYEFFEKCRLKYGDVFSFMLLGKVMTVYLGPKGHEFIYNAKLSDVSAEEAYTHLTTPVFGKGVIYDCPNSRLMEQKKFAKFALTTDSFKTYVPKIREEVLNYFVNDVSFKTKERDHGVASVMKTQPEITIFTASRCLFGDEMRKSFDRSFAQLYADLDKGFTPINFVFPNLPLPHYWRRDAAQRKISAHYMKEIKRRRESGDIDPKRDLIDSLLVNSTYKDGVKMTDQEIANLLIGVLMGGQHTSASTSAWFL... | 1.14.14.154 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | bile acid biosynthetic process [GO:0006699]; cholesterol homeostasis [GO:0042632]; ergosterol biosynthetic process [GO:0006696] | cortical endoplasmic reticulum [GO:0032541]; membrane [GO:0016020]; perinuclear endoplasmic reticulum [GO:0097038] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxysterol 7-alpha-hydroxylase activity [GO:0008396]; steroid 7-alpha-hydroxylase activity [GO:0008387]; sterol 14-demethylase activity [GO:0008398] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,... | null | PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6. | null | null | FUNCTION: Sterol 14alpha-demethylase that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (By similarity). The third module or late pathway involves the ergosterol synthesis itself t... | Candida tropicalis (Yeast) |
P14270 | PDE4D_RAT | MEAEGSSVPARAGSHEGSDSSGGAALKAPKHLWRHEQHHQYPLRQPQFRLLHPHHHLPPPPPPSPQPQLQPPPPPPLPPPPPPPGATRGRYASSGASRVRHRGYSDTERYLYCRAMDRTSYAVETGHRPGLKKSRMSWPSSFQGLRRFDVDNGTSAGRSPLDPMTSPGSGLILQANFVHSQRRESFLYRSDSDYDLSPKSMSRNSSIASDIHGDDLIVTPFAQVLASLRTVRNNFAALTNLQDRAPSKRSPMCNQPSINKATITEEAYQKLASETLEELDWCLDQLETLQTRHSVSEMASNKFKRMLNRELTHLSEMSRS... | 3.1.4.53 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q08499}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions. {ECO:0000250|UniProtKB:Q08499}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q08499}; Name=Mn(2+); Xref=ChE... | adrenergic receptor signaling pathway [GO:0071875]; cAMP catabolic process [GO:0006198]; cAMP-mediated signaling [GO:0019933]; cellular response to cAMP [GO:0071320]; cellular response to epinephrine stimulus [GO:0071872]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; cellular response to lip... | calcium channel complex [GO:0034704]; centrosome [GO:0005813]; cytosol [GO:0005829]; membrane [GO:0016020]; myofibril [GO:0030016]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; potassium channel complex [GO:0034705]; protein-containing complex [GO:0032991]; voltage-gated calcium channel complex [... | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; 3',5'-cyclic-nucleotide phosphodiesterase activity [GO:0004114]; ATPase binding [GO:0051117]; beta-2 adrenergic receptor binding [GO:0031698]; calcium channel regulator activity [GO:0005246]; cAMP binding... | PF18100;PF00233; | 1.10.1300.10; | Cyclic nucleotide phosphodiesterase family, PDE4 subfamily | PTM: Isoform 1 and isoform 9 are rapidly activated by PKA through phosphorylation. Long isoforms that share a conserved PKA phosphorylation site in the N-terminus are also activated. {ECO:0000269|PubMed:10187850}.; PTM: Sumoylation of long isoforms by PIAS4 augments their activation by PKA phosphorylation and represses... | SUBCELLULAR LOCATION: Apical cell membrane. Cytoplasm. Membrane. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Found in the soluble fraction, associated with membranes, and associated with the cytoskeleton and the centrosome. Colocalized with SHANK2 to the apical memb... | CATALYTIC ACTIVITY: Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165, ChEBI:CHEBI:456215; EC=3.1.4.53; Evidence={ECO:0000250|UniProtKB:Q08499}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278; Evidence={ECO:0000250|UniProtKB:Q08499}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=18 pmol/min/mg enzyme for cAMP (in the absence of follicle-stimulating hormone (FSH)) {ECO:0000269|PubMed:17261351}; Vmax=5 pmol/min/mg enzyme for cAMP (in the presence of follicle-stimulating hormone (FSH)) {ECO:0000269|PubMed:17261351}; | PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1. | null | null | FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. | Rattus norvegicus (Rat) |
P14271 | UCP1_RABIT | MVGTTTTDVPPTMGVKIFSAGVAACLADVITFPLDTAKVRQQIQGEFPITSGIRYKGVLGTITTLAKTEGPLKLYSGLPAGLQRQISFASLRIGLYDTVQEFFTSGEETPSLGSKISAGLTTGGVAVFIGQPTEVVKVRLQAQSHLHGLKPRYTGTYNAYRIIATTESLTSLWKGTTPNLLRNVIINCTELVTYDLMKGALVRNEILADDVPCHFVSALIAGFCTTLLSSPVDVVKTRFINSPPGQYASVPNCAMTMFTKEGPTAFFKGFVPSFLRLGSWNVIMFVCFEKLKGELMRSRQTVDCAT | null | null | adaptive thermogenesis [GO:1990845]; cellular response to fatty acid [GO:0071398]; cellular response to hormone stimulus [GO:0032870]; cellular response to reactive oxygen species [GO:0034614]; mitochondrial transmembrane transport [GO:1990542]; proton transmembrane transport [GO:1902600]; regulation of reactive oxygen... | mitochondrial inner membrane [GO:0005743] | cardiolipin binding [GO:1901612]; long-chain fatty acid binding [GO:0036041]; oxidative phosphorylation uncoupler activity [GO:0017077]; purine ribonucleotide binding [GO:0032555] | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | PTM: May undergo sulfenylation upon cold exposure. May increase the sensitivity of UCP1 thermogenic function to the activation by noradrenaline probably through structural effects. {ECO:0000250|UniProtKB:P12242}.; PTM: May undergo ubiquitin-mediated proteasomal degradation. {ECO:0000250|UniProtKB:P04633}. | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P12242}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P04633}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:P25874}; | null | null | null | null | FUNCTION: Mitochondrial protein responsible for thermogenic respiration, a specialized capacity of brown adipose tissue and beige fat that participates in non-shivering adaptive thermogenesis to temperature and diet variations and more generally to the regulation of energy balance. Functions as a long-chain fatty acid/... | Oryctolagus cuniculus (Rabbit) |
P14272 | KLKB1_RAT | MILFKQVGYFVSLFATVSCGCLSQLYANTFFRGGDLAAIYTPDAQHCQKMCTFHPRCLLFSFLAVSPTKETDKRFGCFMKESITGTLPRIHRTGAISGHSLKQCGHQLSACHQDIYEGLDMRGSNFNISKTDSIEECQKLCTNNIHCQFFTYATKAFHRPEYRKSCLLKRSSSGTPTSIKPVDNLVSGFSLKSCALSEIGCPMDIFQHFAFADLNVSQVVTPDAFVCRTVCTFHPNCLFFTFYTNEWETESQRNVCFLKTSKSGRPSPPIIQENAVSGYSLFTCRKARPEPCHFKIYSGVAFEGEELNATFVQGADACQE... | 3.4.21.34 | null | blood coagulation [GO:0007596]; fibrinolysis [GO:0042730]; inflammatory response [GO:0006954]; liver regeneration [GO:0097421]; plasminogen activation [GO:0031639]; positive regulation of fibrinolysis [GO:0051919] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252] | PF00024;PF00089; | 3.50.4.10;2.40.10.10; | Peptidase S1 family, Plasma kallikrein subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Cleaves selectively Arg-|-Xaa and Lys-|-Xaa bonds, including Lys-|-Arg and Arg-|-Ser bonds in (human) kininogen to release bradykinin.; EC=3.4.21.34; | null | null | null | null | FUNCTION: The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin. | Rattus norvegicus (Rat) |
P14280 | PME1_SOLLC | MANPQQPLLIKTHKQNPIISFKILSFVITLFVALFLVAPYQVEIKHSNLCKTAQDSQLCLSYVSDLISNEIVTTESDGHSILMKFLVNYVHQMNNAIPVVRKMKNQINDIRQHGALTDCLELLDQSVDFASDSIAAIDKRSRSEHANAQSWLSGVLTNHVTCLDELDSFTKAMINGTNLEELISRAKVALAMLASLTTQDEDVFMTVLGKMPSWVSSMDRKLMESSGKDIIANAVVAQDGTGDYQTLAEAVAAAPDKSKTRYVIYVKRGTYKENVEVASNKMNLMIVGDGMYATTITGSLNVVDGSTTFRSATLAAVGQG... | 3.1.1.11 | null | cell wall modification [GO:0042545]; fruit ripening [GO:0009835]; pectin catabolic process [GO:0045490] | extracellular region [GO:0005576] | aspartyl esterase activity [GO:0045330]; pectinesterase activity [GO:0030599]; pectinesterase inhibitor activity [GO:0046910] | PF01095;PF04043; | 1.20.140.40;2.160.20.10; | PMEI family; Pectinesterase family | null | SUBCELLULAR LOCATION: Secreted, cell wall. | CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol; Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11; | null | PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5. | null | null | FUNCTION: Pectinesterase may play a role in cell wall metabolism during fruit growth and development prior to ripening and may be required for preparing cell walls for softening by polygalacturonase during fruit ripening. | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
P14283 | PERT_BORPE | MNMSLSRIVKAAPLRRTTLAMALGALGAAPAAHADWNNQSIVKTGERQHGIHIQGSDPGGVRTASGTTIKVSGRQAQGILLENPAAELQFRNGSVTSSGQLSDDGIRRFLGTVTVKAGKLVADHATLANVGDTWDDDGIALYVAGEQAQASIADSTLQGAGGVQIERGANVTVQRSAIVDGGLHIGALQSLQPEDLPPSRVVLRDTNVTAVPASGAPAAVSVLGASELTLDGGHITGGRAAGVAAMQGAVVHLQRATIRRGDAPAGGAVPGGAVPGGAVPGGFGPGGFGPVLDGWYGVDVSGSSVELAQSIVEAPELGAA... | null | null | cell adhesion [GO:0007155] | cell outer membrane [GO:0009279]; cell surface [GO:0009986]; extracellular region [GO:0005576]; periplasmic space [GO:0042597] | null | PF03797;PF03212; | 2.160.20.20;2.40.128.130; | null | null | SUBCELLULAR LOCATION: [Pertactin autotransporter]: Periplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Outer membrane protein P.69]: Secreted. Cell surface.; SUBCELLULAR LOCATION: [Pertactin translocator]: Cell outer membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=The cleaved C-terminal fragment (a... | null | null | null | null | null | FUNCTION: Agglutinogen that binds to eukaryotic cells; a process mediated by the R-G-D sequence. Pertactin may have a role in bacterial adhesion, and thus play a role in virulence. May contribute to the disease state of whooping cough. | Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) |
P14284 | DPOZ_YEAST | MSRESNDTIQSDTVRSSSKSDYFRIQLNNQDYYMSKPTFLDPSHGESLPLNQFSQVPNIRVFGALPTGHQVLCHVHGILPYMFIKYDGQITDTSTLRHQRCAQVHKTLEVKIRASFKRKKDDKHDLAGDKLGNLNFVADVSVVKGIPFYGYHVGWNLFYKISLLNPSCLSRISELIRDGKIFGKKFEIYESHIPYLLQWTADFNLFGCSWINVDRCYFRSPVLNSILDIDKLTINDDLQLLLDRFCDFKCNVLSRRDFPRVGNGLIEIDILPQFIKNREKLQHRDIHHDFLEKLGDISDIPVKPYVSSARDMINELTMQR... | 2.7.7.7 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:22119860}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:22119860}; | DNA replication [GO:0006260]; double-strand break repair via homologous recombination [GO:0000724]; error-free translesion synthesis [GO:0070987]; error-prone translesion synthesis [GO:0042276] | mitochondrion [GO:0005739]; nucleus [GO:0005634]; zeta DNA polymerase complex [GO:0016035] | 4 iron, 4 sulfur cluster binding [GO:0051539]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166] | PF00136;PF03104;PF14260; | 1.10.132.60;3.30.342.10;1.10.287.690;3.90.1600.10;3.30.420.10; | DNA polymerase type-B family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16452144}. Nucleus {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000269|PubMed:11316789}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=543 uM for dGTP (insertion opposite abasic site) {ECO:0000269|PubMed:11316789}; KM=81 uM for dATP (insertion opposite abasic site) {ECO:0000269|PubMed:11316789}; KM=125 uM for dTTP (insertion opposite abasic site) {ECO:0000269|PubMed:11316789}; KM=113 uM for dCTP (... | null | null | null | FUNCTION: Nonessential DNA polymerase. Required for DNA damage induced mutagenesis. Involved in DNA repair, mitochondrial DNA repair and translesion synthesis. Translesion synthesis in S.cerevisiae may use a specialized DNA polymerase that is not required for other DNA replicative processes. Has a role in the bypass of... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14287 | OSTP_PIG | MRIAVIAFCLWGFASALPVKQTNSGSSEEKLLSNKYTDAVATLLKPDPSQKQTFLAPQNTISSEETDDFKQETLPSKSNESPEQTDDVDDDDDEDHVDSRDTDSEEADHADDADRSDESHHSDESDELVTDFPTDTPATDVTPAVPTGDPNDGRGDSVVYGLRSKSKKFRRSEAQQLDATEEDLTSHVESEETDGTPKAILVAQRLHVASDLDSQEKDSQETSQPDDRSVETRSQEQSKEYTIKTYDGSNEHSNVIESQENPKVSQEFHSHEDKLVPDSKSEEDKHLKLRVSHELESASSEIN | null | null | androgen catabolic process [GO:0006710]; biomineral tissue development [GO:0031214]; cell adhesion [GO:0007155]; cellular response to testosterone stimulus [GO:0071394]; osteoblast differentiation [GO:0001649]; positive regulation of bone resorption [GO:0045780]; positive regulation of DNA-templated transcription [GO:0... | extracellular space [GO:0005615]; Golgi apparatus [GO:0005794] | cytokine activity [GO:0005125]; extracellular matrix binding [GO:0050840]; integrin binding [GO:0005178]; ion binding [GO:0043167] | PF00865; | null | Osteopontin family | PTM: Extensively phosphorylated by FAM20C in the extracellular medium at multiple sites within the S-x-E/pS motif (By similarity). The phosphorylated form inhibits hydroxyapatite crystallization. Dephosphorylation via a mechanism involving ALPL/TNAP promotes hydroxyapatite crystallization (By similarity). {ECO:0000250|... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P10451}. | null | null | null | null | null | FUNCTION: Major non-collagenous bone protein that binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. {ECO:0000250|UniProtKB:P31096}.; FUNCTION: Acts as a cytokine involved in enhancing production of interferon-gamma and interleukin... | Sus scrofa (Pig) |
P14291 | RED1_YEAST | MEGLKKKIFGVCLKNDLAQTRNETKGIHYGLMTLETSKQLQEFLHLLVIKREVIQNFELLFHIINVAVKITDSNLPSDDIWHFILKLRFSSEINIDEDSKVLNYLLETGIAMENPVSWKCLAVISSILSSVPQSKKIITNLIETEHAKKIGQLFDNIQDLQQGNFLVEILSNCFKKSASNSKKVEKIPQLWQSRSKNKFFFENEFYPFSSKNGSLQTCQFLCNNFMSTLSFTGILRQVSYSGSETLKNLRIFKKKDDENSYFIQCIYNKIYLWLDEKAPLEFERKKIRITKNLKNKIQIKLRQPFHECVRTTADKTALLF... | null | null | homologous chromosome pairing at meiosis [GO:0007129]; homologous recombination [GO:0035825]; meiotic recombination checkpoint signaling [GO:0051598]; reciprocal meiotic recombination [GO:0007131]; sporulation resulting in formation of a cellular spore [GO:0030435]; synaptonemal complex assembly [GO:0007130] | condensed nuclear chromosome [GO:0000794]; lateral element [GO:0000800]; synaptonemal complex [GO:0000795] | chromatin DNA binding [GO:0031490]; identical protein binding [GO:0042802]; structural molecule activity [GO:0005198] | PF07964; | null | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Probable constituent of the synaptonemal complex during meiosis. May interact with HOP1. Required for meiosis I chromosome segregation. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14294 | TOP3_ECOLI | MRLFIAEKPSLARAIADVLPKPHRKGDGFIECGNGQVVTWCIGHLLEQAQPDAYDSRYARWNLADLPIVPEKWQLQPRPSVTKQLNVIKRFLHEASEIVHAGDPDREGQLLVDEVLDYLQLAPEKRQQVQRCLINDLNPQAVERAIDRLRSNSEFVPLCVSALARARADWLYGINMTRAYTILGRNAGYQGVLSVGRVQTPVLGLVVRRDEEIENFVAKDFFEVKAHIVTPADERFTAIWQPSEACEPYQDEEGRLLHRPLAEHVVNRISGQPAIVTSYNDKRESESAPLPFSLSALQIEAAKRFGLSAQNVLDICQKLY... | 5.6.2.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00953, ECO:0000269|PubMed:6326814}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_00953, ECO:0000269|PubMed:6326814}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP-Rule:MF_00953, ECO:0000269|... | chromosome separation [GO:0051304]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA topological change [GO:0006265]; DNA-templated DNA replication [GO:0006261] | cytoplasmic replication fork [GO:0043597] | DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917]; magnesium ion binding [GO:0000287]; sequence-specific single stranded DNA binding [GO:0098847] | PF01131;PF01751; | 3.40.50.140;1.10.460.10;2.70.20.10;1.10.290.10; | Type IA topoisomerase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00953, ECO:0000269|PubMed:6326814}; | null | null | null | null | FUNCTION: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is ... | Escherichia coli (strain K12) |
P14306 | CPYI_YEAST | MNQAIDFAQASIDSYKKHGILEDVIHDTSFQPSGILAVEYSSSAPVAMGNTLPTEKARSKPQFQFTFNKQMQKSVPQANAYVPQDDDLFTLVMTDPDAPSKTDHKWSEFCHLVECDLKLLNEATHETSGATEFFASEFNTKGSNTLIEYMGPAPPKGSGPHRYVFLLYKQPKGVDSSKFSKIKDRPNWGYGTPATGVGKWAKENNLQLVASNFFYAETK | null | null | regulation of proteolysis [GO:0030162]; regulation of Ras protein signal transduction [GO:0046578] | cytoplasm [GO:0005737]; fungal-type vacuole lumen [GO:0000328]; fungal-type vacuole membrane [GO:0000329] | peptidase inhibitor activity [GO:0030414]; phospholipid binding [GO:0005543]; serine-type endopeptidase inhibitor activity [GO:0004867] | PF01161; | 3.90.280.10; | Phosphatidylethanolamine-binding protein family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Specific and potent inhibitor of carboxypeptidase Y. {ECO:0000269|PubMed:9521655}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14314 | GLU2B_HUMAN | MLLPLLLLLPMCWAVEVKRPRGVSLTNHHFYDESKPFTCLDGSATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYIPSNRVNDGVCDCCDGTDEYNSGVICENTCKEKGRKERESLQQMAEVTREGFRLKKILIEDWKKAREEKQKKLIELQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQHQKLWEEQLAAAKAQQEQELAADAFKELDDDMDGTVSVTELQTHPELDTDGDGALSEAEAQALLSGDTQTDATSFYDRVWAAIRDKYRSEALPTDLPAPSAPDLTEPKEEQPPVPSSPTEEEEEEEE... | null | null | intracellular signal transduction [GO:0035556]; liver development [GO:0001889]; N-glycan processing [GO:0006491] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; glucosidase II complex [GO:0017177]; intracellular membrane-bounded organelle [GO:0043231] | calcium ion binding [GO:0005509]; phosphoprotein binding [GO:0051219]; protein kinase C binding [GO:0005080]; transmembrane transporter binding [GO:0044325] | PF13202;PF12999;PF13015; | 1.10.238.10;4.10.400.10;2.70.130.10; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000305|PubMed:10929008}. | null | null | PATHWAY: Glycan metabolism; N-glycan metabolism. {ECO:0000269|PubMed:10929008}. | null | null | FUNCTION: Regulatory subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins (PubMed:10929008). Required for efficient PKD1/Polycystin-1 biogenesis and trafficking to the plasma membrane of t... | Homo sapiens (Human) |
P14315 | CAPZB_CHICK | MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYLLCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVYLWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTNKTGSGTMNLGGSLTRQMEKDETVSDSSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIVNGLRSIDAIPDNQKYKQLQRELSQVLTQRQIYIQPDN | null | null | actin polymerization or depolymerization [GO:0008154]; barbed-end actin filament capping [GO:0051016]; cell morphogenesis [GO:0000902]; cytoskeleton organization [GO:0007010]; lamellipodium assembly [GO:0030032]; negative regulation of filopodium assembly [GO:0051490]; regulation of cell morphogenesis [GO:0022604]; reg... | brush border [GO:0005903]; cortical cytoskeleton [GO:0030863]; cytosol [GO:0005829]; F-actin capping protein complex [GO:0008290]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; lamellipodium [GO:0030027]; membrane [GO:0016020]; postsynaptic density [GO:0014069]; Schaffer collateral - CA1 synapse [GO:0098685]; sp... | actin filament binding [GO:0051015] | PF01115; | 1.20.58.570;6.10.250.30;3.90.1150.210; | F-actin-capping protein beta subunit family | null | SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:7929588}. Note=In cardiac muscle, isoform 1 is located at Z-disks of sarcomeres. {ECO:0000269|PubMed:7929588}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, myofibril, sarcomere, I band {ECO:0000269|PubMed:7929588}. Cytoplas... | null | null | null | null | null | FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the regul... | Gallus gallus (Chicken) |
P14316 | IRF2_HUMAN | MPVERMRMRPWLEEQINSNTIPGLKWLNKEKKIFQIPWMHAARHGWDVEKDAPLFRNWAIHTGKHQPGVDKPDPKTWKANFRCAMNSLPDIEEVKDKSIKKGNNAFRVYRMLPLSERPSKKGKKPKTEKEDKVKHIKQEPVESSLGLSNGVSDLSPEYAVLTSTIKNEVDSTVNIIVVGQSHLDSNIENQEIVTNPPDICQVVEVTTESDEQPVSMSELYPLQISPVSSYAESETTDSVPSDEESAEGRPHWRKRNIEGKQYLSNMGTRGSYLLPGMASFVTSNKPDLQVTIKEESNPVPYNSSWPPFQDLPLSSSMTPA... | null | null | cell population proliferation [GO:0008283]; defense response to virus [GO:0051607]; immune system process [GO:0002376]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; ... | chromatin [GO:0000785]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | 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]; RNA polymerase II cis-regulatory region sequence-specific DNA bindi... | PF00605; | 1.10.10.10; | IRF family | PTM: Acetylated by CBP/ p300 during cell-growth. Acetylation on Lys-75 is required for stimulation of H4 promoter activity. {ECO:0000269|PubMed:12738767}.; PTM: The major sites of sumoylation are Lys-137 and Lys-293. Sumoylation with SUMO1 increases its transcriptional repressor activity on IRF1 and diminishes its abil... | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Specifically binds to the upstream regulatory region of type I IFN and IFN-inducible MHC class I genes (the interferon consensus sequence (ICS)) and represses those genes. Also acts as an activator for several genes including H4 and IL7. Constitutively binds to the ISRE promoter to activate IL7. Involved in c... | Homo sapiens (Human) |
P14317 | HCLS1_HUMAN | MWKSVVGHDVSVSVETQGDDWDTDPDFVNDISEKEQRWGAKTIEGSGRTEHINIHQLRNKVSEEHDVLRKKEMESGPKASHGYGGRFGVERDRMDKSAVGHEYVAEVEKHSSQTDAAKGFGGKYGVERDRADKSAVGFDYKGEVEKHTSQKDYSRGFGGRYGVEKDKWDKAALGYDYKGETEKHESQRDYAKGFGGQYGIQKDRVDKSAVGFNEMEAPTTAYKKTTPIEAASSGTRGLKAKFESMAEEKRKREEEEKAQQVARRQQERKAVTKRSPEAPQPVIAMEEPAVPAPLPKKISSEAWPPVGTPPSSESEPVRTS... | null | null | actin filament organization [GO:0007015]; cellular response to cytokine stimulus [GO:0071345]; erythrocyte differentiation [GO:0030218]; granulocyte colony-stimulating factor signaling pathway [GO:0038158]; intracellular signal transduction [GO:0035556]; negative regulation of leukocyte apoptotic process [GO:2000107]; ... | actin filament [GO:0005884]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endocytic vesicle [GO:0030139]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; site of polarized growth [GO:0030427]; transcription regulator complex [GO:0005667] | actin filament binding [GO:0051015]; protein kinase binding [GO:0019901]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; SH3 domain binding [GO:0017124]; signaling adaptor activity [GO:0035591] | PF02218;PF00018; | 2.30.30.40; | null | PTM: Phosphorylated by FES (By similarity). Phosphorylated by LYN, FYN and FGR after cross-linking of surface IgM on B-cells. Phosphorylation by LYN, FYN and FGR requires prior phosphorylation by SYK or FES. {ECO:0000250, ECO:0000269|PubMed:10066823, ECO:0000269|PubMed:7682714, ECO:0000269|PubMed:8611520}. | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:7682714}; Peripheral membrane protein {ECO:0000269|PubMed:7682714}. Cytoplasm {ECO:0000269|PubMed:7682714}. Mitochondrion {ECO:0000305|PubMed:7682714}. | null | null | null | null | null | FUNCTION: Substrate of the antigen receptor-coupled tyrosine kinase. Plays a role in antigen receptor signaling for both clonal expansion and deletion in lymphoid cells. May also be involved in the regulation of gene expression. | Homo sapiens (Human) |
P14319 | QACC_STAAU | MPYIYLIIAISTEVIGSAFLKSSEGFSKFIPSLGTIISFGICFYFLSKTMQHLPLNITYATWAGLGLVLTTVVSIIIFKEQINLITIVSIVLIIVGVVSLNIFGTSH | null | null | glycine betaine transport [GO:0031460] | plasma membrane [GO:0005886] | amino-acid betaine transmembrane transporter activity [GO:0015199]; antiporter activity [GO:0015297]; choline transmembrane transporter activity [GO:0015220] | PF00893; | 1.10.3730.20; | Drug/metabolite transporter (DMT) superfamily, Small multidrug resistance (SMR) (TC 2.A.7.1) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7751293}; Multi-pass membrane protein {ECO:0000269|PubMed:7751293}. | null | null | null | null | null | FUNCTION: Multidrug exporter. Is implicated for the resistance to bacteriocidal quaternary ammonium compounds and ethidium bromide. {ECO:0000269|PubMed:1615062, ECO:0000269|PubMed:7751293, ECO:0000305|PubMed:2778425}. | Staphylococcus aureus |
P14324 | FPPS_HUMAN | MPLSRWLRSVGVFLLPAPYWAPRERWLGSLRRPSLVHGYPVLAWHSARCWCQAWTEEPRALCSSLRMNGDQNSDVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAIGGKYNRGLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQSSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSV... | 2.5.1.1; 2.5.1.10 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19309137}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:19309137}; | cholesterol biosynthetic process [GO:0006695]; farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654] | dimethylallyltranstransferase activity [GO:0004161]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872]; RNA binding [GO:0003723] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000269|PubMed:16684881}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diph... | null | PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1. | null | null | FUNCTION: Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the ... | Homo sapiens (Human) |
P14335 | POLG_KUNJM | MSKKPGGPGKSRAVNMLKRGMPRVLSLTGLKRAMLSLIDGRGPTRFVLALLAFFRFTAIAPTRAVLDRWRSVNKQTAMKHLLSFKKELGTLTSAINRRSSKQKKRGGKTGIAFMIGLIAGVGAVTLSNFQGKVMMTVNATDVTDIITIPPAAGKNLCIVRAMDVGHMCDDTITYECPVLSAGNDPEDIDCWCTKLAVYVRYGRCTKTRHSRRSRRSLTVQTHGESTLSNKKGAWMDSTKATRYLVKTESWILRNPGYALVAAVIGWMLGSNTMQRVVFAVLLLLVAPAYSFNCLGMSNRDFLEGVSGATWVDLVLEGDSC... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity [GO:0039574]; sym... | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization activity [GO:0046983]; RNA he... | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-m... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763... | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:... | null | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migr... | Kunjin virus (strain MRM61C) |
P14336 | POLG_TBEVW | MVKKAILKGKGGGPPRRVSKETATKTRQPRVQMPNGLVLMRMMGILWHAVAGTARNPVLKAFWNSVPLKQATAALRKIKRTVSALMVGLQKRGKRRSATDWMSWLLVITLLGMTLAATVRKERDGSTVIRAEGKDAATQVRVENGTCVILATDMGSWCDDSLSYECVTIDQGEEPVDVDCFCRNVDGVYLEYGRCGKQEGSRTRRSVLIPSHAQGELTGRGHKWLEGDSLRTHLTRVEGWVWKNKLLALAMVTVVWLTLESVVTRVAVLVVLLCLAPVYASRCTHLENRDFVTGTQGTTRVTLVLELGGCVTITAEGKPS... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbion... | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization activity [GO:0046983]; RNA he... | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-m... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763... | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:... | null | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migr... | Tick-borne encephalitis virus European subtype (strain Neudoerfl) (NEUV) (Neudoerfl virus) |
P14337 | POLG_DEN28 | MNNQRKKAKNTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLFMALVAFLRFLTIPPTAGILKRWGTIKKSKAINVLRGFRKEIGRMLNILNRRRRSAGMIIMLIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTEDGVNMCTLMAMDLGELCEDTITYKCPLLRQNEPEDIDCWCNSTSTWVTYGTCTTTGEHRREKRSVALVPHVGMGLETRTETWMSSEGAWKHAQRIETWILRHPGFTIMAAILAYTIGTTHFQRALIFILLTAVAPSMTMRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPT... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont-mediated suppression of host cytoplasmic pattern recog... | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell mitochondrion [GO:0033650]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:00550... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; prot... | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;2.40.10.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-m... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763... | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:... | null | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migr... | Dengue virus type 2 (isolate Thailand/0168/1979) (DENV-2) |
P14340 | POLG_DEN2N | MNNQRKKARNTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLFMALVAFLRFLTIPPTAGILKRWGTIKKSKAINVLRGFRKEIGRMLNILNRRRRTAGMIIMLIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTEDGVNMCTLMAMDLGELCEDTITYKCPFLKQNEPEDIDCWCNSTSTWVTYGTCTTTGEHRREKRSVALVPHVGMGLETRTETWMSSEGAWKHAQRIETWILRHPGFTIMAAILAYTIGTTHFQRALIFILLTAVAPSMTMRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPT... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont-mediated suppression of host cytoplasmic pattern recog... | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell mitochondrion [GO:0033650]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:00550... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; prot... | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;2.40.10.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-m... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763... | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=29.3 uM for triphosphorylated RNA {ECO:0000269|PubMed:15917225}; Note=Vmax with 0.65 nmol/s/ug enzyme for RTPase activity with triphosphorylated RNA as substrate. {ECO:0000269|PubMed:15917225}; | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migr... | Dengue virus type 2 (strain Thailand/NGS-C/1944) (DENV-2) |
P14349 | GAG_FOAMV | MASGSNVEEYELDVEALVVILRDRNIPRNPLHGEVIGLRLTEGWWGQIERFQMVRLILQDDDNEPLQRPRYEVIQRAVNPHTMFMISGPLAELQLAFQDLDLPEGPLRFGPLANGHYVQGDPYSSSYRPVTMAETAQMTRDELEDVLNTQSEIEIQMINLLELYEVETRALRRQLAERSSTGQGGISPGAPRSRPPVSSFSGLPSLPSIPGIHPRAPSPPRATSTPGNIPWSLGDDSPPSSSFPGPSQPRVSFHPGNPFVEEEGHRPRSQSRERRREILPAPVPSAPPMIQYIPVPPPPPIGTVIPIQHIRSVTGEPPRN... | null | null | microtubule-dependent intracellular transport of viral material towards nucleus [GO:0075521]; symbiont entry into host cell [GO:0046718]; viral budding via host ESCRT complex [GO:0039702]; viral release from host cell [GO:0019076] | host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cytoskeleton [GO:0044163]; viral nucleocapsid [GO:0019013] | DNA binding [GO:0003677]; RNA binding [GO:0003723] | PF20672;PF20673;PF03276; | 1.20.5.1500; | null | PTM: Specific enzymatic cleavages in vivo by viral protease yield mature proteins. The protease is not cleaved off from Pol. Since cleavage efficiency is not optimal for all sites, intermediary molecules are expressed. {ECO:0000269|PubMed:10438890}. | SUBCELLULAR LOCATION: [Gag protein]: Virion. Host nucleus. Host cytoplasm. Note=Nuclear at initial phase, cytoplasmic at assembly. Shortly after infection, Gag protein is targeted to centrosomes. It is then actively transported into the nucleus thanks to its nuclear localization signal. In the late phases of infection,... | null | null | null | null | null | FUNCTION: Involved in capsid formation and genome binding. Shortly after infection, interaction between incoming particle-associated Gag proteins and host dynein allows centrosomal targeting of the viral genome (associated to Gag), prior to nucleus translocation and integration into host genome. {ECO:0000269|PubMed:128... | Human spumaretrovirus (SFVcpz(hu)) (Human foamy virus) |
P14350 | POL_FOAMV | MNPLQLLQPLPAEIKGTKLLAHWDSGATITCIPESFLEDEQPIKKTLIKTIHGEKQQNVYYVTFKVKGRKVEAEVIASPYEYILLSPTDVPWLTQQPLQLTILVPLQEYQEKILSKTALPEDQKQQLKTLFVKYDNLWQHWENQVGHRKIRPHNIATGDYPPRPQKQYPINPKAKPSIQIVIDDLLKQGVLTPQNSTMNTPVYPVPKPDGRWRMVLDYREVNKTIPLTAAQNQHSAGILATIVRQKYKTTLDLANGFWAHPITPESYWLTAFTWQGKQYCWTRLPQGFLNSPALFTADVVDLLKEIPNVQVYVDDIYLSH... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO: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]; viral genome integration into host DNA [GO:0044826]; viral penetration into host nucleus [GO:0075732] | host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; virion component [GO:0044423] | aspartic-type endopeptidase activity [GO:0004190]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523] | PF17921;PF00075;PF17919;PF00665;PF00078;PF18103;PF03539; | 1.10.340.70;2.30.30.140;3.30.70.270;6.10.20.110;2.40.70.10;3.10.10.10;3.30.420.10; | null | PTM: Specific enzymatic cleavages in vivo by viral protease yield mature proteins. The protease is not cleaved off from Pol. Since cleavage efficiency is not optimal for all sites, long and active p65Pro-RT, p87Pro-RT-RNaseH and even some Pr125Pol are detected in infected cells. {ECO:0000269|PubMed:9696869}. | SUBCELLULAR LOCATION: [Integrase]: Virion {ECO:0000305}. Host nucleus. Host cytoplasm {ECO:0000305}. Note=Nuclear at initial phase, cytoplasmic at assembly. {ECO:0000305}.; SUBCELLULAR LOCATION: [Protease/Reverse transcriptase/ribonuclease H]: Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000305}. Note=Nuclear at in... | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CH... | null | null | null | null | FUNCTION: The aspartyl protease activity mediates proteolytic cleavages of Gag and Pol polyproteins. The reverse transcriptase (RT) activity converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell (early reverse transcription) or after proviral DNA transcription (late reverse ... | Human spumaretrovirus (SFVcpz(hu)) (Human foamy virus) |
P14351 | ENV_FOAMV | MAPPMTLQQWIIWKKMNKAHEALQNTTTVTEQQKEQIILDIQNEEVQPTRRDKFRYLLYTCCATSSRVLAWMFLVCILLIIVLVSCFVTISRIQWNKDIQVLGPVIDWNVTQRAVYQPLQTRRIARSLRMQHPVPKYVEVNMTSIPQGVYYEPHPEPIVVKERVLGLSQILMINSENIANNANLTQEVKKLLTEMVNEEMQSLSDVMIDFEIPLGDPRDQEQYIHRKCYQEFANCYLVKYKEPKPWPKEGLIADQCPLPGYHAGLTYNRQSIWDYYIKVESIRPANWTTKSKYGQARLGSFYIPSSLRQINVSHVLFCSD... | null | null | null | host cell endoplasmic reticulum membrane [GO:0044167]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF03408; | null | null | PTM: Envelope glycoproteins are synthesized as an inactive precursor that is processed by host furin or a furin-like protease to yield a functional hetero-oligomeric complex. {ECO:0000250}.; PTM: The transmembrane protein and the surface protein are N-glycosylated. {ECO:0000250}.; PTM: Mono- and polyubiquitinated leade... | SUBCELLULAR LOCATION: [Envelope glycoprotein gp130]: Host endoplasmic reticulum membrane. Note=The polyprotein has a highly unusual biosynthesis for a retroviral glycoprotein. It is translated as a full-length precursor protein into the rough endoplasmic reticulum and initially has a type III protein configuration with... | null | null | null | null | null | FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to the cell receptor. This interaction triggers the refolding of transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity). {ECO:0000250}.; FUNCTION: The transmembrane pr... | Human spumaretrovirus (SFVcpz(hu)) (Human foamy virus) |
P14353 | BEL1_FOAMV | MDSYEKEESVASTSGIQDLQTLSELVGPENAGEGELTIAEEPEENPRRPRRYTKREVKCVSYHAYKEIEDKHPQHIKLQDWIPTPEEMSKSLCKRLILCGLYSAEKASEILRMPFTVSWEQSDTDPDCFIVSYTCIFCDAVIHDPMPIRWDPEVGIWVKYKPLRGIVGSAVFIMHKHQRNCSLVKPSTSCSEGPKPRPRHDPVLRCDMFEKHHKPRQKRPRRRSIDNESCASSSDTMANEPGSLCTNPLWNPGPLLSGLLEESSNLPNLEVHMSGGPFWEEVYGDSILGPPSGSGEHSVL | null | null | positive regulation of DNA-templated transcription [GO:0045893]; viral process [GO:0016032] | host cell nucleus [GO:0042025] | DNA binding [GO:0003677] | PF03274; | null | null | null | SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:8383217}. | null | null | null | null | null | FUNCTION: Transcriptional transactivator that activates the viral internal promoter (IP), thereby enhancing its own expression. This transactivation is repressed by nuclear factor I. Also transactivates the long terminal repeat (LTR) promoter, thereby inducing structural gene expression, initiating the late phase of in... | Human spumaretrovirus (SFVcpz(hu)) (Human foamy virus) |
P14373 | TRI27_HUMAN | MASGSVAECLQQETTCPVCLQYFAEPMMLDCGHNICCACLARCWGTAETNVSCPQCRETFPQRHMRPNRHLANVTQLVKQLRTERPSGPGGEMGVCEKHREPLKLYCEEDQMPICVVCDRSREHRGHSVLPLEEAVEGFKEQIQNQLDHLKRVKDLKKRRRAQGEQARAELLSLTQMEREKIVWEFEQLYHSLKEHEYRLLARLEELDLAIYNSINGAITQFSCNISHLSSLIAQLEEKQQQPTRELLQDIGDTLSRAERIRIPEPWITPPDLQEKIHIFAQKCLFLTESLKQFTEKMQSDMEKIQELREAQLYSVDVTL... | 2.3.2.27 | null | Arp2/3 complex-mediated actin nucleation [GO:0034314]; innate immune response [GO:0045087]; negative regulation of adaptive immune response [GO:0002820]; negative regulation of autophagy [GO:0010507]; negative regulation of calcium ion import [GO:0090281]; negative regulation of gene expression, epigenetic [GO:0045814]... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; endosome [GO:0005768]; fibrillar center [GO:0001650]; mitochondrion [GO:0005739]; nuclear membrane [GO:0031965]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605] | DNA binding [GO:0003677]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]; SUMO transferase activity [GO:0019789]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842... | PF13765;PF00622;PF00643;PF15227; | 2.60.120.920;3.30.160.60;3.30.40.10; | TRIM/RBCC family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17156811}. Cytoplasm {ECO:0000269|PubMed:17156811, ECO:0000269|PubMed:36111389}. Nucleus, PML body {ECO:0000250}. Early endosome {ECO:0000269|PubMed:1437549, ECO:0000269|PubMed:23452853, ECO:0000269|PubMed:9247190}. Mitochondrion {ECO:0000269|PubMed:24144979}. Note=Nucl... | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:22829933, ECO:0000269|PubMed:24144979, ECO:0000269|PubMed:263581... | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:22128329, ECO:0000269|PubMed:22829933, ECO:0000269|PubMed:26358190, ECO:0000269|PubMed:35670107}. | null | null | FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of various substrates and thereby plays a role in diffent processes including proliferation, innate immunity, apoptosis, immune response or autophagy (PubMed:22829933, PubMed:24144979, PubMed:29688809, PubMed:36111389). Ubiquitinates PIK3C2B and inhibit... | Homo sapiens (Human) |
P14377 | ZRAS_ECOLI | MRFMQRSKDSLAKWLSAILPVVIVGLVGLFAVTVIRDYGRASEADRQALLEKGNVLIRALESGSRVGMGMRMHHVQQQALLEEMAGQPGVLWFAVTDAQGIIILHSDPDKVGRALYSPDEMQKLKPEENSRWRLLGKTETTPALEVYRLFQPMSAPWRHGMHNMPRCNGKAVPQVDAQQAIFIAVDASDLVATQSGEKRNTLIILFALATVLLASVLSFFWYRRYLRSRQLLQDEMKRKEKLVALGHLAAGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMAKEADRLNRVVSELLELVKPTHLALQAVDLNTL... | 2.7.13.3 | null | cellular response to cell envelope stress [GO:0036460]; cellular response to lead ion [GO:0071284]; cellular response to zinc ion [GO:0071294]; signal transduction [GO:0007165] | membrane [GO:0016020]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; phosphorelay sensor kinase activity [GO:0000155]; protein histidine kinase activity [GO:0004673] | PF02518;PF00512; | 1.10.287.130;3.30.565.10;3.30.450.20; | null | PTM: Autophosphorylated. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; | null | null | null | null | FUNCTION: Member of the two-component regulatory system ZraS/ZraR. May function as a membrane-associated protein kinase that phosphorylates ZraR in response to high concentrations of zinc or lead in the medium. {ECO:0000269|PubMed:15522865}. | Escherichia coli (strain K12) |
P14384 | CBPM_HUMAN | MDFPCLWLGLLLPLVAALDFNYHRQEGMEAFLKTVAQNYSSVTHLHSIGKSVKGRNLWVLVVGRFPKEHRIGIPEFKYVANMHGDETVGRELLLHLIDYLVTSDGKDPEITNLINSTRIHIMPSMNPDGFEAVKKPDCYYSIGRENYNQYDLNRNFPDAFEYNNVSRQPETVAVMKWLKTETFVLSANLHGGALVASYPFDNGVQATGALYSRSLTPDDDVFQYLAHTYASRNPNMKKGDECKNKMNFPNGVTNGYSWYPLQGGMQDYNYIWAQCFEITLELSCCKYPREEKLPSFWNNNKASLIEYIKQVHLGVKGQVF... | 3.4.17.12 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:15066430}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:15066430}; | anatomical structure morphogenesis [GO:0009653]; peptide metabolic process [GO:0006518]; protein processing [GO:0016485] | cell surface [GO:0009986]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | carboxypeptidase activity [GO:0004180]; metallocarboxypeptidase activity [GO:0004181]; zinc ion binding [GO:0008270] | PF13620;PF00246; | 2.60.40.1120;3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12457462}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12457462}. | CATALYTIC ACTIVITY: Reaction=Cleavage of C-terminal arginine or lysine residues from polypeptides.; EC=3.4.17.12; Evidence={ECO:0000269|PubMed:12457462}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=59 uM for synthetic dansyl-Ala-Arg {ECO:0000269|PubMed:12457462}; KM=57 uM for placental peptide hormones {ECO:0000269|PubMed:12457462}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:12457462}; | null | FUNCTION: Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins. {ECO:0000269|PubMed:12457462}. | Homo sapiens (Human) |
P14403 | POLG_JAEVN | SVAMKHLTSFKRELGTLIDAVNKRGRKQNKRGGNEGSIMWLASLAVVIACAGAMKLSNFQGKLLMTVNNTDIADVIVIPNPSKGENRCWVRAIDVGYMCEDTITYECPKLTMGNDPEDVDCWCDNQEVYVQYGRCTRTRHSKRSRRSVSVQTHGESSLVNKKEAWLDSTKATRYLMKTENWIVRNPGYAFLAAILGWMLGSNNGQRRWYFTILLLLVAPAYSFNCLGMGNRDFIEGASGATWVDLVLEGDSCLTIMANDKPTLDVRMINIEAVQLAEVRSYCYHASVTDISTVARCPTTGEAHNEKRADSSYVCKQGFTD... | 3.4.21.91; 3.6.1.15; 3.6.4.13 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=For RNA-directed RNA polymerase NS5 activity; Mn(2+) is more effective than Mg(2+). {ECO:0000250|UniProtKB:P27395}; | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; proteolysis [GO:0006508]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host JAK-STAT cascade via... | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; protein dimerization activity [GO:0046983]; RNA helicase activity [GO:0003724]; serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198] | PF01003;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01570; | 1.10.10.930;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;2.60.98.10;3.30.67.10;3.30.387.10; | null | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-m... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763... | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, Ch... | null | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migr... | Japanese encephalitis virus (strain Nakayama) (JEV) |
P14404 | MECOM_MOUSE | MRSKGRARKLATSNECAYGNYPEIPLEEMPDADADGITSVPSLHIQEPCSPATSSESFTPKEGSPYKAPIYIPDDIPIPDEFELRESTMPGAGLGIWTKRKIEIGEKFGPYMGEQRSDLKDSSYGWEILDEFCNVKFCIDASQPDVGSWLKYIRFAGCYDQHNLVACQINDQIFYRVVADIAPGEELLLFMKSEEDPHEPMAPDIHEERQHRCEDCDQLFESKAELADHQKFPCSTPHSAFSMVEEDLQQNLESESDLREIHGNQDCKECDRVFPDLQSLEKHMLSHTEEREYKCDQCPKAFNWKSNLIRHQMSHDSGKH... | 2.1.1.367 | null | apoptotic process [GO:0006915]; embryonic forelimb morphogenesis [GO:0035115]; embryonic hindlimb morphogenesis [GO:0035116]; forebrain development [GO:0030900]; hematopoietic stem cell proliferation [GO:0071425]; heterochromatin organization [GO:0070828]; in utero embryonic development [GO:0001701]; inflammatory respo... | cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; histone H3K9 methyltransferase activity [GO:0046974]; histone H3K9 monomethyltransferase activity [GO:0140948]; histone H3K9me2 methyltransferase activ... | PF21549;PF00096;PF13912; | 3.30.160.60;2.170.270.10; | null | PTM: May be acetylated by CREBBP and KAT2B. {ECO:0000250|UniProtKB:Q03112}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2106070}. Nucleus speckle {ECO:0000250|UniProtKB:Q03112}. Cytoplasm {ECO:0000250|UniProtKB:Q03112}. | CATALYTIC ACTIVITY: Reaction=L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60280, Rhea:RHEA-COMP:15542, Rhea:RHEA-COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1... | null | null | null | null | FUNCTION: [Isoform 1]: Functions as a transcriptional regulator binding to DNA sequences in the promoter region of target genes and regulating positively or negatively their expression. Oncogene which plays a role in development, cell proliferation and differentiation. May also play a role in apoptosis through regulati... | Mus musculus (Mouse) |
P14406 | CX7A2_HUMAN | MLRNLLALRQIGQRTISTASRRHFKNKVPEKQKLFQEDDEIPLYLKGGVADALLYRATMILTVGGTAYAIYELAVASFPKKQE | null | null | cellular respiration [GO:0045333]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial respirasome assembly [GO:0097250]; regulation of oxidative phosphorylation [GO:0002082] | mitochondrial membrane [GO:0031966]; mitochondrial respirasome [GO:0005746]; mitochondrial respiratory chain complex IV [GO:0005751] | oxidoreductase activity [GO:0016491] | PF02238; | 4.10.91.10; | Cytochrome c oxidase VIIa family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:30030519}; Single-pass membrane protein {ECO:0000269|PubMed:30030519}. | null | null | PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000250|UniProtKB:P10174}. | null | null | FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... | Homo sapiens (Human) |
P14407 | FUMB_ECOLI | MSNKPFIYQAPFPMGKDNTEYYLLTSDYVSVADFDGETILKVEPEALTLLAQQAFHDASFMLRPAHQKQVAAILHDPEASENDKYVALQFLRNSEIAAKGVLPTCQDTGTAIIVGKKGQRVWTGGGDEETLSKGVYNTYIEDNLRYSQNAALDMYKEVNTGTNLPAQIDLYAVDGDEYKFLCVAKGGGSANKTYLYQETKALLTPGKLKNFLVEKMRTLGTAACPPYHIAFVIGGTSAETNLKTVKLASAHYYDELPTEGNEHGQAFRDVQLEQELLEEAQKLGLGAQFGGKYFAHDIRVIRLPRHGASCPVGMGVSCSA... | 4.2.1.2; 4.2.1.81 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:23405168}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:23405168}; | DNA damage response [GO:0006974]; single-species biofilm formation [GO:0044010]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829] | 4 iron, 4 sulfur cluster binding [GO:0051539]; D(-)-tartrate dehydratase activity [GO:0047808]; fumarate hydratase activity [GO:0004333]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803] | PF05681;PF05683; | 3.20.130.10; | Class-I fumarase family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460, ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2; Evidence={ECO:0000269|PubMed:23405168}; CATALYTIC ACTIVITY: Reaction=(S,S)-tartrate = H2O + oxaloacetate; Xref=Rhea:RHEA:18289, ChEBI:CHEBI:15377, ChEBI:CHEBI:16452, ChEBI... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=300 uM for (S)-malate {ECO:0000269|PubMed:23405168}; KM=320 uM for fumarate {ECO:0000269|PubMed:23405168}; KM=800 uM for D-tartrate {ECO:0000269|PubMed:23405168}; Vmax=490 umol/min/mg enzyme for (S)-malate dehydration {ECO:0000269|PubMed:23405168}; Vmax=1430 umol/m... | null | null | null | FUNCTION: Catalyzes the reversible hydration of fumarate to (S)-malate. Functions in the generation of fumarate for use as an anaerobic electron acceptor. To a lesser extent, also displays D-tartrate dehydratase activity, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Is required for anaerobic grow... | Escherichia coli (strain K12) |
P14408 | FUMH_RAT | MNRAFCLLARSRRFPRVPSAGAVLSGEAATLPRCAPNVVRMASQNSFRIEYDTFGELKVPTDKYYGAQTVRSTMNFKIGGATERMPIPVIKAFGILKRAAAEVNQEYGLDPKIASAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAALEVHQVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMERIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVE... | 4.2.1.2 | null | DNA damage response [GO:0006974]; DNA repair [GO:0006281]; fumarate metabolic process [GO:0006106]; homeostasis of number of cells within a tissue [GO:0048873]; malate metabolic process [GO:0006108]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of double-strand break repair via no... | chromosome [GO:0005694]; cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; tricarboxylic acid cycle enzyme complex [GO:0045239] | fumarate hydratase activity [GO:0004333] | PF10415;PF00206; | 1.10.40.30;1.20.200.10;1.10.275.10; | Class-II fumarase/aspartase family, Fumarase subfamily | PTM: [Isoform Cytoplasmic]: Phosphorylation at Thr-233 by PRKDC in response to DNA damage promotes translocation to the nucleus and recruitment to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:P07954}. | SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion {ECO:0000269|PubMed:2914923}.; SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm, cytosol {ECO:0000269|PubMed:2914923}. Nucleus {ECO:0000250|UniProtKB:P07954}. Chromosome {ECO:0000250|UniProtKB:P07954}. Note=Translocates to the nucleus in response to DNA... | CATALYTIC ACTIVITY: [Isoform Mitochondrial]: Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460, ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2; Evidence={ECO:0000250|UniProtKB:P10173}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12462; Evidence={ECO:0000250|UniProtKB:P10173}; CATA... | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. {ECO:0000250|UniProtKB:P10173}. | null | null | FUNCTION: Catalyzes the reversible stereospecific interconversion of fumarate to L-malate (By similarity). Experiments in other species have demonstrated that specific isoforms of this protein act in defined pathways and favor one direction over the other (Probable). {ECO:0000250|UniProtKB:P07954, ECO:0000305}.; FUNCTI... | Rattus norvegicus (Rat) |
P14410 | SUIS_HUMAN | MARKKFSGLEISLIVLFVIVTIIAIALIVVLATKTPAVDEISDSTSTPATTRVTTNPSDSGKCPNVLNDPVNVRINCIPEQFPTEGICAQRGCCWRPWNDSLIPWCFFVDNHGYNVQDMTTTSIGVEAKLNRIPSPTLFGNDINSVLFTTQNQTPNRFRFKITDPNNRRYEVPHQYVKEFTGPTVSDTLYDVKVAQNPFSIQVIRKSNGKTLFDTSIGPLVYSDQYLQISTRLPSDYIYGIGEQVHKRFRHDLSWKTWPIFTRDQLPGDNNNNLYGHQTFFMCIEDTSGKSFGVFLMNSNAMEIFIQPTPIVTYRVTGGI... | 3.2.1.10; 3.2.1.48 | null | polysaccharide digestion [GO:0044245]; sucrose catabolic process [GO:0005987] | apical plasma membrane [GO:0016324]; brush border [GO:0005903]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886] | alpha-1,4-glucosidase activity [GO:0004558]; carbohydrate binding [GO:0030246]; oligo-1,6-glucosidase activity [GO:0004574]; sucrose alpha-glucosidase activity [GO:0004575] | PF13802;PF01055;PF21365;PF00088; | 3.20.20.80;2.60.40.1760;2.60.40.1180;4.10.110.10; | Glycosyl hydrolase 31 family | PTM: The precursor is proteolytically cleaved when exposed to pancreatic proteases in the intestinal lumen.; PTM: Sulfated. {ECO:0000250}. | SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II membrane protein. Note=Brush border. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action.; EC=3.2.1.48; CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.; EC=3.2.1.10; | null | null | null | null | FUNCTION: Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides. {ECO:0000269|PubMed:20356844}. | Homo sapiens (Human) |
P14411 | PA2BA_BUNFA | AVCVSLLGAANIPPQPLNLYQFKNMIQCAGTQLWVAYVNYGCYCGKGGSGTPVDQLDRCCQTHDHCYHNAKRFGKCNPYFKTYEYTCNKPNLTCRGAKGSCGRNVCDCDRAAAICFAAAPYNLSNFGINKKTHCK | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; fatty acid biosynthetic process [GO:0006633]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]; positive regulation of fibroblast proliferation [GO:0048146] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (By similarity). {ECO:0000250}. | Bungarus fasciatus (Banded krait) (Pseudoboa fasciata) |
P14412 | KATG_GEOSE | MENQNRQNAAQCPFHGSVTNQSSNRTTNKDWWPNQLNLSILHQHDRKTNPHDEEFNYAEEFQKLDYWALKEDLRKLMTESQDWWPADYGHYGPLFIRMAWHSAGTYRIGDGRGGASTGTQRFAPLNSWPDNANLDKARRLLWPIKKKYGNKISWADLFILAGNVAIESMGGKTIGFGGGRVDVWHPEEDVYWGSEKEWLASERYSGDRELENPLAAVQMGLIYVNPEGPDGKPDPKAAARDIRETFRRMGMNDEETVALIAGGHTFGKAHGAGPATHVGPEPEAAPIEAQGLGWISSYGKGKGSDTITSGIEGAWTPTPT... | 1.11.1.21 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.; | cellular response to hydrogen peroxide [GO:0070301]; hydrogen peroxide catabolic process [GO:0042744] | cytosol [GO:0005829] | catalase activity [GO:0004096]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00141; | 1.10.520.10;1.10.420.10; | Peroxidase family, Peroxidase/catalase subfamily | PTM: Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme. {ECO:0000255|HAMAP-Rule:MF_01961}. | null | CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01961}; CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=90 mM for H(2)O(2) for the catalase reaction (at pH 5.5-6.0) {ECO:0000269|PubMed:18178143}; KM=3.7 mM for H(2)O(2) for the catalase reaction (at pH 7.0) {ECO:0000269|PubMed:18178143}; KM=210 mM for H(2)O(2) for the peroxidase reaction {ECO:0000269|PubMed:18178143};... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0 for the peroxidase reaction. {ECO:0000269|PubMed:18178143}; | null | FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Also displays NADH oxidase, INH lyase and isonicotinoyl-NAD synthase activities. | Geobacillus stearothermophilus (Bacillus stearothermophilus) |
P14415 | AT1B2_HUMAN | MVIQKEKKSCGQVVEEWKEFVWNPRTHQFMGRTGTSWAFILLFYLVFYGFLTAMFTLTMWVMLQTVSDHTPKYQDRLATPGLMIRPKTENLDVIVNVSDTESWDQHVQKLNKFLEPYNDSIQAQKNDVCRPGRYYEQPDNGVLNYPKRACQFNRTQLGNCSGIGDSTHYGYSTGQPCVFIKMNRVINFYAGANQSMNVTCAGKRDEDAENLGNFVMFPANGNIDLMYFPYYGKKFHVNYTQPLVAVKFLNVTPNVEVNVECRINAANIATDDERDKFAGRVAFKLRINKT | null | null | cell communication by electrical coupling involved in cardiac conduction [GO:0086064]; cell-substrate adhesion [GO:0031589]; intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; lateral ventricle development [GO:0021670]; membrane repolarization [GO:0086009]; motor be... | apical plasma membrane [GO:0016324]; astrocyte end-foot [GO:0097450]; astrocyte projection [GO:0097449]; cell body membrane [GO:0044298]; cell periphery [GO:0071944]; cell projection membrane [GO:0031253]; cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; lateral plasma membrane [GO:0016328]; membr... | ATPase activator activity [GO:0001671]; ATPase binding [GO:0051117]; protein heterodimerization activity [GO:0046982]; protein-macromolecule adaptor activity [GO:0030674] | PF00287; | 1.20.5.170;2.60.40.1660; | X(+)/potassium ATPases subunit beta family | null | SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. | null | null | null | null | null | FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-2 subunit is not known.; FUNCTION: Mediates cell adhesion of neurons and astrocytes, and promotes neurite ... | Homo sapiens (Human) |
P14416 | DRD2_HUMAN | MDPLNLSWYDDDLERQNWSRPFNGSDGKADRPHYNYYATLLTLLIAVIVFGNVLVCMAVSREKALQTTTNYLIVSLAVADLLVATLVMPWVVYLEVVGEWKFSRIHCDIFVTLDVMMCTASILNLCAISIDRYTAVAMPMLYNTRYSSKRRVTVMISIVWVLSFTISCPLLFGLNNADQNECIIANPAFVVYSSIVSFYVPFIVTLLVYIKIYIVLRRRRKRVNTKRSSRAFRAHLRAPLKGNCTHPEDMKLCTVIMKSNGSFPVNRRRVEAARRAQELEMEMLSSTSPPERTRYSPIPPSHHQLTLPDPSHHGLHSTPD... | null | null | acid secretion [GO:0046717]; adenohypophysis development [GO:0021984]; adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adenylate cyclase-inhibiting dopamine receptor signaling pathway [GO:0007195]; adult walking behavior [GO:0007628]; arachidonic acid secretion [GO:0050482]; associative... | acrosomal vesicle [GO:0001669]; axon [GO:0030424]; axon terminus [GO:0043679]; ciliary membrane [GO:0060170]; cilium [GO:0005929]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; dopaminergic synapse [GO:0098691]; endocytic vesicle [GO:0030139]; G protein-coupled receptor complex [GO:0097648]; GABA-ergic synapse [... | dopamine binding [GO:0035240]; dopamine neurotransmitter receptor activity, coupled via Gi/Go [GO:0001591]; G protein-coupled receptor activity [GO:0004930]; G-protein alpha-subunit binding [GO:0001965]; heterocyclic compound binding [GO:1901363]; heterotrimeric G-protein binding [GO:0032795]; identical protein binding... | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | PTM: Palmitoylated. Palmitoylation which is required for proper localization to the plasma membrane and stability of the receptor could be carried on by ZDHHC4, ZDHHC3 and ZDHHC8. {ECO:0000269|PubMed:26535572}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21645528, ECO:0000269|PubMed:26535572}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:26535572}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase (PubMed:21645528). Positively regulates postnatal regression of retinal hyaloid vessels via suppression of VEGFR2/KDR activity, downstream of OPN5 (By similarity). {ECO:0000250|UniProtKB:P61168, ECO:0000269|PubMed:216455... | Homo sapiens (Human) |
P14418 | PA2A_GLOHA | SLIQFETLIMKVAKKSGMFWYSNYGCYCGWGGQGRPQDATDRCCFVHDCCYGKVTGCDPKMDVYSFSEENGDIVCGGDDPCKKEICECDRAAAICFRDNLTLYNDKKYWAFGAKNCPQEESEPC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305|PubMed:8636969, ECO:0000305|PubMed:9663694}; Note=Binds 1 Ca(2+) ion. {ECO:0000305|PubMed:8636969, ECO:0000305|PubMed:9663694}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3617077}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that acts in vivo as an anti-thrombotic agent. Inhibits platelet aggregation induced by ADP, arachidonic acid, and thrombin. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:18456297}. | Gloydius halys (Chinese water mocassin) (Agkistrodon halys) |
P14419 | PA21B_SHEEP | ALWQFNGMIKCKIPSSEPLLDFNNYGCYCGLGGSGTPVDDLDRCCQTHDNCYKQAKKLDSCKVLVDNPYTNSYSYSCSNKQITCSSENNACEAFICNCDRNAAICFSEVPYNNEHKNLDKKYC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P00593}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00593}; | arachidonic acid secretion [GO:0050482]; fatty acid biosynthetic process [GO:0006633]; lipid catabolic process [GO:0016042]; phosphatidylglycerol metabolic process [GO:0046471]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of podocyte apoptotic process [GO:1904635] | extracellular region [GO:0005576] | bile acid binding [GO:0032052]; calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102] | PF00068; | 1.20.90.10; | Phospholipase A2 family | PTM: Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically. {ECO:0000250|UniProtKB:P04054}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04054}. Note=Secreted from pancreatic acinar cells in its inactive form. {ECO:0000250|UniProtKB:P04054}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:P04054, ECO:0000250|U... | null | null | null | null | FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols ov... | Ovis aries (Sheep) |
P14420 | PA2B_VIPAE | NLFQFAKMINGKLGAFSVWNYISYGCYCGWGGQGTPKDATDRCCFVHDCCYGRVRGCNPKLAIYSYSFKKGNIVCGKNNGCLRDICECDRVAANCFHQNKNTYNKNYKFLSSSRCRQTSEQC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P14418}; Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P14418}; | arachidonic acid secretion [GO:0050482]; killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Heterodimer: postsynaptic neurotoxin.; FUNCTION: Monomer: snake venom phospholipase A2 (PLA2) that shows hemolytic activity and inhibition of platelet aggregation. The hemolytic activity occurs only in presence of fatty acids (unsaturated fatty acids facilitate induce a strong hemolytic activity, whereas satu... | Vipera ammodytes meridionalis (Eastern sand viper) |
P14421 | PA2N_GLOHA | NLLQFNKMIKEETGKNAIPFYAFYGCYCGGGGQGKPKDGTDRCCFVHDCCYGRLVNCNTKSDIYSYSLKEGYITCGKGTNCEEQICECDRVAAECFRRNLDTYNNGYMFYRDSKCTETSEEC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305|PubMed:10666574}; Note=Binds 1 Ca(2+) ion. {ECO:0000305|PubMed:10666574}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:15032748}. | Gloydius halys (Chinese water mocassin) (Agkistrodon halys) |
P14422 | PA2GA_RABIT | HLLDFRKMIRYTTGKEATTSYGAYGCHCGVGGRGAPKXAKFLSYKFSMKKAAAACFKYQFYPNNRCXG | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:2668261}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P14555}; | arachidonic acid secretion [GO:0050482]; defense response to Gram-positive bacterium [GO:0050830]; inflammatory response [GO:0006954]; intestinal stem cell homeostasis [GO:0036335]; killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042]; phosphatidylcholine metabolic process [GO:0046470... | extracellular region [GO:0005576]; mitochondrial outer membrane [GO:0005741]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498] | PF00068; | 1.20.90.10; | Phospholipase A2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2668261}. Cell membrane {ECO:0000250|UniProtKB:P14555}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14555}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P14555}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14555}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+); Xref=Rhea:RHEA:44604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; Evidence={ECO:0000269|PubMed:2668261}; PhysiologicalDir... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:2668261}; | null | FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids with implications in host antimicrobial defense, inflammatory response and tissue regeneration (By similarity). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phosphol... | Oryctolagus cuniculus (Rabbit) |
P14423 | PA2GA_RAT | MKVLLLLAVVIMAFGSIQVQGSLLEFGQMILFKTGKRADVSYGFYGCHCGVGGRGSPKDATDWCCVTHDCCYNRLEKRGCGTKFLTYKFSYRGGQISCSTNQDSCRKQLCQCDKAAAECFARNKKSYSLKYQFYPNKFCKGKTPSC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:3356705}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P14555}; | arachidonic acid secretion [GO:0050482]; cell population proliferation [GO:0008283]; defense response to Gram-positive bacterium [GO:0050830]; inflammatory response [GO:0006954]; intestinal stem cell homeostasis [GO:0036335]; killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042]; negat... | endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; mitochondrial outer membrane [GO:0005741]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; secretory granule [GO:0030141] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipase A2 activity [GO:0004623]; phospholipid binding [GO:0005543] | PF00068; | 1.20.90.10; | Phospholipase A2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2722857}. Cell membrane {ECO:0000269|PubMed:2722857}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14555}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P14555}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14555}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+); Xref=Rhea:RHEA:44604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; Evidence={ECO:0000269|PubMed:3356705}; PhysiologicalDir... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-9.5. {ECO:0000269|PubMed:3356705}; | null | FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids with implications in host antimicrobial defense, inflammatory response and tissue regeneration (By similarity). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phosphol... | Rattus norvegicus (Rat) |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.