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PMK2_CAEEL
ID   PMK2_CAEEL              Reviewed;         419 AA.
AC   Q8MXI4; Q8MXI3;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 165.
DE   RecName: Full=Mitogen-activated protein kinase pmk-2;
DE            EC=2.7.11.24;
DE   AltName: Full=Stress-activated protein kinase pmk-2;
DE   AltName: Full=p38 MAP kinase 2;
GN   Name=pmk-2; ORFNames=F42G8.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), FUNCTION, SUBCELLULAR
RP   LOCATION, AND ACTIVITY REGULATION.
RC   STRAIN=Bristol N2;
RX   PubMed=11703092; DOI=10.1006/mcbr.2001.0300;
RA   Berman K., McKay J., Avery L., Cobb M.;
RT   "Isolation and characterization of pmk-(1-3): three p38 homologs in
RT   Caenorhabditis elegans.";
RL   Mol. Cell Biol. Res. Commun. 4:337-344(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Responds to activation by environmental stress and pro-
CC       inflammatory cytokines by phosphorylating downstream targets.
CC       {ECO:0000269|PubMed:11703092}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24;
CC         Evidence={ECO:0000269|PubMed:11703092};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.24; Evidence={ECO:0000269|PubMed:11703092};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:11703092};
CC   -!- ACTIVITY REGULATION: Activated by phosphorylation on threonine and
CC       tyrosine. Inhibited by pyridinyl-imidazole related compounds.
CC       {ECO:0000269|PubMed:11703092}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11703092}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a {ECO:0000305};
CC         IsoId=Q8MXI4-1; Sequence=Displayed;
CC       Name=b {ECO:0000305};
CC         IsoId=Q8MXI4-2; Sequence=VSP_009272, VSP_050273;
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Dually phosphorylated on Thr-222 and Tyr-224, which activates the
CC       enzyme. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR   EMBL; FO080126; CCD61402.1; -; Genomic_DNA.
DR   EMBL; FO080126; CCD61403.1; -; Genomic_DNA.
DR   RefSeq; NP_741457.2; NM_171392.5.
DR   RefSeq; NP_741458.2; NM_171913.4. [Q8MXI4-2]
DR   AlphaFoldDB; Q8MXI4; -.
DR   SMR; Q8MXI4; -.
DR   BioGRID; 42724; 3.
DR   DIP; DIP-24927N; -.
DR   IntAct; Q8MXI4; 1.
DR   STRING; 6239.F42G8.3a; -.
DR   PaxDb; Q8MXI4; -.
DR   PeptideAtlas; Q8MXI4; -.
DR   EnsemblMetazoa; F42G8.3a.1; F42G8.3a.1; WBGene00004056.
DR   EnsemblMetazoa; F42G8.3b.1; F42G8.3b.1; WBGene00004056. [Q8MXI4-2]
DR   GeneID; 177611; -.
DR   KEGG; cel:CELE_F42G8.3; -.
DR   UCSC; F42G8.3a; c. elegans. [Q8MXI4-1]
DR   CTD; 177611; -.
DR   WormBase; F42G8.3a; CE49565; WBGene00004056; pmk-2.
DR   WormBase; F42G8.3b; CE34862; WBGene00004056; pmk-2. [Q8MXI4-2]
DR   eggNOG; KOG0660; Eukaryota.
DR   HOGENOM; CLU_000288_181_1_1; -.
DR   InParanoid; Q8MXI4; -.
DR   OrthoDB; 683132at2759; -.
DR   PhylomeDB; Q8MXI4; -.
DR   BRENDA; 2.7.11.24; 1045.
DR   Reactome; R-CEL-168638; NOD1/2 Signaling Pathway.
DR   Reactome; R-CEL-171007; p38MAPK events.
DR   Reactome; R-CEL-198753; ERK/MAPK targets.
DR   Reactome; R-CEL-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-CEL-376172; DSCAM interactions.
DR   Reactome; R-CEL-418592; ADP signalling through P2Y purinoceptor 1.
DR   Reactome; R-CEL-432142; Platelet sensitization by LDL.
DR   Reactome; R-CEL-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-CEL-450302; activated TAK1 mediates p38 MAPK activation.
DR   Reactome; R-CEL-450341; Activation of the AP-1 family of transcription factors.
DR   Reactome; R-CEL-525793; Myogenesis.
DR   Reactome; R-CEL-5675221; Negative regulation of MAPK pathway.
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   PRO; PR:Q8MXI4; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00004056; Expressed in embryo and 3 other tissues.
DR   ExpressionAtlas; Q8MXI4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; IDA:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0006970; P:response to osmotic stress; IDA:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR008352; MAPK_p38-like.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01773; P38MAPKINASE.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS01351; MAPK; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..419
FT                   /note="Mitogen-activated protein kinase pmk-2"
FT                   /id="PRO_0000186304"
FT   DOMAIN          49..350
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOTIF           222..224
FT                   /note="TXY"
FT   ACT_SITE        210
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         55..63
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         222
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         224
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         190..206
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_009272"
FT   VAR_SEQ         366..370
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_050273"
SQ   SEQUENCE   419 AA;  48026 MW;  621C52BFAB7EF37B CRC64;
     MGMSATMGDS ASIPGVFFAD FGPAPPEITP EGYHEVELNK TKWVLPQWYN SLKPLGEGAY
     GVVCTAEYEP TGDRVAIKKF FRPFQSTIHA KRTYRELKLL RTLQHDNVLE MIDVFTPDPD
     ASSLNNVYFV SVLMGSDLQN IMKIQRLTDE QIQLLIYQVL RGLKYIHSAG IIHRDLKPSN
     IAVNERCEVK VFLSFSQLSF LILSFFKILD FGLARAQDAE MTGYVATRWY RAPEIMLNWM
     HYTQTVDVWS VGCILAELVS GRPLFPGDDH IDQLTKIMSV VGTPKEEFWS KIQSEEARNY
     IKNRSPIIRQ DFVTLFPMAS PYALELLEMM LILDPDRRIS VSSALRHDYL REYSVPNDEP
     VAMDTVINSI VTIDPAEERA TTLSDWRELI WNEIRLFQNS ARRLSFVSCT DTEEEPMKI
 
 
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