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 27-MAR-2024, entry version 172. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.1; -. DR PaxDb; 6239-F42G8-3a; -. 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 AGR; WB:WBGene00004056; -. 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; 158564at2759; -. 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-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 PRO; PR:Q8MXI4; -. DR Proteomes; UP000001940; Chromosome IV. DR Bgee; WBGene00004056; Expressed in embryo and 3 other cell types or 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0006970; P:response to osmotic stress; IDA:UniProtKB. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1. DR PANTHER; PTHR24055:SF158; MITOGEN-ACTIVATED PROTEIN KINASE P38A-RELATED; 1. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR01773; P38MAPKINASE. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 //