ID ERK1_DICDI Reviewed; 529 AA. AC P42525; Q54LX6; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 2. DT 27-MAR-2024, entry version 160. DE RecName: Full=Extracellular signal-regulated kinase 1; DE Short=ERK1; DE EC=2.7.11.24; DE AltName: Full=MAP kinase 1; GN Name=erkA; Synonyms=erk1; ORFNames=DDB_G0286353; OS Dictyostelium discoideum (Social amoeba). OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; OC Dictyosteliaceae; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 96-529, AND FUNCTION. RC STRAIN=AX3; RX PubMed=7935416; DOI=10.1128/mcb.14.10.6996-7012.1994; RA Gaskins C.J., Maeda M., Firtel R.A.; RT "Identification and functional analysis of a developmentally regulated RT extracellular signal-regulated kinase gene in Dictyostelium discoideum."; RL Mol. Cell. Biol. 14:6996-7012(1994). CC -!- FUNCTION: Kinase involved in a signal transduction pathway. CC {ECO:0000269|PubMed:7935416}. 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 -!- 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; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- ACTIVITY REGULATION: Activated by tyrosine and threonine CC phosphorylation. {ECO:0000250}. CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues CC whose phosphorylation activates the MAP kinases. {ECO:0000250}. CC -!- PTM: Dually phosphorylated on Thr-309 and Tyr-311, 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 -!- SEQUENCE CAUTION: CC Sequence=AAA59387.1; Type=Erroneous initiation; Evidence={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; AAFI02000085; EAL64201.1; -; Genomic_DNA. DR EMBL; U11077; AAA59387.1; ALT_INIT; mRNA. DR PIR; A56042; A56042. DR RefSeq; XP_637704.1; XM_632612.1. DR AlphaFoldDB; P42525; -. DR SMR; P42525; -. DR BioGRID; 1250572; 1. DR STRING; 44689.P42525; -. DR PaxDb; 44689-DDB0201635; -. DR EnsemblProtists; EAL64201; EAL64201; DDB_G0286353. DR GeneID; 8625569; -. DR KEGG; ddi:DDB_G0286353; -. DR dictyBase; DDB_G0286353; erkA. DR eggNOG; KOG0660; Eukaryota. DR HOGENOM; CLU_000288_181_1_1; -. DR InParanoid; P42525; -. DR OMA; NRYTDLN; -. DR PhylomeDB; P42525; -. DR BRENDA; 2.7.11.24; 1939. DR Reactome; R-DDI-110056; MAPK3 (ERK1) activation. DR Reactome; R-DDI-111995; phospho-PLA2 pathway. DR Reactome; R-DDI-112409; RAF-independent MAPK1/3 activation. DR Reactome; R-DDI-112411; MAPK1 (ERK2) activation. DR Reactome; R-DDI-1169408; ISG15 antiviral mechanism. DR Reactome; R-DDI-170968; Frs2-mediated activation. DR Reactome; R-DDI-198753; ERK/MAPK targets. DR Reactome; R-DDI-198765; Signalling to ERK5. DR Reactome; R-DDI-202670; ERKs are inactivated. DR Reactome; R-DDI-2029482; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; R-DDI-3371453; Regulation of HSF1-mediated heat shock response. DR Reactome; R-DDI-437239; Recycling pathway of L1. DR Reactome; R-DDI-445144; Signal transduction by L1. DR Reactome; R-DDI-5663213; RHO GTPases Activate WASPs and WAVEs. DR Reactome; R-DDI-5673001; RAF/MAP kinase cascade. DR Reactome; R-DDI-5674135; MAP2K and MAPK activation. DR Reactome; R-DDI-5674499; Negative feedback regulation of MAPK pathway. DR Reactome; R-DDI-5675221; Negative regulation of MAPK pathway. DR Reactome; R-DDI-5687128; MAPK6/MAPK4 signaling. DR Reactome; R-DDI-6798695; Neutrophil degranulation. DR Reactome; R-DDI-9634635; Estrogen-stimulated signaling through PRKCZ. DR PRO; PR:P42525; -. DR Proteomes; UP000002195; Chromosome 4. DR GO; GO:0005938; C:cell cortex; IDA:dictyBase. DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:dictyBase. DR GO; GO:0005634; C:nucleus; IDA:dictyBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004707; F:MAP kinase activity; IDA:dictyBase. 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:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase. DR GO; GO:0019954; P:asexual reproduction; IMP:dictyBase. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase. DR GO; GO:0042742; P:defense response to bacterium; IDA:dictyBase. DR GO; GO:0140986; P:G protein-coupled chemorepellent receptor signaling pathway; IMP:dictyBase. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IGI:dictyBase. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0000165; P:MAPK cascade; IMP:dictyBase. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0110094; P:polyphosphate-mediated signaling; IMP:dictyBase. DR GO; GO:0031157; P:regulation of aggregate size involved in sorocarp development; IMP:dictyBase. DR GO; GO:0031153; P:slug development involved in sorocarp development; IMP:dictyBase. DR GO; GO:0030587; P:sorocarp development; HMP:dictyBase. DR CDD; cd07858; STKc_TEY_MAPK; 1. 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 InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1. DR PANTHER; PTHR24055:SF588; MITOGEN-ACTIVATED PROTEIN KINASE 7; 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. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 2: Evidence at transcript level; KW ATP-binding; Cell cycle; Cell division; Kinase; Mitosis; KW Nucleotide-binding; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..529 FT /note="Extracellular signal-regulated kinase 1" FT /id="PRO_0000186308" FT DOMAIN 149..439 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 100..131 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 309..311 FT /note="TXY" FT ACT_SITE 275 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 155..163 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 178 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 309 FT /note="Phosphothreonine" FT /evidence="ECO:0000250" FT MOD_RES 311 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250" FT CONFLICT 389 FT /note="R -> RSL (in Ref. 1; AAA59387)" FT /evidence="ECO:0000305" FT CONFLICT 517 FT /note="Q -> P (in Ref. 1; AAA59387)" FT /evidence="ECO:0000305" FT CONFLICT 529 FT /note="N -> INN (in Ref. 1; AAA59387)" FT /evidence="ECO:0000305" SQ SEQUENCE 529 AA; 61303 MW; 495C8ACD0215A3A7 CRC64; MEPEFDHFQS QMDSDNTHQS TMFNVQDNNA ILMSGMENVL QSPRQLQAAA QAQQQAAAQA QQQQVQAQQV QAQQAQQQQQ QQQNQQQQQQ QQNQQNQQQQ QNQQQQSQQM TQQQLQQLMP PPPTSDTSNF NDNISYFVYG SQFTVPRRYS IVKCIGHGAY GVVCSAKDNL TGEKVAIKKI SKAFDNLKDT KRTLREIHLL RHFKHENLIS IKDILKPNSK EQFEDVYIVS ELMDTDLHQI ITSPQPLSDD HCQYFVYQML RGLKHIHSAN VLHRDLKPSN LLINEDCLLK ICDLGLARVE DATHQGFMTE YVATRWYRAP EVILSWNKYT KAIDIWSVGC IFAELLGRKP LFQGKDYIHQ ITLIIETIGS PSEEDICNIA NEQARQFIRN MGNQPKVNFA NMFPKANPDA IDLLERMLYF DPSKRLTVEE ALAHPYFQSL HDPSDEPICL HKFSLNFEAW DLNRDLLKEL IYNEMLAYHP EDPQAPYYTD LNNPNFNLSR IQSSSELFNL LQQQKQQIHQ QVNQQSIKN //