ERK1_DICDI
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 03-AUG-2022, entry version 152.
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 (Slime mold).
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};
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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.DDB0201635; -.
DR PaxDb; P42525; -.
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; YTDLNPV; -.
DR PhylomeDB; P42525; -.
DR BRENDA; 2.7.11.24; 1939.
DR Reactome; R-DDI-193648; NRAGE signals death through JNK.
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-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DDI-2871796; FCERI mediated MAPK activation.
DR Reactome; R-DDI-4086398; Ca2+ pathway.
DR Reactome; R-DDI-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-DDI-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-DDI-9007892; Interleukin-38 signaling.
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: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:0110094; P:polyphosphate-mediated signaling; IMP:dictyBase.
DR GO; GO:1903669; P:positive regulation of chemorepellent activity; IMP:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 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 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.
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
