ERK1_CANAW
ID ERK1_CANAW Reviewed; 415 AA.
AC C4YGK0; P28869; P87079; P87080; P87081; P87082; P87083; P87084; P87085;
AC P87086; P87322;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Extracellular signal-regulated kinase 1;
DE Short=ERK1;
DE EC=2.7.11.24;
DE AltName: Full=MAP kinase 1;
DE Short=MAPK 1;
GN Name=CEK1; Synonyms=ERK1; ORFNames=CAWG_03179;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=1409649; DOI=10.1073/pnas.89.20.9410;
RA Whiteway M., Dignard D., Thomas D.Y.;
RT "Dominant negative selection of heterologous genes: isolation of Candida
RT albicans genes that interfere with Saccharomyces cerevisiae mating factor-
RT induced cell cycle arrest.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:9410-9414(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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.
CC -!- PTM: Dually phosphorylated on Thr-226 and Tyr-228, 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=AAA34343.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M76585; AAA34343.2; ALT_INIT; Genomic_DNA.
DR EMBL; CH672349; EEQ44882.1; -; Genomic_DNA.
DR PIR; A47211; A47211.
DR AlphaFoldDB; C4YGK0; -.
DR SMR; C4YGK0; -.
DR STRING; 5476.C4YGK0; -.
DR EnsemblFungi; EEQ44882; EEQ44882; CAWG_03179.
DR VEuPathDB; FungiDB:CAWG_03179; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR OMA; EIMTFRP; -.
DR BRENDA; 2.7.11.24; 1096.
DR Proteomes; UP000001429; Chromosome 4, Supercontig 1.4.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
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 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 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Kinase; Mitosis;
KW Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..415
FT /note="Extracellular signal-regulated kinase 1"
FT /id="PRO_0000413039"
FT DOMAIN 66..369
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 226..228
FT /note="TXY"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 72..80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 226
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 228
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT CONFLICT 53
FT /note="S -> SS (in Ref. 1; AAA34343)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 47836 MW; 572857CFD5B00B67 CRC64;
MNIDQHHQLQ QQHQQQMLQQ QAQAQAQAQA QAQQQQQAAA AAAAANAAAT TSSSPRQVSF
NVSDHYQILE IVGEGAYGIV CSAIHKPSQQ KVAIKKIEPF ERSMLCLRTL RELKLLKHFN
HENIISILAI QRPINYESFN EIYLIQELME TDLHRVIRTQ NLSDDHIQYF IYQTLRALKA
MHSANVLHRD LKPSNLLLNS NCDLKICDFG LARSIASQED NYGFMTEYVA TRWYRAPEIM
LTFQEYTTAI DVWSVGCILA EMLSGRPLFP GRDYHNQLWL IMEVLGTPNM EDYYNIKSKR
AREYIRSLPF CKKIPFSELF ANTNNNTSTS NTGGRTNINP LALDLLEKLL IFNPAKRITV
EDALKHPYLQ LYHDPNDEPI SDKIPEDFFD FDKMKDQLTI EDLKKLLYEE IMKPL
