ERK1_CANAL
ID ERK1_CANAL Reviewed; 421 AA.
AC Q5A1D3; A0A1D8PMK1; O13435; P28869; P87079; P87080; P87081; P87082; P87083;
AC P87084; P87085; P87086; P87322; Q6LC13;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 3.
DT 03-AUG-2022, entry version 135.
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; OrderedLocusNames=CAALFM_C406480CA;
GN ORFNames=CaO19.10404, CaO19.2886;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
RC STRAIN=ATCC 36232, ATCC 60193 / S-24, R-2436, R-2535, R-2540, R-2607,
RC R-2617, R-2621, R-2624, R-2777, and R-2805;
RX PubMed=9544777; DOI=10.1111/j.1574-695x.1998.tb01116.x;
RA Metzgar D., Field D., Haubrich R., Wills C.;
RT "Sequence analysis of a compound coding-region microsatellite in Candida
RT albicans resolves homoplasies and provides a high-resolution tool for
RT genotyping.";
RL FEMS Immunol. Med. Microbiol. 20:103-109(1998).
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 -!- INTERACTION:
CC Q5A1D3; P32917: STE5; Xeno; NbExp=2; IntAct=EBI-8783371, EBI-18373;
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-230 and Tyr-232, 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; CP017626; AOW29372.1; -; Genomic_DNA.
DR EMBL; U95784; AAB88588.1; -; Genomic_DNA.
DR EMBL; U95785; AAB88589.1; -; Genomic_DNA.
DR EMBL; U95786; AAB88590.1; -; Genomic_DNA.
DR EMBL; U95787; AAB88591.1; -; Genomic_DNA.
DR EMBL; U95788; AAB88592.1; -; Genomic_DNA.
DR EMBL; U95789; AAB88593.1; -; Genomic_DNA.
DR EMBL; U95790; AAB88594.1; -; Genomic_DNA.
DR EMBL; U95791; AAB88595.1; -; Genomic_DNA.
DR EMBL; U95792; AAB88596.1; -; Genomic_DNA.
DR EMBL; U95793; AAB88597.1; -; Genomic_DNA.
DR EMBL; U95794; AAB88598.1; -; Genomic_DNA.
DR EMBL; U95795; AAB88599.1; -; Genomic_DNA.
DR EMBL; U95796; AAB88600.1; -; Genomic_DNA.
DR EMBL; U95797; AAB88601.1; -; Genomic_DNA.
DR EMBL; U95798; AAB88602.1; -; Genomic_DNA.
DR RefSeq; XP_715542.2; XM_710449.2.
DR AlphaFoldDB; Q5A1D3; -.
DR SMR; Q5A1D3; -.
DR BioGRID; 1225837; 9.
DR IntAct; Q5A1D3; 2.
DR STRING; 237561.Q5A1D3; -.
DR GeneID; 3642789; -.
DR KEGG; cal:CAALFM_C406480CA; -.
DR CGD; CAL0000176774; CEK1.
DR VEuPathDB; FungiDB:C4_06480C_A; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q5A1D3; -.
DR OMA; PYVAAYH; -.
DR OrthoDB; 741207at2759; -.
DR PHI-base; PHI:107; -.
DR PHI-base; PHI:6837; -.
DR PHI-base; PHI:7663; -.
DR PRO; PR:Q5A1D3; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IMP:CGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:1990277; P:parasexual reproduction with cellular fusion; IMP:CGD.
DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IBA:GO_Central.
DR GO; GO:1900445; P:positive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
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 1: Evidence at protein 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..421
FT /note="Extracellular signal-regulated kinase 1"
FT /id="PRO_0000186325"
FT DOMAIN 70..375
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 230..232
FT /note="TXY"
FT ACT_SITE 194
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 76..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 230
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 232
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT VARIANT 32..35
FT /note="Missing (in strain: ATCC 60193 / S-24; in allele 237
FT B)"
FT VARIANT 33
FT /note="Q -> QA (in strain: R-2617; in allele 249 D)"
FT VARIANT 34..35
FT /note="QQ -> AQAQA (in strain: R-2805; in allele 255 A)"
FT VARIANT 34
FT /note="Q -> A (in strain: R-2617, R-2624, R-2777 and R-
FT 2805; in allele 246 D, 249 E, 249 C and 246 E)"
FT VARIANT 38..43
FT /note="Missing (in strain: ATCC 36232; in allele 225 A)"
FT VARIANT 38..41
FT /note="Missing (in strain: R-2621; in allele 237 A)"
FT VARIANT 41
FT /note="Q -> QQ (in strain: R-2621; in allele 249 B)"
FT VARIANT 41
FT /note="Missing (in strain: R-2540; in allele 243 A)"
FT VARIANT 52
FT /note="A -> T (in strain: R-2617; in allele 246 D)"
SQ SEQUENCE 421 AA; 48536 MW; EC070EC9E6501B52 CRC64;
MNIDQHHQLQ QQHQQQMLQQ QAQAQAQAQA QAQQQQQQQQ QAAAAAAAAN AAATTSSSPR
QVSFNVSDHY QILEIVGEGA YGIVCSAIHK PSQQKVAIKK IEPFERSMLC LRTLRELKLL
KHFNHENIIS ILAIQRPINY ESFNEIYLIQ ELMETDLHRV IRTQNLSDDH IQYFIYQTLR
ALKAMHSANV LHRDLKPSNL LLNSNCDLKI CDFGLARSIA SQEDNYGFMT EYVATRWYRA
PEIMLTFQEY TTAIDVWSVG CILAEMLSGR PLFPGRDYHN QLWLIMEVLG TPNMEDYYNI
KSKRAREYIR SLPFCKKIPF SELFANTNNN TSTSTSNTGG RTNINPLALD LLEKLLIFNP
AKRITVEDAL KHPYLQLYHD PNDEPISDKI PEDFFDFDKM KDQLTIEDLK KLLYEEIMKP
L
