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Database: UniProt/SWISS-PROT
Entry: ERK1_CANAL
LinkDB: ERK1_CANAL
Original site: ERK1_CANAL 
ID   ERK1_CANAL              Reviewed;         421 AA.
AC   Q5A1D3; A0A1D8PMK1; O13435; P28869; P87079; P87080; P87081; P87082;
AC   P87083; P87084; P87085; P87086; P87322; Q6LC13;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 3.
DT   05-DEC-2018, entry version 115.
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;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   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.,
RA   Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
RA   Davis R.W., 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
RT   aligned on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
RP   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
RT   allele-specific measurements and provides a simple model for repeat
RT   and indel 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
RT   Candida albicans resolves homoplasies and provides a high-resolution
RT   tool for 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,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         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       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
CC       the enzyme. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. MAP kinase subfamily.
CC       {ECO:0000305}.
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   SMR; Q5A1D3; -.
DR   BioGrid; 1225837; 6.
DR   IntAct; Q5A1D3; 2.
DR   PRIDE; Q5A1D3; -.
DR   GeneID; 3642789; -.
DR   KEGG; cal:CAALFM_C406480CA; -.
DR   CGD; CAL0000176774; CEK1.
DR   InParanoid; Q5A1D3; -.
DR   KO; K04371; -.
DR   OMA; WELPRRY; -.
DR   OrthoDB; EOG092C2FL8; -.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0035690; P:cellular response to drug; IMP:CGD.
DR   GO; GO:0071310; P:cellular response to organic substance; IBA:GO_Central.
DR   GO; GO:0071470; P:cellular response to osmotic stress; IBA:GO_Central.
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 conjugation with cellular fusion; IMP:CGD.
DR   GO; GO:0009405; P:pathogenesis; 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:0010468; P:regulation of gene expression; IBA:GO_Central.
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; Complete proteome; Kinase;
KW   Mitosis; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    421       Extracellular signal-regulated kinase 1.
FT                                /FTId=PRO_0000186325.
FT   DOMAIN       70    375       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND      76     84       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOTIF       230    232       TXY.
FT   COMPBIAS      5     53       Ala/Gln-rich.
FT   ACT_SITE    194    194       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING      99     99       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     230    230       Phosphothreonine. {ECO:0000250}.
FT   MOD_RES     232    232       Phosphotyrosine. {ECO:0000250}.
FT   VARIANT      32     35       Missing (in strain: ATCC 60193 / S-24; in
FT                                allele 237 B).
FT   VARIANT      33     33       Q -> QA (in strain: R-2617; in allele 249
FT                                D).
FT   VARIANT      34     35       QQ -> AQAQA (in strain: R-2805; in allele
FT                                255 A).
FT   VARIANT      34     34       Q -> A (in strain: R-2617, R-2624, R-2777
FT                                and R-2805; in allele 246 D, 249 E, 249 C
FT                                and 246 E).
FT   VARIANT      38     43       Missing (in strain: ATCC 36232; in allele
FT                                225 A).
FT   VARIANT      38     41       Missing (in strain: R-2621; in allele 237
FT                                A).
FT   VARIANT      41     41       Q -> QQ (in strain: R-2621; in allele 249
FT                                B).
FT   VARIANT      41     41       Missing (in strain: R-2540; in allele 243
FT                                A).
FT   VARIANT      52     52       A -> T (in strain: R-2617; in allele 246
FT                                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
//
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