IKS1_YEAST
ID IKS1_YEAST Reviewed; 667 AA.
AC P47042; D6VWC5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Probable serine/threonine-protein kinase IKS1;
DE EC=2.7.11.1;
DE AltName: Full=IRA1 kinase suppressor 1;
GN Name=IKS1; OrderedLocusNames=YJL057C; ORFNames=J1143;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=10407277;
RX DOI=10.1002/(sici)1097-0061(199907)15:10b<973::aid-yea402>3.0.co;2-l;
RA Rieger K.-J., El-Alama M., Stein G., Bradshaw C., Slonimski P.P.,
RA Maundrell K.;
RT "Chemotyping of yeast mutants using robotics.";
RL Yeast 15:973-986(1999).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(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=2.7.11.1;
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=2.7.11.1;
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to copper sulfate.
CC {ECO:0000269|PubMed:10407277}.
CC -!- MISCELLANEOUS: Present with 892 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; Z49332; CAA89348.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08741.1; -; Genomic_DNA.
DR PIR; S56829; S56829.
DR RefSeq; NP_012478.3; NM_001181490.3.
DR AlphaFoldDB; P47042; -.
DR SMR; P47042; -.
DR BioGRID; 33697; 152.
DR DIP; DIP-1521N; -.
DR IntAct; P47042; 10.
DR MINT; P47042; -.
DR STRING; 4932.YJL057C; -.
DR iPTMnet; P47042; -.
DR MaxQB; P47042; -.
DR PaxDb; P47042; -.
DR PRIDE; P47042; -.
DR EnsemblFungi; YJL057C_mRNA; YJL057C; YJL057C.
DR GeneID; 853389; -.
DR KEGG; sce:YJL057C; -.
DR SGD; S000003593; IKS1.
DR VEuPathDB; FungiDB:YJL057C; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_010228_2_1_1; -.
DR InParanoid; P47042; -.
DR OMA; PELWLYS; -.
DR BioCyc; YEAST:G3O-31520-MON; -.
DR Reactome; R-SCE-381042; PERK regulates gene expression.
DR PRO; PR:P47042; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47042; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006468; P:protein phosphorylation; HDA:SGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..667
FT /note="Probable serine/threonine-protein kinase IKS1"
FT /id="PRO_0000086138"
FT DOMAIN 173..530
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 179..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 667 AA; 75327 MW; 11C129782900C8B2 CRC64;
MSLVPYEEGS LILDDPNSKS VVVVNPTSGT LSFFQQDNSN NDSELNEDQT ASLSALDFPS
GIHQYKSPIA SYVCPQCGTE INPDIINRRQ LHRRASAGVE SESSRLSIPE NTVPLGFEFA
NSSFSRRYFQ SLERNHRHYA LQNDSNNKQG QFSKNKYFIP DDLFIPGYFR KFFKILSLLG
NGARGSVYKV VHTIGNTELG VFALKKIPIG NDMEWFNKCI REVKALSSLT HKSANLITYN
HVWLEMDSSV GFVRSIDGSQ SDSQEEVPCI FILQQYCSGG NLEDCILRKV FNRFSDTESP
EERKKKFRTR KKNHGKSGEV GLSTEQLVSI IRDIARGLHE LHSIGLIHRD LKPSNCLLLT
PFKSDNENDN VYDREHNSDE FFPSIVIGDL GESQLEGESR LGTGCTGTLE FTAPDLIIQG
RPVSSSTLPS RSSHTYNEYT FASDMYSLGM ICYFIVFGEL PFEPQLDIVD LKVRIKNFRF
DTEGMIEKHQ AMKLKPIDRR IFHLMDALLQ PNNDARPTAK TVEETLDEML INSKPGKKFW
KENVDSTLNF STISEVNENT NSFTDDYIDG DNVTLSLPAP EENLSTVSTQ NLQKYSALNR
TIQVCYKLVS MILTIIIFKC TKTGSWLSYM SLILLGMVFK SPADERGKHA RALVLLAFIA
ACKKYIY
