SKS1_YEAST
ID SKS1_YEAST Reviewed; 502 AA.
AC Q12505; D6W3Y7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Serine/threonine-protein kinase SKS1;
DE EC=2.7.11.1;
DE AltName: Full=Suppressor kinase of SNF3;
GN Name=SKS1; Synonyms=SHA3; OrderedLocusNames=YPL026C; ORFNames=LPB5;
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 [GENOMIC DNA].
RX PubMed=8948096;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1407::aid-yea36>3.0.co;2-1;
RA Yang Z., Bisson L.F.;
RT "The SKS1 protein kinase is a multicopy suppressor of the snf3 mutation of
RT Saccharomyces cerevisiae.";
RL Yeast 12:1407-1419(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
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 [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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May have a role in glucose regulation.
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 -!- MISCELLANEOUS: Present with 2810 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; U30613; AAC49570.1; -; Genomic_DNA.
DR EMBL; U36624; AAB68161.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11403.1; -; Genomic_DNA.
DR PIR; S61935; S61935.
DR RefSeq; NP_015299.1; NM_001183840.1.
DR AlphaFoldDB; Q12505; -.
DR BioGRID; 36152; 141.
DR DIP; DIP-2879N; -.
DR IntAct; Q12505; 21.
DR MINT; Q12505; -.
DR STRING; 4932.YPL026C; -.
DR MaxQB; Q12505; -.
DR PaxDb; Q12505; -.
DR PRIDE; Q12505; -.
DR EnsemblFungi; YPL026C_mRNA; YPL026C; YPL026C.
DR GeneID; 856081; -.
DR KEGG; sce:YPL026C; -.
DR SGD; S000005947; SKS1.
DR VEuPathDB; FungiDB:YPL026C; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000176825; -.
DR HOGENOM; CLU_000288_172_4_1; -.
DR InParanoid; Q12505; -.
DR OMA; ICCNACR; -.
DR BioCyc; YEAST:G3O-33942-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR PRO; PR:Q12505; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12505; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:SGD.
DR GO; GO:0006468; P:protein phosphorylation; HDA:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR GO; GO:0010827; P:regulation of glucose transmembrane transport; IGI:SGD.
DR GO; GO:0009749; P:response to glucose; IGI:SGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; 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; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..502
FT /note="Serine/threonine-protein kinase SKS1"
FT /id="PRO_0000086657"
FT DOMAIN 10..338
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 376..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 16..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MUTAGEN 39
FT /note="K->R: Loss of activity."
SQ SEQUENCE 502 AA; 57844 MW; B106D084BAFA61E5 CRC64;
MLSDCLLNNF RITAQIGSGA YGLVFHVVDI LTSREYAVKT VFKSSSMDEF YNKNGLNNNS
QVARTTLLQT QLYHFFKSFQ KKLFLPSVDL DSILQLTENE LNRLPHYREI AFQLRVQSHG
NIVKIHQVLE SSIATFIVMD YYDRDLFTSI VDDKHFVNHG ILIKKVFLQL CSALDHCHRL
GIYHCDIKPE NVLLDRNDNA YLCDFGLSTK SKYLAPNVCV GSSYYMAPER ILYCLNTTTN
GIHVDECCSS LPTDTGDIWS LGIILINLTC IRNPWLKAHQ KEDNTFQHFA NDNNVLKKIL
PISDELFTVL TKILQLNPYT RIDMKTLMSE VSSLTSFTRE GPLSQVPILS SEVYMTHIIR
NENLFLSDLS HFSADQEQQQ QQQQQQQQVQ EQEQEQKQEQ IQNQEQAQQQ QEEEDAEPES
DIPSTYNSDG SMEKYEYTNN HNNSTFLTSS MDSTPYQSDI DDVSASKDCK FQQDTLRNRL
LCLQMNFSTL TDGPNEKWLP DY
