KSP1_YEAST
ID KSP1_YEAST Reviewed; 1029 AA.
AC P38691; D3DL33;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Serine/threonine-protein kinase KSP1;
DE EC=2.7.11.1;
GN Name=KSP1; OrderedLocusNames=YHR082C;
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].
RC STRAIN=M335 /2A;
RX PubMed=8676864; DOI=10.1007/bf02174449;
RA Fleischmann M., Stagljar I., Aebi M.;
RT "Allele-specific suppression of a Saccharomyces cerevisiae prp20 mutation
RT by overexpression of a nuclear serine/threonine protein kinase.";
RL Mol. Gen. Genet. 250:614-625(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; THR-526; SER-646 AND
RP SER-845, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526; SER-529; SER-845 AND
RP SER-1014, AND IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-419; THR-501;
RP THR-504; SER-646; SER-845; SER-884; THR-1005 AND SER-1014, AND
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).
RN [9]
RP PHOSPHORYLATION BY PKA.
RX PubMed=20702584; DOI=10.1091/mbc.e10-03-0182;
RA Soulard A., Cremonesi A., Moes S., Schutz F., Jeno P., Hall M.N.;
RT "The rapamycin-sensitive phosphoproteome reveals that TOR controls protein
RT kinase A toward some but not all substrates.";
RL Mol. Biol. Cell 21:3475-3486(2010).
CC -!- FUNCTION: May act on PRP20.
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 -!- INTERACTION:
CC P38691; P38873: KOG1; NbExp=3; IntAct=EBI-9937, EBI-24864;
CC P38691; P35169: TOR1; NbExp=2; IntAct=EBI-9937, EBI-19374;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylated by PKA in a TORC1-dependent manner. Phosphorylation
CC at PKA consensus sites RRxS/T decreases upon rapamycin treatment.
CC {ECO:0000269|PubMed:20702584}.
CC -!- MISCELLANEOUS: Present with 1270 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. CK2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; X80329; CAA56578.1; -; Genomic_DNA.
DR EMBL; U10556; AAB68896.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06777.1; -; Genomic_DNA.
DR PIR; S64731; S64731.
DR RefSeq; NP_011950.1; NM_001179212.1.
DR AlphaFoldDB; P38691; -.
DR BioGRID; 36517; 495.
DR DIP; DIP-2972N; -.
DR IntAct; P38691; 62.
DR MINT; P38691; -.
DR STRING; 4932.YHR082C; -.
DR iPTMnet; P38691; -.
DR MaxQB; P38691; -.
DR PaxDb; P38691; -.
DR PRIDE; P38691; -.
DR EnsemblFungi; YHR082C_mRNA; YHR082C; YHR082C.
DR GeneID; 856482; -.
DR KEGG; sce:YHR082C; -.
DR SGD; S000001124; KSP1.
DR VEuPathDB; FungiDB:YHR082C; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_008377_0_0_1; -.
DR InParanoid; P38691; -.
DR OMA; KSFCYFA; -.
DR BioCyc; YEAST:G3O-31129-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR PRO; PR:P38691; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38691; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
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; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IMP:SGD.
DR GO; GO:0008104; P:protein localization; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0010570; P:regulation of filamentous growth; IMP:SGD.
DR GO; GO:2000220; P:regulation of pseudohyphal growth; IMP:SGD.
DR GO; GO:0043555; P:regulation of translation in response to stress; IMP:SGD.
DR GO; GO:0031929; P:TOR signaling; IMP: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; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1029
FT /note="Serine/threonine-protein kinase KSP1"
FT /id="PRO_0000086228"
FT DOMAIN 18..351
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 56..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..78
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 501
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 504
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 526
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 884
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1005
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1014
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1029 AA; 117082 MW; 99E2A1FC7CEB3D5A CRC64;
MTLDYEIYKE GGILNNRYQK IEDISEGSYG YVSLAKDVRE KRLVAVKYIF KLEDDGQYDG
PQDDENDCDS SDCDDDEDTK VDTDRHENEN GNASSNNGSS REKKHNLYKH KKSLISSKVK
SRLSNNICLE AMYEVDIQTK IGRHQNIAAL LDFFDSYIIM EYCSGGDLYE AIKADAVPKK
TKSITHIITQ IMDAIEYVHN KGIYHRDIKP ENILISGIDW TIKLTDWGLA TTDKTSMDRN
VGSERYMSPE LFDSNLDIKE RKEPYDCAKV DLWAMGIVFL NIVFHKNPFS IANQSDKSFC
YFAANREALF DVFSTMAYDF FQVLRYSLTI DPANRDLKMM RTELQNLSEY TLDDEYYNNL
DEGYEETMID GLPPQPVPPS SAPVSLPTPI SSSNKQHMPE FKKDFNFNNV NERKRSDVSQ
NQNVASGFFK KPSTQQQKFF NQGYNTTLST HERAKSAPKF KFKKRNKYGR TDNQFSKPVN
IEDRKKSKIL KKSRKPLGIP TPNTHMNNFF HDYKARDEFN TRDFFTPPSV QHRYMEGFSN
NNNKQYRQNR NYNNNNNNSN NNHGSNYNNF NNGNSYIKGW NKNFNKYRRP SSSSYTGKSP
LSRYNMSYNH NNNSSINGYA RRGSTTTVQH SPGAYIPPNA RNHHVSPTNQ FLRVPQSTAP
DISTVLGGKP SYQEHYTQDS MDSEGDHDSD DVLFTLEEGD HDFVNGMDNL SINDHLPHTT
VGSHNEVFVH ASTNHNNNGN NNHIDTNSTT NQYHRQYIPP PLTTSLHINN NNNESNELPD
LLKSPASSEA HLNLSSGPID PILTGNIGNR YSHSSDSKEL EQERRLSMEQ KFKNGVYVPP
HHRKSFNLGT QVPPMNMKTS NEATLSVSHN SVNFGGSYNS RRSSANESNP LHMNKALEKL
SSSPGAKSSF VGFPKPLLPR NHSSTTIALQ NEDVFADSNN DAIIFEDEEY EGESDKMAHG
KMEGGDNESS STSPDERQIF GPYEIYAQTF AGSTHDKKLG AGRKTSIQDE MVGSLEQYKN
NWLILQQQD
