SOK1_YEAST
ID SOK1_YEAST Reviewed; 901 AA.
AC P40317; D6VRZ4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Protein SOK1;
GN Name=SOK1; OrderedLocusNames=YDR006C; ORFNames=YD8119.12C;
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] OF 337-901.
RC STRAIN=SGY101;
RX PubMed=8065298; DOI=10.1128/mcb.14.9.5619-5627.1994;
RA Ward M.P., Garrett S.;
RT "Suppression of a yeast cyclic AMP-dependent protein kinase defect by
RT overexpression of SOK1, a yeast gene exhibiting sequence similarity to a
RT developmentally regulated mouse gene.";
RL Mol. Cell. Biol. 14:5619-5627(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP 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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-191; SER-193 AND
RP SER-245, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-191; SER-193 AND
RP SER-245, AND 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 -!- FUNCTION: High copy suppressor of a cyclic AMP-dependent protein kinase
CC mutant.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the TCP11 family. {ECO:0000305}.
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DR EMBL; U12027; AAA56922.1; -; Genomic_DNA.
DR EMBL; Z48008; CAA88066.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11854.1; -; Genomic_DNA.
DR PIR; S50987; S50987.
DR RefSeq; NP_010289.3; NM_001180314.3.
DR AlphaFoldDB; P40317; -.
DR BioGRID; 32059; 191.
DR DIP; DIP-5173N; -.
DR IntAct; P40317; 4.
DR MINT; P40317; -.
DR STRING; 4932.YDR006C; -.
DR iPTMnet; P40317; -.
DR MaxQB; P40317; -.
DR PaxDb; P40317; -.
DR PRIDE; P40317; -.
DR EnsemblFungi; YDR006C_mRNA; YDR006C; YDR006C.
DR GeneID; 851569; -.
DR KEGG; sce:YDR006C; -.
DR SGD; S000002413; SOK1.
DR VEuPathDB; FungiDB:YDR006C; -.
DR eggNOG; KOG1981; Eukaryota.
DR GeneTree; ENSGT00940000174079; -.
DR HOGENOM; CLU_009875_0_0_1; -.
DR InParanoid; P40317; -.
DR OMA; NIYRHLY; -.
DR BioCyc; YEAST:G3O-29628-MON; -.
DR PRO; PR:P40317; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P40317; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0010737; P:protein kinase A signaling; IGI:SGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR008862; Tcp11.
DR PANTHER; PTHR12832; PTHR12832; 1.
DR Pfam; PF05794; Tcp11; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..901
FT /note="Protein SOK1"
FT /id="PRO_0000072035"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..209
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CONFLICT 645
FT /note="A -> R (in Ref. 1; AAA56922)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 901 AA; 101082 MW; C900DF2889541B98 CRC64;
MDQPRTHSGP TTASNPAPSS TNSSSAPSAT NSKQERSSSS LSKPSSVVPS KDSPDGDAIA
KTQAAALKND MKSGDTSTLD GSSQNIIPNR ASMQKYIDQS SDLLSRSSGV ITPSMSLNAS
TNATNNDSSG NSANSSDLKI PIDRDNTIFK TFDTKTGQFL KNDDNEEEIR RNNKVDSIPP
KNIYTNINNP SPSPPPSSKQ PPSASAPQLP PATEPHKEQA AQQQPPGNAS NFLRIFSNKK
MRSHSVPTIL HSSLRKLSSH NQYYRNQNIL LNHPTPSGIS KKKFSRNHHQ PYLHSNNPLS
SNPLSLKRAI FLNQQISGNA STNANNDNIN NSTATSMTNQ SFLSSSNFDL TLEDRINYIK
ATPTPVPFPP INLQGLKEID LQEILKNPQL RHDIIFDPLL QFRPNLDGER GNKKRQLANI
YWNDVQNEIY VYSKRPEIFQ YNRSRLVPLF DTLRDVLLTI VPQKESPMIN NVLDTELNIQ
ELLKGSLIMS NLSGWLADLF KHHCAPMRDP WVDKMSNKFK EAERDSSLTR LIEGLRLVFQ
ILETMKLDIA NHQIRILRPA LLSNAVEFEK QYFNTLIASK RVNLNTSLLW FDKKFNENVT
AGLVRNPSSI TIPDVYNICI RSIINLLSCR KMVREYPTPL SFDHARLILL RADIRQIVCI
LVCRLLFQQL VANDPSMDKA TKEYVIHTYS TKRLKNEIIS IITDEHGNCR WTKNTMSIAV
HLCKVIDDLH REYDNNGSCE QARRPQLPSL DNSKITFAKS WLSKQTQPLS EVYGVLENRV
FKSLEDAIFN RSECTIDGRV KQDFVYLYNT NNGNVGSTNT LSTTTDTASV KISPSLMSPS
KTSTTTPTGN AIASRGLFAA TELEEFENVY RHLYALINLH WSVFGPHYIE MLGDKVNKKG
I
