SIC1_YEAST
ID SIC1_YEAST Reviewed; 284 AA.
AC P38634; D6VY79;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Protein SIC1;
DE AltName: Full=CDK inhibitor p40;
GN Name=SIC1; Synonyms=SDB25; OrderedLocusNames=YLR079W; ORFNames=L9449.8;
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], AND PROTEIN SEQUENCE OF 182-188; 238-250
RP AND 260-283.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8164683; DOI=10.1128/mcb.14.5.3320-3328.1994;
RA Nugroho T.T., Mendenhall M.D.;
RT "An inhibitor of yeast cyclin-dependent protein kinase plays an important
RT role in ensuring the genomic integrity of daughter cells.";
RL Mol. Cell. Biol. 14:3320-3328(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7958845; DOI=10.1101/gad.8.14.1640;
RA Donovan J.D., Toyn J.H., Johnson A.L., Johnston L.H.;
RT "P40SDB25, a putative CDK inhibitor, has a role in the M/G1 transition in
RT Saccharomyces cerevisiae.";
RL Genes Dev. 8:1640-1653(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [4]
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 [5]
RP PHOSPHORYLATION AT THR-5; THR-33 AND SER-76.
RX PubMed=9725902; DOI=10.1091/mbc.9.9.2393;
RA Nishizawa M., Kawasumi M., Fujino M., Toh-e A.;
RT "Phosphorylation of Sic1, a cyclin-dependent kinase (Cdk) inhibitor, by Cdk
RT including Pho85 kinase is required for its prompt degradation.";
RL Mol. Biol. Cell 9:2393-2405(1998).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
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 [8]
RP FUNCTION, PHOSPHORYLATION AT THR-173, MUTAGENESIS OF THR-173, AND
RP INTERACTION WITH HOG1.
RX PubMed=15448699; DOI=10.1038/ncb1174;
RA Escote X., Zapater M., Clotet J., Posas F.;
RT "Hog1 mediates cell-cycle arrest in G1 phase by the dual targeting of
RT Sic1.";
RL Nat. Cell Biol. 6:997-1002(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-173 AND SER-201, AND
RP 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 [11]
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198 AND SER-201, 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).
CC -!- FUNCTION: Substrate and inhibitor of the cyclin-dependent protein
CC kinase CDC28. Its activity could be important for faithful segregation
CC of chromosomes to daughter cells. It acts in response to a signal from
CC a post-start checkpoint. {ECO:0000269|PubMed:15448699}.
CC -!- SUBUNIT: Interacts with HOG1. {ECO:0000269|PubMed:15448699}.
CC -!- INTERACTION:
CC P38634; Q00684: CDC14; NbExp=2; IntAct=EBI-17127, EBI-4192;
CC P38634; P07834: CDC4; NbExp=5; IntAct=EBI-17127, EBI-4434;
CC P38634; P32485: HOG1; NbExp=4; IntAct=EBI-17127, EBI-8437;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Phosphorylated by cyclin-dependent kinases CDC28 and PHO85 in
CC association with G1-cyclins, promoting degradation of SIC1 and exit
CC form G1. {ECO:0000269|PubMed:15448699, ECO:0000269|PubMed:9725902}.
CC -!- PTM: May contain a covalently attached chromophore.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Present with 768 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U01300; AAA20052.1; -; Genomic_DNA.
DR EMBL; X78309; CAA55118.1; -; Genomic_DNA.
DR EMBL; Z73251; CAA97638.1; -; Genomic_DNA.
DR EMBL; U53880; AAB67583.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09395.1; -; Genomic_DNA.
DR PIR; S47921; S47921.
DR RefSeq; NP_013180.1; NM_001181966.1.
DR PDB; 3V7D; X-ray; 2.31 A; E=67-85.
DR PDB; 6G86; X-ray; 1.74 A; C/D=46-61.
DR PDBsum; 3V7D; -.
DR PDBsum; 6G86; -.
DR AlphaFoldDB; P38634; -.
DR BMRB; P38634; -.
DR SMR; P38634; -.
DR BioGRID; 31352; 713.
DR DIP; DIP-6817N; -.
DR ELM; P38634; -.
DR IntAct; P38634; 23.
DR MINT; P38634; -.
DR STRING; 4932.YLR079W; -.
DR iPTMnet; P38634; -.
DR MaxQB; P38634; -.
DR PaxDb; P38634; -.
DR PRIDE; P38634; -.
DR EnsemblFungi; YLR079W_mRNA; YLR079W; YLR079W.
DR GeneID; 850768; -.
DR KEGG; sce:YLR079W; -.
DR SGD; S000004069; SIC1.
DR VEuPathDB; FungiDB:YLR079W; -.
DR eggNOG; ENOG502S3ZS; Eukaryota.
DR HOGENOM; CLU_086083_0_0_1; -.
DR InParanoid; P38634; -.
DR OMA; KNWNNNS; -.
DR BioCyc; YEAST:G3O-32230-MON; -.
DR PRO; PR:P38634; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P38634; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IDA:SGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IGI:SGD.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IMP:SGD.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:SGD.
DR DisProt; DP00631; -.
DR IDEAL; IID50275; -.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..284
FT /note="Protein SIC1"
FT /id="PRO_0000097751"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="Phosphothreonine; by PHO85"
FT /evidence="ECO:0000269|PubMed:9725902"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:9725902"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:9725902"
FT MOD_RES 173
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15448699,
FT ECO:0007744|PubMed:17330950"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 268
FT /note="Lysine derivative"
FT MOD_RES 272
FT /note="Lysine derivative"
FT MOD_RES 274
FT /note="Lysine derivative"
FT MUTAGEN 173
FT /note="T->A: Impairs the ability to arrest the cell cycle."
FT /evidence="ECO:0000269|PubMed:15448699"
FT CONFLICT 167
FT /note="I -> T (in Ref. 2; CAA55118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 32223 MW; 7913636340678F78 CRC64;
MTPSTPPRSR GTRYLAQPSG NTSSSALMQG QKTPQKPSQN LVPVTPSTTK SFKNAPLLAP
PNSNMGMTSP FNGLTSPQRS PFPKSSVKRT LFQFESHDNG TVREEQEPLG RVNRILFPTQ
QNVDIDAAEE EEEGEVLLPP SRPTSARQLH LSLERDEFDQ THRKKIIKDV PGTPSDKVIT
FELAKNWNNN SPKNDARSQE SEDEEDIIIN PVRVGKNPFA SDELVTQEIR NERKRAMLRE
NPDIEDVITY VNKKGEVVEK RRLTDEEKRR FKPKALFQSR DQEH
