SIP5_YEAST
ID SIP5_YEAST Reviewed; 489 AA.
AC P40210; D6VZW3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein SIP5;
DE AltName: Full=SNF1-interacting protein 5;
GN Name=SIP5; OrderedLocusNames=YMR140W; ORFNames=YM9375.09;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
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 FUNCTION, AND INTERACTION WITH SNF1 AND REG1.
RX PubMed=10628972; DOI=10.1093/genetics/154.1.99;
RA Sanz P., Ludin K., Carlson M.;
RT "Sip5 interacts with both the Reg1/Glc7 protein phosphatase and the Snf1
RT protein kinase of Saccharomyces cerevisiae.";
RL Genetics 154:99-107(2000).
RN [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=16170412; DOI=10.1371/journal.pgen.0010036;
RA Li W., Mo W., Shen D., Sun L., Wang J., Lu S., Gitschier J.M., Zhou B.;
RT "Yeast model uncovers dual roles of mitochondria in action of
RT artemisinin.";
RL PLoS Genet. 1:329-334(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND THR-433, 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 [8]
RP INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18086883; DOI=10.1128/mcb.01035-07;
RA Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
RA Pemberton L.F.;
RT "Phosphorylation by casein kinase 2 regulates Nap1 localization and
RT function.";
RL Mol. Cell. Biol. 28:1313-1325(2008).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; THR-183; SER-436 AND
RP THR-438, 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: May negatively regulate the SNF1 kinase by promoting the
CC interaction of the REG1/GLC7 phosphatase complex with the kinase.
CC Deletion of SIP5 promotes resistance to artimisin, which is probably an
CC indirect effect of an action on the electron transport chain.
CC {ECO:0000269|PubMed:10628972, ECO:0000269|PubMed:16170412}.
CC -!- SUBUNIT: Interacts with NPA1, SNF1 and REG1.
CC {ECO:0000269|PubMed:10628972, ECO:0000269|PubMed:18086883}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 556 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SIP5 family. {ECO:0000305}.
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DR EMBL; Z47071; CAA87354.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10037.1; -; Genomic_DNA.
DR PIR; S50396; S50396.
DR RefSeq; NP_013860.1; NM_001182642.1.
DR AlphaFoldDB; P40210; -.
DR BioGRID; 35317; 148.
DR DIP; DIP-4656N; -.
DR IntAct; P40210; 7.
DR MINT; P40210; -.
DR STRING; 4932.YMR140W; -.
DR iPTMnet; P40210; -.
DR MaxQB; P40210; -.
DR PaxDb; P40210; -.
DR PRIDE; P40210; -.
DR EnsemblFungi; YMR140W_mRNA; YMR140W; YMR140W.
DR GeneID; 855171; -.
DR KEGG; sce:YMR140W; -.
DR SGD; S000004748; SIP5.
DR VEuPathDB; FungiDB:YMR140W; -.
DR eggNOG; KOG2789; Eukaryota.
DR HOGENOM; CLU_009068_2_0_1; -.
DR InParanoid; P40210; -.
DR OMA; ISEPANC; -.
DR BioCyc; YEAST:G3O-32833-MON; -.
DR PRO; PR:P40210; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P40210; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0042149; P:cellular response to glucose starvation; IMP:SGD.
DR InterPro; IPR039301; Sip5/DA2.
DR PANTHER; PTHR31315; PTHR31315; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..489
FT /note="Protein SIP5"
FT /id="PRO_0000203303"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 433
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 438
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 489 AA; 55859 MW; 9DC434EB7F8224A2 CRC64;
MGNVPGKIDQ EDSFNDVRPD SSYNTTSSNS VIKQYDEEAS SRVRTRRTTS LVNNILNGNN
ARTKTGSHLS STSRRKTSRE KELAKEAHAK QLVVRCSETV DGGFLAPFGC YSFEKLDYDA
TVVKNLIIKR KLAPFYTPLQ DFDESWTRDE LIKIVDGLPL HDTFDENLEE FEDVPIGNLR
KSTFNELIDK SLSKKEQRRM HAKIFRARLY KKRILWQENE NETFLERKLE MKRIGSKSSN
VEDNTSSQPR KNYHLPSDDL KYTLYKNGSE CPICFLYFPG PFNYSKCCQQ PICTECFVQI
KRADPHFPHD EVDPTEPQTN DSEKDPNLLT SEPANCPYCA TASFSITYQP PTNRETGIGG
MPADSYVYKD AAISRADGGQ PNISAITSDT IRPDWEIKLN KERARLMRRS ANATAIHISN
RLIDPSHSRR RNTSHSITPI HDESTSASRS PEPTINELED QMVREAIRLS LEDQDNRKKS
KNRNTSLRP
