VHS2_YEAST
ID VHS2_YEAST Reviewed; 436 AA.
AC P40463; D6VVF1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein VHS2;
DE AltName: Full=Viable in a HAL3 SIT4 background protein 2;
GN Name=VHS2; OrderedLocusNames=YIL135C;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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.
RX PubMed=12518319; DOI=10.1002/yea.938;
RA Munoz I., Simon E., Casals N., Clotet J., Arino J.;
RT "Identification of multicopy suppressors of cell cycle arrest at the G1-S
RT transition in Saccharomyces cerevisiae.";
RL Yeast 20:157-169(2003).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303 AND SER-325, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND IDENTIFICATION BY
RP 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-53; SER-61; SER-102; SER-172;
RP SER-299 AND SER-303, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: Can suppress the synthetic lethality of the hal3 sit4 double
CC mutation when overexpressed, suggesting that it is involved in the G1-S
CC transition. {ECO:0000269|PubMed:12518319}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2200 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: To yeast MFL3. {ECO:0000305}.
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DR EMBL; Z38059; CAA86143.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08417.1; -; Genomic_DNA.
DR PIR; S48399; S48399.
DR RefSeq; NP_012131.1; NM_001179483.1.
DR AlphaFoldDB; P40463; -.
DR BioGRID; 34856; 106.
DR DIP; DIP-5269N; -.
DR IntAct; P40463; 6.
DR MINT; P40463; -.
DR STRING; 4932.YIL135C; -.
DR CarbonylDB; P40463; -.
DR iPTMnet; P40463; -.
DR MaxQB; P40463; -.
DR PaxDb; P40463; -.
DR PRIDE; P40463; -.
DR EnsemblFungi; YIL135C_mRNA; YIL135C; YIL135C.
DR GeneID; 854671; -.
DR KEGG; sce:YIL135C; -.
DR SGD; S000001397; VHS2.
DR VEuPathDB; FungiDB:YIL135C; -.
DR eggNOG; ENOG502S4KQ; Eukaryota.
DR GeneTree; ENSGT00940000176806; -.
DR HOGENOM; CLU_628749_0_0_1; -.
DR InParanoid; P40463; -.
DR OMA; AQRENDN; -.
DR BioCyc; YEAST:G3O-31386-MON; -.
DR PRO; PR:P40463; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40463; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0032186; P:cellular bud neck septin ring organization; IMP:SGD.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IGI:SGD.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..436
FT /note="Protein VHS2"
FT /id="PRO_0000065812"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
SQ SEQUENCE 436 AA; 47961 MW; FDD206463FBFF234 CRC64;
MDTSNHNQDH DSHVAAQREN DNNYMPPSPS MSESSMIFER NVEDPSYLYK TVSNNAANSL
SRQSSRTSLF NHNNSSNRNF HNLSQRSSAV NLHLQPSRTN ESIASYQTYN PDFVVQTPLD
HRRTLENFVP PALDAGCSIV TDDTTGLDDV DMVYSRRPST IGLDRALGRT RSLSSQSFDN
ETSPAHPRSP NDHGSRLLRF YSYADMLSDD NNNNVSNATS TSSTANPLRR PPMQGHYSFS
SSLLNSPSHL PSPPSASASP PQHMNFTNPF IISRRYSNTT INNANGGTSA GSTTGAALSR
SPSNQQYLLK QQRSPSGSAR SRRNSNRPGS AANIMIGKPK SKFHMESSGS EGFSSEEEDN
TMIERDKLNL KQKLQSQLAQ PPSIANMVND NHNNTNKHKN TINNNIKNSP AFTNSNPSSK
SNSNSTITSM NPDTTK
