HOS4_YEAST
ID HOS4_YEAST Reviewed; 1083 AA.
AC P40480; D6VVH5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Protein HOS4;
GN Name=HOS4; OrderedLocusNames=YIL112W;
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 IDENTIFICATION IN A COMPLEX WITH HOS2; HST1; SNT1; SIF2; CPR1 AND SET3.
RX PubMed=11711434; DOI=10.1101/gad.207401;
RA Pijnappel W.W.M.P., Schaft D., Roguev A., Shevchenko A., Tekotte H.,
RA Wilm M., Rigaut G., Seraphin B., Aasland R., Stewart A.F.;
RT "The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and
RT Hst1, and is a meiotic-specific repressor of the sporulation gene
RT program.";
RL Genes Dev. 15:2991-3004(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-778, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-698 AND THR-700, AND
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-16; THR-37; SER-290;
RP SER-507 AND SER-778, 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).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Unknown. Component of the Set3C complex, which is required to
CC repress early/middle sporulation genes during meiosis.
CC -!- SUBUNIT: Identified in the Set3C complex with HOS2, HST1, SNT1, SIF2,
CC CPR1 and SET3. {ECO:0000269|PubMed:11711434}.
CC -!- INTERACTION:
CC P40480; P38262: SIF2; NbExp=5; IntAct=EBI-8492, EBI-17136;
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z38125; CAA86268.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08441.1; -; Genomic_DNA.
DR PIR; S48460; S48460.
DR RefSeq; NP_012154.1; NM_001179460.1.
DR AlphaFoldDB; P40480; -.
DR SMR; P40480; -.
DR BioGRID; 34879; 194.
DR ComplexPortal; CPX-1342; SET3C histone deacetylase complex.
DR DIP; DIP-1765N; -.
DR IntAct; P40480; 11.
DR MINT; P40480; -.
DR STRING; 4932.YIL112W; -.
DR iPTMnet; P40480; -.
DR MaxQB; P40480; -.
DR PaxDb; P40480; -.
DR PRIDE; P40480; -.
DR EnsemblFungi; YIL112W_mRNA; YIL112W; YIL112W.
DR GeneID; 854694; -.
DR KEGG; sce:YIL112W; -.
DR SGD; S000001374; HOS4.
DR VEuPathDB; FungiDB:YIL112W; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000173654; -.
DR HOGENOM; CLU_006901_0_0_1; -.
DR InParanoid; P40480; -.
DR OMA; EAVKFGH; -.
DR BioCyc; YEAST:G3O-31366-MON; -.
DR PRO; PR:P40480; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40480; protein.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0034967; C:Set3 complex; IDA:SGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IC:ComplexPortal.
DR GO; GO:0009267; P:cellular response to starvation; IC:ComplexPortal.
DR GO; GO:0016575; P:histone deacetylation; IDA:SGD.
DR GO; GO:0045835; P:negative regulation of meiotic nuclear division; IDA:ComplexPortal.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13857; Ank_5; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 1: Evidence at protein level;
KW ANK repeat; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1083
FT /note="Protein HOS4"
FT /id="PRO_0000066998"
FT REPEAT 329..359
FT /note="ANK 1"
FT REPEAT 363..392
FT /note="ANK 2"
FT REPEAT 398..427
FT /note="ANK 3"
FT REPEAT 532..561
FT /note="ANK 4"
FT REPEAT 593..622
FT /note="ANK 5"
FT REGION 1..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..186
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 37
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 700
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1083 AA; 123556 MW; D73BADE71241955D CRC64;
MNETTTKQPL KKRSLSSYLS NVSTRREELE KISKQETSEE EDTAGKHEQR ETLSEEVSDK
FPENVASFRS QTTSVHQATQ NNLNAKESED LAHKNDASSH EGEVNGDSRP DDVPETNEKI
SQAIRAKISS SSSSPNVRNV DIQNHQPFSR DQLRAMLKEP KRKTVDDFIE EEGLGAVEEE
DLSDEVLEKN TTEPENVEKD IEYSDSDKDT DDVGSDDPTA PNSPIKLGRR KLVRGDQLDA
TTSSMFNNES DSELSDIDDS KNIALSSSLF RGGSSPVKET NNNLSNMNSS PAQNPKRGSV
SRSNDSNKSS HIAVSKRPKQ KKGIYRDSGG RTRLQIACDK GKYDVVKKMI EEGGYDINDQ
DNAGNTALHE AALQGHIEIV ELLIENGADV NIKSIEMFGD TPLIDASANG HLDVVKYLLK
NGADPTIRNA KGLTAFESVD DESEFDDEED QKILREIKKR LSIAAKKWTN RAGIHNDKSK
NGNNAHTIDQ PPFDNTTKAK NEKAADSPSM ASNIDEKAPE EEFYWTDVTS RAGKEKLFKA
SKEGHLPYVG TYVENGGKID LRSFFESVKC GHEDITSIFL AFGFPVNQTS RDNKTSALMV
AVGRGHLGTV KLLLEAGADP TKRDKKGRTA LYYAKNSIMG ITNSEEIQLI ENAINNYLKK
HSEDNNDDDD DDDNNNETYK HEKKREKTQS PILASRRSAT PRIEDEEDDT RMLNLADDDF
NNDRDVKEST TSDSRKRLDD NENVGTQYSL DWKKRKTNAL QDEEKLKSIS PLSMEPHSPK
KAKSVEISKI HEETAAEREA RLKEEEEYRK KRLEKKRKKE QELLQKLAED EKKRIEEQEK
QKVLEMERLE KATLEKARKM EREKEMEEIS YRRAVRDLYP LGLKIINFND KLDYKRFLPL
YYFVDEKNDK FVLDLQVMIL LKDIDLLSKD NQPTSEKIPV DPSHLTPLWN MLKFIFLYGG
SYDDKKNNME NKRYVVNFDG VDLDTKIGYE LLEYKKFVSL PMAWIKWDNV VIENHAKRKE
IEGNMIQISI NEFARWRNDK LNKAQQPTRK QRSLKIPREL PVKFQHRMSI SSVLQQTSKE
PFW
