SAP30_YEAST
ID SAP30_YEAST Reviewed; 201 AA.
AC P38429; D6W089; Q03501;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Transcriptional regulatory protein SAP30;
GN Name=SAP30; OrderedLocusNames=YMR263W; ORFNames=YM8156.05;
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].
RA Manning A.M., Rosenbloom C.L., Beaudet A.L.;
RT "A large open reading frame in the yeast genome containing homology to the
RT cif1 gene.";
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
RX PubMed=9651585; DOI=10.1016/s1097-2765(00)80102-1;
RA Zhang Y., Sun Z.-W., Iratni R., Erdjument-Bromage H., Tempst P.,
RA Hampsey M., Reinberg D.;
RT "SAP30, a novel protein conserved between human and yeast, is a component
RT of a histone deacetylase complex.";
RL Mol. Cell 1:1021-1031(1998).
RN [6]
RP FUNCTION.
RX PubMed=10388812; DOI=10.1093/genetics/152.3.921;
RA Sun Z.-W., Hampsey M.;
RT "A general requirement for the Sin3-Rpd3 histone deacetylase complex in
RT regulating silencing in Saccharomyces cerevisiae.";
RL Genetics 152:921-932(1999).
RN [7]
RP IDENTIFICATION IN THE RPD3 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12672825; DOI=10.1074/jbc.c300036200;
RA Nourani A., Howe L., Pray-Grant M.G., Workman J.L., Grant P.A., Cote J.;
RT "Opposite role of yeast ING family members in p53-dependent transcriptional
RT activation.";
RL J. Biol. Chem. 278:19171-19175(2003).
RN [8]
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 [9]
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 [10]
RP IDENTIFICATION IN THE RPD3C(L) COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16314178; DOI=10.1016/j.bbaexp.2005.09.005;
RA Carrozza M.J., Florens L., Swanson S.K., Shia W.-J., Anderson S., Yates J.,
RA Washburn M.P., Workman J.L.;
RT "Stable incorporation of sequence specific repressors Ash1 and Ume6 into
RT the Rpd3L complex.";
RL Biochim. Biophys. Acta 1731:77-87(2005).
RN [11]
RP IDENTIFICATION IN THE RPD3C(L) COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16286008; DOI=10.1016/j.cell.2005.10.025;
RA Keogh M.-C., Kurdistani S.K., Morris S.A., Ahn S.H., Podolny V.,
RA Collins S.R., Schuldiner M., Chin K., Punna T., Thompson N.J., Boone C.,
RA Emili A., Weissman J.S., Hughes T.R., Strahl B.D., Grunstein M.,
RA Greenblatt J.F., Buratowski S., Krogan N.J.;
RT "Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a
RT repressive Rpd3 complex.";
RL Cell 123:593-605(2005).
CC -!- FUNCTION: Component of the RPD3C(L) histone deacetylase complex (HDAC)
CC responsible for the deacetylation of lysine residues on the N-terminal
CC part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation
CC gives a tag for epigenetic repression and plays an important role in
CC transcriptional regulation, cell cycle progression and developmental
CC events. {ECO:0000269|PubMed:10388812, ECO:0000269|PubMed:9651585}.
CC -!- SUBUNIT: Component of the RPD3C(L) complex composed of at least ASH1,
CC CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6.
CC {ECO:0000269|PubMed:12672825, ECO:0000269|PubMed:16286008,
CC ECO:0000269|PubMed:16314178}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 704 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SAP30 family. {ECO:0000305}.
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DR EMBL; M88172; AAA35222.1; -; Genomic_DNA.
DR EMBL; Z49260; CAA89246.1; -; Genomic_DNA.
DR EMBL; AY557972; AAS56298.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10163.1; -; Genomic_DNA.
DR PIR; S54475; S54475.
DR RefSeq; NP_013990.1; NM_001182770.1.
DR AlphaFoldDB; P38429; -.
DR BioGRID; 35441; 608.
DR ComplexPortal; CPX-1852; RPD3L histone deacetylase complex.
DR DIP; DIP-3846N; -.
DR IntAct; P38429; 16.
DR MINT; P38429; -.
DR STRING; 4932.YMR263W; -.
DR MaxQB; P38429; -.
DR PaxDb; P38429; -.
DR PRIDE; P38429; -.
DR EnsemblFungi; YMR263W_mRNA; YMR263W; YMR263W.
DR GeneID; 855305; -.
DR KEGG; sce:YMR263W; -.
DR SGD; S000004876; SAP30.
DR VEuPathDB; FungiDB:YMR263W; -.
DR eggNOG; ENOG502RZ9X; Eukaryota.
DR HOGENOM; CLU_106811_0_0_1; -.
DR InParanoid; P38429; -.
DR OMA; THITNNH; -.
DR BioCyc; YEAST:G3O-32937-MON; -.
DR Reactome; R-SCE-3214815; HDACs deacetylate histones.
DR PRO; PR:P38429; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P38429; protein.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0033698; C:Rpd3L complex; IDA:SGD.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; HDA:SGD.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:SGD.
DR GO; GO:0061188; P:negative regulation of ribosomal DNA heterochromatin assembly; IMP:SGD.
DR GO; GO:0061186; P:negative regulation of silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; IMP:SGD.
DR GO; GO:0006334; P:nucleosome assembly; IC:ComplexPortal.
DR GO; GO:2000219; P:positive regulation of invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 6.10.160.20; -; 1.
DR InterPro; IPR024145; His_deAcase_SAP30/SAP30L.
DR InterPro; IPR038291; SAP30_C_sf.
DR InterPro; IPR025718; SAP30_Sin3-bd.
DR PANTHER; PTHR13286; PTHR13286; 1.
DR Pfam; PF13867; SAP30_Sin3_bdg; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..201
FT /note="Transcriptional regulatory protein SAP30"
FT /id="PRO_0000203345"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 31
FT /note="C -> S (in Ref. 1; AAA35222)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="N -> S (in Ref. 1; AAA35222)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 201 AA; 23026 MW; 6C0D2734C50DD72E CRC64;
MARPVNTNAE TESRGRPTQG GGYASNNNGS CNNNNGSNNN NNNNNNNNNN SNNSNNNNGP
TSSGRTNGKQ RLTAAQQQYI KNLIETHITD NHPDLRPKSH PMDFEEYTDA FLRRYKDHFQ
LDVPDNLTLQ GYLLGSKLGA KTYSYKRNTQ GQHDKRIHKR DLANVVRRHF DEHSIKETDC
IPQFIYKVKN QKKKFKMEFR G
