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Database: UniProt
Entry: P36124
LinkDB: P36124
Original site: P36124 
ID   SET3_YEAST              Reviewed;         751 AA.
AC   P36124; D6VX94;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   13-FEB-2019, entry version 158.
DE   RecName: Full=SET domain-containing protein 3;
GN   Name=SET3; OrderedLocusNames=YKR029C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
RA   Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
RA   Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
RA   Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   IDENTIFICATION IN A COMPLEX WITH HOS2; HST1; SNT1; SIF2; CPR1 AND
RP   YIL112W.
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,
RT   Hos2 and Hst1, and is a meiotic-specific repressor of the sporulation
RT   gene program.";
RL   Genes Dev. 15:2991-3004(2001).
RN   [4]
RP   FUNCTION.
RX   PubMed=12434058; DOI=10.1126/science.1077790;
RA   Wang A., Kurdistani S.K., Grunstein M.;
RT   "Requirement of Hos2 histone deacetylase for gene activity in yeast.";
RL   Science 298:1412-1414(2002).
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.,
RA   Dephoure N., 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-236 AND SER-741, 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
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684; SER-718 AND
RP   THR-719, 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
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Transcriptional regulator that acts via the formation of
CC       large multiprotein complexes that modify and/or remodel the
CC       chromatin. Required for both gene activation and repression. Part
CC       of the Set3C complex, which is required to repress early/middle
CC       sporulation genes during meiosis. Required for the transcriptional
CC       activation of genes with high activity.
CC       {ECO:0000269|PubMed:12434058}.
CC   -!- SUBUNIT: Identified in the Set3C complex with HOS2, HST1, SNT1,
CC       SIF2, CPR1 and HOS4/YIL112W. {ECO:0000269|PubMed:11711434}.
CC   -!- INTERACTION:
CC       P02309:HHF2; NbExp=2; IntAct=EBI-16993, EBI-8113;
CC       P61830:HHT2; NbExp=2; IntAct=EBI-16993, EBI-8098;
CC   -!- MISCELLANEOUS: Present with 623 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SET3 family. {ECO:0000305}.
DR   EMBL; Z28254; CAA82101.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09184.1; -; Genomic_DNA.
DR   PIR; S38101; S38101.
DR   RefSeq; NP_012954.3; NM_001179819.3.
DR   PDB; 5TDR; X-ray; 1.42 A; A=116-184.
DR   PDB; 5TDW; X-ray; 1.70 A; A=116-184.
DR   PDBsum; 5TDR; -.
DR   PDBsum; 5TDW; -.
DR   ProteinModelPortal; P36124; -.
DR   SMR; P36124; -.
DR   BioGrid; 34162; 412.
DR   ComplexPortal; CPX-1342; SET3C histone deacetylase complex.
DR   DIP; DIP-5632N; -.
DR   IntAct; P36124; 125.
DR   MINT; P36124; -.
DR   STRING; 4932.YKR029C; -.
DR   iPTMnet; P36124; -.
DR   MaxQB; P36124; -.
DR   PaxDb; P36124; -.
DR   PRIDE; P36124; -.
DR   EnsemblFungi; YKR029C_mRNA; YKR029C_mRNA; YKR029C.
DR   GeneID; 853900; -.
DR   KEGG; sce:YKR029C; -.
DR   EuPathDB; FungiDB:YKR029C; -.
DR   SGD; S000001737; SET3.
DR   GeneTree; ENSGT00940000168747; -.
DR   HOGENOM; HOG000141785; -.
DR   InParanoid; P36124; -.
DR   KO; K07117; -.
DR   OMA; FTIQCDH; -.
DR   BioCyc; YEAST:G3O-32005-MONOMER; -.
DR   PRO; PR:P36124; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   GO; GO:0070210; C:Rpd3L-Expanded complex; HDA:SGD.
DR   GO; GO:0034967; C:Set3 complex; IDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0035064; F:methylated histone binding; IDA:SGD.
DR   GO; GO:0016575; P:histone deacetylation; IDA:SGD.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0045835; P:negative regulation of meiotic nuclear division; IMP:SGD.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:SGD.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Chromatin regulator; Complete proteome;
KW   Meiosis; Metal-binding; Phosphoprotein; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    751       SET domain-containing protein 3.
FT                                /FTId=PRO_0000097696.
FT   DOMAIN      313    456       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     117    166       PHD-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   MOD_RES     236    236       Phosphoserine.
FT                                {ECO:0000244|PubMed:18407956}.
FT   MOD_RES     684    684       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     718    718       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     719    719       Phosphothreonine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     741    741       Phosphoserine.
FT                                {ECO:0000244|PubMed:18407956}.
FT   STRAND      129    133       {ECO:0000244|PDB:5TDR}.
FT   TURN        135    137       {ECO:0000244|PDB:5TDR}.
FT   STRAND      140    142       {ECO:0000244|PDB:5TDR}.
FT   HELIX       143    146       {ECO:0000244|PDB:5TDR}.
FT   HELIX       151    153       {ECO:0000244|PDB:5TDR}.
FT   TURN        161    163       {ECO:0000244|PDB:5TDR}.
FT   HELIX       170    183       {ECO:0000244|PDB:5TDR}.
SQ   SEQUENCE   751 AA;  85480 MW;  934621768C36230B CRC64;
     MSVPNSKEQS LLDDASTLLL FSKGKKRAEE ASKIGSKTDT IEHDESHERE KKGAIEMAAA
     ALATASTVSL PLKKATEQSA AEAATSTAAK EETENQPQKQ PQWPVPDSYI VDPDAGIITC
     ICDLNDDDGF TIQCDHCNRW QHAICYGIKD IGMAPDDYLC NSCDPREVDI NLARKIQQER
     INVKTVEPSS SNNSASNKNN GRDRASSTTI SDVGDSFSTD QDNTNHRDKR RKRNPSNNSI
     DSKNESASVN SSDGLTSMPK KKEHFLSAKD AYGAIYLPLK DNVFKSDLIE PFLNKHMDDN
     WVIQYPHKTF KSVSIEVKPY ADIAYSRTYP GFTKLGVYLK KDCIKGDFIQ EILGELDFYK
     NYLTDPRNHY RIWGTAKRRV IFHSHWPIYI DARLSGNSTR YLRRSCQPNV ELVTIKLQDT
     DNRNDKSSGR KSSRIKFVLR ALRDISEDEE LYIKWQWDSK HPILKLIKGM TIDSLDDLER
     YGLINSVETI LSNGECGCGN NSKDCYLLKV KRYAQSLYKS VKSRGKMNNR YKLNEILNQY
     NCKKRREPPI LHRLEEKAQN TIERAPILLN NFYRQKFLNR NNGPKIPQKN TIDSTNNPDD
     IAKPFKFALF AQHSSNISVP KKNETSEKPL IITKSTDYDE SHITNIEELP IPVLLPINKT
     SRQTANDVEE SQSKNEHKLS RTPSLSNFNK ELSKEAQHSQ AKTKEIMTEA SVNSRRESTP
     ESIMHLSDFS SSQLHSKKKL SFADYRKKLL K
//
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