SET3_YEAST
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 03-AUG-2022, entry version 175.
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; 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=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., Bossier P.,
RA 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., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA 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., 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 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, 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 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., 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-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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684; SER-718 AND THR-719, AND
RP 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: Transcriptional regulator that acts via the formation of
CC large multiprotein complexes that modify and/or remodel the chromatin.
CC Required for both gene activation and repression. Part of the Set3C
CC complex, which is required to repress early/middle sporulation genes
CC during meiosis. Required for the transcriptional activation of genes
CC with high activity. {ECO:0000269|PubMed:12434058}.
CC -!- SUBUNIT: Identified in the Set3C complex with HOS2, HST1, SNT1, SIF2,
CC CPR1 and HOS4/YIL112W. {ECO:0000269|PubMed:11711434}.
CC -!- INTERACTION:
CC P36124; P02309: HHF2; NbExp=2; IntAct=EBI-16993, EBI-8113;
CC P36124; P61830: HHT2; NbExp=2; IntAct=EBI-16993, EBI-8098;
CC -!- MISCELLANEOUS: Present with 623 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SET3 family. {ECO:0000305}.
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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 AlphaFoldDB; P36124; -.
DR SMR; P36124; -.
DR BioGRID; 34162; 433.
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; YKR029C.
DR GeneID; 853900; -.
DR KEGG; sce:YKR029C; -.
DR SGD; S000001737; SET3.
DR VEuPathDB; FungiDB:YKR029C; -.
DR eggNOG; KOG1844; Eukaryota.
DR GeneTree; ENSGT00940000168747; -.
DR HOGENOM; CLU_017047_0_0_1; -.
DR InParanoid; P36124; -.
DR OMA; WQHAICY; -.
DR BioCyc; YEAST:G3O-32005-MON; -.
DR Reactome; R-SCE-3214841; PKMTs methylate histone lysines.
DR PRO; PR:P36124; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36124; protein.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
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:0006974; P:cellular response to DNA damage stimulus; IC:ComplexPortal.
DR GO; GO:0009267; P:cellular response to starvation; IC:ComplexPortal.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IDA:ComplexPortal.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045835; P:negative regulation of meiotic nuclear division; IDA:ComplexPortal.
DR GO; GO:0006479; P:protein methylation; IMP:SGD.
DR GO; GO:0035065; P:regulation of histone acetylation; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:SGD.
DR CDD; cd19183; SET_SpSET3-like; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR044435; Set3/4_SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
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 Pfam; PF00856; SET; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR SUPFAM; SSF82199; SSF82199; 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; Meiosis; Metal-binding;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..751
FT /note="SET domain-containing protein 3"
FT /id="PRO_0000097696"
FT DOMAIN 313..456
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 117..166
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 24..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 719
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:5TDR"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:5TDR"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:5TDR"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:5TDR"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:5TDR"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:5TDR"
FT HELIX 170..183
FT /evidence="ECO:0007829|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
