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SDC1_YEAST
ID   SDC1_YEAST              Reviewed;         175 AA.
AC   Q03323; D6VT93;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=COMPASS component SDC1;
DE   AltName: Full=Complex proteins associated with SET1 protein SDC1;
DE   AltName: Full=Set1C component SDC1;
DE   AltName: Full=Suppressor of CDC25 protein 1;
GN   Name=SDC1; Synonyms=CPS25, SAF19; OrderedLocusNames=YDR469W;
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=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(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, AND SUBUNIT.
RX   PubMed=11742990; DOI=10.1093/emboj/20.24.7137;
RA   Roguev A., Schaft D., Shevchenko A., Pijnappel W.W.M.P., Wilm M.,
RA   Aasland R., Stewart A.F.;
RT   "The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and
RT   methylates histone 3 lysine 4.";
RL   EMBO J. 20:7137-7148(2001).
RN   [4]
RP   FUNCTION.
RX   PubMed=11805083; DOI=10.1074/jbc.c200023200;
RA   Krogan N.J., Dover J., Khorrami S., Greenblatt J.F., Schneider J.,
RA   Johnston M., Shilatifard A.;
RT   "COMPASS, a histone H3 (Lysine 4) methyltransferase required for telomeric
RT   silencing of gene expression.";
RL   J. Biol. Chem. 277:10753-10755(2002).
RN   [5]
RP   SUBUNIT.
RX   PubMed=11687631; DOI=10.1073/pnas.231473398;
RA   Miller T., Krogan N.J., Dover J., Erdjument-Bromage H., Tempst P.,
RA   Johnston M., Greenblatt J.F., Shilatifard A.;
RT   "COMPASS: a complex of proteins associated with a trithorax-related SET
RT   domain protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12902-12907(2001).
RN   [6]
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   [7]
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).
CC   -!- FUNCTION: The COMPASS (Set1C) complex specifically mono-, di- and
CC       trimethylates histone H3 to form H3K4me1/2/3, which subsequently
CC       activates gene expression by regulating transcription elongation and
CC       plays a role in telomere length maintenance.
CC       {ECO:0000269|PubMed:11742990, ECO:0000269|PubMed:11805083}.
CC   -!- SUBUNIT: Component of the COMPASS (Set1C) complex which consists of
CC       SET1(2), BRE2(2), SPP1(2), SDC1(1), SHG1(1), SWD1(1), SWD2(1), and
CC       SWD3(1). {ECO:0000269|PubMed:11687631, ECO:0000269|PubMed:11742990}.
CC   -!- INTERACTION:
CC       Q03323; P43132: BRE2; NbExp=7; IntAct=EBI-38307, EBI-27115;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 937 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the dpy-30 family. {ECO:0000305}.
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DR   EMBL; U33050; AAB64903.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12303.1; -; Genomic_DNA.
DR   PIR; S69636; S69636.
DR   RefSeq; NP_010757.3; NM_001180777.3.
DR   PDB; 6BX3; EM; 4.30 A; M/N=122-163.
DR   PDB; 6VEN; EM; 3.37 A; P/Q=1-175.
DR   PDBsum; 6BX3; -.
DR   PDBsum; 6VEN; -.
DR   AlphaFoldDB; Q03323; -.
DR   SMR; Q03323; -.
DR   BioGRID; 32522; 498.
DR   ComplexPortal; CPX-1039; COMPASS complex.
DR   DIP; DIP-1738N; -.
DR   IntAct; Q03323; 15.
DR   MINT; Q03323; -.
DR   STRING; 4932.YDR469W; -.
DR   iPTMnet; Q03323; -.
DR   MaxQB; Q03323; -.
DR   PaxDb; Q03323; -.
DR   PRIDE; Q03323; -.
DR   EnsemblFungi; YDR469W_mRNA; YDR469W; YDR469W.
DR   GeneID; 852080; -.
DR   KEGG; sce:YDR469W; -.
DR   SGD; S000002877; SDC1.
DR   VEuPathDB; FungiDB:YDR469W; -.
DR   eggNOG; KOG4109; Eukaryota.
DR   HOGENOM; CLU_1526376_0_0_1; -.
DR   InParanoid; Q03323; -.
DR   OMA; RDIVMSE; -.
DR   BioCyc; YEAST:G3O-29996-MON; -.
DR   PRO; PR:Q03323; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q03323; protein.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0044666; C:MLL3/4 complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IPI:SGD.
DR   GO; GO:0051568; P:histone H3-K4 methylation; IDA:SGD.
DR   GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR   InterPro; IPR007858; Dpy-30_motif.
DR   InterPro; IPR037856; Sdc1/DPY30.
DR   PANTHER; PTHR23356; PTHR23356; 1.
DR   Pfam; PF05186; Dpy-30; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Nucleus; Reference proteome.
FT   CHAIN           1..175
FT                   /note="COMPASS component SDC1"
FT                   /id="PRO_0000114686"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..162
FT                   /note="DPY-30"
FT   COMPBIAS        1..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           121..128
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   HELIX           131..143
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   HELIX           149..160
FT                   /evidence="ECO:0007829|PDB:6VEN"
SQ   SEQUENCE   175 AA;  19446 MW;  B40247D641124306 CRC64;
     MNESENSPQH NEVTVPMVED TSSNADIPME QIQREDNKNY DKHDNECFDM NGNHNNNSDN
     LQFDSVPSSA TKDLKNIKSV TNQNVKIEES SSTNSVIEES SEPKISKLEN VNLAATVGGS
     QTRKYLNTNV TPHLLAGMRL IAVQQPEDPL RVLGEYLIEQ SNILKSGEKE SNASK
 
 
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