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SWD2_YEAST
ID   SWD2_YEAST              Reviewed;         329 AA.
AC   P36104; D6VXR8;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 186.
DE   RecName: Full=COMPASS component SWD2;
DE   AltName: Full=Complex proteins associated with SET1 protein SWD2;
DE   AltName: Full=Set1C component SWD2;
GN   Name=SWD2; Synonyms=CPS35, SAF37; OrderedLocusNames=YKL018W;
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].
RX   PubMed=8154185; DOI=10.1002/yea.320091208;
RA   Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J.,
RA   Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.;
RT   "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI
RT   from Saccharomyces cerevisiae reveals 23 open reading frames including the
RT   FAS1 gene.";
RL   Yeast 9:1343-1348(1993).
RN   [2]
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   [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, 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   [6]
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   [7]
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   [8]
RP   IDENTIFICATION IN THE CPF COMPLEX, COMPOSITION OF THE APT COMPLEX,
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=12819204; DOI=10.1074/jbc.m304454200;
RA   Nedea E., He X., Kim M., Pootoolal J., Zhong G., Canadien V., Hughes T.,
RA   Buratowski S., Moore C.L., Greenblatt J.;
RT   "Organization and function of APT, a subcomplex of the yeast cleavage and
RT   polyadenylation factor involved in the formation of mRNA and small
RT   nucleolar RNA 3'-ends.";
RL   J. Biol. Chem. 278:33000-33010(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   FUNCTION.
RX   PubMed=15024081; DOI=10.1128/mcb.24.7.2932-2943.2004;
RA   Cheng H., He X., Moore C.;
RT   "The essential WD repeat protein Swd2 has dual functions in RNA polymerase
RT   II transcription termination and lysine 4 methylation of histone H3.";
RL   Mol. Cell. Biol. 24:2932-2943(2004).
CC   -!- FUNCTION: The COMPASS (Set1C) complex specifically mono-, di- and
CC       trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays
CC       a role in telomere length maintenance and transcription elongation
CC       regulation.
CC   -!- FUNCTION: Involved in mediating RNA polymerase II termination.
CC       Component of the cleavage and polyadenylation factor (CPF) complex,
CC       which plays a key role in polyadenylation-dependent pre-mRNA 3'-end
CC       formation and cooperates with cleavage factors including the CFIA
CC       complex and NAB4/CFIB. Component of the APT complex, which may be
CC       involved in polyadenylation-independent transcript 3'-end formation.
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). Component of the cleavage and polyadenylation factor (CPF)
CC       complex, which is composed of PTI1, SYC1, SSU72, GLC7, MPE1, REF2,
CC       PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1.
CC       Component of the APT complex, which is a subcomplex of CPF, and is
CC       composed of PTI1, SYC1, SSU72, GLC7, REF2, PTA1 and SWD2.
CC       {ECO:0000269|PubMed:11687631, ECO:0000269|PubMed:11742990,
CC       ECO:0000269|PubMed:12819204}.
CC   -!- INTERACTION:
CC       P36104; P32598: GLC7; NbExp=5; IntAct=EBI-26608, EBI-13715;
CC       P36104; P38827: SET1; NbExp=6; IntAct=EBI-26608, EBI-16977;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12819204}.
CC       Chromosome, telomere {ECO:0000269|PubMed:12819204}.
CC   -!- MISCELLANEOUS: Present with 704 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the WD repeat SWD2 family. {ECO:0000305}.
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DR   EMBL; X74152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z28018; CAA81853.1; -; Genomic_DNA.
DR   EMBL; AY558094; AAS56420.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09138.1; -; Genomic_DNA.
DR   PIR; S37831; S37831.
DR   RefSeq; NP_012907.3; NM_001179584.3.
DR   AlphaFoldDB; P36104; -.
DR   SMR; P36104; -.
DR   BioGRID; 34114; 170.
DR   ComplexPortal; CPX-1039; COMPASS complex.
DR   ComplexPortal; CPX-1053; Cleavage and polyadenylation specificity factor complex.
DR   DIP; DIP-6844N; -.
DR   IntAct; P36104; 35.
DR   MINT; P36104; -.
DR   STRING; 4932.YKL018W; -.
DR   iPTMnet; P36104; -.
DR   MaxQB; P36104; -.
DR   PaxDb; P36104; -.
DR   PRIDE; P36104; -.
DR   EnsemblFungi; YKL018W_mRNA; YKL018W; YKL018W.
DR   GeneID; 853851; -.
DR   KEGG; sce:YKL018W; -.
DR   SGD; S000001501; SWD2.
DR   VEuPathDB; FungiDB:YKL018W; -.
DR   eggNOG; KOG1446; Eukaryota.
DR   GeneTree; ENSGT00530000063965; -.
DR   HOGENOM; CLU_044117_3_0_1; -.
DR   InParanoid; P36104; -.
DR   OMA; CVLNGDH; -.
DR   BioCyc; YEAST:G3O-31827-MON; -.
DR   PRO; PR:P36104; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36104; protein.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IPI:SGD.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0051568; P:histone H3-K4 methylation; IDA:SGD.
DR   GO; GO:0080182; P:histone H3-K4 trimethylation; IBA:GO_Central.
DR   GO; GO:0034729; P:histone H3-K79 methylation; IMP:SGD.
DR   GO; GO:0031124; P:mRNA 3'-end processing; IMP:SGD.
DR   GO; GO:0006378; P:mRNA polyadenylation; IDA:ComplexPortal.
DR   GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IDA:ComplexPortal.
DR   GO; GO:0031126; P:sno(s)RNA 3'-end processing; IMP:SGD.
DR   GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR   GO; GO:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; IC:ComplexPortal.
DR   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR037867; Swd2/WDR82.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR19861; PTHR19861; 1.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Chromosome; mRNA processing; Nucleus; Reference proteome; Repeat; Telomere;
KW   WD repeat.
FT   CHAIN           1..329
FT                   /note="COMPASS component SWD2"
FT                   /id="PRO_0000051253"
FT   REPEAT          25..64
FT                   /note="WD 1"
FT   REPEAT          111..150
FT                   /note="WD 2"
FT   REPEAT          152..191
FT                   /note="WD 3"
FT   REPEAT          199..238
FT                   /note="WD 4"
FT   REPEAT          246..287
FT                   /note="WD 5"
FT   REPEAT          298..328
FT                   /note="WD 6"
SQ   SEQUENCE   329 AA;  37122 MW;  5453C193A5C0AEEC CRC64;
     MTTVSINKPN LLKFKHVKSF QPQEKDCGPV TSLNFDDNGQ FLLTSSSNDT MQLYSATNCK
     FLDTIASKKY GCHSAIFTHA QNECIYSSTM KNFDIKYLNL ETNQYLRYFS GHGALVNDLK
     MNPVNDTFLS SSYDESVRLW DLKISKPQVI IPSLVPNCIA YDPSGLVFAL GNPENFEIGL
     YNLKKIQEGP FLIIKINDAT FSQWNKLEFS NNGKYLLVGS SIGKHLIFDA FTGQQLFELI
     GTRAFPMREF LDSGSACFTP DGEFVLGTDY DGRIAIWNHS DSISNKVLRP QGFIPCVSHE
     TCPRSIAFNP KYSMFVTADE TVDFYVYDE
 
 
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