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Database: UniProt
Entry: P38827
LinkDB: P38827
Original site: P38827 
ID   SET1_YEAST              Reviewed;        1080 AA.
AC   P38827; D3DL69;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   13-FEB-2019, entry version 175.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific;
DE            EC=2.1.1.43;
DE   AltName: Full=COMPASS component SET1;
DE   AltName: Full=Lysine N-methyltransferase 2;
DE   AltName: Full=SET domain-containing protein 1;
GN   Name=SET1; Synonyms=KMT2, YTX1; OrderedLocusNames=YHR119W;
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=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J.,
RA   Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J.,
RA   Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y.,
RA   Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L.,
RA   Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K.,
RA   Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R.,
RA   Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(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   FUNCTION.
RX   PubMed=9398665; DOI=10.1091/mbc.8.12.2421;
RA   Nislow C., Ray E., Pillus L.;
RT   "SET1, a yeast member of the Trithorax family, functions in
RT   transcriptional silencing and diverse cellular processes.";
RL   Mol. Biol. Cell 8:2421-2436(1997).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH MEC3.
RX   PubMed=9988274; DOI=10.1038/5991;
RA   Corda Y., Schramke V., Longhese M.P., Smokvina T., Paciotti V.,
RA   Brevet V., Gilson E., Geli V.;
RT   "Interaction between Set1p and checkpoint protein Mec3p in DNA repair
RT   and telomere functions.";
RL   Nat. Genet. 21:204-208(1999).
RN   [5]
RP   IDENTIFICATION IN THE SET1 COMPLEX, AND FUNCTION OF THE SET1 COMPLEX.
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
RT   and methylates histone 3 lysine 4.";
RL   EMBO J. 20:7137-7148(2001).
RN   [6]
RP   FUNCTION.
RX   PubMed=11751634; DOI=10.1101/gad.940201;
RA   Briggs S.D., Bryk M., Strahl B.D., Cheung W.L., Davie J.K.,
RA   Dent S.Y.R., Winston F., Allis C.D.;
RT   "Histone H3 lysine 4 methylation is mediated by Set1 and required for
RT   cell growth and rDNA silencing in Saccharomyces cerevisiae.";
RL   Genes Dev. 15:3286-3295(2001).
RN   [7]
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
RT   SET domain protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12902-12907(2001).
RN   [8]
RP   FUNCTION.
RX   PubMed=11818070; DOI=10.1016/S0960-9822(01)00652-2;
RA   Bryk M., Briggs S.D., Strahl B.D., Curcio M.J., Allis C.D.,
RA   Winston F.;
RT   "Evidence that Set1, a factor required for methylation of histone H3,
RT   regulates rDNA silencing in S. cerevisiae by a Sir2-independent
RT   mechanism.";
RL   Curr. Biol. 12:165-170(2002).
RN   [9]
RP   ENZYME ACTIVITY, AND 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
RT   telomeric silencing of gene expression.";
RL   J. Biol. Chem. 277:10753-10755(2002).
RN   [10]
RP   FUNCTION.
RX   PubMed=12353038; DOI=10.1038/nature01080;
RA   Santos-Rosa H., Schneider R., Bannister A.J., Sherriff J.,
RA   Bernstein B.E., Emre N.C.T., Schreiber S.L., Mellor J., Kouzarides T.;
RT   "Active genes are tri-methylated at K4 of histone H3.";
RL   Nature 419:407-411(2002).
RN   [11]
RP   IDENTIFICATION IN THE SET1 COMPLEX, AND FUNCTION OF THE SET1 COMPLEX.
RX   PubMed=11752412; DOI=10.1073/pnas.221596698;
RA   Nagy P.L., Griesenbeck J., Kornberg R.D., Cleary M.L.;
RT   "A trithorax-group complex purified from Saccharomyces cerevisiae is
RT   required for methylation of histone H3.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:90-94(2002).
RN   [12]
RP   FUNCTION.
RX   PubMed=12060701; DOI=10.1073/pnas.082249499;
RA   Bernstein B.E., Humphrey E.L., Erlich R.L., Schneider R., Bouman P.,
RA   Liu J.S., Kouzarides T., Schreiber S.L.;
RT   "Methylation of histone H3 Lys 4 in coding regions of active genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:8695-8700(2002).
RN   [13]
RP   FUNCTION.
RX   PubMed=14636589; DOI=10.1016/S1097-2765(03)00438-6;
RA   Santos-Rosa H., Schneider R., Bernstein B.E., Karabetsou N.,
RA   Morillon A., Weise C., Schreiber S.L., Mellor J., Kouzarides T.;
RT   "Methylation of histone H3 K4 mediates association of the Isw1p ATPase
RT   with chromatin.";
RL   Mol. Cell 12:1325-1332(2003).
RN   [14]
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   [15]
RP   FUNCTION.
RX   PubMed=12845608; DOI=10.1002/yea.995;
RA   Boa S., Coert C., Patterton H.-G.;
RT   "Saccharomyces cerevisiae Set1p is a methyltransferase specific for
RT   lysine 4 of histone H3 and is required for efficient gene
RT   expression.";
RL   Yeast 20:827-835(2003).
RN   [16]
RP   FUNCTION OF THE COMPASS COMPLEX.
RX   PubMed=15949446; DOI=10.1016/j.molcel.2005.05.009;
RA   Morillon A., Karabetsou N., Nair A., Mellor J.;
RT   "Dynamic lysine methylation on histone H3 defines the regulatory phase
RT   of gene transcription.";
RL   Mol. Cell 18:723-734(2005).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-625, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-625 AND THR-875, 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
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Catalytic component of the COMPASS (Set1C) complex that
CC       specifically mono-, di- and trimethylates histone H3 to form
CC       H3K4me1/2/3, which subsequently plays a role in telomere length
CC       maintenance and transcription elongation regulation.
CC       {ECO:0000269|PubMed:11742990, ECO:0000269|PubMed:11751634,
CC       ECO:0000269|PubMed:11752412, ECO:0000269|PubMed:11805083,
CC       ECO:0000269|PubMed:11818070, ECO:0000269|PubMed:12060701,
CC       ECO:0000269|PubMed:12353038, ECO:0000269|PubMed:12845608,
CC       ECO:0000269|PubMed:14636589, ECO:0000269|PubMed:15949446,
CC       ECO:0000269|PubMed:9398665, ECO:0000269|PubMed:9988274}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000269|PubMed:11805083};
CC   -!- SUBUNIT: Component of the COMPASS (Set1C) complex which consists
CC       of SET1(2), BRE2(2), SPP1(2), SDC1(1), SHG1(1), SWD1(1), SWD2(1),
CC       and SWD3(1). Interacts with MEC3. {ECO:0000269|PubMed:11687631,
CC       ECO:0000269|PubMed:11742990, ECO:0000269|PubMed:11752412,
CC       ECO:0000269|PubMed:9988274}.
CC   -!- INTERACTION:
CC       P43132:BRE2; NbExp=7; IntAct=EBI-16977, EBI-27115;
CC       Q02574:MEC3; NbExp=3; IntAct=EBI-16977, EBI-10658;
CC       P38337:SHG1; NbExp=5; IntAct=EBI-16977, EBI-21106;
CC       P0CS90:SSC1; NbExp=2; IntAct=EBI-16977, EBI-8637;
CC       P36104:SWD2; NbExp=6; IntAct=EBI-16977, EBI-26608;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 172 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; U00059; AAB68867.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06813.1; -; Genomic_DNA.
DR   PIR; S48961; S48961.
DR   RefSeq; NP_011987.1; NM_001179249.1.
DR   PDB; 2J8A; X-ray; 3.00 A; A=247-375.
DR   PDBsum; 2J8A; -.
DR   ProteinModelPortal; P38827; -.
DR   SMR; P38827; -.
DR   BioGrid; 36552; 452.
DR   ComplexPortal; CPX-1039; COMPASS complex.
DR   DIP; DIP-4616N; -.
DR   ELM; P38827; -.
DR   IntAct; P38827; 36.
DR   MINT; P38827; -.
DR   STRING; 4932.YHR119W; -.
DR   iPTMnet; P38827; -.
DR   MaxQB; P38827; -.
DR   PaxDb; P38827; -.
DR   PRIDE; P38827; -.
DR   EnsemblFungi; YHR119W_mRNA; YHR119W_mRNA; YHR119W.
DR   GeneID; 856519; -.
DR   KEGG; sce:YHR119W; -.
DR   EuPathDB; FungiDB:YHR119W; -.
DR   SGD; S000001161; SET1.
DR   GeneTree; ENSGT00940000169211; -.
DR   HOGENOM; HOG000066111; -.
DR   InParanoid; P38827; -.
DR   KO; K11422; -.
DR   OMA; PSCTAKI; -.
DR   BioCyc; YEAST:G3O-31161-MONOMER; -.
DR   Reactome; R-SCE-3214841; PKMTs methylate histone lysines.
DR   EvolutionaryTrace; P38827; -.
DR   PRO; PR:P38827; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   GO; GO:0000781; C:chromosome, telomeric region; IGI:ARUK-UCL.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IPI:SGD.
DR   GO; GO:0042054; F:histone methyltransferase activity; ISS:SGD.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IMP:SGD.
DR   GO; GO:0003723; F:RNA binding; IDA:SGD.
DR   GO; GO:0030437; P:ascospore formation; IMP:SGD.
DR   GO; GO:0030466; P:chromatin silencing at silent mating-type cassette; IMP:SGD.
DR   GO; GO:0006348; P:chromatin silencing at telomere; IMP:SGD.
DR   GO; GO:0044648; P:histone H3-K4 dimethylation; IMP:CACAO.
DR   GO; GO:0051568; P:histone H3-K4 methylation; IDA:SGD.
DR   GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:CACAO.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; IMP:SGD.
DR   GO; GO:0035066; P:positive regulation of histone acetylation; IGI:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:1902275; P:regulation of chromatin organization; IMP:SGD.
DR   GO; GO:1903341; P:regulation of meiotic DNA double-strand break formation; IMP:SGD.
DR   GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IMP:SGD.
DR   GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR024657; COMPASS_Set1_N-SET.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR017111; Set1.
DR   InterPro; IPR024636; SET_assoc.
DR   InterPro; IPR001214; SET_dom.
DR   PANTHER; PTHR22884:SF462; PTHR22884:SF462; 1.
DR   Pfam; PF11764; N-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF11767; SET_assoc; 1.
DR   PIRSF; PIRSF037104; Histone_H3-K4_mtfrase_Set1_fun; 1.
DR   SMART; SM01291; N-SET; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS51572; SAM_MT43_1; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chromatin regulator; Chromosome; Complete proteome;
KW   Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1   1080       Histone-lysine N-methyltransferase, H3
FT                                lysine-4 specific.
FT                                /FTId=PRO_0000186086.
FT   DOMAIN      938   1055       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1064   1080       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   MOD_RES     625    625       Phosphoserine.
FT                                {ECO:0000244|PubMed:17330950,
FT                                ECO:0000244|PubMed:19779198}.
FT   MOD_RES     875    875       Phosphothreonine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   STRAND      249    258       {ECO:0000244|PDB:2J8A}.
FT   HELIX       265    273       {ECO:0000244|PDB:2J8A}.
FT   STRAND      279    285       {ECO:0000244|PDB:2J8A}.
FT   TURN        287    289       {ECO:0000244|PDB:2J8A}.
FT   STRAND      292    299       {ECO:0000244|PDB:2J8A}.
FT   HELIX       310    320       {ECO:0000244|PDB:2J8A}.
FT   TURN        321    324       {ECO:0000244|PDB:2J8A}.
FT   STRAND      326    328       {ECO:0000244|PDB:2J8A}.
FT   STRAND      331    337       {ECO:0000244|PDB:2J8A}.
FT   HELIX       342    364       {ECO:0000244|PDB:2J8A}.
SQ   SEQUENCE   1080 AA;  123912 MW;  B7FA5D60F71063FD CRC64;
     MSNYYRRAHA SSGSYRQPQE QPQYSRSGHY QYSNGHSHQQ YSSQYNQRRR YNHNDGTRRR
     YNDDRPHSSN NASTRQYYAT NNSQSGPYVN KKSDISSRRG MSQSRYSNSN VHNTLASSSG
     SLPTESALLL QQRPPSVLRY NTDNLKSKFH YFDPIKGEFF NKDKMLSWKA TDKEFSETGY
     YVVKELQDGQ FKFKIKHRHP EIKASDPRNE NGIMTSGKVA THRKCRNSLI LLPRISYDRY
     SLGPPPSCEI VVYPAQDSTT TNIQDISIKN YFKKYGEISH FEAFNDPNSA LPLHVYLIKY
     ASSDGKINDA AKAAFSAVRK HESSGCFIMG FKFEVILNKH SILNNIISKF VEINVKKLQK
     LQENLKKAKE KEAENEKAKE LQGKDITLPK EPKVDTLSHS SGSEKRIPYD LLGVVNNRPV
     LHVSKIFVAK HRFCVEDFKY KLRGYRCAKF IDHPTGIYII FNDIAHAQTC SNAESGNLTI
     MSRSRRIPIL IKFHLILPRF QNRTRFNKSS SSSNSTNVPI KYESKEEFIE ATAKQILKDL
     EKTLHVDIKK RLIGPTVFDA LDHANFPELL AKRELKEKEK RQQIASKIAE DELKRKEEAK
     RDFDLFGLYG GYAKSNKRNL KRHNSLALDH TSLKRKKLSN GIKPMAHLLN EETDSKETTP
     LNDEGITRVS KEHDEEDENM TSSSSEEEEE EAPDKKFKSE SEPTTPESDH LHGIKPLVPD
     QNGSSDVLDA SSMYKPTATE IPEPVYPPEE YDLKYSQTLS SMDLQNAIKD EEDMLILKQL
     LSTYTPTVTP ETSAALEYKI WQSRRKVLEE EKASDWQIEL NGTLFDSELQ PGSSFKAEGF
     RKIADKLKIN YLPHRRRVHQ PLNTVNIHNE RNEYTPELCQ REESSNKEPS DSVPQEVSSS
     RDNRASNRRF QQDIEAQKAA IGTESELLSL NQLNKRKKPV MFARSAIHNW GLYALDSIAA
     KEMIIEYVGE RIRQPVAEMR EKRYLKNGIG SSYLFRVDEN TVIDATKKGG IARFINHCCD
     PNCTAKIIKV GGRRRIVIYA LRDIAASEEL TYDYKFEREK DDEERLPCLC GAPNCKGFLN
//
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