ID   SET5_YEAST              Reviewed;         526 AA.
AC   P38890; D3DLF6;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Histone-lysine N-methyltransferase SET5;
DE            EC=2.1.1.- {ECO:0000269|PubMed:22343720};
DE   AltName: Full=SET domain-containing protein 5;
GN   Name=SET5 {ECO:0000303|PubMed:22343720, ECO:0000312|SGD:S000001250};
GN   OrderedLocusNames=YHR207C;
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=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., 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., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   DOMAIN.
RX   PubMed=9171100; DOI=10.1093/nar/25.12.2464;
RA   Boehm S., Frishman D., Mewes H.-W.;
RT   "Variations of the C2H2 zinc finger motif in the yeast genome and
RT   classification of yeast zinc finger proteins.";
RL   Nucleic Acids Res. 25:2464-2469(1997).
RN   [4]
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   [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   FUNCTION.
RX   PubMed=14671320; DOI=10.1073/pnas.2536857100;
RA   Kushner D.B., Lindenbach B.D., Grdzelishvili V.Z., Noueiry A.O., Paul S.M.,
RA   Ahlquist P.;
RT   "Systematic, genome-wide identification of host genes affecting replication
RT   of a positive-strand RNA virus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:15764-15769(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, AND IDENTIFICATION BY
RP   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   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   TYR-402.
RX   PubMed=22343720; DOI=10.1038/nsmb.2252;
RA   Green E.M., Mas G., Young N.L., Garcia B.A., Gozani O.;
RT   "Methylation of H4 lysines 5, 8 and 12 by yeast Set5 calibrates chromatin
RT   stress responses.";
RL   Nat. Struct. Mol. Biol. 19:361-363(2012).
CC   -!- FUNCTION: Histone methyltransferase that monomethylates 'Lys-5', 'Lys-
CC       8' and 'Lys-12' of histone H4 (H4K5me1, H4K8me1 and H4K12me1,
CC       respectively), thereby controlling gene expression and remodeling
CC       chromatin structures (PubMed:22343720). Functions together with the
CC       chromatin-modifying complexes COMPASS and NuA4 to regulate cell growth
CC       and stress responses (PubMed:22343720). {ECO:0000269|PubMed:22343720}.
CC   -!- FUNCTION: (Microbial infection) Acts as a virus host factor involved in
CC       the replication of positive-strand RNA viruses like the MBV.
CC       {ECO:0000269|PubMed:14671320}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-
CC         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;
CC         Evidence={ECO:0000269|PubMed:22343720};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10025;
CC         Evidence={ECO:0000269|PubMed:22343720};
CC   -!- INTERACTION:
CC       P38890; P02309: HHF2; NbExp=3; IntAct=EBI-24263, EBI-8113;
CC       P38890; P61830: HHT2; NbExp=2; IntAct=EBI-24263, EBI-8098;
CC       P38890; P62805: H4C9; Xeno; NbExp=2; IntAct=EBI-24263, EBI-302023;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:22343720}. Chromosome {ECO:0000269|PubMed:22343720}.
CC       Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22343720}.
CC   -!- MISCELLANEOUS: Present with 5000 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. Histone-lysine methyltransferase family. SET5 subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR   EMBL; U00029; AAB69736.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06900.1; -; Genomic_DNA.
DR   PIR; S48988; S48988.
DR   RefSeq; NP_012077.1; NM_001179338.1.
DR   AlphaFoldDB; P38890; -.
DR   BioGRID; 36641; 63.
DR   DIP; DIP-2725N; -.
DR   IntAct; P38890; 16.
DR   MINT; P38890; -.
DR   STRING; 4932.YHR207C; -.
DR   iPTMnet; P38890; -.
DR   MaxQB; P38890; -.
DR   PaxDb; 4932-YHR207C; -.
DR   PeptideAtlas; P38890; -.
DR   EnsemblFungi; YHR207C_mRNA; YHR207C; YHR207C.
DR   GeneID; 856614; -.
DR   KEGG; sce:YHR207C; -.
DR   AGR; SGD:S000001250; -.
DR   SGD; S000001250; SET5.
DR   VEuPathDB; FungiDB:YHR207C; -.
DR   eggNOG; KOG2084; Eukaryota.
DR   HOGENOM; CLU_031650_0_0_1; -.
DR   InParanoid; P38890; -.
DR   OMA; CEPNVRY; -.
DR   OrthoDB; 56553at2759; -.
DR   BioCyc; YEAST:G3O-31233-MONOMER; -.
DR   BioGRID-ORCS; 856614; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P38890; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38890; Protein.
DR   GO; GO:0000785; C:chromatin; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:SGD.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR   CDD; cd20071; SET_SMYD; 1.
DR   Gene3D; 1.10.220.160; -; 1.
DR   Gene3D; 6.10.140.2220; -; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   PANTHER; PTHR46402:SF2; HISTONE-LYSINE N-TRIMETHYLTRANSFERASE SMYD5; 1.
DR   PANTHER; PTHR46402; SET AND MYND DOMAIN-CONTAINING PROTEIN 5; 1.
DR   Pfam; PF00856; SET; 2.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Chromosome; Cytoplasm; Methyltransferase; Nucleus; Phosphoprotein;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..526
FT                   /note="Histone-lysine N-methyltransferase SET5"
FT                   /id="PRO_0000202942"
FT   DOMAIN          112..403
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   REGION          450..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         517
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MUTAGEN         402
FT                   /note="Y->A: Abolished histone methyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:22343720"
SQ   SEQUENCE   526 AA;  60547 MW;  1113CB9C5223DC7D CRC64;
     MTLTIKIGTL NDSDQSAVHN GTENGSDFRK ITPTEEEICD DVVLLWKEEP GTEDATIQHL
     YDRITERNQS WKLSASRFRK ILNEHHLYDT DLETVSLYKD KIHFPKALDS DAKVEVKFID
     DEHGRGLFAK RDFSKGQIIL KENKPIVYIP PLDKLFLISN GKACARCGKA LYDLTQHKIM
     VHYLDCEVCK AIWCSEKCKK AHASLHELLY HSWRSNRIDI LHAGNWKRFV NYCEKYCFTA
     AFSVGLIYGS MLLDTTGEVK EQWQKLASIS QRERIKLRDA SGIGSTFSLL NGTTVHTEEE
     SDNGTKKGVE KNIDDETVWE KCYELFCGAF PKASEEIDFE KFLTMIGTFN INQYNGQVYH
     WISFINHDCE PNAYIEQVEE HEELRLHARK PIKKGEQIRI TYVNPLHGVR LRRRELRVNW
     GFLCQCDRCQ NELSTFERVP NLEKKNADAN LGVEKIDSND SSEDGSKKST GNRKSSMREA
     QPDLKEILKN GKEFELDIPE TVDTQGNVRK TSVRFDSNVS VAVDER
//