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Database: UniProt
Entry: P38890
LinkDB: P38890
Original site: P38890 
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   13-FEB-2019, entry version 142.
DE   RecName: Full=Putative protein lysine methyltransferase SET5;
DE            EC=2.1.1.-;
DE   AltName: Full=SET domain-containing protein 5;
GN   Name=SET5; OrderedLocusNames=YHR207C;
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   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.,
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   [6]
RP   FUNCTION.
RX   PubMed=14671320; DOI=10.1073/pnas.2536857100;
RA   Kushner D.B., Lindenbach B.D., Grdzelishvili V.Z., Noueiry A.O.,
RA   Paul S.M., Ahlquist P.;
RT   "Systematic, genome-wide identification of host genes affecting
RT   replication 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
RT   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
RP   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
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Putative protein lysine methyltransferase that acts as a
CC       virus host factor involved in the replication of positive-strand
CC       RNA viruses like the MBV. {ECO:0000269|PubMed:14671320}.
CC   -!- INTERACTION:
CC       P02309:HHF2; NbExp=3; IntAct=EBI-24263, EBI-8113;
CC       P61830:HHT2; NbExp=2; IntAct=EBI-24263, EBI-8098;
CC       P62805:HIST2H4B (xeno); NbExp=2; IntAct=EBI-24263, EBI-302023;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC       Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 5000 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. Histone-lysine methyltransferase
CC       family. SET5 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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   ProteinModelPortal; P38890; -.
DR   BioGrid; 36641; 59.
DR   DIP; DIP-2725N; -.
DR   IntAct; P38890; 16.
DR   MINT; P38890; -.
DR   STRING; 4932.YHR207C; -.
DR   iPTMnet; P38890; -.
DR   MaxQB; P38890; -.
DR   PaxDb; P38890; -.
DR   PRIDE; P38890; -.
DR   EnsemblFungi; YHR207C_mRNA; YHR207C_mRNA; YHR207C.
DR   GeneID; 856614; -.
DR   KEGG; sce:YHR207C; -.
DR   EuPathDB; FungiDB:YHR207C; -.
DR   SGD; S000001250; SET5.
DR   HOGENOM; HOG000074714; -.
DR   InParanoid; P38890; -.
DR   KO; K07117; -.
DR   OMA; WSVSEKR; -.
DR   BioCyc; YEAST:G3O-31233-MONOMER; -.
DR   PRO; PR:P38890; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:SGD.
DR   GO; GO:0034968; P:histone lysine methylation; IDA:SGD.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Methyltransferase; Nucleus;
KW   Phosphoprotein; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN         1    526       Putative protein lysine methyltransferase
FT                                SET5.
FT                                /FTId=PRO_0000202942.
FT   DOMAIN      112    403       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   MOD_RES     517    517       Phosphoserine.
FT                                {ECO:0000244|PubMed:18407956}.
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
//
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