SET5_YEAST
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 03-AUG-2022, entry version 159.
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; 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).
CC -!- FUNCTION: Putative protein lysine methyltransferase that acts as a
CC virus host factor involved in the replication of positive-strand RNA
CC viruses like the MBV. {ECO:0000269|PubMed:14671320}.
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: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
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; 60.
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; YHR207C.
DR GeneID; 856614; -.
DR KEGG; sce:YHR207C; -.
DR SGD; S000001250; SET5.
DR VEuPathDB; FungiDB:YHR207C; -.
DR eggNOG; KOG2084; Eukaryota.
DR HOGENOM; CLU_031650_0_0_1; -.
DR InParanoid; P38890; -.
DR OMA; TYVNPLH; -.
DR BioCyc; YEAST:G3O-31233-MON; -.
DR Reactome; R-SCE-3214841; PKMTs methylate histone lysines.
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:0018024; F:histone-lysine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:SGD.
DR GO; GO:0034968; P:histone lysine methylation; IDA:SGD.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..526
FT /note="Putative protein lysine 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"
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
