GenomeNet

Database: UniProt
Entry: Q9VFK6
LinkDB: Q9VFK6
Original site: Q9VFK6 
ID   KMT5A_DROME             Reviewed;         691 AA.
AC   Q9VFK6; Q53ZQ8;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   16-JAN-2019, entry version 154.
DE   RecName: Full=Histone-lysine N-methyltransferase PR-Set7 {ECO:0000303|PubMed:12086618};
DE            EC=2.1.1.43;
DE   AltName: Full=Lysine N-methyltransferase 5A;
DE   AltName: Full=PR/SET domain-containing protein 07;
DE   AltName: Full=dSET8 {ECO:0000303|PubMed:12121615};
GN   Name=PR-Set7 {ECO:0000303|PubMed:12086618,
GN   ECO:0000312|FlyBase:FBgn0011474}; Synonyms=KMT5A;
GN   ORFNames=CG3307 {ECO:0000312|FlyBase:FBgn0011474};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12086618; DOI=10.1016/S1097-2765(02)00548-8;
RA   Nishioka K., Rice J.C., Sarma K., Erdjument-Bromage H., Werner J.,
RA   Wang Y., Chuikov S., Valenzuela P., Tempst P., Steward R., Lis J.T.,
RA   Allis C.D., Reinberg D.;
RT   "PR-Set7 is a nucleosome-specific methyltransferase that modifies
RT   lysine 20 of histone H4 and is associated with silent chromatin.";
RL   Mol. Cell 9:1201-1213(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12121615; DOI=10.1016/S0960-9822(02)00924-7;
RA   Fang J., Feng Q., Ketel C.S., Wang H., Cao R., Xia L.,
RA   Erdjument-Bromage H., Tempst P., Simon J.A., Zhang Y.;
RT   "Purification and functional characterization of SET8, a nucleosomal
RT   histone H4-lysine 20-specific methyltransferase.";
RL   Curr. Biol. 12:1086-1099(2002).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=15681608; DOI=10.1101/gad.1263005;
RA   Karachentsev D., Sarma K., Reinberg D., Steward R.;
RT   "PR-Set7-dependent methylation of histone H4 Lys 20 functions in
RT   repression of gene expression and is essential for mitosis.";
RL   Genes Dev. 19:431-435(2005).
RN   [7]
RP   FUNCTION.
RX   PubMed=17227890; DOI=10.1083/jcb.200607178;
RA   Sakaguchi A., Steward R.;
RT   "Aberrant monomethylation of histone H4 lysine 20 activates the DNA
RT   damage checkpoint in Drosophila melanogaster.";
RL   J. Cell Biol. 176:155-162(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195; SER-250; THR-252;
RP   SER-281; THR-344; SER-346; SER-383; SER-388 AND SER-392, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       monomethylates 'Lys-20' of histone H4. H4 'Lys-20' monomethylation
CC       is enriched during mitosis and represents a specific tag for
CC       epigenetic transcriptional repression. Mainly functions in
CC       euchromatin regions, thereby playing a central role in the
CC       silencing of euchromatic genes. Required for cell proliferation,
CC       possibly by contributing to the maintenance of proper higher-order
CC       structure of DNA and chromosome condensation during mitosis.
CC       {ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:12121615,
CC       ECO:0000269|PubMed:15681608, ECO:0000269|PubMed:17227890}.
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:0000255|PROSITE-ProRule:PRU00904};
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Specifically
CC       localizes to mitotic chromosomes. Associates to chromatin-dense
CC       and transcriptionally silent euchromatic regions.
CC   -!- DEVELOPMENTAL STAGE: Present in ovary, early embryos and
CC       throughout the development (at protein level). Deposed in the egg
CC       during oogenesis. {ECO:0000269|PubMed:15681608}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. PR/SET subfamily. {ECO:0000255|PROSITE-ProRule:PRU00904}.
DR   EMBL; AY283060; AAP35083.1; -; mRNA.
DR   EMBL; AE014297; AAF55047.2; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13605.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13606.1; -; Genomic_DNA.
DR   EMBL; AY102673; AAM27502.1; -; mRNA.
DR   RefSeq; NP_001247100.1; NM_001260171.2.
DR   RefSeq; NP_650354.1; NM_142097.4.
DR   RefSeq; NP_731900.1; NM_169577.3.
DR   UniGene; Dm.36781; -.
DR   ProteinModelPortal; Q9VFK6; -.
DR   SMR; Q9VFK6; -.
DR   BioGrid; 66819; 11.
DR   IntAct; Q9VFK6; 1.
DR   MINT; Q9VFK6; -.
DR   STRING; 7227.FBpp0082387; -.
DR   BindingDB; Q9VFK6; -.
DR   ChEMBL; CHEMBL2169717; -.
DR   iPTMnet; Q9VFK6; -.
DR   PaxDb; Q9VFK6; -.
DR   PRIDE; Q9VFK6; -.
DR   EnsemblMetazoa; FBtr0082929; FBpp0082388; FBgn0011474.
DR   EnsemblMetazoa; FBtr0082930; FBpp0082389; FBgn0011474.
DR   EnsemblMetazoa; FBtr0309996; FBpp0301702; FBgn0011474.
DR   GeneID; 41743; -.
DR   KEGG; dme:Dmel_CG3307; -.
DR   UCSC; CG3307-RA; d. melanogaster.
DR   CTD; 41743; -.
DR   FlyBase; FBgn0011474; PR-Set7.
DR   eggNOG; KOG1085; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000163293; -.
DR   HOGENOM; HOG000106485; -.
DR   InParanoid; Q9VFK6; -.
DR   KO; K11428; -.
DR   OMA; HRILCPS; -.
DR   OrthoDB; 362367at2759; -.
DR   PhylomeDB; Q9VFK6; -.
DR   Reactome; R-DME-3214841; PKMTs methylate histone lysines.
DR   GenomeRNAi; 41743; -.
DR   PRO; PR:Q9VFK6; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0011474; Expressed in 44 organ(s), highest expression level in embryo.
DR   ExpressionAtlas; Q9VFK6; baseline and differential.
DR   Genevisible; Q9VFK6; DM.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR   GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IMP:FlyBase.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0030261; P:chromosome condensation; IDA:FlyBase.
DR   GO; GO:0000077; P:DNA damage checkpoint; IDA:FlyBase.
DR   GO; GO:0034771; P:histone H4-K20 monomethylation; IMP:FlyBase.
DR   GO; GO:0016571; P:histone methylation; IMP:FlyBase.
DR   GO; GO:0035067; P:negative regulation of histone acetylation; TAS:FlyBase.
DR   InterPro; IPR016858; Hist_H4-K20_MeTrfase.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS51571; SAM_MT43_PR_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Chromatin regulator; Chromosome;
KW   Complete proteome; Methyltransferase; Mitosis; Nucleus;
KW   Phosphoprotein; Reference proteome; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase.
FT   CHAIN         1    691       Histone-lysine N-methyltransferase PR-
FT                                Set7.
FT                                /FTId=PRO_0000186082.
FT   DOMAIN      555    676       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      565    567       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00904}.
FT   REGION      637    638       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00904}.
FT   COMPBIAS    414    437       Gln-rich.
FT   COMPBIAS    438    456       Asp-rich.
FT   BINDING     610    610       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190,
FT                                ECO:0000255|PROSITE-ProRule:PRU00904}.
FT   MOD_RES     195    195       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     250    250       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     252    252       Phosphothreonine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     281    281       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     344    344       Phosphothreonine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     346    346       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     383    383       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     388    388       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     392    392       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
SQ   SEQUENCE   691 AA;  76493 MW;  3462A761ED44A2D1 CRC64;
     MIMVRRRQRP AKEAASSSSG GASSGSGIPV DQALPLNVAG NLLEDQYFAS PKRKDCRLMK
     VTQNGQLPEA TMMAHNKDNK AGRTIGVPLA TRSQTRTIEN FFKANAAAKD SQKTIHTEEQ
     LNLGNQELKL DDEELNGQIK LDDEVLKLAD KQINENLPFA DEVDAKAEQK LMDEELQQVV
     EELLFDGSSR ASSNSPFYQH DMDVMQEIQQ TPEIPHIKKV TEPLEGLGSL ADFQTHRSAL
     RDSHSSTHSS STDNIFLQEP VLTLDIDRTP TKASSIKINR SFELAGAVFS SPPSVLNACL
     NGRFNQIVSL NGQKEALDLP HFDLDQHDSS SCDSGVACGL TANTESPAGQ PRRRKPATPH
     RILCPSPIKT ALKVTGGICK VGSADPLSPR KSPRKLPTTT AAVAACKSRR RLNQPKPQAP
     YQPQLQKPPS QQQQQQQDDI VVVLDDDDDE GDDEDDVRAL IKAAEERENQ NKAPATANSN
     KAGMKTMLKP APVKSKTKSK GPTKGQPPLP LAATNGNREM TDFFPVRRSV RKTKTAVKEE
     WMRGLEQAVL EERCDGLQVR HFMGKGRGVV ADRPFKRNEF VVEYVGDLIS IGEAAEREKR
     YALDENAGCY MYYFKHKSQQ YCIDATVDTG KLGRLINHSR AGNLMTKVVL IKQRPHLVLL
     AKDDIEPGEE LTYDYGDRSK ESLLHHPWLA F
//
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