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Histone-lysine N-methyltransferase pr-set7 (EC 2.1.1.43) (Lysine N-methyltransferase 5A) (PR/SET domain-containing protein 07) (dSET8)

 KMT5A_DROME             Reviewed;         691 AA.
Q9VFK6; Q53ZQ8;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 2.
25-OCT-2017, entry version 146.
RecName: Full=Histone-lysine N-methyltransferase pr-set7;
EC=2.1.1.43;
AltName: Full=Lysine N-methyltransferase 5A;
AltName: Full=PR/SET domain-containing protein 07;
AltName: Full=dSET8;
Name=pr-set7; Synonyms=KMT5A; ORFNames=CG3307;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12086618; DOI=10.1016/S1097-2765(02)00548-8;
Nishioka K., Rice J.C., Sarma K., Erdjument-Bromage H., Werner J.,
Wang Y., Chuikov S., Valenzuela P., Tempst P., Steward R., Lis J.T.,
Allis C.D., Reinberg D.;
"PR-Set7 is a nucleosome-specific methyltransferase that modifies
lysine 20 of histone H4 and is associated with silent chromatin.";
Mol. Cell 9:1201-1213(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12121615; DOI=10.1016/S0960-9822(02)00924-7;
Fang J., Feng Q., Ketel C.S., Wang H., Cao R., Xia L.,
Erdjument-Bromage H., Tempst P., Simon J.A., Zhang Y.;
"Purification and functional characterization of SET8, a nucleosomal
histone H4-lysine 20-specific methyltransferase.";
Curr. Biol. 12:1086-1099(2002).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=15681608; DOI=10.1101/gad.1263005;
Karachentsev D., Sarma K., Reinberg D., Steward R.;
"PR-Set7-dependent methylation of histone H4 Lys 20 functions in
repression of gene expression and is essential for mitosis.";
Genes Dev. 19:431-435(2005).
[7]
FUNCTION.
PubMed=17227890; DOI=10.1083/jcb.200607178;
Sakaguchi A., Steward R.;
"Aberrant monomethylation of histone H4 lysine 20 activates the DNA
damage checkpoint in Drosophila melanogaster.";
J. Cell Biol. 176:155-162(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195; SER-250; THR-252;
SER-281; THR-344; SER-346; SER-383; SER-388 AND SER-392, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: Histone methyltransferase that specifically
monomethylates 'Lys-20' of histone H4. H4 'Lys-20' monomethylation
is enriched during mitosis and represents a specific tag for
epigenetic transcriptional repression. Mainly functions in
euchromatin regions, thereby playing a central role in the
silencing of euchromatic genes. Required for cell proliferation,
possibly by contributing to the maintenance of proper higher-order
structure of DNA and chromosome condensation during mitosis.
{ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:12121615,
ECO:0000269|PubMed:15681608, ECO:0000269|PubMed:17227890}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000255|PROSITE-ProRule:PRU00904}.
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Specifically
localizes to mitotic chromosomes. Associates to chromatin-dense
and transcriptionally silent euchromatic regions.
-!- DEVELOPMENTAL STAGE: Present in ovary, early embryos and
throughout the development (at protein level). Deposed in the egg
during oogenesis. {ECO:0000269|PubMed:15681608}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. PR/SET subfamily. {ECO:0000255|PROSITE-ProRule:PRU00904}.
-----------------------------------------------------------------------
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EMBL; AY283060; AAP35083.1; -; mRNA.
EMBL; AE014297; AAF55047.2; -; Genomic_DNA.
EMBL; AE014297; AAN13605.1; -; Genomic_DNA.
EMBL; AE014297; AAN13606.1; -; Genomic_DNA.
EMBL; AY102673; AAM27502.1; -; mRNA.
RefSeq; NP_001247100.1; NM_001260171.2.
RefSeq; NP_650354.1; NM_142097.4.
RefSeq; NP_731900.1; NM_169577.3.
UniGene; Dm.36781; -.
ProteinModelPortal; Q9VFK6; -.
SMR; Q9VFK6; -.
BioGrid; 66819; 9.
IntAct; Q9VFK6; 1.
STRING; 7227.FBpp0082387; -.
BindingDB; Q9VFK6; -.
ChEMBL; CHEMBL2169717; -.
iPTMnet; Q9VFK6; -.
PaxDb; Q9VFK6; -.
PRIDE; Q9VFK6; -.
EnsemblMetazoa; FBtr0082929; FBpp0082388; FBgn0011474.
EnsemblMetazoa; FBtr0082930; FBpp0082389; FBgn0011474.
EnsemblMetazoa; FBtr0309996; FBpp0301702; FBgn0011474.
GeneID; 41743; -.
KEGG; dme:Dmel_CG3307; -.
UCSC; CG3307-RA; d. melanogaster.
CTD; 41743; -.
FlyBase; FBgn0011474; pr-set7.
eggNOG; KOG1085; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00410000025501; -.
HOGENOM; HOG000106485; -.
InParanoid; Q9VFK6; -.
KO; K11428; -.
OMA; HRILCPS; -.
OrthoDB; EOG091G0UBI; -.
PhylomeDB; Q9VFK6; -.
Reactome; R-DME-3214841; PKMTs methylate histone lysines.
GenomeRNAi; 41743; -.
PRO; PR:Q9VFK6; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0011474; -.
ExpressionAtlas; Q9VFK6; differential.
Genevisible; Q9VFK6; DM.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IMP:FlyBase.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0030261; P:chromosome condensation; IDA:FlyBase.
GO; GO:0000077; P:DNA damage checkpoint; IDA:FlyBase.
GO; GO:0034771; P:histone H4-K20 monomethylation; IMP:FlyBase.
GO; GO:0016571; P:histone methylation; IMP:FlyBase.
GO; GO:0035067; P:negative regulation of histone acetylation; TAS:FlyBase.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR016858; Hist_H4-K20_MeTrfase.
InterPro; IPR001214; SET_dom.
Pfam; PF00856; SET; 1.
SMART; SM00317; SET; 1.
PROSITE; PS51571; SAM_MT43_PR_SET; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
Cell cycle; Cell division; Chromatin regulator; Chromosome;
Complete proteome; Methyltransferase; Mitosis; Nucleus;
Phosphoprotein; Reference proteome; Repressor;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase.
CHAIN 1 691 Histone-lysine N-methyltransferase pr-
set7.
/FTId=PRO_0000186082.
DOMAIN 555 676 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
REGION 565 567 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00904}.
REGION 637 638 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00904}.
COMPBIAS 414 437 Gln-rich.
COMPBIAS 438 456 Asp-rich.
BINDING 610 610 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190,
ECO:0000255|PROSITE-ProRule:PRU00904}.
MOD_RES 195 195 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 250 250 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 252 252 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 281 281 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 344 344 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 346 346 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 383 383 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 388 388 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 392 392 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
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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