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N-lysine methyltransferase KMT5A (EC 2.1.1.-) (H4-K20-HMTase KMT5A) (Histone-lysine N-methyltransferase KMT5A) (EC 2.1.1.43) (Lysine N-methyltransferase 5A) (Lysine-specific methylase 5A) (PR/SET domain-containing protein 07) (PR-Set7) (PR/SET07) (SET domain-containing protein 8)

 KMT5A_HUMAN             Reviewed;         393 AA.
Q9NQR1; A8K9D0; Q86W83; Q8TD09;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
15-NOV-2002, sequence version 3.
27-SEP-2017, entry version 164.
RecName: Full=N-lysine methyltransferase KMT5A {ECO:0000305};
EC=2.1.1.-;
AltName: Full=H4-K20-HMTase KMT5A;
AltName: Full=Histone-lysine N-methyltransferase KMT5A;
EC=2.1.1.43;
AltName: Full=Lysine N-methyltransferase 5A;
AltName: Full=Lysine-specific methylase 5A {ECO:0000312|HGNC:HGNC:29489};
AltName: Full=PR/SET domain-containing protein 07;
Short=PR-Set7;
Short=PR/SET07;
AltName: Full=SET domain-containing protein 8;
Name=KMT5A {ECO:0000312|HGNC:HGNC:29489};
Synonyms=PRSET7, SET07, SET8, SETD8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 108-131;
220-231 AND 349-393, FUNCTION, SUBCELLULAR LOCATION, CATALYTIC
ACTIVITY, AND MUTAGENESIS OF ARG-336.
TISSUE=Cervix carcinoma;
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 [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 83-103;
109-134; 141-151; 162-172; 221-230; 245-260; 280-297 AND 350-393,
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-340 AND
385-ILE--HIS-393.
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tain F., Huang S.;
"A novel PR/SET domain-containing gene, SET07, as a candidate tumor
suppressor.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=12208845; DOI=10.1101/gad.1014902;
Rice J.C., Nishioka K., Sarma K., Steward R., Reinberg D., Allis C.D.;
"Mitotic-specific methylation of histone H4 Lys 20 follows increased
PR-Set7 expression and its localization to mitotic chromosomes.";
Genes Dev. 16:2225-2230(2002).
[7]
FUNCTION, AND INDUCTION.
PubMed=15200950; DOI=10.1016/j.molcel.2004.06.008;
Julien E., Herr W.;
"A switch in mitotic histone H4 lysine 20 methylation status is linked
to M phase defects upon loss of HCF-1.";
Mol. Cell 14:713-725(2004).
[8]
CATALYTIC ACTIVITY.
PubMed=15964846; DOI=10.1074/jbc.M501691200;
Yin Y., Liu C., Tsai S.N., Zhou B., Ngai S.M., Zhu G.;
"SET8 recognizes the sequence RHRK20VLRDN within the N terminus of
histone H4 and mono-methylates lysine 20.";
J. Biol. Chem. 280:30025-30031(2005).
[9]
FUNCTION.
PubMed=16517599; DOI=10.1074/jbc.M513462200;
Sims J.K., Houston S.I., Magazinnik T., Rice J.C.;
"A trans-tail histone code defined by monomethylated H4 Lys-20 and H3
Lys-9 demarcates distinct regions of silent chromatin.";
J. Biol. Chem. 281:12760-12766(2006).
[10]
FUNCTION, AND MUTAGENESIS OF ASP-379.
PubMed=17707234; DOI=10.1016/j.molcel.2007.07.012;
Shi X., Kachirskaia I., Yamaguchi H., West L.E., Wen H., Wang E.W.,
Dutta S., Appella E., Gozani O.;
"Modulation of p53 function by SET8-mediated methylation at lysine
382.";
Mol. Cell 27:636-646(2007).
[11]
INTERACTION WITH L3MBTL1.
PubMed=18408754; DOI=10.1038/onc.2008.67;
Kalakonda N., Fischle W., Boccuni P., Gurvich N., Hoya-Arias R.,
Zhao X., Miyata Y., Macgrogan D., Zhang J., Sims J.K., Rice J.C.,
Nimer S.D.;
"Histone H4 lysine 20 monomethylation promotes transcriptional
repression by L3MBTL1.";
Oncogene 27:4293-4304(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
MUTAGENESIS OF ASP-379.
PubMed=20870725; DOI=10.1074/jbc.M110.139527;
West L.E., Roy S., Lachmi-Weiner K., Hayashi R., Shi X., Appella E.,
Kutateladze T.G., Gozani O.;
"The MBT repeats of L3MBTL1 link SET8-mediated p53 methylation at
lysine 382 to target gene repression.";
J. Biol. Chem. 285:37725-37732(2010).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
ACETYLATION AT LYS-172, DEACETYLATION AT LYS-172 BY SIRT2, INTERACTION
WITH SIRT2, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-172, AND MASS
SPECTROMETRY (ISOFORM 2).
PubMed=23468428; DOI=10.1101/gad.211342.112;
Serrano L., Martinez-Redondo P., Marazuela-Duque A., Vazquez B.N.,
Dooley S.J., Voigt P., Beck D.B., Kane-Goldsmith N., Tong Q.,
Rabanal R.M., Fondevila D., Munoz P., Kruger M., Tischfield J.A.,
Vaquero A.;
"The tumor suppressor SirT2 regulates cell cycle progression and
genome stability by modulating the mitotic deposition of H4K20
methylation.";
Genes Dev. 27:639-653(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-181, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
FUNCTION, INDUCTION, UBIQUITINATION, AND MUTAGENESIS OF ARG-336 AND
ASP-379.
PubMed=23478445; DOI=10.1016/j.molcel.2013.02.003;
Abbas T., Mueller A.C., Shibata E., Keaton M., Rossi M., Dutta A.;
"CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and
regulates Pr-Set7/Set8-mediated cellular migration.";
Mol. Cell 49:1147-1158(2013).
[18]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 233-393 IN COMPLEX WITH
HISTONE H4 AND S-ADENOSYLMETHIONINE, AND FUNCTION.
PubMed=15933069; DOI=10.1101/gad.1315905;
Xiao B., Jing C., Kelly G., Walker P.A., Muskett F.W., Frenkiel T.A.,
Martin S.R., Sarma K., Reinberg D., Gamblin S.J., Wilson J.R.;
"Specificity and mechanism of the histone methyltransferase Pr-Set7.";
Genes Dev. 19:1444-1454(2005).
[19]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 231-393 IN COMPLEX WITH
HISTONE H4 AND S-ADENOSYLMETHIONINE, FUNCTION, AND MUTAGENESIS OF
TYR-286; GLU-300; CYS-311; TYR-375; ASP-379 AND HIS-388.
PubMed=15933070; DOI=10.1101/gad.1318405;
Couture J.-F., Collazo E., Brunzelle J.S., Trievel R.C.;
"Structural and functional analysis of SET8, a histone H4 'Lys-20'
methyltransferase.";
Genes Dev. 19:1455-1465(2005).
-!- FUNCTION: Protein-lysine N-methyltransferase that monomethylates
both histones and non-histone proteins. Specifically
monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 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,
probably by contributing to the maintenance of proper higher-order
structure of DNA during mitosis. Involved in chromosome
condensation and proper cytokinesis. Nucleosomes are preferred as
substrate compared to free histones. Mediates monomethylation of
p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes.
Plays a negative role in TGF-beta response regulation and a
positive role in cell migration. {ECO:0000269|PubMed:12086618,
ECO:0000269|PubMed:12121615, ECO:0000269|PubMed:15200950,
ECO:0000269|PubMed:15933069, ECO:0000269|PubMed:15933070,
ECO:0000269|PubMed:16517599, ECO:0000269|PubMed:17707234,
ECO:0000269|PubMed:23478445}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000255|PROSITE-ProRule:PRU00904,
ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:12121615,
ECO:0000269|PubMed:15964846}.
-!- SUBUNIT: Interacts with L3MBTL1. Isoform 2 interacts with SIRT2
(phosphorylated form); the interaction is direct, stimulates
KMT5A-mediated methyltransferase activity at histone H4 'Lys-20'
(H4K20me1) and is increased in a H(2)O(2)-induced oxidative
stress-dependent manner. {ECO:0000269|PubMed:15933069,
ECO:0000269|PubMed:15933070, ECO:0000269|PubMed:18408754,
ECO:0000269|PubMed:23468428}.
-!- INTERACTION:
P62805:HIST2H4B; NbExp=5; IntAct=EBI-1268946, EBI-302023;
Q15672:TWIST1; NbExp=5; IntAct=EBI-1268946, EBI-1797287;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Specifically
localizes to mitotic chromosomes. Colocalized with SIRT2 at
mitotic foci. Associates with chromosomes during mitosis;
association is increased in a H(2)O(2)-induced oxidative stress-
dependent manner. Associates with silent chromatin on euchromatic
arms. Not associated with constitutive heterochromatin.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NQR1-1; Sequence=Displayed;
Name=2;
IsoId=Q9NQR1-2; Sequence=VSP_002226, VSP_002227;
-!- DEVELOPMENTAL STAGE: Not detected during G1 phase. First detected
during S through G2 phases, and peaks during mitosis (at protein
level). {ECO:0000269|PubMed:12208845}.
-!- INDUCTION: By HCFC1 C-terminal chain, independently of HCFC1 N-
terminal chain. Transiently induced by TGF-beta and during the
cell cycle. {ECO:0000269|PubMed:15200950,
ECO:0000269|PubMed:23478445}.
-!- DOMAIN: Although the SET domain contains the active site of
enzymatic activity, both sequences upstream and downstream of the
SET domain are required for methyltransferase activity.
-!- PTM: Acetylated at Lys-172; does not change methyltransferase
activity. Deacetylated at Lys-172 by SIRT2; does not change
methyltransferase activity. {ECO:0000269|PubMed:23468428}.
-!- PTM: Ubiquitinated and degraded by the DCX(DTL) complex.
{ECO:0000305|PubMed:23478445}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. PR/SET subfamily. {ECO:0000255|PROSITE-ProRule:PRU00904}.
-!- CAUTION: It is uncertain whether Met-1 or Met-72 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAL40879.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AY064546; AAL40879.1; ALT_INIT; mRNA.
EMBL; AY102937; AAM47033.1; -; mRNA.
EMBL; AF287261; AAF97812.2; -; mRNA.
EMBL; AK292645; BAF85334.1; -; mRNA.
EMBL; BC050346; AAH50346.1; -; mRNA.
CCDS; CCDS9247.1; -. [Q9NQR1-2]
RefSeq; NP_001311433.1; NM_001324504.1.
RefSeq; NP_001311434.1; NM_001324505.1.
RefSeq; NP_001311435.1; NM_001324506.1.
RefSeq; NP_065115.3; NM_020382.4. [Q9NQR1-2]
UniGene; Hs.443735; -.
UniGene; Hs.572262; -.
PDB; 1ZKK; X-ray; 1.45 A; A/B/C/D=231-393.
PDB; 2BQZ; X-ray; 1.50 A; A/E=233-393.
PDB; 3F9W; X-ray; 1.60 A; A/B/C/D=232-393.
PDB; 3F9X; X-ray; 1.25 A; A/B/C/D=232-393.
PDB; 3F9Y; X-ray; 1.50 A; A/B=232-393.
PDB; 3F9Z; X-ray; 1.60 A; A/B/C/D=232-393.
PDB; 4IJ8; X-ray; 2.00 A; A/B=232-393.
PDB; 5HQ2; X-ray; 4.50 A; M=194-393.
PDB; 5T5G; X-ray; 2.10 A; A=234-380.
PDB; 5TEG; X-ray; 1.30 A; A/B=234-393.
PDB; 5TH7; X-ray; 1.95 A; A/B=234-380.
PDB; 5W1Y; X-ray; 1.70 A; A/B=232-393.
PDBsum; 1ZKK; -.
PDBsum; 2BQZ; -.
PDBsum; 3F9W; -.
PDBsum; 3F9X; -.
PDBsum; 3F9Y; -.
PDBsum; 3F9Z; -.
PDBsum; 4IJ8; -.
PDBsum; 5HQ2; -.
PDBsum; 5T5G; -.
PDBsum; 5TEG; -.
PDBsum; 5TH7; -.
PDBsum; 5W1Y; -.
ProteinModelPortal; Q9NQR1; -.
SMR; Q9NQR1; -.
BioGrid; 132490; 22.
DIP; DIP-39133N; -.
IntAct; Q9NQR1; 3.
MINT; MINT-3072203; -.
STRING; 9606.ENSP00000332995; -.
BindingDB; Q9NQR1; -.
ChEMBL; CHEMBL1795176; -.
GuidetoPHARMACOLOGY; 2704; -.
iPTMnet; Q9NQR1; -.
PhosphoSitePlus; Q9NQR1; -.
DMDM; 25091219; -.
MaxQB; Q9NQR1; -.
PaxDb; Q9NQR1; -.
PeptideAtlas; Q9NQR1; -.
PRIDE; Q9NQR1; -.
DNASU; 387893; -.
Ensembl; ENST00000402868; ENSP00000384629; ENSG00000183955. [Q9NQR1-2]
GeneID; 387893; -.
KEGG; hsa:387893; -.
UCSC; uc001uew.4; human. [Q9NQR1-1]
CTD; 387893; -.
DisGeNET; 387893; -.
EuPathDB; HostDB:ENSG00000183955.12; -.
GeneCards; KMT5A; -.
H-InvDB; HIX0037637; -.
HGNC; HGNC:29489; KMT5A.
HPA; HPA064495; -.
MIM; 607240; gene.
neXtProt; NX_Q9NQR1; -.
OpenTargets; ENSG00000183955; -.
PharmGKB; PA143485616; -.
eggNOG; KOG1085; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00410000025501; -.
HOGENOM; HOG000020818; -.
HOVERGEN; HBG067546; -.
InParanoid; Q9NQR1; -.
KO; K11428; -.
OMA; KQFSRGE; -.
OrthoDB; EOG091G0UBI; -.
PhylomeDB; Q9NQR1; -.
TreeFam; TF335181; -.
BRENDA; 2.1.1.43; 2681.
Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
Reactome; R-HSA-6804760; Regulation of TP53 Activity through Methylation.
SIGNOR; Q9NQR1; -.
EvolutionaryTrace; Q9NQR1; -.
GeneWiki; SETD8; -.
GenomeRNAi; 387893; -.
PRO; PR:Q9NQR1; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000183955; -.
CleanEx; HS_SETD8; -.
ExpressionAtlas; Q9NQR1; baseline and differential.
Genevisible; Q9NQR1; HS.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); TAS:Reactome.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:UniProtKB.
GO; GO:0016278; F:lysine N-methyltransferase activity; TAS:Reactome.
GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0018026; P:peptidyl-lysine monomethylation; IDA:UniProtKB.
GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR016858; Hist_H4-K20_MeTrfase.
InterPro; IPR001214; SET_dom.
Pfam; PF00856; SET; 1.
PIRSF; PIRSF027717; Histone_H4-K20_mtfrase; 1.
SMART; SM00317; SET; 1.
PROSITE; PS51571; SAM_MT43_PR_SET; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell cycle;
Cell division; Chromatin regulator; Chromosome; Coiled coil;
Complete proteome; Direct protein sequencing; Methyltransferase;
Mitosis; Nucleus; Phosphoprotein; Reference proteome; Repressor;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase; Ubl conjugation.
CHAIN 1 393 N-lysine methyltransferase KMT5A.
/FTId=PRO_0000186081.
DOMAIN 257 378 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
REGION 267 269 S-adenosyl-L-methionine binding.
REGION 339 340 S-adenosyl-L-methionine binding.
COILED 134 163 {ECO:0000255}.
COMPBIAS 6 67 Ala-rich.
COMPBIAS 29 32 Poly-Arg.
BINDING 312 312 S-adenosyl-L-methionine.
MOD_RES 100 100 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 172 172 N6-acetyllysine.
{ECO:0000269|PubMed:23468428}.
MOD_RES 181 181 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 41 Missing (in isoform 2).
{ECO:0000303|PubMed:12121615,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_002226.
VAR_SEQ 42 57 PGRAAGGKMSKPCAVE -> MARGRKMSKPRAVEAA (in
isoform 2). {ECO:0000303|PubMed:12121615,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_002227.
MUTAGEN 172 172 K->Q: Inhibits the interaction with
SIRT2. Increases the number of mitotic
foci formation. Does not change
methyltransferase activity.
{ECO:0000269|PubMed:23468428}.
MUTAGEN 172 172 K->R: Increases the interaction with
SIRT2. Reduces the number of mitotic foci
formation. Does not change
methyltransferase activity.
{ECO:0000269|PubMed:23468428}.
MUTAGEN 286 286 Y->A,F: Strongly reduces affinity for
histone H4 and abolishes
methyltransferase activity.
{ECO:0000269|PubMed:15933070}.
MUTAGEN 300 300 E->A: Strongly reduces affinity for
histone H4.
{ECO:0000269|PubMed:15933070}.
MUTAGEN 311 311 C->A: Strongly reduces affinity for
histone H4.
{ECO:0000269|PubMed:15933070}.
MUTAGEN 336 336 R->G: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:12086618,
ECO:0000269|PubMed:23478445}.
MUTAGEN 340 340 H->A: Strongly decreases
methyltransferase activity.
{ECO:0000269|PubMed:12121615}.
MUTAGEN 375 375 Y->A: Strongly reduces affinity for
histone H4 and methyltransferase
activity. {ECO:0000269|PubMed:15933070}.
MUTAGEN 375 375 Y->F: Alters methyltransferase activity,
so that both monomethylation and
dimethylation take place.
{ECO:0000269|PubMed:15933070}.
MUTAGEN 379 379 D->A,N: Abolishes histone H4 binding and
methyltransferase activity.
{ECO:0000269|PubMed:15933070,
ECO:0000269|PubMed:17707234,
ECO:0000269|PubMed:20870725,
ECO:0000269|PubMed:23478445}.
MUTAGEN 385 393 Missing: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:12121615}.
MUTAGEN 388 388 H->A,E: Strongly reduces affinity for
histone H4.
{ECO:0000269|PubMed:15933070}.
MUTAGEN 388 388 H->F: Increases affinity for histone H4.
{ECO:0000269|PubMed:15933070}.
CONFLICT 162 163 KG -> RR (in Ref. 3; AAF97812).
{ECO:0000305}.
CONFLICT 281 281 D -> A (in Ref. 3; AAF97812).
{ECO:0000305}.
CONFLICT 343 343 C -> R (in Ref. 3; AAF97812).
{ECO:0000305}.
CONFLICT 357 357 P -> R (in Ref. 5; AAH50346).
{ECO:0000305}.
CONFLICT 373 373 L -> P (in Ref. 3; AAF97812).
{ECO:0000305}.
HELIX 236 253 {ECO:0000244|PDB:3F9X}.
STRAND 259 264 {ECO:0000244|PDB:3F9X}.
TURN 265 267 {ECO:0000244|PDB:3F9X}.
STRAND 268 275 {ECO:0000244|PDB:3F9X}.
STRAND 282 285 {ECO:0000244|PDB:3F9X}.
STRAND 288 292 {ECO:0000244|PDB:3F9X}.
HELIX 293 303 {ECO:0000244|PDB:3F9X}.
HELIX 307 309 {ECO:0000244|PDB:5TH7}.
HELIX 310 312 {ECO:0000244|PDB:4IJ8}.
STRAND 313 318 {ECO:0000244|PDB:3F9X}.
STRAND 321 326 {ECO:0000244|PDB:3F9X}.
HELIX 335 337 {ECO:0000244|PDB:3F9X}.
STRAND 338 340 {ECO:0000244|PDB:5TH7}.
STRAND 345 353 {ECO:0000244|PDB:3F9X}.
STRAND 356 365 {ECO:0000244|PDB:3F9X}.
STRAND 372 375 {ECO:0000244|PDB:5TH7}.
HELIX 382 387 {ECO:0000244|PDB:3F9X}.
HELIX 389 392 {ECO:0000244|PDB:3F9X}.
SEQUENCE 393 AA; 42890 MW; 2DCD9B697834B5BD CRC64;
MGEGGAAAAL VAAAAAAAAA AAAVVAGQRR RRLGRRARCH GPGRAAGGKM SKPCAVEAAA
AAVAATAPGP EMVERRGPGR PRTDGENVFT GQSKIYSYMS PNKCSGMRFP LQEENSVTHH
EVKCQGKPLA GIYRKREEKR NAGNAVRSAM KSEEQKIKDA RKGPLVPFPN QKSEAAEPPK
TPPSSCDSTN AAIAKQALKK PIKGKQAPRK KAQGKTQQNR KLTDFYPVRR SSRKSKAELQ
SEERKRIDEL IESGKEEGMK IDLIDGKGRG VIATKQFSRG DFVVEYHGDL IEITDAKKRE
ALYAQDPSTG CYMYYFQYLS KTYCVDATRE TNRLGRLINH SKCGNCQTKL HDIDGVPHLI
LIASRDIAAG EELLYDYGDR SKASIEAHPW LKH


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