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Database: UniProt/SWISS-PROT
Entry: KMT5A_MOUSE
LinkDB: KMT5A_MOUSE
Original site: KMT5A_MOUSE 
ID   KMT5A_MOUSE             Reviewed;         349 AA.
AC   Q2YDW7; Q8C0J9;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   28-MAR-2018, entry version 103.
DE   RecName: Full=N-lysine methyltransferase KMT5A {ECO:0000305};
DE            EC=2.1.1.-;
DE   AltName: Full=H4-K20-HMTase KMT5A;
DE   AltName: Full=Histone-lysine N-methyltransferase KMT5A;
DE            EC=2.1.1.43;
DE   AltName: Full=Lysine-specific methylase 5A {ECO:0000250|UniProtKB:Q9NQR1};
DE   AltName: Full=PR/SET domain-containing protein 07;
DE            Short=PR-Set7;
DE            Short=PR/SET07;
DE   AltName: Full=SET domain-containing protein 8;
GN   Name=Kmt5a {ECO:0000250|UniProtKB:Q9NQR1}; Synonyms=Setd8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NMRI; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-138, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=23468428; DOI=10.1101/gad.211342.112;
RA   Serrano L., Martinez-Redondo P., Marazuela-Duque A., Vazquez B.N.,
RA   Dooley S.J., Voigt P., Beck D.B., Kane-Goldsmith N., Tong Q.,
RA   Rabanal R.M., Fondevila D., Munoz P., Kruger M., Tischfield J.A.,
RA   Vaquero A.;
RT   "The tumor suppressor SirT2 regulates cell cycle progression and
RT   genome stability by modulating the mitotic deposition of H4K20
RT   methylation.";
RL   Genes Dev. 27:639-653(2013).
CC   -!- FUNCTION: Protein-lysine N-methyltransferase that monomethylates
CC       both histones and non-histone proteins. Specifically
CC       monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is
CC       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       probably by contributing to the maintenance of proper higher-order
CC       structure of DNA during mitosis. Involved in chromosome
CC       condensation and proper cytokinesis. Nucleosomes are preferred as
CC       substrate compared to free histones. Mediates monomethylation of
CC       p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes.
CC       Plays a negative role in TGF-beta response regulation and a
CC       positive role in cell migration (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {ECO:0000255|PROSITE-ProRule:PRU00904}.
CC   -!- SUBUNIT: Interacts with L3MBTL1. Interacts with SIRT2
CC       (phosphorylated form); the interaction is direct, stimulates
CC       KMT5A-mediated methyltransferase activity at histone H4 'Lys-20'
CC       (H4K20me1) and is increased in a H(2)O(2)-induced oxidative
CC       stress-dependent manner (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {ECO:0000269|PubMed:23468428}. Note=Specifically localizes to
CC       mitotic chromosomes. Associates with silent chromatin on
CC       euchromatic arms. Not associated with constitutive heterochromatin
CC       (By similarity). Colocalized with SIRT2 at mitotic foci.
CC       Associates with chromosomes during mitosis; association is
CC       increased in a H(2)O(2)-induced oxidative stress-dependent manner.
CC       {ECO:0000250}.
CC   -!- DOMAIN: Although the SET domain contains the active site of
CC       enzymatic activity, both sequences upstream and downstream of the
CC       SET domain are required for methyltransferase activity.
CC       {ECO:0000250}.
CC   -!- PTM: Acetylated at Lys-129; does not change methyltransferase
CC       activity. Deacetylated at Lys-129 by SIRT2; does not change
CC       methyltransferase activity (By similarity). {ECO:0000250}.
CC   -!- PTM: Ubiquitinated and degraded by the DCX(DTL) complex.
CC       {ECO:0000305}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27178.1; Type=Frameshift; Positions=20; Evidence={ECO:0000305};
DR   EMBL; AK030904; BAC27178.1; ALT_FRAME; mRNA.
DR   EMBL; BC108333; AAI08334.1; -; mRNA.
DR   RefSeq; NP_001297652.1; NM_001310723.1.
DR   RefSeq; NP_001297656.1; NM_001310727.1.
DR   RefSeq; NP_084517.2; NM_030241.3.
DR   UniGene; Mm.137966; -.
DR   UniGene; Mm.472072; -.
DR   ProteinModelPortal; Q2YDW7; -.
DR   SMR; Q2YDW7; -.
DR   BioGrid; 212564; 2.
DR   IntAct; Q2YDW7; 2.
DR   MINT; Q2YDW7; -.
DR   STRING; 10090.ENSMUSP00000052953; -.
DR   iPTMnet; Q2YDW7; -.
DR   PhosphoSitePlus; Q2YDW7; -.
DR   MaxQB; Q2YDW7; -.
DR   PaxDb; Q2YDW7; -.
DR   PRIDE; Q2YDW7; -.
DR   GeneID; 67956; -.
DR   KEGG; mmu:67956; -.
DR   CTD; 387893; -.
DR   MGI; MGI:1915206; Kmt5a.
DR   eggNOG; KOG1085; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000020818; -.
DR   HOVERGEN; HBG067546; -.
DR   InParanoid; Q2YDW7; -.
DR   KO; K11428; -.
DR   ChiTaRS; Kmt5a; mouse.
DR   PRO; PR:Q2YDW7; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
DR   GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   InterPro; IPR016858; Hist_H4-K20_MeTrfase.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00856; SET; 1.
DR   PIRSF; PIRSF027717; Histone_H4-K20_mtfrase; 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   Acetylation; Cell cycle; Cell division; Chromatin regulator;
KW   Chromosome; Complete proteome; Methyltransferase; Mitosis; Nucleus;
KW   Phosphoprotein; Reference proteome; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation.
FT   CHAIN         1    349       N-lysine methyltransferase KMT5A.
FT                                /FTId=PRO_0000228689.
FT   DOMAIN      213    334       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      223    225       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00904}.
FT   REGION      295    296       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00904}.
FT   COMPBIAS     12     24       Ala-rich.
FT   BINDING     268    268       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190,
FT                                ECO:0000255|PROSITE-ProRule:PRU00904}.
FT   MOD_RES      57     57       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NQR1}.
FT   MOD_RES     129    129       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9NQR1}.
FT   MOD_RES     138    138       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CONFLICT    204    204       N -> ID (in Ref. 1; BAC27178).
FT                                {ECO:0000305}.
FT   CONFLICT    260    260       V -> A (in Ref. 1; BAC27178).
FT                                {ECO:0000305}.
SQ   SEQUENCE   349 AA;  38845 MW;  C89BAE59660DA5AF CRC64;
     MARGRKMCKP RAVEAAAAAV AATAPGPEMV EQRGPGRPRS DGENVFAGQS KIYAYMSPNK
     CSAMRSPLQE ENSVAHHEVK CPGKPLAGIY RKREEKRNTG NVIRSAVKSD EQKSKDTRRG
     PLAPFPNQKS EAAEPPKTPP PSCDSTNVAV AKQALKKSLK GKQAPRKKSQ GKTQQNRKLT
     DFYPVRRSSR KSKAELQSEE RKKNELIESG KEEGMKIDLI DGKGRGVIAT KQFSRGDFVV
     EYHGDLIEIT DAKKREALYV QDPSTGCYMY YFQYLSKTYC VDATQETNRL GRLINHSKCG
     NCQTKLHDID GVPHLILIAS RDIAAGEELL YDYGDRSKAS IEAYPWLKH
//
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