GenomeNet

Database: UniProt/SWISS-PROT
Entry: KMT5B_RAT
LinkDB: KMT5B_RAT
Original site: KMT5B_RAT 
ID   KMT5B_RAT               Reviewed;         883 AA.
AC   P0C2N5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   10-MAY-2017, entry version 80.
DE   RecName: Full=Histone-lysine N-methyltransferase KMT5B {ECO:0000305};
DE            EC=2.1.1.43;
DE   AltName: Full=Lysine-specific methyltransferase 5B {ECO:0000312|RGD:1311637};
DE   AltName: Full=Suppressor of variegation 4-20 homolog 1;
DE            Short=Su(var)4-20 homolog 1;
DE            Short=Suv4-20h1;
GN   Name=Kmt5b {ECO:0000312|RGD:1311637}; Synonyms=Suv420h1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation
CC       represents a specific tag for epigenetic transcriptional
CC       repression. Mainly functions in pericentric heterochromatin
CC       regions, thereby playing a central role in the establishment of
CC       constitutive heterochromatin in these regions. KMT5B is targeted
CC       to histone H3 via its interaction with RB1 family proteins (RB1,
CC       RBL1 and RBL2). Plays a role in myogenesis by regulating the
CC       expression of target genes, such as EID3 (By similarity).
CC       {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:PRU00903}.
CC   -!- SUBUNIT: Interacts with HP1 proteins CBX1, CBX3 and CBX5.
CC       Interacts with RB1 family proteins RB1, RBL1 and RBL2. Interacts
CC       (via C-terminus) with FRG1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000250}.
CC       Note=Associated with pericentric heterochromatin. CBX1 and CBX5
CC       are required for the localization to pericentric heterochromatin
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar4-20 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00903}.
DR   EMBL; AABR03001123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001101982.1; NM_001108512.1.
DR   UniGene; Rn.203473; -.
DR   ProteinModelPortal; P0C2N5; -.
DR   SMR; P0C2N5; -.
DR   STRING; 10116.ENSRNOP00000022486; -.
DR   iPTMnet; P0C2N5; -.
DR   PhosphoSitePlus; P0C2N5; -.
DR   PaxDb; P0C2N5; -.
DR   PRIDE; P0C2N5; -.
DR   Ensembl; ENSRNOT00000022486; ENSRNOP00000022486; ENSRNOG00000016790.
DR   GeneID; 361688; -.
DR   KEGG; rno:361688; -.
DR   UCSC; RGD:1311637; rat.
DR   CTD; 51111; -.
DR   RGD; 1311637; Kmt5b.
DR   eggNOG; KOG2589; Eukaryota.
DR   eggNOG; ENOG410XPH8; LUCA.
DR   GeneTree; ENSGT00520000055640; -.
DR   HOVERGEN; HBG105761; -.
DR   InParanoid; P0C2N5; -.
DR   KO; K11429; -.
DR   OMA; SGCLTRH; -.
DR   OrthoDB; EOG091G0IUY; -.
DR   PhylomeDB; P0C2N5; -.
DR   TreeFam; TF106433; -.
DR   Reactome; R-RNO-3214841; PKMTs methylate histone lysines.
DR   PRO; PR:P0C2N5; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000016790; -.
DR   Genevisible; P0C2N5; RN.
DR   GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IEA:Ensembl.
DR   GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IEA:Ensembl.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0034773; P:histone H4-K20 trimethylation; IEA:InterPro.
DR   GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   InterPro; IPR025790; Hist-Lys_N-MTase_Suvar4-20.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS51570; SAM_MT43_SUVAR420_2; 1.
DR   PROSITE; PS50280; SET; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; Chromosome; Complete proteome; Isopeptide bond;
KW   Methyltransferase; Myogenesis; Nucleus; Reference proteome; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation.
FT   CHAIN         1    883       Histone-lysine N-methyltransferase KMT5B.
FT                                /FTId=PRO_0000281789.
FT   DOMAIN      193    308       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   CROSSLNK    555    555       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q4FZB7}.
SQ   SEQUENCE   883 AA;  98668 MW;  1C5EAE2B39D2542F CRC64;
     MKWLGDSKNM VVNGRRNGSK LSNDHQQNQS KLQHAGKDAL KTGRNAVERR PNRCHGNSGF
     EGQSRYVPSS GMSAKELCEN DDLATSLVLD PYLGFQTHKM NTSAFPSRSS RHISKADSFS
     HNNPMRFRPI KGRQEELKEV IERFKKDEHL EKAFKCLTSG EWARHYFLNK NKMQEKLFKE
     HVFIYLRMFA TDSGFEILPC NRYSSEQNGA KIVATKEWKR NDKIELLVGC IAELSEIEEN
     MLLRHGENDF SVMYSTRKNC AQLWLGPAAF INHDCRPNCK FVSTGRDTAC VKALRDIEPG
     EEISCYYGDG FFGENNEFCE CYTCERRGTG AFKSRVGLPA PAPVINSKYG LRETDKRLNR
     LKKLGDSSKS SDSQSVSSNT DADTTQEKDN ATSNRKSSVG VKKNSKSRAL TRQSMPRVPA
     ASNSTSPKLV HMNNSRVPKK LRKPAKPLLS KIKLRNHCKR LDQKSTSRKL EMGNLVLKEP
     KVVLYKNLPI KKEREAEGPV HAAVGSGCLT RHAAREHRQN PGRGAHSQGD SLPCTYTTRR
     SLRTRTGLKE TTDIKLAPSP LDGYKNGILE PYPDSGQQPT PEVLEELAPE TALREEASQE
     CPKSDSCPSR KKFRQGKPVK HLAKTEDCSP EHSFPGKDGL PDLPGPHPDQ GEPSGTVRVP
     VSYTDSAPSP VGCSIVTPDS FTTKDSFRTA QSKKKRRVTR YDAQLILENS SGIPKLTLRR
     RHDSSSKTND HESDSVNSSK ISIKLSKDHE SDSNLYVAKL SNGVSSGPGS SSTKLKIQLK
     RDEESRGPCA EGLHENGVCC SDPLSLLESQ MEVDDYSQYE EDSTDDSSSS EGEEEEEDCE
     DDFDDDFIPL PPAKRLRLIV GKDSIDIDIS SRRREDQSLR LNA
//
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