GenomeNet

Database: UniProt
Entry: Q6Q783
LinkDB: Q6Q783
Original site: Q6Q783 
ID   KMT5C_MOUSE             Reviewed;         468 AA.
AC   Q6Q783; Q5RKP6; Q8R1C5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   10-APR-2019, entry version 112.
DE   RecName: Full=Histone-lysine N-methyltransferase KMT5C {ECO:0000305};
DE            EC=2.1.1.43;
DE   AltName: Full=Lysine-specific methyltransferase 5C {ECO:0000250|UniProtKB:Q86Y97};
DE   AltName: Full=Suppressor of variegation 4-20 homolog 2;
DE            Short=Su(var)4-20 homolog 2;
DE            Short=Suv4-20h2;
GN   Name=Kmt5c {ECO:0000250|UniProtKB:Q86Y97}; Synonyms=Suv420h2;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, AND INTERACTION WITH CBX1; CBX3 AND CBX5.
RC   STRAIN=FVB/N;
RX   PubMed=15145825; DOI=10.1101/gad.300704;
RA   Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G.,
RA   Reinberg D., Jenuwein T.;
RT   "A silencing pathway to induce H3-K9 and H4-K20 trimethylation at
RT   constitutive heterochromatin.";
RL   Genes Dev. 18:1251-1262(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Dendritic cell;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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   [4]
RP   INTERACTION WITH RB1; RBL1 AND RBL2.
RX   PubMed=15750587; DOI=10.1038/ncb1235;
RA   Gonzalo S., Garcia-Cao M., Fraga M.F., Schotta G., Peters A.H.F.M.,
RA   Cotter S.E., Eguia R., Dean D.C., Esteller M., Jenuwein T.,
RA   Blasco M.A.;
RT   "Role of the RB1 family in stabilizing histone methylation at
RT   constitutive heterochromatin.";
RL   Nat. Cell Biol. 7:420-428(2005).
RN   [5]
RP   INTERACTION WITH RB1; RBL1 AND RBL2.
RX   PubMed=16612004; DOI=10.1128/MCB.26.9.3659-3671.2006;
RA   Isaac C.E., Francis S.M., Martens A.L., Julian L.M., Seifried L.A.,
RA   Erdmann N., Binne U.K., Harrington L., Sicinski P., Berube N.G.,
RA   Dyson N.J., Dick F.A.;
RT   "The retinoblastoma protein regulates pericentric heterochromatin.";
RL   Mol. Cell. Biol. 26:3659-3671(2006).
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. KMT5C is targeted
CC       to histone H3 via its interaction with RB1 family proteins (RB1,
CC       RBL1 and RBL2). {ECO:0000269|PubMed:15145825}.
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:PRU00903,
CC         ECO:0000269|PubMed:15145825};
CC   -!- SUBUNIT: Interacts with HP1 proteins CBX1, CBX3 and CBX5.
CC       Interacts with RB1 family proteins RB1, RBL1 and RBL2.
CC       {ECO:0000269|PubMed:15145825, ECO:0000269|PubMed:15750587,
CC       ECO:0000269|PubMed:16612004}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15145825}.
CC       Chromosome {ECO:0000269|PubMed:15145825}. Note=Associated with
CC       pericentric heterochromatin. CBX1 and CBX5 are required for the
CC       localization to pericentric heterochromatin.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH24816.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH85473.2; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AY555193; AAT00540.1; -; mRNA.
DR   EMBL; AK154848; BAE32874.1; -; mRNA.
DR   EMBL; BC024816; AAH24816.1; ALT_INIT; mRNA.
DR   EMBL; BC085473; AAH85473.2; ALT_INIT; mRNA.
DR   CCDS; CCDS20743.2; -.
DR   RefSeq; NP_001108490.1; NM_001115018.1.
DR   RefSeq; NP_666289.2; NM_146177.2.
DR   RefSeq; XP_006539837.1; XM_006539774.1.
DR   UniGene; Mm.247844; -.
DR   PDB; 4AU7; X-ray; 2.07 A; A/B=1-246.
DR   PDBsum; 4AU7; -.
DR   ProteinModelPortal; Q6Q783; -.
DR   SMR; Q6Q783; -.
DR   BioGrid; 231299; 3.
DR   STRING; 10090.ENSMUSP00000104223; -.
DR   iPTMnet; Q6Q783; -.
DR   PhosphoSitePlus; Q6Q783; -.
DR   jPOST; Q6Q783; -.
DR   MaxQB; Q6Q783; -.
DR   PaxDb; Q6Q783; -.
DR   PeptideAtlas; Q6Q783; -.
DR   PRIDE; Q6Q783; -.
DR   Ensembl; ENSMUST00000098853; ENSMUSP00000096452; ENSMUSG00000059851.
DR   Ensembl; ENSMUST00000108582; ENSMUSP00000104223; ENSMUSG00000059851.
DR   Ensembl; ENSMUST00000108583; ENSMUSP00000104224; ENSMUSG00000059851.
DR   GeneID; 232811; -.
DR   KEGG; mmu:232811; -.
DR   UCSC; uc009eyi.2; mouse.
DR   CTD; 84787; -.
DR   MGI; MGI:2385262; Kmt5c.
DR   eggNOG; KOG2589; Eukaryota.
DR   eggNOG; ENOG410XPH8; LUCA.
DR   GeneTree; ENSGT00940000161700; -.
DR   HOGENOM; HOG000154453; -.
DR   HOVERGEN; HBG095676; -.
DR   InParanoid; Q6Q783; -.
DR   KO; K11429; -.
DR   OMA; PQQDWHW; -.
DR   OrthoDB; 236983at2759; -.
DR   PhylomeDB; Q6Q783; -.
DR   TreeFam; TF106433; -.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   ChiTaRS; Suv420h2; mouse.
DR   PRO; PR:Q6Q783; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000059851; Expressed in 268 organ(s), highest expression level in muscle tissue.
DR   ExpressionAtlas; Q6Q783; baseline and differential.
DR   Genevisible; Q6Q783; MM.
DR   GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IDA:MGI.
DR   GO; GO:0005720; C:nuclear heterochromatin; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005721; C:pericentric heterochromatin; ISO:MGI.
DR   GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IDA:MGI.
DR   GO; GO:0034773; P:histone H4-K20 trimethylation; IDA:MGI.
DR   GO; GO:0016571; P:histone methylation; IDA:MGI.
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   1: Evidence at protein level;
KW   3D-structure; Chromatin regulator; Chromosome; Complete proteome;
KW   Methyltransferase; Nucleus; Reference proteome; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase.
FT   CHAIN         1    468       Histone-lysine N-methyltransferase KMT5C.
FT                                /FTId=PRO_0000281794.
FT   DOMAIN      104    218       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      348    441       Required for heterochromatin
FT                                localization.
FT   HELIX         8     21       {ECO:0000244|PDB:4AU7}.
FT   HELIX        23     27       {ECO:0000244|PDB:4AU7}.
FT   HELIX        45     58       {ECO:0000244|PDB:4AU7}.
FT   HELIX        61     68       {ECO:0000244|PDB:4AU7}.
FT   HELIX        74     77       {ECO:0000244|PDB:4AU7}.
FT   TURN         78     81       {ECO:0000244|PDB:4AU7}.
FT   HELIX        83     99       {ECO:0000244|PDB:4AU7}.
FT   HELIX       102    104       {ECO:0000244|PDB:4AU7}.
FT   STRAND      106    111       {ECO:0000244|PDB:4AU7}.
FT   STRAND      118    127       {ECO:0000244|PDB:4AU7}.
FT   STRAND      134    144       {ECO:0000244|PDB:4AU7}.
FT   HELIX       147    152       {ECO:0000244|PDB:4AU7}.
FT   TURN        155    157       {ECO:0000244|PDB:4AU7}.
FT   STRAND      160    165       {ECO:0000244|PDB:4AU7}.
FT   TURN        166    169       {ECO:0000244|PDB:4AU7}.
FT   STRAND      170    176       {ECO:0000244|PDB:4AU7}.
FT   HELIX       177    180       {ECO:0000244|PDB:4AU7}.
FT   STRAND      188    193       {ECO:0000244|PDB:4AU7}.
FT   STRAND      195    205       {ECO:0000244|PDB:4AU7}.
FT   TURN        219    222       {ECO:0000244|PDB:4AU7}.
FT   HELIX       232    237       {ECO:0000244|PDB:4AU7}.
FT   HELIX       240    243       {ECO:0000244|PDB:4AU7}.
SQ   SEQUENCE   468 AA;  53159 MW;  D43D7A25DBDF3BB1 CRC64;
     MGPDRVTARE LCENDDLATS LVLDPYLGFR THKMNVSPVP TLRRQHHLRS ALEAFLRQRD
     LEAAFRALTL GGWMAHYFQS RAPRQEAALK THIFCYLRAF LPESGFTILP CTRYSMETNG
     AKIVSTRAWK KNEKLELLVG CIAELREEDE DLLRAGENDF SIMYSTRKRS AQLWLGPAAF
     INHDCKPNCK FVPSDGNTAC VKVLRDIEPG DEVTCFYGEG FFGEKNEHCE CYTCERKGEG
     AFRLQPREPE LRPKPLDKYE LRETKRRLQQ GLVSSQQSLM SRWACSHLSP LRPDPFCAAC
     QPSCLLPASP HMDYLPLWLQ RAPQPQPIVP PRKRHRRRRP RIRQASLPPV LRTACVPLHR
     WGGCGPHCQL RAEAMVTLHL RPQTRWTPQQ DWYWARRYGL PSVGRVELTR LAPALPAAPA
     PAGNPGPVPT PDFIPKQALA FAPFCPPKRL RLVVSHGSID LDINSGEP
//
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