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Histone-lysine N-methyltransferase KMT5B (EC 2.1.1.43) (Lysine-specific methyltransferase 5B) (Suppressor of variegation 4-20 homolog 1) (Su(var)4-20 homolog 1) (Suv4-20h1)

 KMT5B_MOUSE             Reviewed;         883 AA.
Q3U8K7; Q3UTP6; Q6DI74; Q6Q784; Q8BU67; Q8BUN0; Q8BUT7; Q8BW73;
Q8BZ24; Q91X81;
03-APR-2007, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 2.
10-MAY-2017, entry version 101.
RecName: Full=Histone-lysine N-methyltransferase KMT5B {ECO:0000305};
EC=2.1.1.43;
AltName: Full=Lysine-specific methyltransferase 5B {ECO:0000250|UniProtKB:Q4FZB7};
AltName: Full=Suppressor of variegation 4-20 homolog 1;
Short=Su(var)4-20 homolog 1;
Short=Suv4-20h1;
Name=Kmt5b {ECO:0000250|UniProtKB:Q4FZB7}; Synonyms=Suv420h1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
SUBCELLULAR LOCATION, AND INTERACTION WITH CBX1; CBX3 AND CBX5.
STRAIN=C57BL/6J;
PubMed=15145825; DOI=10.1101/gad.300704;
Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G.,
Reinberg D., Jenuwein T.;
"A silencing pathway to induce H3-K9 and H4-K20 trimethylation at
constitutive heterochromatin.";
Genes Dev. 18:1251-1262(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
STRAIN=C57BL/6J;
TISSUE=Bone marrow, Cerebellum, Hippocampus, Lung, Oviduct, and
Vagina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor, and Salivary gland;
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).
[4]
INTERACTION WITH RB1; RBL1 AND RBL2.
PubMed=15750587; DOI=10.1038/ncb1235;
Gonzalo S., Garcia-Cao M., Fraga M.F., Schotta G., Peters A.H.F.M.,
Cotter S.E., Eguia R., Dean D.C., Esteller M., Jenuwein T.,
Blasco M.A.;
"Role of the RB1 family in stabilizing histone methylation at
constitutive heterochromatin.";
Nat. Cell Biol. 7:420-428(2005).
[5]
INTERACTION WITH RB1; RBL1 AND RBL2.
PubMed=16612004; DOI=10.1128/MCB.26.9.3659-3671.2006;
Isaac C.E., Francis S.M., Martens A.L., Julian L.M., Seifried L.A.,
Erdmann N., Binne U.K., Harrington L., Sicinski P., Berube N.G.,
Dyson N.J., Dick F.A.;
"The retinoblastoma protein regulates pericentric heterochromatin.";
Mol. Cell. Biol. 26:3659-3671(2006).
[6]
FUNCTION, INTERACTION WITH FRG1, AND DISRUPTION PHENOTYPE.
PubMed=23720823; DOI=10.1093/jmcb/mjt018;
Neguembor M.V., Xynos A., Onorati M.C., Caccia R., Bortolanza S.,
Godio C., Pistoni M., Corona D.F., Schotta G., Gabellini D.;
"FSHD muscular dystrophy region gene 1 binds Suv4-20h1 histone
methyltransferase and impairs myogenesis.";
J. Mol. Cell Biol. 5:294-307(2013).
-!- FUNCTION: Histone methyltransferase that specifically
trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation
represents a specific tag for epigenetic transcriptional
repression. Mainly functions in pericentric heterochromatin
regions, thereby playing a central role in the establishment of
constitutive heterochromatin in these regions. KMT5B is targeted
to histone H3 via its interaction with RB1 family proteins (RB1,
RBL1 and RBL2). Plays a role in myogenesis by regulating the
expression of target genes, such as EID3.
{ECO:0000269|PubMed:15145825, ECO:0000269|PubMed:23720823}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000255|PROSITE-ProRule:PRU00903,
ECO:0000269|PubMed:15145825}.
-!- SUBUNIT: Interacts with HP1 proteins CBX1, CBX3 and CBX5.
Interacts with RB1 family proteins RB1, RBL1 and RBL2. Interacts
(via C-terminus) with FRG1. {ECO:0000269|PubMed:15145825,
ECO:0000269|PubMed:15750587, ECO:0000269|PubMed:16612004,
ECO:0000269|PubMed:23720823}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15145825}.
Chromosome {ECO:0000269|PubMed:15145825}. Note=Associated with
pericentric heterochromatin. CBX1 and CBX5 are required for the
localization to pericentric heterochromatin.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q3U8K7-1; Sequence=Displayed;
Name=2;
IsoId=Q3U8K7-2; Sequence=VSP_024055, VSP_024056;
Name=3;
IsoId=Q3U8K7-3; Sequence=VSP_024053;
Name=4;
IsoId=Q3U8K7-4; Sequence=VSP_024054;
Name=5;
IsoId=Q3U8K7-5; Sequence=VSP_024053, VSP_024057;
Note=No experimental confirmation available.;
-!- DISRUPTION PHENOTYPE: Partial muscle-specific knockout mice
display several signs of muscular dystrophy including necrosis and
an increased number of centrally nucleated myofibers. RNAi-
mediated knockdown in C2C12 muscle cells causes reduced myogenic
differentiation of the cells. {ECO:0000269|PubMed:23720823}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. Suvar4-20 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00903}.
-!- SEQUENCE CAUTION:
Sequence=AAH11214.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAT00539.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAC39834.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAE23934.1; Type=Erroneous termination; Positions=3; Note=Translated as Trp.; Evidence={ECO:0000305};
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EMBL; AY555192; AAT00539.1; ALT_INIT; mRNA.
EMBL; AK036880; BAC29617.1; -; mRNA.
EMBL; AK054093; BAC35652.1; -; mRNA.
EMBL; AK082660; BAC38565.1; -; mRNA.
EMBL; AK083227; BAC38817.1; -; mRNA.
EMBL; AK087267; BAC39834.1; ALT_INIT; mRNA.
EMBL; AK139255; BAE23934.1; ALT_SEQ; mRNA.
EMBL; AK152179; BAE31010.1; -; mRNA.
EMBL; BC011214; AAH11214.1; ALT_INIT; mRNA.
EMBL; BC075709; AAH75709.1; -; mRNA.
CCDS; CCDS29399.1; -. [Q3U8K7-3]
CCDS; CCDS50343.1; -. [Q3U8K7-1]
CCDS; CCDS50344.1; -. [Q3U8K7-2]
CCDS; CCDS50345.1; -. [Q3U8K7-4]
RefSeq; NP_001161356.1; NM_001167884.1. [Q3U8K7-4]
RefSeq; NP_001161357.1; NM_001167885.1. [Q3U8K7-1]
RefSeq; NP_001161358.1; NM_001167886.1. [Q3U8K7-3]
RefSeq; NP_001161359.1; NM_001167887.1. [Q3U8K7-1]
RefSeq; NP_001161360.1; NM_001167888.1. [Q3U8K7-4]
RefSeq; NP_001161361.1; NM_001167889.1. [Q3U8K7-2]
RefSeq; NP_659120.3; NM_144871.4. [Q3U8K7-3]
RefSeq; XP_006531790.1; XM_006531727.3. [Q3U8K7-1]
RefSeq; XP_006531791.1; XM_006531728.3. [Q3U8K7-1]
RefSeq; XP_006531794.1; XM_006531731.2. [Q3U8K7-5]
RefSeq; XP_011246925.1; XM_011248623.2. [Q3U8K7-1]
RefSeq; XP_011246926.1; XM_011248624.2. [Q3U8K7-3]
RefSeq; XP_017173632.1; XM_017318143.1. [Q3U8K7-1]
UniGene; Mm.278578; -.
PDB; 4BUP; X-ray; 2.17 A; A/B=70-336.
PDBsum; 4BUP; -.
ProteinModelPortal; Q3U8K7; -.
SMR; Q3U8K7; -.
BioGrid; 230441; 3.
STRING; 10090.ENSMUSP00000109605; -.
iPTMnet; Q3U8K7; -.
PhosphoSitePlus; Q3U8K7; -.
MaxQB; Q3U8K7; -.
PaxDb; Q3U8K7; -.
PeptideAtlas; Q3U8K7; -.
PRIDE; Q3U8K7; -.
DNASU; 225888; -.
Ensembl; ENSMUST00000005518; ENSMUSP00000005518; ENSMUSG00000045098. [Q3U8K7-4]
Ensembl; ENSMUST00000052699; ENSMUSP00000060162; ENSMUSG00000045098. [Q3U8K7-2]
Ensembl; ENSMUST00000113968; ENSMUSP00000109601; ENSMUSG00000045098. [Q3U8K7-4]
Ensembl; ENSMUST00000113970; ENSMUSP00000109603; ENSMUSG00000045098. [Q3U8K7-2]
Ensembl; ENSMUST00000113972; ENSMUSP00000109605; ENSMUSG00000045098. [Q3U8K7-1]
Ensembl; ENSMUST00000113973; ENSMUSP00000109606; ENSMUSG00000045098. [Q3U8K7-1]
Ensembl; ENSMUST00000113974; ENSMUSP00000109607; ENSMUSG00000045098. [Q3U8K7-3]
Ensembl; ENSMUST00000113977; ENSMUSP00000109610; ENSMUSG00000045098. [Q3U8K7-3]
Ensembl; ENSMUST00000176262; ENSMUSP00000135563; ENSMUSG00000045098. [Q3U8K7-3]
GeneID; 225888; -.
KEGG; mmu:225888; -.
UCSC; uc008fww.2; mouse. [Q3U8K7-4]
UCSC; uc008fwz.2; mouse. [Q3U8K7-2]
UCSC; uc008fxa.2; mouse. [Q3U8K7-1]
UCSC; uc008fxc.2; mouse. [Q3U8K7-3]
CTD; 51111; -.
MGI; MGI:2444557; Kmt5b.
eggNOG; KOG2589; Eukaryota.
eggNOG; ENOG410XPH8; LUCA.
GeneTree; ENSGT00520000055640; -.
HOVERGEN; HBG105761; -.
InParanoid; Q3U8K7; -.
KO; K11429; -.
OMA; SGCLTRH; -.
OrthoDB; EOG091G0IUY; -.
PhylomeDB; Q3U8K7; -.
TreeFam; TF106433; -.
Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
ChiTaRS; Suv420h1; mouse.
PRO; PR:Q3U8K7; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000045098; -.
ExpressionAtlas; Q3U8K7; baseline and differential.
Genevisible; Q3U8K7; MM.
GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IDA:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IDA:MGI.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; ISO:MGI.
GO; GO:0034773; P:histone H4-K20 trimethylation; IEA:InterPro.
GO; GO:0016571; P:histone methylation; IDA:MGI.
GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR025790; Hist-Lys_N-MTase_Suvar4-20.
InterPro; IPR001214; SET_dom.
Pfam; PF00856; SET; 1.
SMART; SM00317; SET; 1.
PROSITE; PS51570; SAM_MT43_SUVAR420_2; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator; Chromosome;
Complete proteome; Isopeptide bond; Methyltransferase; Myogenesis;
Nucleus; Reference proteome; Repressor; S-adenosyl-L-methionine;
Transcription; Transcription regulation; Transferase; Ubl conjugation.
CHAIN 1 883 Histone-lysine N-methyltransferase KMT5B.
/FTId=PRO_0000281788.
DOMAIN 194 309 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
CROSSLNK 556 556 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q4FZB7}.
VAR_SEQ 104 126 Missing (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_024053.
VAR_SEQ 328 883 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_024054.
VAR_SEQ 393 394 TS -> SK (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_024055.
VAR_SEQ 395 883 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_024056.
VAR_SEQ 831 883 EGEEEEEDCEDDFDDDFIPLPPAKRLRLIVGKDSIDIDISS
RRREDQSLRLNA -> SGKAAEANCW (in isoform
5). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_024057.
CONFLICT 53 53 S -> N (in Ref. 3; AAH75709).
{ECO:0000305}.
CONFLICT 153 153 K -> E (in Ref. 2; AAH11214).
{ECO:0000305}.
CONFLICT 292 292 V -> L (in Ref. 1; BAC39834).
{ECO:0000305}.
CONFLICT 328 328 R -> Q (in Ref. 2; BAE31010).
{ECO:0000305}.
CONFLICT 428 428 P -> A (in Ref. 3; AAH75709).
{ECO:0000305}.
CONFLICT 472 472 E -> G (in Ref. 1; BAC38817).
{ECO:0000305}.
CONFLICT 521 521 N -> S (in Ref. 3; AAH75709).
{ECO:0000305}.
CONFLICT 590 590 P -> H (in Ref. 1; BAC38817).
{ECO:0000305}.
CONFLICT 595 595 R -> G (in Ref. 2; BAE31010).
{ECO:0000305}.
CONFLICT 664 664 H -> Y (in Ref. 3; AAH75709).
{ECO:0000305}.
CONFLICT 678 678 A -> T (in Ref. 3; AAH75709).
{ECO:0000305}.
HELIX 75 89 {ECO:0000244|PDB:4BUP}.
HELIX 91 94 {ECO:0000244|PDB:4BUP}.
HELIX 138 148 {ECO:0000244|PDB:4BUP}.
HELIX 151 158 {ECO:0000244|PDB:4BUP}.
HELIX 162 167 {ECO:0000244|PDB:4BUP}.
HELIX 173 187 {ECO:0000244|PDB:4BUP}.
HELIX 188 190 {ECO:0000244|PDB:4BUP}.
STRAND 196 201 {ECO:0000244|PDB:4BUP}.
STRAND 208 217 {ECO:0000244|PDB:4BUP}.
STRAND 224 235 {ECO:0000244|PDB:4BUP}.
HELIX 237 243 {ECO:0000244|PDB:4BUP}.
TURN 246 248 {ECO:0000244|PDB:4BUP}.
STRAND 253 256 {ECO:0000244|PDB:4BUP}.
TURN 257 260 {ECO:0000244|PDB:4BUP}.
STRAND 261 267 {ECO:0000244|PDB:4BUP}.
HELIX 268 271 {ECO:0000244|PDB:4BUP}.
STRAND 279 296 {ECO:0000244|PDB:4BUP}.
TURN 310 313 {ECO:0000244|PDB:4BUP}.
HELIX 315 317 {ECO:0000244|PDB:4BUP}.
HELIX 323 328 {ECO:0000244|PDB:4BUP}.
HELIX 331 333 {ECO:0000244|PDB:4BUP}.
SEQUENCE 883 AA; 98580 MW; 2B24461F582CC5F1 CRC64;
MKWLGDSKNM VVNGRRNGGK LSNDHQQNQS KLQQHSGKDT LKTGRNAVER RSSRCHGNSG
FEGQSRYVPS SGMSAKELCE NDDLATSLVL DPYLGFQTHK MNTSAFPSRS SRHISKADSF
SHNNPVRFRP IKGRQEELKE VIERFKKDEH LEKAFKCLTS GEWARHYFLN KNKMQEKLFK
EHVFIYLRMF ATDSGFEILP CNRYSSEQNG AKIVATKEWK RNDKIELLVG CIAELSEIEE
NMLLRHGEND FSVMYSTRKN CAQLWLGPAA FINHDCRPNC KFVSTGRDTA CVKALRDIEP
GEEISCYYGD GFFGENNEFC ECYTCERRGT GAFKSRVGLP APAPVINSKY GLRETDKRLN
RLKKLGDSSK NSDSQSVSSN TDADTTQEKD NATSNRKSSV GVKKSSKSRA LTRPSMPRVP
AASNSTSPKL VHTNNPRVPK KLRKPAKPLL SKIRLRNHCK RLDQKSASRK LEMGSLVLKE
PKVVLYKNLP IKKEREPEGP AHAAVGSGCL TRHAAREHRQ NHGRGAHSQG DSLPCTYTTR
RSLRTRTGLK ETTDIKLEPS PLDGYKNGIL EPCPDSGQQP TPEVLEELAP ETAHREEASQ
ECPKNDSCLS RKKFRQVKPV KHLAKTEDCS PEHSFPGKDG LPDLPGSHPD QGEPSGTVRV
PVSHTDSAPS PVGCSVVAPD SFTKDSFRTA QSKKKRRVTR YDAQLILENS SGIPKLTLRR
RHDSSSKTND HESDGVNSSK ISIKLSKDHD SDSNLYVAKL SNGVSAGPGS SSTKLKIQLK
RDEESRGPCA EGLHENGVCC SDPLSLLESQ MEVDDYSQYE EDSTDESSSS EGEEEEEDCE
DDFDDDFIPL PPAKRLRLIV GKDSIDIDIS SRRREDQSLR LNA


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EIAAB40615 H3-K9-HMTase 1,Histone H3-K9 methyltransferase 1,Histone-lysine N-methyltransferase SUV39H1,Homo sapiens,Human,KMT1A,Lysine N-methyltransferase 1A,Position-effect variegation 3-9 homolog,Su(var)3-9 ho
EIAAB40617 H3-K9-HMTase 2,Histone H3-K9 methyltransferase 2,Histone-lysine N-methyltransferase SUV39H2,Mouse,Mus musculus,Su(var)3-9 homolog 2,Suppressor of variegation 3-9 homolog 2,Suv39h2
EIAAB40614 Bos taurus,Bovine,Histone-lysine N-methyltransferase SUV39H1,Su(var)3-9 homolog 1,Suppressor of variegation 3-9 homolog 1,SUV39H1
EIAAB40616 Bos taurus,Bovine,Histone-lysine N-methyltransferase SUV39H2,Su(var)3-9 homolog 2,Suppressor of variegation 3-9 homolog 2,SUV39H2
EIAAB11717 DOT1L,DOT1-like protein,H3-K79-HMTase,Histone H3-K79 methyltransferase,Histone-lysine N-methyltransferase, H3 lysine-79 specific,Homo sapiens,Human,KIAA1814,KMT4,Lysine N-methyltransferase 4
EIAAB40619 Chicken,Gallus gallus,Histone-lysine N-methyltransferase SUV39H2,RCJMB04_5f7,Su(var)3-9 homolog 2,Suppressor of variegation 3-9 homolog 2,SUV39H2
20-272-190786 SUV39H1 - Mouse monoclonal [44.1] to SUV39H1; EC 2.1.1.43; Suppressor of variegation 3-9 homolog 1; Su(var)3-9 homolog 1; Position-effect variegation 3-9 homolog; Histone H3-K9 methyltransferase 1; H3 0.05 ml
EIAAB13541 Enhancer of zeste homolog 2,ENX-1,EZH2,Histone-lysine N-methyltransferase EZH2,Homo sapiens,Human,KMT6,Lysine N-methyltransferase 6
EIAAB12652 Ehmt1,Euchromatic histone-lysine N-methyltransferase 1,Euhmtase1,Eu-HMTase1,G9a-like protein 1,GLP,Glp,GLP1,Histone-lysine N-methyltransferase EHMT1,Kmt1d,Lysine N-methyltransferase 1D,Mouse,Mus muscu
EIAAB37955 ERG-associated protein with SET domain,ESET,H3-K9-HMTase 4,Histone H3-K9 methyltransferase 4,Histone-lysine N-methyltransferase SETDB1,Homo sapiens,Human,KIAA0067,KMT1E,Lysine N-methyltransferase 1E,S
EIAAB37951 Histone-lysine N-methyltransferase SETD1A,Homo sapiens,hSET1A,Human,KIAA0339,KMT2F,Lysine N-methyltransferase 2F,SET domain-containing protein 1A,SET1,Set1_Ash2 histone methyltransferase complex subun
EIAAB24944 Histone-lysine N-methyltransferase MLL4,Homo sapiens,HRX2,Human,KIAA0304,KMT2D,KMT2D,Lysine N-methyltransferase 2D,MLL2,MLL4,Myeloid_lymphoid or mixed-lineage leukemia protein 4,Trithorax homolog 2,TR
EIAAB37977 H4-K20-HMTase SETD8,Histone-lysine N-methyltransferase SETD8,Homo sapiens,Human,KMT5A,Lysine N-methyltransferase 5A,N-lysine methyltransferase SETD8,PR_SET domain-containing protein 07,PR_SET07,PRSET7
NSD1_MOUSE ELISA Kit FOR Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific; organism: Mouse; gene name: Nsd1 96T
CSB-EL016100HU Human Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific(NSD1) ELISA kit SpeciesHuman 96T


 

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