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Histone-lysine N-methyltransferase EHMT1 (EC 2.1.1.-) (EC 2.1.1.43) (Euchromatic histone-lysine N-methyltransferase 1) (Eu-HMTase1) (G9a-like protein 1) (GLP) (GLP1) (Lysine N-methyltransferase 1D)

 EHMT1_MOUSE             Reviewed;        1296 AA.
Q5DW34; A2AIS3; A2AIS4; Q5EBR1; Q6PGM0;
08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
08-MAR-2011, sequence version 2.
12-SEP-2018, entry version 130.
RecName: Full=Histone-lysine N-methyltransferase EHMT1;
EC=2.1.1.-;
EC=2.1.1.43;
AltName: Full=Euchromatic histone-lysine N-methyltransferase 1;
Short=Eu-HMTase1;
AltName: Full=G9a-like protein 1;
Short=GLP;
Short=GLP1;
AltName: Full=Lysine N-methyltransferase 1D;
Name=Ehmt1; Synonyms=Euhmtase1, Glp, Kmt1d;
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, DISRUPTION PHENOTYPE, INTERACTION WITH EHMT2,
AND TISSUE SPECIFICITY.
PubMed=15774718; DOI=10.1101/gad.1284005;
Tachibana M., Ueda J., Fukuda M., Takeda N., Ohta T., Iwanari H.,
Sakihama T., Kodama T., Hamakubo T., Shinkai Y.;
"Histone methyltransferases G9a and GLP form heteromeric complexes and
are both crucial for methylation of euchromatin at H3-K9.";
Genes Dev. 19:815-826(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-1296 (ISOFORM 2), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-1296 (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Brain;
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]
FUNCTION, AND MUTAGENESIS OF TYR-1153; 1198-ASN--CYS-1201; CYS-1201
AND TYR-1240.
PubMed=18818694; DOI=10.1038/emboj.2008.192;
Tachibana M., Matsumura Y., Fukuda M., Kimura H., Shinkai Y.;
"G9a/GLP complexes independently mediate H3K9 and DNA methylation to
silence transcription.";
EMBO J. 27:2681-2690(2008).
[5]
DOMAIN ANK REPEATS, AND INTERACTION WITH RELA.
PubMed=21131967; DOI=10.1038/ni.1968;
Levy D., Kuo A.J., Chang Y., Schaefer U., Kitson C., Cheung P.,
Espejo A., Zee B.M., Liu C.L., Tangsombatvisit S., Tennen R.I.,
Kuo A.Y., Tanjing S., Cheung R., Chua K.F., Utz P.J., Shi X.,
Prinjha R.K., Lee K., Garcia B.A., Bedford M.T., Tarakhovsky A.,
Cheng X., Gozani O.;
"Lysine methylation of the NF-kappaB subunit RelA by SETD6 couples
activity of the histone methyltransferase GLP at chromatin to tonic
repression of NF-kappaB signaling.";
Nat. Immunol. 12:29-36(2011).
-!- FUNCTION: Histone methyltransferase that specifically mono- and
dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2,
respectively) in euchromatin. H3K9me represents a specific tag for
epigenetic transcriptional repression by recruiting HP1 proteins
to methylated histones. Also weakly methylates 'Lys-27' of histone
H3 (H3K27me). Also required for DNA methylation, the histone
methyltransferase activity is not required for DNA methylation,
suggesting that these 2 activities function independently.
Probably targeted to histone H3 by different DNA-binding proteins
like E2F6, MGA, MAX and/or DP1. During G0 phase, it probably
contributes to silencing of MYC- and E2F-responsive genes,
suggesting a role in G0/G1 transition in cell cycle. In addition
to the histone methyltransferase activity, also methylates non-
histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53.
{ECO:0000269|PubMed:15774718, ECO:0000269|PubMed:18818694}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000269|PubMed:15774718}.
-!- ACTIVITY REGULATION: Methyltransferase activity is inhibited by
BIX-01294. Efficiently inhibited by compound E72, a BIX-01294
derivative in which the diazepane ring and the benzyl are replaced
with a 3-dimethylaminopropyl and a 5-aminopentyl group at sites B
and C, respectively (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with WIZ. Part of the E2F6.com-1 complex in G0
phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EHMT1, RING1,
RNF2, MBLR, L3MBTL2 and YAF2. Interacts with MPHOSPH8 (By
similarity). Interacts with CDYL. Interacts with REST only in the
presence of CDYL. Part of a complex containing at least CDYL,
REST, WIZ, SETB1, EHMT1 and EHMT2 (By similarity). Heterodimer;
heterodimerizes with EHMT2. Interacts (via ANK repeats) with RELA
(when monomethylated at 'Lys-310'). {ECO:0000250,
ECO:0000269|PubMed:15774718, ECO:0000269|PubMed:21131967}.
-!- INTERACTION:
A2A935-3:Prdm16; NbExp=2; IntAct=EBI-16080518, EBI-16080455;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15774718}.
Chromosome {ECO:0000269|PubMed:15774718}. Note=Associates with
euchromatic regions.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q5DW34-1; Sequence=Displayed;
Name=2;
IsoId=Q5DW34-2; Sequence=VSP_040724, VSP_040725;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q5DW34-3; Sequence=VSP_040726;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15774718}.
-!- DOMAIN: The ANK repeats specifically recognize and bind H3K9me1
and H3K9me2 (By similarity). They also specifically recognize and
bind RELA subunit of NF-kappa-B, when RELA is monomethylated at
'Lys-310'. {ECO:0000250, ECO:0000269|PubMed:21131967}.
-!- DOMAIN: The SET domain mediates interaction with WIZ.
{ECO:0000250}.
-!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that
are arranged in a triangular cluster; some of these Cys residues
contribute to the binding of two zinc ions within the cluster.
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Embryos die around E9.5. Levels of H3K9me1
and H3K9me2 are drastically reduced.
{ECO:0000269|PubMed:15774718}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
-!- SEQUENCE CAUTION:
Sequence=CAM22112.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB205007; BAD90007.1; -; mRNA.
EMBL; AL732525; CAM22112.1; ALT_INIT; Genomic_DNA.
EMBL; AL732525; CAM22113.1; -; Genomic_DNA.
EMBL; AL732525; CAM22114.1; -; Genomic_DNA.
EMBL; BC056938; AAH56938.1; -; mRNA.
EMBL; BC089302; AAH89302.1; -; mRNA.
CCDS; CCDS15740.1; -. [Q5DW34-1]
CCDS; CCDS59634.1; -. [Q5DW34-2]
CCDS; CCDS59636.1; -. [Q5DW34-3]
RefSeq; NP_001012536.2; NM_001012518.3. [Q5DW34-1]
RefSeq; NP_001103156.1; NM_001109686.2. [Q5DW34-2]
RefSeq; NP_001103157.1; NM_001109687.2. [Q5DW34-3]
UniGene; Mm.24176; -.
ProteinModelPortal; Q5DW34; -.
SMR; Q5DW34; -.
BioGrid; 218847; 12.
DIP; DIP-49000N; -.
DIP; DIP-59572N; -.
IntAct; Q5DW34; 9.
MINT; Q5DW34; -.
STRING; 10090.ENSMUSP00000100002; -.
iPTMnet; Q5DW34; -.
PhosphoSitePlus; Q5DW34; -.
PaxDb; Q5DW34; -.
PeptideAtlas; Q5DW34; -.
PRIDE; Q5DW34; -.
Ensembl; ENSMUST00000046227; ENSMUSP00000046077; ENSMUSG00000036893. [Q5DW34-3]
Ensembl; ENSMUST00000114432; ENSMUSP00000110075; ENSMUSG00000036893. [Q5DW34-2]
Ensembl; ENSMUST00000147147; ENSMUSP00000119057; ENSMUSG00000036893. [Q5DW34-1]
GeneID; 77683; -.
KEGG; mmu:77683; -.
UCSC; uc008iph.4; mouse. [Q5DW34-3]
UCSC; uc008ipi.4; mouse. [Q5DW34-1]
UCSC; uc012brr.3; mouse. [Q5DW34-2]
CTD; 79813; -.
MGI; MGI:1924933; Ehmt1.
eggNOG; KOG1082; Eukaryota.
eggNOG; COG0666; LUCA.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00780000121845; -.
HOGENOM; HOG000231216; -.
HOVERGEN; HBG028394; -.
InParanoid; Q5DW34; -.
KO; K11420; -.
OMA; CGEEASK; -.
OrthoDB; EOG091G00U6; -.
PhylomeDB; Q5DW34; -.
TreeFam; TF106443; -.
Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
Reactome; R-MMU-6804760; Regulation of TP53 Activity through Methylation.
Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6.
ChiTaRS; Ehmt1; mouse.
PRO; PR:Q5DW34; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000036893; Expressed in 242 organ(s), highest expression level in pes.
ExpressionAtlas; Q5DW34; baseline and differential.
Genevisible; Q5DW34; MM.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:UniProtKB.
GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IDA:UniProtKB.
GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:UniProtKB.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; ISO:MGI.
GO; GO:0008168; F:methyltransferase activity; ISO:MGI.
GO; GO:0002039; F:p53 binding; ISO:MGI.
GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006325; P:chromatin organization; ISO:MGI.
GO; GO:0006306; P:DNA methylation; IDA:UniProtKB.
GO; GO:0016571; P:histone methylation; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0018027; P:peptidyl-lysine dimethylation; IMP:UniProtKB.
GO; GO:0018026; P:peptidyl-lysine monomethylation; IMP:UniProtKB.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
GO; GO:0045995; P:regulation of embryonic development; IMP:UniProtKB.
GO; GO:0060992; P:response to fungicide; IEA:Ensembl.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR038035; EHMT1.
InterPro; IPR007728; Pre-SET_dom.
InterPro; IPR001214; SET_dom.
PANTHER; PTHR22884:SF364; PTHR22884:SF364; 1.
Pfam; PF12796; Ank_2; 2.
Pfam; PF05033; Pre-SET; 1.
Pfam; PF00856; SET; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 7.
SMART; SM00468; PreSET; 1.
SMART; SM00317; SET; 1.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 5.
PROSITE; PS50867; PRE_SET; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ANK repeat; Chromatin regulator;
Chromosome; Complete proteome; Isopeptide bond; Metal-binding;
Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
Repeat; S-adenosyl-L-methionine; Transferase; Ubl conjugation; Zinc.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9H9B1}.
CHAIN 2 1296 Histone-lysine N-methyltransferase EHMT1.
/FTId=PRO_0000405844.
REPEAT 735 764 ANK 1.
REPEAT 770 799 ANK 2.
REPEAT 803 832 ANK 3.
REPEAT 836 866 ANK 4.
REPEAT 870 899 ANK 5.
REPEAT 903 932 ANK 6.
REPEAT 936 965 ANK 7.
REPEAT 969 1002 ANK 8.
DOMAIN 1058 1121 Pre-SET. {ECO:0000255|PROSITE-
ProRule:PRU00157}.
DOMAIN 1124 1241 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
REGION 903 905 Histone H3K9me binding. {ECO:0000250}.
REGION 1134 1136 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 1160 1179 Interaction with histone H3.
{ECO:0000250}.
REGION 1198 1199 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 1240 1243 Interaction with histone H3.
{ECO:0000250}.
COMPBIAS 440 447 Poly-Arg.
COMPBIAS 1290 1293 Poly-Ala.
METAL 1060 1060 Zinc 1. {ECO:0000250}.
METAL 1060 1060 Zinc 2. {ECO:0000250}.
METAL 1062 1062 Zinc 1. {ECO:0000250}.
METAL 1066 1066 Zinc 1. {ECO:0000250}.
METAL 1066 1066 Zinc 3. {ECO:0000250}.
METAL 1071 1071 Zinc 1. {ECO:0000250}.
METAL 1073 1073 Zinc 2. {ECO:0000250}.
METAL 1103 1103 Zinc 2. {ECO:0000250}.
METAL 1103 1103 Zinc 3. {ECO:0000250}.
METAL 1107 1107 Zinc 2. {ECO:0000250}.
METAL 1109 1109 Zinc 3. {ECO:0000250}.
METAL 1113 1113 Zinc 3. {ECO:0000250}.
METAL 1201 1201 Zinc 4. {ECO:0000250}.
METAL 1254 1254 Zinc 4. {ECO:0000250}.
METAL 1256 1256 Zinc 4. {ECO:0000250}.
METAL 1261 1261 Zinc 4. {ECO:0000250}.
BINDING 1153 1153 Histone H3K9me. {ECO:0000250}.
BINDING 1171 1171 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
BINDING 1255 1255 S-adenosyl-L-methionine; via amide
nitrogen. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q9H9B1}.
MOD_RES 433 433 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H9B1}.
MOD_RES 481 481 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H9B1}.
MOD_RES 1046 1046 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H9B1}.
CROSSLNK 23 23 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:Q9H9B1}.
CROSSLNK 23 23 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q9H9B1}.
CROSSLNK 191 191 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9H9B1}.
CROSSLNK 229 229 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9H9B1}.
CROSSLNK 232 232 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9H9B1}.
CROSSLNK 315 315 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9H9B1}.
CROSSLNK 325 325 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9H9B1}.
CROSSLNK 430 430 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9H9B1}.
CROSSLNK 559 559 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9H9B1}.
CROSSLNK 644 644 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9H9B1}.
CROSSLNK 659 659 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9H9B1}.
CROSSLNK 729 729 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9H9B1}.
VAR_SEQ 273 279 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_040724.
VAR_SEQ 455 500 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_040725.
VAR_SEQ 550 597 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_040726.
MUTAGEN 1153 1153 Y->V: In LM7; does not prevent
methyltransferase activity; when
associated with F-1240.
{ECO:0000269|PubMed:18818694}.
MUTAGEN 1198 1201 Missing: In LM3; does not form
heterodimer with EHMT2 and is defective
in mediating both H3K9me and DNA
methylation.
{ECO:0000269|PubMed:18818694}.
MUTAGEN 1201 1201 C->A: In LM4; does not prevent
methyltransferase activity.
{ECO:0000269|PubMed:18818694}.
MUTAGEN 1240 1240 Y->F: In LM7; does not prevent
methyltransferase activity; when
associated with V-1153.
{ECO:0000269|PubMed:18818694}.
CONFLICT 411 411 E -> D (in Ref. 1; BAD90007).
{ECO:0000305}.
SEQUENCE 1296 AA; 141999 MW; B7783B6F38D3C7CB CRC64;
MAAADAEQAV LAKQETKQDC CMKTELLRED TPMAADEGST EKQEGETPMA ADGETNGSCE
KSGDPSHLNA PKHTQENTRA SPQEGTNRVS RVAENGVSER DTEVGKQNHV TADDFMQTSV
IGSNGYFLNK PALQGQPLRT PNILTSSLPG HAAKTLPGGA SKCRTLSALP QTPTTAPTVP
GEGSADTEDR KPTASGTDVR VHRARKTMPK SILGLHAASK DHREVQDHKE PKEDINRNIS
ECGRQQLLPT FPALHQSLPQ NQCYMATTKS QTACLPFVLA AAVSRKKKRR MGTYSLVPKK
KTKVLKQRTV IEMFKSITHS TVGAKGEKAL DDSALHVNGE SLEMDSEDED SDELEDDEDH
GAEQAAAFPT EDSRTSKESM SETDRAAKMD GDSEEEQESP DTGEDEDGGD ESDLSSESSI
KKKFLKRRGK TDSPWIKPAR KRRRRSRKKP SSMLGSEACK SSPGSMEQAA LGDSAGYMEV
SLDSLDLRVR GILSSQTENE GLASGPDVLG TDGLQEVPLC SCRMETPKSR EISTLANNQC
MATESVDHEL GRCTNSVVKY ELMRPSNKAP LLVLCEDHRG RMVKHQCCPG CGYFCTAGNF
MECQPESSIS HRFHKDCASR VNNASYCPHC GEEASKAKEV TIAKADTTST VTLAPGQEKS
LAAEGRADTT TGSIAGAPED ERSQSTAPQA PECFDPAGPA GLVRPTSGLS QGPGKETLES
ALIALDSEKP KKLRFHPKQL YFSARQGELQ KVLLMLVDGI DPNFKMEHQS KRSPLHAAAE
AGHVDICHML VQAGANIDTC SEDQRTPLME AAENNHLDAV KYLIKAGAQV DPKDAEGSTC
LHLAAKKGHY DVVQYLLSNG QMDVNCQDDG GWTPMIWATE YKHVELVKLL LSKGSDINIR
DNEENICLHW AAFSGCVDIA EILLAAKCDL HAVNIHGDSP LHIAARENRY DCVVLFLSRD
SDVTLKNKEG ETPLQCASLS SQVWSALQMS KALRDSAPDK PVAVEKTVSR DIARGYERIP
IPCVNAVDSE LCPTNYKYVS QNCVTSPMNI DRNITHLQYC VCVDDCSSST CMCGQLSMRC
WYDKDGRLLP EFNMAEPPLI FECNHACSCW RNCRNRVVQN GLRARLQLYR TQDMGWGVRS
LQDIPLGTFV CEYVGELISD SEADVREEDS YLFDLDNKDG EVYCIDARFY GNVSRFINHH
CEPNLVPVRV FMSHQDLRFP RIAFFSTRLI QAGEQLGFDY GERFWDVKGK LFSCRCGSSK
CRHSSAALAQ RQASAAQEPQ ENGLPDTSSA AAADPL


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EIAAB12654 Bat8,Ehmt2,Euchromatic histone-lysine N-methyltransferase 2,G9a,H3-K9-HMTase 3,Histone H3-K9 methyltransferase 3,Histone-lysine N-methyltransferase EHMT2,HLA-B-associated transcript 8,Mouse,Mus muscul
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
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
EIAAB40618 H3-K9-HMTase 2,Histone H3-K9 methyltransferase 2,Histone-lysine N-methyltransferase SUV39H2,Homo sapiens,Human,KMT1B,Lysine N-methyltransferase 1B,Su(var)3-9 homolog 2,Suppressor of variegation 3-9 ho
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
EI24 EHMT1 Gene euchromatic histone-lysine N-methyltransferase 1
EIAAB37975 H3-K4-HMTase SETD7,Histone H3-K4 methyltransferase SETD7,Histone-lysine N-methyltransferase SETD7,Homo sapiens,Human,KIAA1717,KMT7,Lysine N-methyltransferase 7,SET domain-containing protein 7,SET7,SET
EIAAB38899 Histone methyltransferase SMYD2,Homo sapiens,HSKM-B,Human,KMT3C,Lysine N-methyltransferase 3C,N-lysine methyltransferase SMYD2,SET and MYND domain-containing protein 2,SMYD2
EIAAB37958 C13orf4,Chronic lymphocytic leukemia deletion region gene 8 protein,CLLD8,Histone-lysine N-methyltransferase SETDB2,Homo sapiens,Human,KMT1F,Lysine N-methyltransferase 1F,SET domain bifurcated 2,SETDB
EIAAB37954 Histone-lysine N-methyltransferase SETD1B,Homo sapiens,hSET1B,Human,KIAA1076,KMT2G,Lysine N-methyltransferase 2G,SET domain-containing protein 1B,SET1B,SETD1B
18-003-42222 Histone-lysine N-methyltransferase. H3 lysine-9 specific 1 - EC 2.1.1.43; Histone H3-K9 methyltransferase 1; H3-K9-HMTase 1; Suppressor of variegation 3-9 homolog 1; Su(var)3-9 homolog 1 Polyclonal 0.1 mg Protein A
NSD1_MOUSE ELISA Kit FOR Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific; organism: Mouse; gene name: Nsd1 96T
CSB-EL016100MO Mouse Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific(NSD1) ELISA kit SpeciesMouse 96T
CSB-EL016100HU Human Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific(NSD1) ELISA kit SpeciesHuman 96T
EIAAB27934 DC28,Histone-lysine N-methyltransferase NSD3,Homo sapiens,Human,NSD3,Nuclear SET domain-containing protein 3,Protein whistle,WHSC1L1,WHSC1-like 1 isoform 9 with methyltransferase activity to lysine,WH
CSB-EL016100HU Human Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific(NSD1) ELISA kit 96T
CSB-EL016100MO Mouse Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific(NSD1) ELISA kit 96T
CSB-EL007496MO Mouse euchromatic histone-lysine N-methyltransferase 1 (EHMT1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL007496HU Human euchromatic histone-lysine N-methyltransferase 1 (EHMT1) ELISA kit, Species Human, Sample Type serum, plasma 96T
EIAAB13541 Enhancer of zeste homolog 2,ENX-1,EZH2,Histone-lysine N-methyltransferase EZH2,Homo sapiens,Human,KMT6,Lysine N-methyltransferase 6


 

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