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Histone-lysine N-methyltransferase SETDB1 (EC 2.1.1.43) (ERG-associated protein with SET domain) (ESET) (SET domain bifurcated 1)

 SETB1_MOUSE             Reviewed;        1307 AA.
O88974; Q6AXH8; Q78N64; Q78N65; Q80U84; Q8BTV6; Q8CIX7; Q922K1;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
28-MAR-2018, entry version 157.
RecName: Full=Histone-lysine N-methyltransferase SETDB1;
EC=2.1.1.43;
AltName: Full=ERG-associated protein with SET domain;
Short=ESET;
AltName: Full=SET domain bifurcated 1;
Name=Setdb1; Synonyms=Eset, Kiaa0067;
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] (ISOFORMS 1 AND 2), ENZYME ACTIVITY,
INTERACTION WITH ERG, AND MUTAGENESIS OF CYS-798 AND CYS-1242.
STRAIN=BDF1; TISSUE=Blood;
PubMed=11791185; DOI=10.1038/sj.onc.1204998;
Yang L., Xia L., Wu D.Y., Wang H., Chansky H.A., Schubach W.H.,
Hickstein D.D., Zhang Y.;
"Molecular cloning of ESET, a novel histone H3-specific
methyltransferase that interacts with ERG transcription factor.";
Oncogene 21:148-152(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE [GENOMIC
DNA], ALTERNATIVE SPLICING (ISOFORM 6), AND TISSUE SPECIFICITY.
STRAIN=BDF1, and C57BL/6J X DBA/2;
PubMed=14522075; DOI=10.1016/S0167-4781(03)00155-6;
Blackburn M.L., Chansky H.A., Zielinska-Kwiatkowska A., Matsui Y.,
Yang L.;
"Genomic structure and expression of the mouse ESET gene encoding an
ERG-associated histone methyltransferase with a SET domain.";
Biochim. Biophys. Acta 1629:8-14(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 7).
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 145-1307 (ISOFORM 4).
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-1307 (ISOFORM 4).
STRAIN=NOD; TISSUE=Thymus;
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).
[6]
INTERACTION WITH HDAC1; HDAC2; SIN3A AND SIN3B.
PubMed=12398767; DOI=10.1042/BJ20020854;
Yang L., Mei Q., Zielinska-Kwiatkowska A., Matsui Y., Blackburn M.L.,
Benedetti D., Krumm A.A., Taborsky G.J. Jr., Chansky H.A.;
"An ERG (ets-related gene)-associated histone methyltransferase
interacts with histone deacetylases 1/2 and transcription co-
repressors mSin3A/B.";
Biochem. J. 369:651-657(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-117 AND
THR-120, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Lung, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Histone methyltransferase that specifically
trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation
represents a specific tag for epigenetic transcriptional
repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to
methylated histones. Mainly functions in euchromatin regions,
thereby playing a central role in the silencing of euchromatic
genes. H3 'Lys-9' trimethylation is coordinated with DNA
methylation. Probably forms a complex with MBD1 and ATF7IP that
represses transcription and couples DNA methylation and histone
'Lys-9' trimethylation. Its activity is dependent on MBD1 and is
heritably maintained through DNA replication by being recruited by
CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor
recruited by KRAB zinc-finger proteins. Probably forms a
corepressor complex required for activated KRAS-mediated promoter
hypermethylation and transcriptional silencing of tumor suppressor
genes (TSGs) or other tumor-related genes in colorectal cancer
(CRC) cells (By similarity). Also required to maintain a
transcriptionally repressive state of genes in undifferentiated
embryonic stem cells (ESCs) (By similarity). Associates at
promoter regions of tumor suppressor genes (TSGs) leading to their
gene silencing. The SETDB1-TRIM28-ZNF274 complex may play a role
in recruiting ATRX to the 3'-exons of zinc-finger coding genes
with atypical chromatin signatures to establish or
maintain/protect H3K9me3 at these transcriptionally active regions
(By similarity). {ECO:0000250|UniProtKB:Q15047}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000255|PROSITE-ProRule:PRU00906,
ECO:0000269|PubMed:11791185}.
-!- SUBUNIT: Part of a complex containing at least CDYL, REST, WIZ,
SETB1, EHMT1 and EHMT2. During DNA replication, it is recruited by
SETDB1 to form a S phase-specific complex that facilitates
methylation of H3 'Lys-9' during replication-coupled chromatin
assembly and is at least composed of the CAF-1 subunit CHAF1A,
MBD1 and SETDB1. Probably part of a corepressor complex containing
ZNF304, TRIM28, SETDB1 and DNMT1. Interacts with TRIM28/TIF1B.
Interacts with ATF7IP and ATF7IP2; the interaction with ATF7IP is
required to stimulate histone methyltransferase activity and
facilitate the conversion of dimethylated to trimethylated H3
'Lys-9'. Interacts with MBD1; interaction is abolished when MBD1
is sumoylated. Interacts with CBX1 and CBX5. Interacts with DNMT3A
and DNMT3B. Interacts with SUMO2. Interacts with CHD7, NLK1 and
PPARG. Interacts with MPHOSPH8 (By similarity). Interacts with ERG
(PubMed:11791185). Interacts with HDAC1, HDAC2, SIN3A, SIN3B
(PubMed:12398767). Interacts with ATRX. Forms a complex with ATRX,
TRIM28 and ZNF274 (By similarity). {ECO:0000250|UniProtKB:Q15047,
ECO:0000269|PubMed:11791185, ECO:0000269|PubMed:12398767}.
-!- INTERACTION:
P81270:Erg; NbExp=3; IntAct=EBI-79658, EBI-79647;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
{ECO:0000250}. Note=Associated with non-pericentromeric regions of
chromatin. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Comment=Experimental confirmation may be lacking for some
isoforms.;
Name=1;
IsoId=O88974-1; Sequence=Displayed;
Name=2;
IsoId=O88974-2; Sequence=VSP_002219, VSP_002220;
Name=3;
IsoId=O88974-3; Sequence=VSP_002221;
Name=4;
IsoId=O88974-4; Sequence=VSP_024031;
Name=5;
IsoId=O88974-5; Sequence=VSP_024032;
Name=6;
IsoId=O88974-6; Sequence=VSP_024031, VSP_024032;
Name=7;
IsoId=O88974-7; Sequence=VSP_024033;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Strong expression in
liver and testis. {ECO:0000269|PubMed:14522075}.
-!- DOMAIN: The pre-SET, SET and post-SET domains are all required for
methyltransferase activity. The 347-amino-acid insertion in the
SET domain has no effect on the catalytic activity.
-!- 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}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00906}.
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EMBL; AF091628; AAC43039.1; -; mRNA.
EMBL; AY091600; AAM13922.1; -; mRNA.
EMBL; AF546078; AAN52358.1; -; mRNA.
EMBL; AY226577; AAO73535.2; -; Genomic_DNA.
EMBL; AY226577; AAO73536.2; -; Genomic_DNA.
EMBL; BC007176; AAH07176.1; -; mRNA.
EMBL; BC079537; AAH79537.1; -; mRNA.
EMBL; AK122198; BAC65480.3; -; Transcribed_RNA.
EMBL; AK088590; BAC40439.1; -; mRNA.
CCDS; CCDS17613.1; -. [O88974-4]
CCDS; CCDS50991.1; -. [O88974-1]
PIR; T17453; T17453.
UniGene; Mm.490259; -.
ProteinModelPortal; O88974; -.
SMR; O88974; -.
IntAct; O88974; 9.
STRING; 10090.ENSMUSP00000015841; -.
iPTMnet; O88974; -.
PhosphoSitePlus; O88974; -.
EPD; O88974; -.
MaxQB; O88974; -.
PaxDb; O88974; -.
PeptideAtlas; O88974; -.
PRIDE; O88974; -.
UCSC; uc008qjo.2; mouse. [O88974-5]
MGI; MGI:1934229; Setdb1.
eggNOG; KOG1141; Eukaryota.
eggNOG; COG2940; LUCA.
HOVERGEN; HBG061013; -.
InParanoid; O88974; -.
ChiTaRS; Setdb1; mouse.
PRO; PR:O88974; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_SETDB1; -.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0003682; F:chromatin binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0060348; P:bone development; IMP:MGI.
GO; GO:0036124; P:histone H3-K9 trimethylation; IMP:MGI.
GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
GO; GO:0090309; P:positive regulation of methylation-dependent chromatin silencing; ISS:UniProtKB.
GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR016177; DNA-bd_dom_sf.
InterPro; IPR025796; Hist-Lys_N-MeTrfase_SETDB1.
InterPro; IPR001739; Methyl_CpG_DNA-bd.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR007728; Pre-SET_dom.
InterPro; IPR001214; SET_dom.
InterPro; IPR002999; Tudor.
Pfam; PF01429; MBD; 1.
Pfam; PF05033; Pre-SET; 1.
Pfam; PF00856; SET; 1.
SMART; SM00391; MBD; 1.
SMART; SM00468; PreSET; 1.
SMART; SM00317; SET; 1.
SMART; SM00333; TUDOR; 2.
SUPFAM; SSF54171; SSF54171; 1.
PROSITE; PS50982; MBD; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50867; PRE_SET; 1.
PROSITE; PS51573; SAM_MT43_SUVAR39_1; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
Alternative splicing; Chromatin regulator; Chromosome; Coiled coil;
Complete proteome; Isopeptide bond; Metal-binding; Methylation;
Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
Repeat; Repressor; S-adenosyl-L-methionine; Transcription;
Transcription regulation; Transferase; Ubl conjugation; Zinc.
CHAIN 1 1307 Histone-lysine N-methyltransferase
SETDB1.
/FTId=PRO_0000186065.
DOMAIN 257 320 Tudor 1.
DOMAIN 347 403 Tudor 2.
DOMAIN 611 682 MBD. {ECO:0000255|PROSITE-
ProRule:PRU00338}.
DOMAIN 744 817 Pre-SET. {ECO:0000255|PROSITE-
ProRule:PRU00157}.
DOMAIN 820 1282 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 1291 1307 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
REGION 830 832 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 1239 1240 S-adenosyl-L-methionine binding.
{ECO:0000250}.
COILED 30 65 {ECO:0000255}.
METAL 746 746 Zinc 1. {ECO:0000250}.
METAL 746 746 Zinc 2. {ECO:0000250}.
METAL 748 748 Zinc 1. {ECO:0000250}.
METAL 752 752 Zinc 1. {ECO:0000250}.
METAL 752 752 Zinc 3. {ECO:0000250}.
METAL 758 758 Zinc 1. {ECO:0000250}.
METAL 760 760 Zinc 2. {ECO:0000250}.
METAL 798 798 Zinc 2. {ECO:0000250}.
METAL 798 798 Zinc 3. {ECO:0000250}.
METAL 802 802 Zinc 2. {ECO:0000250}.
METAL 804 804 Zinc 3. {ECO:0000250}.
METAL 809 809 Zinc 3. {ECO:0000250}.
METAL 1242 1242 Zinc 4. {ECO:0000250}.
METAL 1295 1295 Zinc 4. {ECO:0000250}.
METAL 1297 1297 Zinc 4. {ECO:0000250}.
METAL 1302 1302 Zinc 4. {ECO:0000250}.
BINDING 868 868 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
BINDING 870 870 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
BINDING 1236 1236 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
MOD_RES 112 112 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 120 120 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 993 993 Phosphothreonine; by NLK.
{ECO:0000250|UniProtKB:Q15047}.
MOD_RES 1042 1042 Phosphoserine.
{ECO:0000250|UniProtKB:Q15047}.
MOD_RES 1186 1186 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:Q15047}.
MOD_RES 1186 1186 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:Q15047}.
MOD_RES 1194 1194 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:Q15047}.
MOD_RES 1194 1194 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:Q15047}.
CROSSLNK 182 182 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q15047}.
CROSSLNK 182 182 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:Q15047}.
CROSSLNK 1049 1049 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:Q15047}.
CROSSLNK 1049 1049 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q15047}.
CROSSLNK 1055 1055 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q15047}.
CROSSLNK 1085 1085 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q15047}.
CROSSLNK 1165 1165 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q15047}.
VAR_SEQ 1 807 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_002221.
VAR_SEQ 474 474 D -> ES (in isoform 4 and isoform 6).
{ECO:0000303|PubMed:12693553,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_024031.
VAR_SEQ 482 486 SRKQV -> AQSQK (in isoform 2).
{ECO:0000303|PubMed:11791185}.
/FTId=VSP_002219.
VAR_SEQ 489 1307 Missing (in isoform 2).
{ECO:0000303|PubMed:11791185}.
/FTId=VSP_002220.
VAR_SEQ 527 1307 Missing (in isoform 5 and isoform 6).
{ECO:0000303|PubMed:14522075}.
/FTId=VSP_024032.
VAR_SEQ 756 1307 Missing (in isoform 7).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_024033.
MUTAGEN 798 798 C->T: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:11791185}.
MUTAGEN 1242 1242 C->T: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:11791185}.
CONFLICT 463 463 I -> M (in Ref. 5; BAC40439).
{ECO:0000305}.
CONFLICT 1092 1092 P -> S (in Ref. 4; BAC65480).
{ECO:0000305}.
SEQUENCE 1307 AA; 144549 MW; 326AED6371D156C2 CRC64;
MSSLPGCMSL AAAPAAADSA EIAELQQAVV EELGISMEEL RQYIDEELEK MDCIQQRKKQ
LAELETWVLQ KESEVAYVDR LFDDASREVT NCESLVKDFY SKLGLQYHDS SSEDEASRPT
EIIEIPDEDD DVLSIDSGDA GSRTPKDQKL REAMAALRKS AQDVQKFMDA VNKKSSSQDL
HKGTLGQVSG ELSKDGDLIV SMRILGKKRT KTWHKGTLIA IQTVGLGKKY KVKFDNKGKS
LLSGNHIAYD YHPPADKLFV GSRVVAKYKD GNQVWLYAGI VAETPNVKNK LRFLIFFDDG
YASYVTQSEL YPICRPLKKT WEDIEDSSCR DFIEEYITAY PNRPMVLLKS GQLIKTEWEG
TWWKSRVEEV DGSLVRILFL DDKRCEWIYR GSTRLEPMFS MKTSSASAME KKQGGQLRTR
PNMGAVRSKG PVVQYTQDLT GTGIQFKPME PLQPIAPPAP LPIPPLSPQA ADTDLESQLA
QSRKQVAKKS TSFRPGSVGS GHSSPTSSTL SENVSAGKLG INQTYRSPLA SVTSTPASAA
PPVPPVPPGP PTPPGPPAPP GPLAPPAFHG MLERAPAEPS YRAPMEKLFY LPHVCSYTCL
SRIRPMRNEQ YRGKNPLLVP LLYDFRRMTA RRRVNRKMGF HVIYKTPCGL CLRTMQEIER
YLFETGCDFL FLEMFCLDPY VLVDRKFQPF KPFYYILDIT YGKEDVPLSC VNEIDTTPPP
QVAYSKERIP GKGVFINTGP EFLVGCDCKD GCRDKSKCAC HQLTIQATAC TPGGQVNPNS
GYQYKRLEEC LPTGVYECNK RCNCDPNMCT NRLVQHGLQV RLQLFKTQNK GWGIRCLDDI
AKGSFVCIYA GKILTDDFAD KEGLEMGDEY FANLDHIESV ENFKEGYESD VPTSSDSSGV
DMKDQEDGNS GSEDPEESND DSSDDNFCKD EDFSTSSVWR SYATRRQTRG QKENELSEMT
SKDSRPPDLG PPHVPIPSSV SVGGCNPPSS EETPKNKVAS WLSCNSVSEG GFADSDSRSS
FKTSEGGDGR AGGGRGEAER ASTSGLSFKD EGDNKQPKKE DPENRNKMPV VTEGSQNHGH
NPPMKSEGLR RPASKMSVLQ SQRVVTSTQS NPDDILTLSS STESEGESGT SRKPTAGHTS
ATAVDSDDIQ TISSGSDGDD FEDKKNLSGP TKRQVAVKST RGFALKSTHG IAIKSTNMAS
VDKGESAPVR KNTRQFYDGE ESCYIIDAKL EGNLGRYLNH SCSPNLFVQN VFVDTHDLRF
PWVAFFASKR IRAGTELTWD YNYEVGSVEG KELLCCCGAI ECRGRLL


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EIAAB37956 ERG-associated protein with SET domain,ESET,Eset,Histone-lysine N-methyltransferase SETDB1,Kiaa0067,Mouse,Mus musculus,SET domain bifurcated 1,Setdb1
18-272-195678 SETDB1 - Rabbit polyclonal to SETDB1; EC 2.1.1.43; SET domain bifurcated 1; ERG-associated protein with SET domain; ESET; Histone H3-K9 methyltransferase 4; H3-K9-HMTase 4 Polyclonal 0.05 mg
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
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
LF-PA41037 anti-SET Domain, Bifurcated 1 (SETDB1) , Rabbit polyclonal to SET Domain, Bifurcated 1 (SETDB1) , Isotype IgG, Host Rabbit 50 ug
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
EIAAB37957 Gm293,Histone-lysine N-methyltransferase SETDB2,Mouse,Mus musculus,SET domain bifurcated 2,Setdb2
EIAAB37978 H4-K20-HMTase SETD8,Histone-lysine N-methyltransferase SETD8,Mouse,Mus musculus,N-lysine methyltransferase SETD8,PR_SET domain-containing protein 07,PR_SET07,PR-Set7,SET domain-containing protein 8,Se
EIAAB37979 Bos taurus,Bovine,H4-K20-HMTase SETD8,Histone-lysine N-methyltransferase SETD8,N-lysine methyltransferase SETD8,PR_SET domain-containing protein 07,PR_SET07,PR-Set7,SET domain-containing protein 8,SET
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
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
EIAAB32313 Gm92,Mouse,Mus musculus,PR domain zinc finger protein 6,PR domain-containing protein 6,PR domain-containing protein in smooth muscle,Prdm6,Prism,Putative histone-lysine N-methyltransferase PRDM6
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
EIAAB37954 Histone-lysine N-methyltransferase SETD1B,Homo sapiens,hSET1B,Human,KIAA1076,KMT2G,Lysine N-methyltransferase 2G,SET domain-containing protein 1B,SET1B,SETD1B
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-EL021110HU Human Histone-lysine N-methyltransferase SETDB1(SETDB1) ELISA kit SpeciesHuman 96T
CSB-EL021110MO Mouse Histone-lysine N-methyltransferase SETDB1(SETDB1) ELISA kit SpeciesMouse 96T
CSB-EL021110HU Human Histone-lysine N-methyltransferase SETDB1(SETDB1) ELISA kit 96T
CSB-EL021110MO Mouse Histone-lysine N-methyltransferase SETDB1(SETDB1) ELISA kit 96T
SETB1_MOUSE ELISA Kit FOR Histone-lysine N-methyltransferase SETDB1; organism: Mouse; gene name: Setdb1 96T
SETDB1 SETDB1 Gene SET domain, bifurcated 1
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
EIAAB32321 Histone-lysine N-methyltransferase PRDM9,Homo sapiens,Human,PFM6,PR domain zinc finger protein 9,PR domain-containing protein 9,PRDM9
EIAAB32316 Homo sapiens,Human,PFM4,PR domain zinc finger protein 7,PR domain-containing protein 7,PRDM7,Probable histone-lysine N-methyltransferase PRDM7
EIAAB32314 Homo sapiens,Human,PFM3,PR domain zinc finger protein 6,PR domain-containing protein 6,PRDM6,Putative histone-lysine N-methyltransferase PRDM6


 

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