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Histone-lysine N-methyltransferase NSD2 (EC 2.1.1.43) (Multiple myeloma SET domain-containing protein) (MMSET) (Nuclear SET domain-containing protein 2) (Protein trithorax-5) (Wolf-Hirschhorn syndrome candidate 1 protein)

 NSD2_HUMAN              Reviewed;        1365 AA.
O96028; A2A2T2; A2A2T3; A2A2T4; A7MCZ1; D3DVQ2; O96031; Q4VBY8;
Q672J1; Q6IS00; Q86V01; Q9BZB4; Q9UI92; Q9UPR2;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
27-SEP-2017, entry version 161.
RecName: Full=Histone-lysine N-methyltransferase NSD2;
EC=2.1.1.43;
AltName: Full=Multiple myeloma SET domain-containing protein;
Short=MMSET;
AltName: Full=Nuclear SET domain-containing protein 2;
AltName: Full=Protein trithorax-5;
AltName: Full=Wolf-Hirschhorn syndrome candidate 1 protein;
Name=NSD2 {ECO:0000312|HGNC:HGNC:12766};
Synonyms=KIAA1090, MMSET, TRX5, WHSC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND CHROMOSOMAL
TRANSLOCATION WITH IGH.
TISSUE=Myeloma;
PubMed=9787135;
Chesi M., Nardini E., Lim R.S.C., Smith K.D., Kuehl W.M.,
Bergsagel P.L.;
"The t(4;14) translocation in myeloma dysregulates both FGFR3 and a
novel gene, MMSET, resulting in IgH/MMSET hybrid transcripts.";
Blood 92:3025-3034(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 3 AND 5), TISSUE
SPECIFICITY, AND CHROMOSOMAL TRANSLOCATION WITH IGH.
PubMed=9618163; DOI=10.1093/hmg/7.7.1071;
Stec I., Wright T.J., van Ommen G.-J.B., de Boer P.A.,
van Haeringen A., Moorman A.F.M., Altherr M.R., den Dunnen J.T.;
"WHSC1, a 90 kb SET domain-containing gene, expressed in early
development and homologous to a Drosophila dysmorphy gene maps in the
Wolf-Hirschhorn syndrome critical region and is fused to IgH in
t(4;14) multiple myeloma.";
Hum. Mol. Genet. 7:1071-1082(1998).
[3]
ERRATUM.
Stec I., Wright T.J., van Ommen G.-J.B., de Boer P.A.,
van Haeringen A., Moorman A.F.M., Altherr M.R., den Dunnen J.T.;
Hum. Mol. Genet. 7:1527-1527(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, AND DNA-BINDING.
PubMed=11152655; DOI=10.1165/ajrcmb.24.1.4224;
Garlisi C.G., Uss A.S., Xiao H., Tian F., Sheridan K.E., Wang L.,
Motasim Billah M., Egan R.W., Stranick K.S., Umland S.P.;
"A unique mRNA initiated within a middle intron of WHSC1/MMSET encodes
a DNA binding protein that suppresses human IL-5 transcription.";
Am. J. Respir. Cell Mol. Biol. 24:90-98(2001).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), AND SUBCELLULAR LOCATION.
PubMed=15677557; DOI=10.1182/blood-2004-09-3704;
Keats J.J., Maxwell C.A., Taylor B.J., Hendzel M.J., Chesi M.,
Bergsagel P.L., Larratt L.M., Mant M.J., Reiman T., Belch A.R.,
Pilarski L.M.;
"Overexpression of transcripts originating from the MMSET locus
characterizes all t(4;14)(p16;q32)-positive multiple myeloma
patients.";
Blood 105:4060-4069(2005).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Angrand P.-O., Valvatne H., Jeanmougin F., Adamson A.,
van der Hoeven F., Olsen L., Tekotte H., Huang N., Poch O.,
Lamerdin J., Chambon P., Losson R., Stewart A., Aasland R.;
"Mammalian trithorax- and ASH1-like proteins: putative chromatin
regulators which contain PHD fingers and SET domains.";
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=10470851; DOI=10.1093/dnares/6.3.197;
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:197-205(1999).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Amygdala;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 6).
TISSUE=Ovary, and Spleen;
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).
[12]
CHROMOSOMAL TRANSLOCATION WITH IGH.
PubMed=10945609;
Malgeri U., Baldini L., Perfetti V., Fabris S., Vignarelli M.C.,
Colombo G., Lotti V., Compasso S., Bogni S., Lombardi L., Maiolo A.T.,
Neri A.;
"Detection of t(4;14)(p16.3;q32) chromosomal translocation in multiple
myeloma by reverse transcription-polymerase chain reaction analysis of
IGH-MMSET fusion transcripts.";
Cancer Res. 60:4058-4061(2000).
[13]
CHROMOSOMAL TRANSLOCATION WITH IGH.
PubMed=11337357; DOI=10.1016/S0002-9440(10)64115-6;
Perfetti V., Coluccia A.M., Intini D., Malgeri U., Vignarelli M.C.,
Casarini S., Merlini G., Neri A.;
"Translocation T(4;14)(p16.3;q32) is a recurrent genetic lesion in
primary amyloidosis.";
Am. J. Pathol. 158:1599-1603(2001).
[14]
CHROMOSOMAL TRANSLOCATION WITH IGH.
PubMed=12433679; DOI=10.1182/blood-2002-09-2801;
Santra M., Zhan F., Tian E., Barlogie B., Shaughnessy J. Jr.;
"A subset of multiple myeloma harboring the t(4;14)(p16;q32)
translocation lacks FGFR3 expression but maintains an IGH/MMSET fusion
transcript.";
Blood 101:2374-2376(2003).
[15]
CHROMOSOMAL TRANSLOCATION WITH IGH.
PubMed=15257719; DOI=10.1111/j.1365-2141.2004.05048.x;
Intini D., Fabris S., Storlazzi T., Otsuki T., Ciceri G., Verdelli D.,
Lombardi L., Rocchi M., Neri A.;
"Identification of a novel IGH-MMSET fusion transcript in a human
myeloma cell line with the t(4;14)(p16.3;q32) chromosomal
translocation.";
Br. J. Haematol. 126:437-439(2004).
[16]
FUNCTION.
PubMed=16115125; DOI=10.1111/j.1365-2141.2005.05664.x;
Hudlebusch H.R., Theilgaard-Moench K., Lodahl M., Johnsen H.E.,
Rasmussen T.;
"Identification of ID-1 as a potential target gene of MMSET in
multiple myeloma.";
Br. J. Haematol. 130:700-708(2005).
[17]
SUBCELLULAR LOCATION.
PubMed=16197452; DOI=10.1111/j.1365-2141.2005.05741.x;
Todoerti K., Ronchetti D., Agnelli L., Castellani S., Marelli S.,
Deliliers G.L., Zanella A., Lombardi L., Neri A.;
"Transcription repression activity is associated with the type I
isoform of the MMSET gene involved in t(4;14) in multiple myeloma.";
Br. J. Haematol. 131:214-218(2005).
[18]
INVOLVEMENT IN WHS.
PubMed=15734578; DOI=10.1016/j.tig.2005.01.008;
Bergemann A.D., Cole F., Hirschhorn K.;
"The etiology of Wolf-Hirschhorn syndrome.";
Trends Genet. 21:188-195(2005).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-544, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[20]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=18172012; DOI=10.1128/MCB.02130-07;
Kim J.Y., Kee H.J., Choe N.W., Kim S.M., Eom G.H., Baek H.J., Kook H.,
Kook H., Seo S.B.;
"Multiple-myeloma-related WHSC1/MMSET isoform RE-IIBP is a histone
methyltransferase with transcriptional repression activity.";
Mol. Cell. Biol. 28:2023-2034(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND THR-544, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110; THR-114; SER-121;
SER-376 AND THR-544, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-544, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110; SER-121; SER-172;
THR-422; THR-544 AND SER-614, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Histone methyltransferase with histone H3 'Lys-27'
(H3K27me) methyltransferase activity. Isoform 2 may act as a
transcription regulator that binds DNA and suppresses IL5
transcription through HDAC recruitment.
{ECO:0000269|PubMed:11152655, ECO:0000269|PubMed:16115125,
ECO:0000269|PubMed:18172012}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000269|PubMed:18172012}.
-!- INTERACTION:
P10275:AR; NbExp=5; IntAct=EBI-2693298, EBI-608057;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00267, ECO:0000269|PubMed:15677557,
ECO:0000269|PubMed:16197452}. Chromosome {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 4: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1;
IsoId=O96028-1; Sequence=Displayed;
Name=2;
IsoId=O96028-2; Sequence=VSP_021414, VSP_021423;
Note=Ref.7 (BAA83042) and Ref.11 (AAI52413) sequences are in
conflict in position: 26:M->V. {ECO:0000305};
Name=3;
IsoId=O96028-3; Sequence=VSP_021419, VSP_021422;
Name=4; Synonyms=RE-IIBP, IL-5 promoter REII-region-binding
protein;
IsoId=O96028-4; Sequence=VSP_021413;
Name=5;
IsoId=O96028-5; Sequence=VSP_021420, VSP_021421;
Name=6;
IsoId=O96028-6; Sequence=VSP_021417, VSP_021418;
Note=No experimental confirmation available.;
Name=7;
IsoId=O96028-7; Sequence=VSP_021415, VSP_021416;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:9618163}.
-!- DISEASE: Note=A chromosomal aberration involving NSD2 is a cause
of multiple myeloma tumors. Translocation t(4;14)(p16.3;q32.3)
with IgH.
-!- DISEASE: Note=NSD2 is located in the Wolf-Hirschhorn syndrome
(WHS) critical region. WHS results from by sub-telomeric deletions
in the short arm of chromosome 4. NSD2 is deleted in every case,
however deletion of linked genes contributes to both the severity
of the core characteristics and the presence of the additional
syndromic problems.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. SET2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
-!- SEQUENCE CAUTION:
Sequence=BAA83042.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/WHSC1ID42809ch4p16.html";
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EMBL; AF071593; AAC24150.1; -; mRNA.
EMBL; AF071594; AAC24151.1; -; mRNA.
EMBL; AF083386; AAD19343.1; -; mRNA.
EMBL; AF083387; AAD21770.1; -; mRNA.
EMBL; AF083388; AAD21771.1; -; mRNA.
EMBL; AF083389; AAD19344.1; -; mRNA.
EMBL; AF083390; AAD19345.1; -; mRNA.
EMBL; AF083391; AAD19346.1; -; mRNA.
EMBL; AF178206; AAF23369.1; -; Genomic_DNA.
EMBL; AF178199; AAF23369.1; JOINED; Genomic_DNA.
EMBL; AF178198; AAF23369.1; JOINED; Genomic_DNA.
EMBL; AF178202; AAF23369.1; JOINED; Genomic_DNA.
EMBL; AF178204; AAF23369.1; JOINED; Genomic_DNA.
EMBL; AF178205; AAF23369.1; JOINED; Genomic_DNA.
EMBL; AF178203; AAF23369.1; JOINED; Genomic_DNA.
EMBL; AF178201; AAF23369.1; JOINED; Genomic_DNA.
EMBL; AF178200; AAF23369.1; JOINED; Genomic_DNA.
EMBL; AF178219; AAF23370.1; -; Genomic_DNA.
EMBL; AF178198; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF178199; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF178200; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF178202; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF178204; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF178207; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF178216; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF178215; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF178214; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF178213; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF178212; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF178211; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF178210; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF178209; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF178208; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF178218; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF178217; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF178205; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF178203; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF178201; AAF23370.1; JOINED; Genomic_DNA.
EMBL; AF330040; AAK00344.1; -; mRNA.
EMBL; AY694128; AAU09264.1; -; mRNA.
EMBL; AJ007042; CAB45386.1; -; mRNA.
EMBL; AB029013; BAA83042.2; ALT_INIT; mRNA.
EMBL; AK289697; BAF82386.1; -; mRNA.
EMBL; AC105448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL132868; CAM15220.1; -; Genomic_DNA.
EMBL; AL132868; CAM15221.1; -; Genomic_DNA.
EMBL; AL132868; CAM15222.1; -; Genomic_DNA.
EMBL; CH471131; EAW82548.1; -; Genomic_DNA.
EMBL; CH471131; EAW82552.1; -; Genomic_DNA.
EMBL; CH471131; EAW82557.1; -; Genomic_DNA.
EMBL; CH471131; EAW82553.1; -; Genomic_DNA.
EMBL; CH471131; EAW82556.1; -; Genomic_DNA.
EMBL; BC052254; AAH52254.1; -; mRNA.
EMBL; BC070176; AAH70176.1; -; mRNA.
EMBL; BC094825; AAH94825.2; -; mRNA.
EMBL; BC141815; AAI41816.1; -; mRNA.
EMBL; BC152412; AAI52413.1; -; mRNA.
CCDS; CCDS3356.1; -. [O96028-3]
CCDS; CCDS33940.1; -. [O96028-1]
CCDS; CCDS46999.1; -. [O96028-5]
RefSeq; NP_001035889.1; NM_001042424.2. [O96028-1]
RefSeq; NP_015627.1; NM_007331.1. [O96028-5]
RefSeq; NP_579877.1; NM_133330.2. [O96028-1]
RefSeq; NP_579878.1; NM_133331.2. [O96028-1]
RefSeq; NP_579889.1; NM_133334.2. [O96028-3]
RefSeq; NP_579890.1; NM_133335.3. [O96028-1]
RefSeq; XP_005248058.1; XM_005248001.3. [O96028-1]
RefSeq; XP_005248062.1; XM_005248005.2. [O96028-3]
RefSeq; XP_006713977.1; XM_006713914.3. [O96028-3]
RefSeq; XP_011511859.1; XM_011513557.2. [O96028-1]
RefSeq; XP_011511862.1; XM_011513560.2. [O96028-4]
RefSeq; XP_016864076.1; XM_017008587.1. [O96028-4]
RefSeq; XP_016864077.1; XM_017008588.1. [O96028-4]
UniGene; Hs.113876; -.
PDB; 5LSU; X-ray; 2.14 A; A/B=973-1203.
PDBsum; 5LSU; -.
ProteinModelPortal; O96028; -.
SMR; O96028; -.
BioGrid; 113306; 70.
DIP; DIP-57224N; -.
IntAct; O96028; 5.
MINT; MINT-7103764; -.
STRING; 9606.ENSP00000372347; -.
BindingDB; O96028; -.
ChEMBL; CHEMBL3108645; -.
iPTMnet; O96028; -.
PhosphoSitePlus; O96028; -.
BioMuta; WHSC1; -.
EPD; O96028; -.
MaxQB; O96028; -.
PaxDb; O96028; -.
PeptideAtlas; O96028; -.
PRIDE; O96028; -.
DNASU; 7468; -.
Ensembl; ENST00000312087; ENSP00000308780; ENSG00000109685. [O96028-3]
Ensembl; ENST00000353275; ENSP00000329167; ENSG00000109685. [O96028-3]
Ensembl; ENST00000382888; ENSP00000372344; ENSG00000109685. [O96028-2]
Ensembl; ENST00000382891; ENSP00000372347; ENSG00000109685. [O96028-1]
Ensembl; ENST00000382892; ENSP00000372348; ENSG00000109685. [O96028-1]
Ensembl; ENST00000382895; ENSP00000372351; ENSG00000109685. [O96028-1]
Ensembl; ENST00000398261; ENSP00000381311; ENSG00000109685. [O96028-3]
Ensembl; ENST00000420906; ENSP00000399251; ENSG00000109685. [O96028-5]
Ensembl; ENST00000436793; ENSP00000416725; ENSG00000109685. [O96028-7]
Ensembl; ENST00000503128; ENSP00000425761; ENSG00000109685. [O96028-3]
Ensembl; ENST00000508803; ENSP00000423972; ENSG00000109685. [O96028-1]
Ensembl; ENST00000512700; ENSP00000427516; ENSG00000109685. [O96028-7]
Ensembl; ENST00000514045; ENSP00000421681; ENSG00000109685. [O96028-5]
GeneID; 7468; -.
KEGG; hsa:7468; -.
UCSC; uc003gdy.2; human. [O96028-1]
CTD; 7468; -.
DisGeNET; 7468; -.
EuPathDB; HostDB:ENSG00000109685.17; -.
GeneCards; WHSC1; -.
GeneReviews; WHSC1; -.
HGNC; HGNC:12766; NSD2.
HPA; CAB068246; -.
HPA; CAB068247; -.
HPA; HPA015801; -.
MalaCards; WHSC1; -.
MIM; 602952; gene.
neXtProt; NX_O96028; -.
OpenTargets; ENSG00000109685; -.
Orphanet; 280; Wolf-Hirschhorn syndrome.
PharmGKB; PA37369; -.
eggNOG; KOG1081; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00780000121845; -.
HOGENOM; HOG000230892; -.
HOVERGEN; HBG053345; -.
InParanoid; O96028; -.
KO; K11424; -.
OMA; CMARIKY; -.
OrthoDB; EOG091G00XD; -.
PhylomeDB; O96028; -.
TreeFam; TF329088; -.
BRENDA; 2.1.1.43; 2681.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
SIGNOR; O96028; -.
ChiTaRS; WHSC1; human.
GeneWiki; WHSC1; -.
GenomeRNAi; 7468; -.
PRO; PR:O96028; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000109685; -.
ExpressionAtlas; O96028; baseline and differential.
Genevisible; O96028; HS.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); TAS:Reactome.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
GO; GO:0003289; P:atrial septum primum morphogenesis; IEA:Ensembl.
GO; GO:0003290; P:atrial septum secundum morphogenesis; IEA:Ensembl.
GO; GO:0060348; P:bone development; IEA:Ensembl.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
GO; GO:0010452; P:histone H3-K36 methylation; IEA:Ensembl.
GO; GO:0003149; P:membranous septum morphogenesis; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0048298; P:positive regulation of isotype switching to IgA isotypes; IEA:Ensembl.
GO; GO:2001032; P:regulation of double-strand break repair via nonhomologous end joining; IEA:Ensembl.
GO; GO:0070201; P:regulation of establishment of protein localization; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.30.10; -; 1.
Gene3D; 3.30.40.10; -; 5.
InterPro; IPR006560; AWS_dom.
InterPro; IPR009071; HMG_box_dom.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR000313; PWWP_dom.
InterPro; IPR001214; SET_dom.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF00505; HMG_box; 1.
Pfam; PF00855; PWWP; 2.
Pfam; PF00856; SET; 1.
SMART; SM00570; AWS; 1.
SMART; SM00398; HMG; 1.
SMART; SM00249; PHD; 4.
SMART; SM00508; PostSET; 1.
SMART; SM00293; PWWP; 2.
SMART; SM00184; RING; 2.
SMART; SM00317; SET; 1.
SUPFAM; SSF47095; SSF47095; 1.
SUPFAM; SSF57903; SSF57903; 3.
PROSITE; PS51215; AWS; 1.
PROSITE; PS50118; HMG_BOX_2; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50812; PWWP; 2.
PROSITE; PS50280; SET; 1.
PROSITE; PS01359; ZF_PHD_1; 2.
PROSITE; PS50016; ZF_PHD_2; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Chromosomal rearrangement; Chromosome; Complete proteome; Cytoplasm;
DNA-binding; Metal-binding; Methyltransferase; Nucleus;
Phosphoprotein; Proto-oncogene; Reference proteome; Repeat;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase; Zinc; Zinc-finger.
CHAIN 1 1365 Histone-lysine N-methyltransferase NSD2.
/FTId=PRO_0000259519.
DOMAIN 222 286 PWWP 1. {ECO:0000255|PROSITE-
ProRule:PRU00162}.
DOMAIN 880 942 PWWP 2. {ECO:0000255|PROSITE-
ProRule:PRU00162}.
DOMAIN 1011 1061 AWS. {ECO:0000255|PROSITE-
ProRule:PRU00562}.
DOMAIN 1063 1180 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 1187 1203 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
DNA_BIND 453 521 HMG box. {ECO:0000255|PROSITE-
ProRule:PRU00267}.
ZN_FING 667 713 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 714 770 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 831 875 PHD-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1239 1286 PHD-type 4; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00146}.
MOD_RES 110 110 Phosphothreonine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 114 114 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 121 121 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 172 172 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 376 376 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 422 422 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 544 544 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 614 614 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 781 Missing (in isoform 4).
{ECO:0000303|PubMed:11152655,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_021413.
VAR_SEQ 1 652 Missing (in isoform 2).
{ECO:0000303|PubMed:10470851,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_021414.
VAR_SEQ 255 273 QKKSARQYHVQFFGDAPER -> IFKSKKFEHLKTSQIVLK
D (in isoform 7).
{ECO:0000303|PubMed:15677557}.
/FTId=VSP_021415.
VAR_SEQ 274 1365 Missing (in isoform 7).
{ECO:0000303|PubMed:15677557}.
/FTId=VSP_021416.
VAR_SEQ 472 484 VAEHPDASGEEIE -> STKLCFMLASFRI (in
isoform 6).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_021417.
VAR_SEQ 485 1365 Missing (in isoform 6).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_021418.
VAR_SEQ 628 647 VSDSPGDEPSESPYESADET -> LLWEPTPVKLDLNPAAL
YCT (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9618163,
ECO:0000303|PubMed:9787135}.
/FTId=VSP_021419.
VAR_SEQ 629 629 S -> K (in isoform 5).
{ECO:0000303|PubMed:9618163}.
/FTId=VSP_021420.
VAR_SEQ 630 1365 Missing (in isoform 5).
{ECO:0000303|PubMed:9618163}.
/FTId=VSP_021421.
VAR_SEQ 648 1365 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9618163,
ECO:0000303|PubMed:9787135}.
/FTId=VSP_021422.
VAR_SEQ 653 712 VSSKKSERGVTAKKEYVCQLCEKPGSLLLCEGPCCGAFHLA
CLGLSRRPEGRFTCSECAS -> MAGSFCWRMLGLVSKVGN
RARCFSSMAASEEELLDFSGSELQFNSCSLHLSLHPFFNFL
L (in isoform 2).
{ECO:0000303|PubMed:10470851,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_021423.
CONFLICT 210 210 T -> A (in Ref. 5; AAU09264).
{ECO:0000305}.
HELIX 974 981 {ECO:0000244|PDB:5LSU}.
HELIX 1010 1012 {ECO:0000244|PDB:5LSU}.
STRAND 1022 1024 {ECO:0000244|PDB:5LSU}.
HELIX 1033 1036 {ECO:0000244|PDB:5LSU}.
TURN 1043 1045 {ECO:0000244|PDB:5LSU}.
TURN 1047 1050 {ECO:0000244|PDB:5LSU}.
HELIX 1056 1059 {ECO:0000244|PDB:5LSU}.
STRAND 1065 1069 {ECO:0000244|PDB:5LSU}.
STRAND 1071 1081 {ECO:0000244|PDB:5LSU}.
STRAND 1088 1092 {ECO:0000244|PDB:5LSU}.
STRAND 1095 1097 {ECO:0000244|PDB:5LSU}.
HELIX 1099 1111 {ECO:0000244|PDB:5LSU}.
STRAND 1119 1123 {ECO:0000244|PDB:5LSU}.
STRAND 1126 1129 {ECO:0000244|PDB:5LSU}.
TURN 1130 1132 {ECO:0000244|PDB:5LSU}.
HELIX 1136 1139 {ECO:0000244|PDB:5LSU}.
STRAND 1147 1155 {ECO:0000244|PDB:5LSU}.
STRAND 1158 1167 {ECO:0000244|PDB:5LSU}.
HELIX 1179 1181 {ECO:0000244|PDB:5LSU}.
STRAND 1183 1185 {ECO:0000244|PDB:5LSU}.
SEQUENCE 1365 AA; 152258 MW; 7B3128E1FA893AAA CRC64;
MEFSIKQSPL SVQSVVKCIK MKQAPEILGS ANGKTPSCEV NRECSVFLSK AQLSSSLQEG
VMQKFNGHDA LPFIPADKLK DLTSRVFNGE PGAHDAKLRF ESQEMKGIGT PPNTTPIKNG
SPEIKLKITK TYMNGKPLFE SSICGDSAAD VSQSEENGQK PENKARRNRK RSIKYDSLLE
QGLVEAALVS KISSPSDKKI PAKKESCPNT GRDKDHLLKY NVGDLVWSKV SGYPWWPCMV
SADPLLHSYT KLKGQKKSAR QYHVQFFGDA PERAWIFEKS LVAFEGEGQF EKLCQESAKQ
APTKAEKIKL LKPISGKLRA QWEMGIVQAE EAASMSVEER KAKFTFLYVG DQLHLNPQVA
KEAGIAAESL GEMAESSGVS EEAAENPKSV REECIPMKRR RRAKLCSSAE TLESHPDIGK
STPQKTAEAD PRRGVGSPPG RKKTTVSMPR SRKGDAASQF LVFCQKHRDE VVAEHPDASG
EEIEELLRSQ WSLLSEKQRA RYNTKFALVA PVQAEEDSGN VNGKKRNHTK RIQDPTEDAE
AEDTPRKRLR TDKHSLRKRD TITDKTARTS SYKAMEAASS LKSQAATKNL SDACKPLKKR
NRASTAASSA LGFSKSSSPS ASLTENEVSD SPGDEPSESP YESADETQTE VSVSSKKSER
GVTAKKEYVC QLCEKPGSLL LCEGPCCGAF HLACLGLSRR PEGRFTCSEC ASGIHSCFVC
KESKTDVKRC VVTQCGKFYH EACVKKYPLT VFESRGFRCP LHSCVSCHAS NPSNPRPSKG
KMMRCVRCPV AYHSGDACLA AGCSVIASNS IICTAHFTAR KGKRHHAHVN VSWCFVCSKG
GSLLCCESCP AAFHPDCLNI EMPDGSWFCN DCRAGKKLHF QDIIWVKLGN YRWWPAEVCH
PKNVPPNIQK MKHEIGEFPV FFFGSKDYYW THQARVFPYM EGDRGSRYQG VRGIGRVFKN
ALQEAEARFR EIKLQREARE TQESERKPPP YKHIKVNKPY GKVQIYTADI SEIPKCNCKP
TDENPCGFDS ECLNRMLMFE CHPQVCPAGE FCQNQCFTKR QYPETKIIKT DGKGWGLVAK
RDIRKGEFVN EYVGELIDEE ECMARIKHAH ENDITHFYML TIDKDRIIDA GPKGNYSRFM
NHSCQPNCET LKWTVNGDTR VGLFAVCDIP AGTELTFNYN LDCLGNEKTV CRCGASNCSG
FLGDRPKTST TLSSEEKGKK TKKKTRRRRA KGEGKRQSED ECFRCGDGGQ LVLCDRKFCT
KAYHLSCLGL GKRPFGKWEC PWHHCDVCGK PSTSFCHLCP NSFCKEHQDG TAFSCTPDGR
SYCCEHDLGA ASVRSTKTEK PPPEPGKPKG KRRRRRGWRR VTEGK


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