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Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific (EC 2.1.1.43) (H3-K36-HMTase) (H4-K20-HMTase) (Nuclear receptor-binding SET domain-containing protein 1) (NR-binding SET domain-containing protein)

 NSD1_MOUSE              Reviewed;        2588 AA.
O88491; Q8C480; Q9CT70;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
18-JUL-2018, entry version 139.
RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific;
EC=2.1.1.43;
AltName: Full=H3-K36-HMTase;
AltName: Full=H4-K20-HMTase;
AltName: Full=Nuclear receptor-binding SET domain-containing protein 1;
Short=NR-binding SET domain-containing protein;
Name=Nsd1 {ECO:0000312|MGI:MGI:1276545};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAC40182.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RARA; THRA;
RXRA AND ESRRA, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-803;
804-SER-THR-805 AND 806-LEU-LEU-807.
TISSUE=Embryo {ECO:0000269|PubMed:9628876};
PubMed=9628876; DOI=10.1093/emboj/17.12.3398;
Huang N., vom Baur E., Garnier J.-M., Lerouge T., Vonesch J.-L.,
Lutz Y., Chambon P., Losson R.;
"Two distinct nuclear receptor interaction domains in NSD1, a novel
SET protein that exhibits characteristics of both corepressors and
coactivators.";
EMBO J. 17:3398-3412(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2220-2588.
STRAIN=C57BL/6J; TISSUE=Embryo;
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] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
CYS-1920 AND THR-1950.
PubMed=12805229; DOI=10.1093/emboj/cdg288;
Rayasam G.V., Wendling O., Angrand P.-O., Mark M., Niederreither K.,
Song L., Lerouge T., Hager G.L., Chambon P., Losson R.;
"NSD1 is essential for early post-implantation development and has a
catalytically active SET domain.";
EMBO J. 22:3153-3163(2003).
[4]
INTERACTION WITH ZNF496.
PubMed=15169884; DOI=10.1128/MCB.24.12.5184-5196.2004;
Nielsen A.L., Jorgensen P., Lerouge T., Cervino M., Chambon P.,
Losson R.;
"Nizp1, a novel multitype zinc finger protein that interacts with the
NSD1 histone lysine methyltransferase through a unique C2HR motif.";
Mol. Cell. Biol. 24:5184-5196(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-118; SER-1408
AND SER-2369, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Lung, 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. Preferentially methylates
'Lys-36' of histone H3 and 'Lys-20' of histone H4 (in vitro).
Transcriptional intermediary factor capable of negatively
influencing transcription. May also positively influence
transcription. Essential for early post-implantation development.
{ECO:0000269|PubMed:12805229, ECO:0000269|PubMed:9628876}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000269|PubMed:12805229}.
-!- SUBUNIT: Interacts with AR DNA- and ligand-binding domains (By
similarity). Interacts with the ligand-binding domains of RARA and
THRA in the absence of ligand; in the presence of ligand the
interaction is severely disrupted but some binding still occurs.
Interacts with the ligand-binding domains of RXRA and ESRRA only
in the presence of ligand. Interacts with ZNF496. {ECO:0000250,
ECO:0000269|PubMed:15169884, ECO:0000269|PubMed:9628876}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9628876}.
Chromosome {ECO:0000305|PubMed:9628876}.
-!- TISSUE SPECIFICITY: Expressed in the embryo and the outer region
of the uterine decidua at early post-implantation E5.5 stage.
Uniformly expressed in embryonic and extraembryonic tissues during
gastrulation stage E7.5. Expressed differentially after stage 14.5
with highest expression in proliferating cells. Enriched in the
telencephalic region of the brain, spinal cord, intestinal crypt,
tooth buds, thymus and salivary glands at stage E16.5. Also
expressed in the ossification region of developing bones and in
the periosteum. {ECO:0000269|PubMed:12805229}.
-!- DOMAIN: Contains 2 adjacent but distinct nuclear receptor
interaction domains (NID+L and NID-L) to which nuclear receptors
bind differentially in the presence and absence of ligand
respectively.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
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EMBL; AF064553; AAC40182.1; -; mRNA.
EMBL; AK082820; BAC38635.1; -; mRNA.
EMBL; AK004485; BAB23326.1; -; mRNA.
PIR; T14342; T14342.
UniGene; Mm.168965; -.
PDB; 2NAA; NMR; -; A=2014-2104.
PDBsum; 2NAA; -.
ProteinModelPortal; O88491; -.
SMR; O88491; -.
IntAct; O88491; 2.
MINT; O88491; -.
STRING; 10090.ENSMUSP00000097089; -.
iPTMnet; O88491; -.
PhosphoSitePlus; O88491; -.
EPD; O88491; -.
MaxQB; O88491; -.
PaxDb; O88491; -.
PeptideAtlas; O88491; -.
PRIDE; O88491; -.
MGI; MGI:1276545; Nsd1.
eggNOG; KOG1081; Eukaryota.
eggNOG; COG2940; LUCA.
HOGENOM; HOG000113857; -.
HOVERGEN; HBG007518; -.
InParanoid; O88491; -.
PhylomeDB; O88491; -.
ChiTaRS; Nsd1; mouse.
PRO; PR:O88491; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_NSD1; -.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0035097; C:histone methyltransferase complex; IC:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0050681; F:androgen receptor binding; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0030331; F:estrogen receptor binding; IPI:UniProtKB.
GO; GO:0042054; F:histone methyltransferase activity; IDA:MGI.
GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IDA:UniProtKB.
GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IDA:UniProtKB.
GO; GO:0042974; F:retinoic acid receptor binding; IPI:UniProtKB.
GO; GO:0046965; F:retinoid X receptor binding; IPI:UniProtKB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0046966; F:thyroid hormone receptor binding; IPI:UniProtKB.
GO; GO:0003712; F:transcription coregulator activity; IDA:MGI.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
GO; GO:0016571; P:histone methylation; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0000414; P:regulation of histone H3-K36 methylation; ISO:MGI.
GO; GO:0033135; P:regulation of peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:1903025; P:regulation of RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 4.
InterPro; IPR006560; AWS_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; PF00855; PWWP; 1.
Pfam; PF00856; SET; 1.
SMART; SM00570; AWS; 1.
SMART; SM00249; PHD; 5.
SMART; SM00508; PostSET; 1.
SMART; SM00293; PWWP; 1.
SMART; SM00317; SET; 1.
SUPFAM; SSF57903; SSF57903; 3.
PROSITE; PS51215; AWS; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50812; PWWP; 1.
PROSITE; PS50280; SET; 1.
PROSITE; PS01359; ZF_PHD_1; 2.
PROSITE; PS50016; ZF_PHD_2; 2.
1: Evidence at protein level;
3D-structure; Activator; Chromatin regulator; Chromosome;
Complete proteome; Developmental protein; Isopeptide bond;
Metal-binding; Methyltransferase; Nucleus; Phosphoprotein; Receptor;
Reference proteome; Repeat; Repressor; S-adenosyl-L-methionine;
Transcription; Transcription regulation; Transferase; Ubl conjugation;
Zinc; Zinc-finger.
CHAIN 1 2588 Histone-lysine N-methyltransferase, H3
lysine-36 and H4 lysine-20 specific.
/FTId=PRO_0000186071.
DOMAIN 1654 1716 PWWP. {ECO:0000255|PROSITE-
ProRule:PRU00162}.
DOMAIN 1788 1838 AWS. {ECO:0000255|PROSITE-
ProRule:PRU00562}.
DOMAIN 1840 1957 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 1964 1980 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
ZN_FING 1441 1487 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1488 1544 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1605 1649 PHD-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 2016 2063 PHD-type 4; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00146}.
REGION 1850 1852 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 1892 1895 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 1918 1919 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 1958 1964 Inhibits enzyme activity in the absence
of bound histone. {ECO:0000250}.
COMPBIAS 841 896 Ser-rich. {ECO:0000255}.
COMPBIAS 2213 2251 Pro-rich. {ECO:0000255}.
BINDING 1963 1963 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
BINDING 1969 1969 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 380 380 Phosphoserine.
{ECO:0000250|UniProtKB:Q96L73}.
MOD_RES 383 383 Phosphoserine.
{ECO:0000250|UniProtKB:Q96L73}.
MOD_RES 1408 1408 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2267 2267 Phosphoserine.
{ECO:0000250|UniProtKB:Q96L73}.
MOD_RES 2360 2360 Phosphothreonine.
{ECO:0000250|UniProtKB:Q96L73}.
MOD_RES 2369 2369 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 802 802 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q96L73}.
CROSSLNK 1237 1237 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q96L73}.
CROSSLNK 2509 2509 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q96L73}.
MUTAGEN 803 803 F->A,Y: No effect on interaction with
nuclear receptors.
{ECO:0000269|PubMed:9628876}.
MUTAGEN 804 805 ST->AA: Abolishes interaction with
nuclear receptors.
{ECO:0000269|PubMed:9628876}.
MUTAGEN 806 807 LL->AA: Strongly decreases interaction
with liganded nuclear receptors. No
effect on interaction with non-liganded
nuclear receptors.
{ECO:0000269|PubMed:9628876}.
MUTAGEN 1920 1920 C->S: Increases methyltransferase
activity towards H3 and H4. Increases
methyltransferase activity; when
associated with E-1950.
{ECO:0000269|PubMed:12805229}.
MUTAGEN 1950 1950 T->E: Does not affect histone
methyltransferase activity. Increases
methyltransferase activity; when
associated with S-1920.
{ECO:0000269|PubMed:12805229}.
STRAND 2017 2019 {ECO:0000244|PDB:2NAA}.
TURN 2020 2022 {ECO:0000244|PDB:2NAA}.
STRAND 2026 2030 {ECO:0000244|PDB:2NAA}.
STRAND 2039 2041 {ECO:0000244|PDB:2NAA}.
TURN 2042 2046 {ECO:0000244|PDB:2NAA}.
HELIX 2058 2060 {ECO:0000244|PDB:2NAA}.
TURN 2063 2065 {ECO:0000244|PDB:2NAA}.
STRAND 2066 2068 {ECO:0000244|PDB:2NAA}.
TURN 2082 2084 {ECO:0000244|PDB:2NAA}.
TURN 2086 2088 {ECO:0000244|PDB:2NAA}.
STRAND 2089 2091 {ECO:0000244|PDB:2NAA}.
TURN 2093 2095 {ECO:0000244|PDB:2NAA}.
STRAND 2098 2100 {ECO:0000244|PDB:2NAA}.
SEQUENCE 2588 AA; 284084 MW; 145DFCF2F285A959 CRC64;
MDRTCELSRR NCLLSFSNPV NLDASEDKDS PFGNGQSNFS EPLNGCTMQL PTAASGTSQN
AYGQDSPSCY IPLRRLQDLA SMINVEYLSG SADGSESFQD PAKSDSRAQS PIVCTSLSPG
GPTALAMKQE PTCNNSPELQ LRVTKTTKNG FLHFENFTGV DDADVDSEMD PEQPVTEDES
IEEIFEETQT NATCNYEPKS ENGVEVAMGS EQDSMPESRH GAVERPFLPL APQTEKQKNK
QRSEVDGSNE KTALLPAPTS LGDTNVTVEE QFNSINLSFQ DDPDSSPSPL GNMLEIPGTS
SPSTSQELPF VPQKILSKWE ASVGLAEQYD VPKGSKNQKC VSSSVKLDSE EDMPFEDCTN
DPDSEHLLLN GCLKSLAFDS EHSADEKEKP CAKSRVRKSS DNIKRTSVKK DLVPFESRKE
ERRGKIPDNL GLDFISGGVS DKQASNELSR IANSLTGSST APGSFLFSSS VQNTAKTDFE
TPDCDSLSGL SESALISKHS GEKKKLHPGQ VCSSKVQLCY VGAGDEEKRS NSVSVSTTSD
DGCSDLDPTE HNSGFQNSVL GITDAFDKTE NALSVHKNET QYSRYPVTNR IKEKQKSLIT
NSHADHLMGS TKTMEPETAE LSQVNLSDLK ISSPIPKPQP EFRNDGLTTK FSAPPGIRNE
NPLTKGGLAN QTLLPLKCRQ PKFRSIKCKH KESPAVAETS ATSEDLSLKC CSSDTNGSPL
ANISKSGKGE GLKLLNNMHE KTRDSSDIET AVVKHVLSEL KELSYRSLSE DVSDSGTAKA
SKPLLFSSAS SQNHIPIEPD YKFSTLLMML KDMHDSKTKE QRLMTAQNLA SYRTPDRGDC
SSGSPVGTSK VLVLGSSTPN SEKPGDSTQD SVHQSPGGGD SALSGELSSS LSSLASDKRE
LPACGKIRSN CIPRRNCGRA KPSSKLRETI SAQMVKPSVN PKALKTERKR KFSRLPAVTL
AANRLGNKES GSVNGPSRGG AEDPGKEEPL QQMDLLRNED THFSDVHFDS KAKQSDPDKN
LEKEPSFENR KGPELGSEMN TENDELHGVN QVVPKKRWQR LNQRRPKPGK RANRFREKEN
SEGAFGVLLP ADAVQKARED YLEQRAPPTS KPEDSAADPN HGSHSESVAP RLNVCEKSSV
GMGDVEKETG IPSLMPQTKL PEPAIRSEKK RLRKPSKWLL EYTEEYDQIF APKKKQKKVQ
EQVHKVSSRC EDESLLARCQ PSAQNKQVDE NSLISTKEEP PVLEREAPFL EGPLAQSDLG
VTHAELPQLT LSVPVAPEAS PRPALESEEL LVKTPGNYES KRQRKPTKKL LESNDLDPGF
MPKKGDLGLS RKCFEASRSG NGIVESRATS HLKEFSGGTT KIFDKPRKRK RQRLVTARVH
YKKVKKEDLT KDTPSSEGEL LIHRTAASPK EILEEGVEHD PGMSASKKLQ VERGGGAALK
ENVCQNCEKL GELLLCEAQC CGAFHLECLG LPEMPRGKFI CNECHTGIHT CFVCKQSGED
VKRCLLPLCG KFYHEECVQK YPPTVTQNKG FRCPLHICIT CHAANPANVS ASKGRLMRCV
RCPVAYHAND FCLAAGSKIL ASNSIICPNH FTPRRGCRNH EHVNVSWCFV CSEGGSLLCC
DSCPAAFHRE CLNIDIPEGN WYCNDCKAGK KPHYREIVWV KVGRYRWWPA EICHPRAVPS
NIDKMRHDVG EFPVLFFGSN DYLWTHQARV FPYMEGDVSS KDKMGKGVDG TYKKALQEAA
ARFEELKARK ELRQLQEDRK NDKKPPPYKH IKVNRPIGRV QIFTADLSEI PRCNCKATDE
NPCGIDSECI NRMLLYECHP TVCPAGVRCQ NQCFSKRQYP DVEIFRTLQR GWGLRTKTDI
KKGEFVNEYV GELIDEEECR ARIRYAQEHD ITNFYMLTLD KDRIIDAGPK GNYARFMNHC
CQPNCETQKW SVNGDTRVGL FALSDIKAGT ELTFNYNLEC LGNGKTVCKC GAPNCSGFLG
VRPKNQPIVT EEKSRKFKRK PHGKRRSQGE VTKEREDECF SCGDAGQLVS CKKPGCPKVY
HADCLNLTKR PAGKWECPWH QCDVCGKEAA SFCEMCPSSF CKQHREGMLF ISKLDGRLSC
TEHDPCGPNP LEPGEIREYV PPTATSPPSP GTQPKEQSSE MATQGPKKSD QPPTDATQLL
PLSKKALTGS CQRPLLPERP PERTDSSSHL LDRIRDLAGS GTKSQSLVSS QRPQDRPPAK
EGPRPQPPDR ASPMTRPSSS PSVSSLPLER PLRMTDSRLD KSIGAASPKS QAVEKTPAST
GLRLSSPDRL LTTNSPKPQI SDRPPEKSHA SLTQRLPPPE KVLSAVVQSL VAKEKALRPV
DQNTQSKHRP AVVMDLIDLT PRQKERAASP QEVTPQADEK TAMLESSSWP SSKGLGHIPR
ATEKISVSES LQPSGKVAAP SEHPWQAVKS LTHARFLSPP SAKAFLYESA TQASGRTPVG
AEQTPGPPSP APGLVKQVKQ LSRGLTAKSG QSFRSLGKIS ASLPNEEKKL TTTEQSPWGL
GKASPGAGLW PIVAGQTLAQ ACWSAGGTQT LAQTCWSLGR GQDPKPENAI QALNQAPSSR
KCADSEKK


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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
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
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
EIAAB12653 EHMT1,Euchromatic histone-lysine N-methyltransferase 1,EUHMTASE1,Eu-HMTase1,G9a-like protein 1,GLP,GLP,GLP1,H3-K9-HMTase 5,Histone H3-K9 methyltransferase 5,Histone-lysine N-methyltransferase EHMT1,Ho
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
EIAAB12655 BAT8,C6orf30,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,Homo sap
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
EIAAB37976 H3-K4-HMTase SETD7,Histone H3-K4 methyltransferase SETD7,Histone-lysine N-methyltransferase SETD7,Kiaa1717,Mouse,Mus musculus,SET domain-containing protein 7,Set7,SET7_9,Set9,Setd7
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
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
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
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
EIAAB37954 Histone-lysine N-methyltransferase SETD1B,Homo sapiens,hSET1B,Human,KIAA1076,KMT2G,Lysine N-methyltransferase 2G,SET domain-containing protein 1B,SET1B,SETD1B
CSB-EL016100MO Mouse Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific(NSD1) ELISA kit 96T
CSB-EL016100HU Human Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific(NSD1) ELISA kit 96T
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


 

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