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Histone-lysine N-methyltransferase SETD1B (EC 2.1.1.43) (Lysine N-methyltransferase 2G) (SET domain-containing protein 1B) (hSET1B)

 SET1B_HUMAN             Reviewed;        1966 AA.
Q9UPS6; F6MFW1;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
19-MAR-2014, sequence version 3.
25-OCT-2017, entry version 130.
RecName: Full=Histone-lysine N-methyltransferase SETD1B;
EC=2.1.1.43;
AltName: Full=Lysine N-methyltransferase 2G;
AltName: Full=SET domain-containing protein 1B;
Short=hSET1B;
Name=SETD1B; Synonyms=KIAA1076, KMT2G, SET1B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RBM15, AND
MUTAGENESIS OF LEU-577 AND ASP-579.
PubMed=22927943; DOI=10.1371/journal.pone.0042965;
Lee J.H., Skalnik D.G.;
"Rbm15-Mkl1 interacts with the Setd1b histone H3-Lys4
methyltransferase via a SPOC domain that is required for cytokine-
independent proliferation.";
PLoS ONE 7:E42965-E42965(2012).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1163-1966 (ISOFORM 1/2).
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).
[4]
ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE SET1
COMPLEX.
PubMed=17355966; DOI=10.1074/jbc.M609809200;
Lee J.-H., Tate C.M., You J.-S., Skalnik D.G.;
"Identification and characterization of the human Set1B histone H3-
Lys4 methyltransferase complex.";
J. Biol. Chem. 282:13419-13428(2007).
[5]
IDENTIFICATION IN SET1 COMPLEX, AND INTERACTION WITH WDR82; ASH2L AND
POLR2A.
PubMed=17998332; DOI=10.1128/MCB.01356-07;
Lee J.H., Skalnik D.G.;
"Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A
Histone H3-Lys4 methyltransferase complex to transcription start sites
of transcribed human genes.";
Mol. Cell. Biol. 28:609-618(2008).
[6]
IDENTIFICATION IN SET1 COMPLEX.
PubMed=18838538; DOI=10.1128/MCB.00976-08;
Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M.,
Shilatifard A.;
"Molecular regulation of H3K4 trimethylation by Wdr82, a component of
human Set1/COMPASS.";
Mol. Cell. Biol. 28:7337-7344(2008).
[7]
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1659, 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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-986; SER-994 AND
SER-1031, 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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1335, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Histone methyltransferase that specifically methylates
'Lys-4' of histone H3, when part of the SET1 histone
methyltransferase (HMT) complex, but not if the neighboring 'Lys-
9' residue is already methylated. H3 'Lys-4' methylation
represents a specific tag for epigenetic transcriptional
activation. The non-overlapping localization with SETD1A suggests
that SETD1A and SETD1B make non-redundant contributions to the
epigenetic control of chromatin structure and gene expression.
Specifically tri-methylates 'Lys-4' of histone H3 in vitro.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000269|PubMed:17355966}.
-!- SUBUNIT: Component of the SET1 complex, at least composed of the
catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5,
ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30. Interacts with HCFC1 and
ASH2L/ASH2. Interacts (via the RRM domain) with WDR82. Interacts
(via the RRM domain) with hyperphosphorylated C-terminal domain
(CTD) of RNA polymerase II large subunit (POLR2A) only in the
presence of WDR82. Binds specifically to CTD heptad repeats
phosphorylated on 'Ser-5' of each heptad. Interacts with RBM15.
{ECO:0000269|PubMed:17355966, ECO:0000269|PubMed:17998332,
ECO:0000269|PubMed:18838538, ECO:0000269|PubMed:22927943}.
-!- INTERACTION:
Q9UBL3-3:ASH2L; NbExp=2; IntAct=EBI-16197836, EBI-16130425;
-!- SUBCELLULAR LOCATION: Nucleus speckle
{ECO:0000269|PubMed:17355966}. Chromosome
{ECO:0000269|PubMed:17355966}. Note=Localizes to a largely non-
overlapping set of euchromatic nuclear speckles with SETD1A,
suggesting that SETD1A and SET1B each bind to a unique set of
target genes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UPS6-1; Sequence=Displayed;
Name=2;
IsoId=Q9UPS6-2; Sequence=VSP_053875, VSP_053876;
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
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EMBL; JF813787; AEG67286.1; -; mRNA.
EMBL; AC079360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC084018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB028999; BAA83028.1; -; mRNA.
RefSeq; NP_055863.1; NM_015048.1. [Q9UPS6-2]
RefSeq; XP_005253915.1; XM_005253858.4. [Q9UPS6-1]
RefSeq; XP_006719359.1; XM_006719296.3. [Q9UPS6-1]
UniGene; Hs.507122; -.
PDB; 3UVO; X-ray; 2.20 A; B=1745-1755.
PDB; 4ES0; X-ray; 1.82 A; C=1741-1754.
PDBsum; 3UVO; -.
PDBsum; 4ES0; -.
ProteinModelPortal; Q9UPS6; -.
SMR; Q9UPS6; -.
BioGrid; 116702; 23.
CORUM; Q9UPS6; -.
DIP; DIP-61947N; -.
ELM; Q9UPS6; -.
IntAct; Q9UPS6; 13.
STRING; 9606.ENSP00000267197; -.
iPTMnet; Q9UPS6; -.
PhosphoSitePlus; Q9UPS6; -.
BioMuta; SETD1B; -.
DMDM; 166977692; -.
EPD; Q9UPS6; -.
PaxDb; Q9UPS6; -.
PeptideAtlas; Q9UPS6; -.
PRIDE; Q9UPS6; -.
Ensembl; ENST00000542440; ENSP00000442924; ENSG00000139718. [Q9UPS6-2]
Ensembl; ENST00000604567; ENSP00000474253; ENSG00000139718. [Q9UPS6-1]
Ensembl; ENST00000619791; ENSP00000481531; ENSG00000139718. [Q9UPS6-1]
GeneID; 23067; -.
KEGG; hsa:23067; -.
UCSC; uc021rfg.2; human. [Q9UPS6-1]
CTD; 23067; -.
DisGeNET; 23067; -.
EuPathDB; HostDB:ENSG00000139718.10; -.
GeneCards; SETD1B; -.
H-InvDB; HIX0011090; -.
HGNC; HGNC:29187; SETD1B.
HPA; HPA021667; -.
HPA; HPA059412; -.
MIM; 611055; gene.
neXtProt; NX_Q9UPS6; -.
OpenTargets; ENSG00000139718; -.
PharmGKB; PA143485611; -.
eggNOG; KOG1080; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00760000119228; -.
HOGENOM; HOG000168216; -.
HOVERGEN; HBG055596; -.
InParanoid; Q9UPS6; -.
KO; K11422; -.
OMA; HHWRSYK; -.
OrthoDB; EOG091G00IV; -.
TreeFam; TF106436; -.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
GenomeRNAi; 23067; -.
PRO; PR:Q9UPS6; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000139718; -.
CleanEx; HS_SETD1B; -.
ExpressionAtlas; Q9UPS6; baseline and differential.
Genevisible; Q9UPS6; HS.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0035097; C:histone methyltransferase complex; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0048188; C:Set1C/COMPASS complex; IDA:UniProtKB.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:Reactome.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0051568; P:histone H3-K4 methylation; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd12549; RRM_Set1B; 1.
InterPro; IPR024657; COMPASS_Set1_N-SET.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR034468; Set1B_RRM.
InterPro; IPR001214; SET_dom.
Pfam; PF11764; N-SET; 1.
Pfam; PF00076; RRM_1; 1.
Pfam; PF00856; SET; 1.
SMART; SM01291; N-SET; 1.
SMART; SM00508; PostSET; 1.
SMART; SM00360; RRM; 1.
SMART; SM00317; SET; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50102; RRM; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Chromatin regulator;
Chromosome; Coiled coil; Complete proteome; Methyltransferase;
Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase.
CHAIN 1 1966 Histone-lysine N-methyltransferase
SETD1B.
/FTId=PRO_0000316993.
DOMAIN 93 181 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 1827 1944 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 1950 1966 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
COILED 1173 1204 {ECO:0000255}.
COMPBIAS 366 1671 Pro-rich.
COMPBIAS 1040 1175 Ser-rich.
COMPBIAS 1068 1312 Glu-rich.
COMPBIAS 1103 1138 Asp-rich.
BINDING 1943 1943 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
MOD_RES 986 986 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 994 994 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1031 1031 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1265 1265 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CFT2}.
MOD_RES 1283 1283 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CFT2}.
MOD_RES 1335 1335 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1659 1659 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1663 1663 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CFT2}.
VAR_SEQ 1043 1068 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_053875.
VAR_SEQ 1088 1104 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_053876.
MUTAGEN 577 577 L->A: Abolishes interaction with RBM15.
{ECO:0000269|PubMed:22927943}.
MUTAGEN 579 579 D->A: Abolishes interaction with RBM15.
{ECO:0000269|PubMed:22927943}.
HELIX 1747 1750 {ECO:0000244|PDB:4ES0}.
SEQUENCE 1966 AA; 212803 MW; 164F81BC84EAD2C2 CRC64;
MENSHPPHHH HQQPPPQPGP SGERRNHHWR SYKLMIDPAL KKGHHKLYRY DGQHFSLAMS
SNRPVEIVED PRVVGIWTKN KELELSVPKF KIDEFYVGPV PPKQVTFAKL NDNIRENFLR
DMCKKYGEVE EVEILYNPKT KKHLGIAKVV FATVRGAKDA VQHLHSTSVM GNIIHVELDT
KGETRMRFYE LLVTGRYTPQ TLPVGELDAV SPIVNETLQL SDALKRLKDG GLSAGCGSGS
SSVTPNSGGT PFSQDTAYSS CRLDTPNSYG QGTPLTPRLG TPFSQDSSYS SRQPTPSYLF
SQDPAVTFKA RRHESKFTDA YNRRHEHHYV HNSPAVTAVA GATAAFRGSS DLPFGAVGGT
GGSSGPPFKA QPQDSATFAH TPPPAQATPA PGFKSAFSPY QTPVAHFPPP PEEPTATAAF
GARDSGEFRR APAPPPLPPA EPLAKEKPGT PPGPPPPDTN SMELGGRPTF GWSPEPCDSP
GTPTLESSPA GPEKPHDSLD SRIEMLLKEQ RTKLLFLREP DSDTELQMEG SPISSSSSQL
SPLAPFGTNS QPGFRGPTPP SSRPSSTGLE DISPTPLPDS DEDEELDLGL GPRPPPEPGP
PDPAGLLSQT AEVALDLVGD RTPTSEKMDE GQQSSGEDME ISDDEMPSAP ITSADCPKPM
VVTPGAAAVA APSVLAPTLP LPPPPGFPPL PPPPPPPPPQ PGFPMPPPLP PPPPPPPPAH
PAVTVPPPPL PAPPGVPPPP ILPPLPPFPP GLFPVMQVDM SHVLGGQWGG MPMSFQMQTQ
VLSRLMTGQG ACPYPPFMAA AAAAASAGLQ FVNLPPYRGP FSLSNSGPGR GQHWPPLPKF
DPSVPPPGYM PRQEDPHKAT VDGVLLVVLK ELKAIMKRDL NRKMVEVVAF RAFDEWWDKK
ERMAKASLTP VKSGEHKDED RPKPKDRIAS CLLESWGKGE GLGYEGLGLG IGLRGAIRLP
SFKVKRKEPP DTTSSGDQKR LRPSTSVDEE DEESERERDR DMADTPCELA KRDPKGVGVR
RRPARPLELD SGGEEDEKES LSASSSSSAS SSSGSSTTSP SSSASDKEEE QESTEEEEEA
EEEEEEEVPR SQLSSSSTSS TSDKDDDDDD SDDRDESEND DEDTALSEAS EKDEGDSDEE
ETVSIVTSKA EATSSSESSE SSEFESSSES SPSSSEDEEE VVAREEEEEE EEEEMVAEES
MASAGPEDFE QDGEEAALAP GAPAVDSLGM EEEVDIETEA VAPEERPSML DEPPLPVGVE
EPADSREPPE EPGLSQEGAM LLSPEPPAKE VEARPPLSPE RAPEHDLEVE PEPPMMLPLP
LQPPLPPPRP PRPPSPPPEP ETTDASHPSV PPEPLAEDHP PHTPGLCGSL AKSQSTETVP
ATPGGEPPLS GGSSGLSLSS PQVPGSPFSY PAPSPSLSSG GLPRTPGRDF SFTPTFSEPS
GPLLLPVCPL PTGRRDERSG PLASPVLLET GLPLPLPLPL PLPLALPAVL RAQARAPTPL
PPLLPAPLAS CPPPMKRKPG RPRRSPPSML SLDGPLVRPP AGAALGRELL LLPGQPQTPV
FPSTHDPRTV TLDFRNAGIP APPPPLPPQP PPPPPPPPVE PTKLPFKELD NQWPSEAIPP
GPRGRDEVTE EYMELAKSRG PWRRPPKKRH EDLVPPAGSP ELSPPQPLFR PRSEFEEMTI
LYDIWNGGID EEDIRFLCVT YERLLQQDNG MDWLNDTLWV YHPSTSLSSA KKKKRDDGIR
EHVTGCARSE GFYTIDKKDK LRYLNSSRAS TDEPPADTQG MSIPAQPHAS TRAGSERRSE
QRRLLSSFTG SCDSDLLKFN QLKFRKKKLK FCKSHIHDWG LFAMEPIAAD EMVIEYVGQN
IRQVIADMRE KRYEDEGIGS SYMFRVDHDT IIDATKCGNF ARFINHSCNP NCYAKVITVE
SQKKIVIYSK QHINVNEEIT YDYKFPIEDV KIPCLCGSEN CRGTLN


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EIAAB37953 Chicken,Gallus gallus,Histone-lysine N-methyltransferase SETD1B,RCJMB04_10j6,SET domain-containing protein 1B,SETD1B
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
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
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
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
CSB-EL021102CH Chicken Histone-lysine N-methyltransferase SETD1B(SETD1B) ELISA kit SpeciesChicken 96T
CSB-EL021102MO Mouse Histone-lysine N-methyltransferase SETD1B(SETD1B) ELISA kit SpeciesMouse 96T
CSB-EL021102HU Human Histone-lysine N-methyltransferase SETD1B(SETD1B) ELISA kit SpeciesHuman 96T
CSB-EL021102MO Mouse Histone-lysine N-methyltransferase SETD1B(SETD1B) ELISA kit 96T
CSB-EL021102CH Chicken Histone-lysine N-methyltransferase SETD1B(SETD1B) ELISA kit 96T
CSB-EL021102HU Human Histone-lysine N-methyltransferase SETD1B(SETD1B) ELISA kit 96T
SET1B_MOUSE ELISA Kit FOR Histone-lysine N-methyltransferase SETD1B; organism: Mouse; gene name: Setd1b 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-EL021102RA Rat Histone-lysine N-methyltransferase SETD1B(SETD1B) ELISA kit 96T
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
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


 

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