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Lysine-specific demethylase 6B (EC 1.14.11.-) (JmjC domain-containing protein 3) (Jumonji domain-containing protein 3)

 KDM6B_MOUSE             Reviewed;        1641 AA.
Q5NCY0; Q3UWY9; Q4VC26; Q6ZQD3;
26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
01-FEB-2005, sequence version 1.
22-NOV-2017, entry version 98.
RecName: Full=Lysine-specific demethylase 6B;
EC=1.14.11.-;
AltName: Full=JmjC domain-containing protein 3;
AltName: Full=Jumonji domain-containing protein 3;
Name=Kdm6b; Synonyms=Jmjd3, Kiaa0346;
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 [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 935-1641.
TISSUE=Embryonic tail;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1138-1641.
STRAIN=C57BL/6J; TISSUE=Egg;
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).
[5]
INTERACTION WITH TLE1.
PubMed=9854018; DOI=10.1042/bj3370013;
Grbavec D., Lo R., Liu Y., Greenfield A., Stifani S.;
"Groucho/transducin-like enhancer of split (TLE) family members
interact with the yeast transcriptional co-repressor SSN6 and
mammalian SSN6-related proteins: implications for evolutionary
conservation of transcription repression mechanisms.";
Biochem. J. 337:13-17(1999).
[6]
FUNCTION, AND INDUCTION.
PubMed=17825402; DOI=10.1016/j.cell.2007.08.019;
De Santa F., Totaro M.G., Prosperini E., Notarbartolo S., Testa G.,
Natoli G.;
"The histone H3 lysine-27 demethylase Jmjd3 links inflammation to
inhibition of polycomb-mediated gene silencing.";
Cell 130:1083-1094(2007).
[7]
FUNCTION, INTERACTION WITH TBX21; SMARCA4; SMARCC1 AND SMARCC2, AND
MUTAGENESIS OF HIS-1388; GLU-1390 AND HIS-1468.
PubMed=21095589; DOI=10.1016/j.molcel.2010.10.028;
Miller S.A., Mohn S.E., Weinmann A.S.;
"Jmjd3 and UTX play a demethylase-independent role in chromatin
remodeling to regulate T-box family member-dependent gene
expression.";
Mol. Cell 40:594-605(2010).
-!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-
27' of histone H3, thereby playing a central role in histone code.
Demethylates trimethylated and dimethylated H3 'Lys-27'. Plays a
central role in regulation of posterior development, by regulating
HOX gene expression. Involved in inflammatory response by
participating in macrophage differentiation in case of
inflammation by regulating gene expression and macrophage
differentiation (PubMed:17825402). Plays a demethylase-independent
role in chromatin remodeling to regulate T-box family member-
dependent gene expression by acting as a link between T-box
factors and the SMARCA4-containing SWI/SNF remodeling complex
(PubMed:21095589). {ECO:0000269|PubMed:17825402,
ECO:0000269|PubMed:21095589}.
-!- COFACTOR:
Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
-!- SUBUNIT: Interacts with TLE1 (PubMed:21095589). Component of the
MLL4 complex, at least composed of KMT2B/MLL4, ASH2L, RBBP5, WDR5,
and KDM6B (By similarity). Interacts with TBX21, SMARCA4, SMARCC1
and SMARCC2 (PubMed:21095589). {ECO:0000250|UniProtKB:O15054,
ECO:0000269|PubMed:21095589, ECO:0000269|PubMed:9854018}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- INDUCTION: By inflammatory stimuli; mediated by NF-kappa-B.
{ECO:0000269|PubMed:17825402}.
-!- SIMILARITY: Belongs to the UTX family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAE22775.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AL596125; CAI35996.1; -; Genomic_DNA.
EMBL; BC075632; AAH75632.1; -; mRNA.
EMBL; AK129121; BAC97931.1; -; mRNA.
EMBL; AK136019; BAE22775.1; ALT_INIT; mRNA.
CCDS; CCDS24895.1; -.
RefSeq; NP_001017426.1; NM_001017426.1.
RefSeq; XP_006532961.1; XM_006532898.1.
RefSeq; XP_011247221.1; XM_011248919.2.
RefSeq; XP_011247222.1; XM_011248920.2.
RefSeq; XP_011247223.1; XM_011248921.1.
RefSeq; XP_011247224.1; XM_011248922.2.
RefSeq; XP_011247225.1; XM_011248923.1.
UniGene; Mm.261201; -.
UniGene; Mm.472522; -.
PDB; 4EYU; X-ray; 2.30 A; A/B=1155-1293, A/B=1321-1641.
PDB; 4EZ4; X-ray; 2.99 A; A/B=1155-1293, A/B=1321-1641.
PDB; 4EZH; X-ray; 2.52 A; A/B=1155-1293, A/B=1321-1641.
PDBsum; 4EYU; -.
PDBsum; 4EZ4; -.
PDBsum; 4EZH; -.
ProteinModelPortal; Q5NCY0; -.
SMR; Q5NCY0; -.
BioGrid; 229803; 5.
DIP; DIP-39160N; -.
IntAct; Q5NCY0; 5.
STRING; 10090.ENSMUSP00000091620; -.
iPTMnet; Q5NCY0; -.
PhosphoSitePlus; Q5NCY0; -.
MaxQB; Q5NCY0; -.
PaxDb; Q5NCY0; -.
PeptideAtlas; Q5NCY0; -.
PRIDE; Q5NCY0; -.
Ensembl; ENSMUST00000094077; ENSMUSP00000091620; ENSMUSG00000018476.
GeneID; 216850; -.
KEGG; mmu:216850; -.
UCSC; uc007jqd.1; mouse.
CTD; 23135; -.
MGI; MGI:2448492; Kdm6b.
eggNOG; KOG1124; Eukaryota.
eggNOG; KOG1246; Eukaryota.
eggNOG; ENOG410ZX0W; LUCA.
GeneTree; ENSGT00410000025758; -.
HOGENOM; HOG000113217; -.
InParanoid; Q5NCY0; -.
KO; K11448; -.
OMA; AQPGLWE; -.
OrthoDB; EOG091G0OL6; -.
PhylomeDB; Q5NCY0; -.
TreeFam; TF317405; -.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-3214842; HDMs demethylate histones.
ChiTaRS; Kdm6b; mouse.
PRO; PR:Q5NCY0; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000018476; -.
CleanEx; MM_JMJD3; -.
Genevisible; Q5NCY0; MM.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
GO; GO:0071558; F:histone demethylase activity (H3-K27 specific); IDA:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:BHF-UCL.
GO; GO:0045165; P:cell fate commitment; IMP:MGI.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:MGI.
GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
GO; GO:0045446; P:endothelial cell differentiation; IMP:BHF-UCL.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0016577; P:histone demethylation; IMP:MGI.
GO; GO:0071557; P:histone H3-K27 demethylation; IDA:BHF-UCL.
GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0048333; P:mesodermal cell differentiation; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:0060992; P:response to fungicide; IEA:Ensembl.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR003347; JmjC_dom.
InterPro; IPR029518; KDM6B.
InterPro; IPR011990; TPR-like_helical_dom_sf.
PANTHER; PTHR14017:SF5; PTHR14017:SF5; 1.
Pfam; PF02373; JmjC; 1.
SMART; SM00558; JmjC; 1.
PROSITE; PS51184; JMJC; 1.
1: Evidence at protein level;
3D-structure; Chromatin regulator; Complete proteome; Dioxygenase;
Inflammatory response; Iron; Isopeptide bond; Metal-binding; Nucleus;
Oxidoreductase; Phosphoprotein; Reference proteome; Ubl conjugation;
Zinc.
CHAIN 1 1641 Lysine-specific demethylase 6B.
/FTId=PRO_0000292008.
DOMAIN 1337 1500 JmjC. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
COMPBIAS 32 85 Pro-rich.
COMPBIAS 195 908 Pro-rich.
COMPBIAS 370 408 Ser-rich.
COMPBIAS 743 766 Thr-rich.
COMPBIAS 1045 1080 Pro-rich.
METAL 1388 1388 Iron. {ECO:0000250}.
METAL 1390 1390 Iron. {ECO:0000250}.
METAL 1468 1468 Iron. {ECO:0000250|UniProtKB:O14607}.
METAL 1573 1573 Zinc. {ECO:0000250|UniProtKB:O14607}.
METAL 1576 1576 Zinc. {ECO:0000250|UniProtKB:O14607}.
METAL 1600 1600 Zinc. {ECO:0000250|UniProtKB:O14607}.
METAL 1603 1603 Zinc. {ECO:0000250|UniProtKB:O14607}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000250|UniProtKB:O15054}.
CROSSLNK 1107 1107 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O15054}.
MUTAGEN 1388 1388 H->A: No loss of its ability to regulate
TBX21-dependent gene expression or its
ability to interact with SMARCA4; when
associated with A-1390 and A-1468.
{ECO:0000269|PubMed:21095589}.
MUTAGEN 1390 1390 E->A: No loss of its ability to regulate
TBX21-dependent gene expression or its
ability to interact with SMARCA4; when
associated with A-1388 and A-1468.
{ECO:0000269|PubMed:21095589}.
MUTAGEN 1468 1468 H->A: No loss of its ability to regulate
TBX21-dependent gene expression or its
ability to interact with SMARCA4; when
associated with A-1388 and A-1390.
{ECO:0000269|PubMed:21095589}.
CONFLICT 172 172 P -> S (in Ref. 2; AAH75632).
{ECO:0000305}.
CONFLICT 965 965 A -> T (in Ref. 3; BAC97931).
{ECO:0000305}.
CONFLICT 1290 1290 L -> LQ (in Ref. 3; BAC97931).
{ECO:0000305}.
HELIX 1160 1162 {ECO:0000244|PDB:4EYU}.
STRAND 1170 1172 {ECO:0000244|PDB:4EYU}.
HELIX 1176 1179 {ECO:0000244|PDB:4EYU}.
STRAND 1185 1187 {ECO:0000244|PDB:4EYU}.
HELIX 1191 1195 {ECO:0000244|PDB:4EYU}.
HELIX 1197 1203 {ECO:0000244|PDB:4EYU}.
STRAND 1209 1214 {ECO:0000244|PDB:4EYU}.
HELIX 1216 1220 {ECO:0000244|PDB:4EYU}.
HELIX 1224 1227 {ECO:0000244|PDB:4EYU}.
HELIX 1229 1236 {ECO:0000244|PDB:4EYU}.
STRAND 1240 1247 {ECO:0000244|PDB:4EYU}.
STRAND 1260 1262 {ECO:0000244|PDB:4EZ4}.
STRAND 1269 1274 {ECO:0000244|PDB:4EYU}.
HELIX 1275 1295 {ECO:0000244|PDB:4EYU}.
STRAND 1323 1331 {ECO:0000244|PDB:4EYU}.
TURN 1335 1338 {ECO:0000244|PDB:4EYU}.
HELIX 1339 1344 {ECO:0000244|PDB:4EYU}.
HELIX 1345 1347 {ECO:0000244|PDB:4EYU}.
HELIX 1350 1352 {ECO:0000244|PDB:4EYU}.
STRAND 1353 1355 {ECO:0000244|PDB:4EYU}.
HELIX 1360 1363 {ECO:0000244|PDB:4EYU}.
STRAND 1364 1366 {ECO:0000244|PDB:4EYU}.
TURN 1369 1371 {ECO:0000244|PDB:4EYU}.
STRAND 1375 1379 {ECO:0000244|PDB:4EYU}.
STRAND 1384 1388 {ECO:0000244|PDB:4EYU}.
HELIX 1391 1393 {ECO:0000244|PDB:4EYU}.
STRAND 1395 1404 {ECO:0000244|PDB:4EYU}.
STRAND 1406 1411 {ECO:0000244|PDB:4EYU}.
HELIX 1413 1415 {ECO:0000244|PDB:4EYU}.
HELIX 1416 1425 {ECO:0000244|PDB:4EYU}.
TURN 1430 1432 {ECO:0000244|PDB:4EYU}.
HELIX 1439 1444 {ECO:0000244|PDB:4EYU}.
STRAND 1450 1454 {ECO:0000244|PDB:4EYU}.
STRAND 1459 1462 {ECO:0000244|PDB:4EYU}.
STRAND 1467 1483 {ECO:0000244|PDB:4EYU}.
HELIX 1488 1503 {ECO:0000244|PDB:4EYU}.
HELIX 1512 1522 {ECO:0000244|PDB:4EYU}.
HELIX 1528 1553 {ECO:0000244|PDB:4EYU}.
TURN 1554 1556 {ECO:0000244|PDB:4EYU}.
STRAND 1559 1561 {ECO:0000244|PDB:4EYU}.
TURN 1574 1576 {ECO:0000244|PDB:4EYU}.
STRAND 1582 1588 {ECO:0000244|PDB:4EYU}.
STRAND 1596 1599 {ECO:0000244|PDB:4EYU}.
HELIX 1601 1607 {ECO:0000244|PDB:4EYU}.
STRAND 1615 1620 {ECO:0000244|PDB:4EYU}.
HELIX 1622 1631 {ECO:0000244|PDB:4EYU}.
SEQUENCE 1641 AA; 176355 MW; 6CBE3620998427EA CRC64;
MHRAVDPPGA RSAREAFALG GLSCAGAWSS CPPHPPPRSS WLPGGRCSAS VGQPPLSAPL
PPSHGSSSGH PNKPYYAPGT PTPRPLHGKL ESLHGCVQAL LREPAQPGLW EQLGQLYESE
HDSEEAVCCY HRALRYGGSF AELGPRIGRL QQAQLWNFHA GSCQHRAKVL PPLEQVWNLL
HLEHKRNYGA KRGGPPVKRS AEPPVVQPMP PAALSGPSGE EGLSPGGKRR RGCSSEQAGL
PPGLPLPPPP PPPPPPPPPP PPPPPPLPGL AISPPFQLTK PGLWNTLHGD AWGPERKGSA
PPERQEQRHS MPHSYPYPAP AYSAHPPSHR LVPNTPLGPG PRPPGAESHG CLPATRPPGS
DLRESRVQRS RMDSSVSPAA STACVPYAPS RPPGLPGTSS SSSSSSSSNN TGLRGVEPSP
GIPGADHYQN PALEISPHQA RLGPSAHSSR KPFLTAPAAT PHLSLPPGTP SSPPPPCPRL
LRPPPPPAWM KGSACRAARE DGEILGELFF GAEGPPRPPP PPLPHRDGFL GPPNPRFSVG
TQDSHNPPIP PTTTSSSSSS NSHSSSPTGP VPFPPPSYLA RSIDPLPRPS SPTLSPQDPP
LPPLTLALPP APPSSCHQNT SGSFRRSESP RPRVSFPKTP EVGQGPPPGP VSKAPQPVPP
GVGELPARGP RLFDFPPTPL EDQFEEPAEF KILPDGLANI MKMLDESIRK EEEQQQQQEA
GVAPPPPLKE PFASLQPPFP SDTAPATTTA APTTATTTTT TTTTTTQEEE KKPPPALPPP
PPLAKFPPPP QPQPPPPPPA SPASLLKSLA SVLEGQKYCY RGTGAAVSTR PGSVPATQYS
PSPASGATAP PPTSVAPSAQ GSPKPSVSSS SQFSTSGGPW AREHRAGEEP APGPVTPAQL
PPPLPLPPAR SESEVLEEIS RACETLVERV GRSAINPVDT ADPVDSGTEP QPPPAQAKEE
SGGVAVAAAG PGSGKRRQKE HRRHRRACRD SVGRRPREGR AKAKAKAPKE KSRRVLGNLD
LQSEEIQGRE KARPDVGGVS KVKTPTAPAP PPAPAPAAQP TPPSAPVPGK KTREEAPGPP
GVSRADMLKL RSLSEGPPKE LKIRLIKVES GDKETFIASE VEERRLRMAD LTISHCAADV
MRASKNAKVK GKFRESYLSP AQSVKPKINT EEKLPREKLN PPTPSIYLES KRDAFSPVLL
QFCTDPRNPI TVIRGLAGSL RLNLGLFSTK TLVEASGEHT VEVRTQVQQP SDENWDLTGT
RQIWPCESSR SHTTIAKYAQ YQASSFQESL QEERESEDEE SEEPDSTTGT SPSSAPDPKN
HHIIKFGTNI DLSDAKRWKP QLQELLKLPA FMRVTSTGNM LSHVGHTILG MNTVQLYMKV
PGSRTPGHQE NNNFCSVNIN IGPGDCEWFA VHEHYWETIS AFCDRHGVDY LTGSWWPILD
DLYASNIPVY RFVQRPGDLV WINAGTVHWV QATGWCNNIA WNVGPLTAYQ YQLALERYEW
NEVKNVKSIV PMIHVSWNVA RTVKISDPDL FKMIKFCLLQ SMKHCQVQRE SLVRAGKKIA
YQGRVKDEPA YYCNECDVEV FNILFVTSEN GSRNTYLVHC EGCARRRSAG LQGVVVLEQY
RTEELAQAYD AFTLAPASTS R


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U1916b CLIA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Bos taurus,Bovine,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6, 96T
U1916m CLIA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Kiaa0585,Lysyl-hydroxyl 96T
E1916c ELISA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Chicken,Gallus gallus,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6, 96T
U1916b CLIA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Bos taurus,Bovine,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6,Lysyl 96T
E1916m ELISA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Kiaa0585,Lysyl-hydroxy 96T
U1916c CLIA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Chicken,Gallus gallus,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6,L 96T
E1916m ELISA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Kiaa0585,Lysyl-hy 96T
U1916m CLIA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Kiaa0585,Lysyl-hyd 96T
U1916c CLIA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Chicken,Gallus gallus,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protei 96T
E1916c ELISA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Chicken,Gallus gallus,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing prote 96T
E1916r ELISA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Lysyl-hydroxylase JMJD 96T
U1916r CLIA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Lysyl-hydroxylase 96T
E1916r ELISA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Lysyl-hydroxylase 96T
U1916r CLIA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Lysyl-hydroxylase JMJD6 96T
18-003-43364 JmjC domain-containing histone demethylation protein 2B - EC 1.14.11.-; Jumonji domain-containing protein 1B; Nuclear protein 5qNCA Polyclonal 0.1 mg Protein A
25-106 JMJD2C is a member of the Jumonji domain 2 (JMJD2) family. It contains one JmjC domain, one JmjN domain, two PHD-type zinc fingers, and two Tudor domains. This nuclear protein functions as a trimethyl 0.05 mg
18-003-43803 JmjC domain-containing protein 6 - Jumonji domain-containing protein 6; Protein PTDSR; Phosphatidylserine receptor Polyclonal 0.05 mg Aff Pur
18-003-42179 JmjC domain-containing histone demethylation protein 3B - EC 1.14.11.-; Jumonji domain-containing protein 2B Polyclonal 0.05 mg Aff Pur
18-003-42309 JmjC domain-containing histone demethylation protein 2A - EC 1.14.11.-; Jumonji domain-containing protein 1A Polyclonal 0.1 mg Protein A


 

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