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

 KDM6B_HUMAN             Reviewed;        1643 AA.
O15054; C9IZ40; Q96G33;
26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 4.
30-AUG-2017, entry version 137.
RecName: Full=Lysine-specific demethylase 6B;
EC=1.14.11.- {ECO:0000269|PubMed:17713478, ECO:0000269|PubMed:17825402, ECO:0000269|PubMed:17851529, ECO:0000269|PubMed:18003914};
AltName: Full=JmjC domain-containing protein 3;
AltName: Full=Jumonji domain-containing protein 3;
AltName: Full=Lysine demethylase 6B;
Name=KDM6B; Synonyms=JMJD3, KIAA0346;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9205841; DOI=10.1093/dnares/4.2.141;
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VII.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 4:141-150(1997).
[2]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1000-1643 (ISOFORM 2).
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).
[5]
INDUCTION BY TPA.
PubMed=17193924; DOI=10.3727/000000006783991791;
Hu L.Y., Tepper C.G., Lo S.H., Lin W.C.;
"An efficient strategy to identify early TPA-responsive genes during
differentiation of HL-60 cells.";
Gene Expr. 13:179-189(2006).
[6]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND
IDENTIFICATION IN THE MLL4 COMPLEX.
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, AND CATALYTIC ACTIVITY.
PubMed=17851529; DOI=10.1038/nature06192;
Lan F., Bayliss P.E., Rinn J.L., Whetstine J.R., Wang J.K., Chen S.,
Iwase S., Alpatov R., Issaeva I., Canaani E., Roberts T.M.,
Chang H.Y., Shi Y.;
"A histone H3 lysine 27 demethylase regulates animal posterior
development.";
Nature 449:689-694(2007).
[8]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=17713478; DOI=10.1038/nature06145;
Agger K., Cloos P.A., Christensen J., Pasini D., Rose S.,
Rappsilber J., Issaeva I., Canaani E., Salcini A.E., Helin K.;
"UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene
regulation and development.";
Nature 449:731-734(2007).
[9]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=18003914; DOI=10.1073/pnas.0707292104;
Hong S., Cho Y.W., Yu L.-R., Yu H., Veenstra T.D., Ge K.;
"Identification of JmjC domain-containing UTX and JMJD3 as histone H3
lysine 27 demethylases.";
Proc. Natl. Acad. Sci. U.S.A. 104:18439-18444(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[11]
FUNCTION, AND MUTAGENESIS OF 1390-HIS--GLU-1392.
PubMed=28262558; DOI=10.1016/j.chembiol.2017.02.006;
Tumber A., Nuzzi A., Hookway E.S., Hatch S.B., Velupillai S.,
Johansson C., Kawamura A., Savitsky P., Yapp C., Szykowska A., Wu N.,
Bountra C., Strain-Damerell C., Burgess-Brown N.A., Ruda G.F.,
Fedorov O., Munro S., England K.S., Nowak R.P., Schofield C.J.,
La Thangue N.B., Pawlyn C., Davies F., Morgan G., Athanasou N.,
Muller S., Oppermann U., Brennan P.E.;
"Potent and Selective KDM5 Inhibitor Stops Cellular Demethylation of
H3K4me3 at Transcription Start Sites and Proliferation of MM1S Myeloma
Cells.";
Cell Chem. Biol. 24:371-380(2017).
[12]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1109, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[13]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1176-1502 IN COMPLEX WITH
NICKEL IONS AND 8-HYDROXYQUINOLINE-5-CARBOXYLIC ACID.
Structural genomics consortium (SGC);
"Crystal structure of the human JMJD3 Jumonji domain.";
Submitted (DEC-2010) to the PDB data bank.
-!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-
27' of histone H3, thereby playing a central role in histone code
(PubMed:17825402, PubMed:17851529, PubMed:17713478,
PubMed:18003914). Demethylates trimethylated and dimethylated H3
'Lys-27' (PubMed:17825402, PubMed:17851529, PubMed:17713478,
PubMed:18003914). Plays a central role in regulation of posterior
development, by regulating HOX gene expression (PubMed:17851529).
Involved in inflammatory response by participating in macrophage
differentiation in case of inflammation by regulating gene
expression and macrophage differentiation (PubMed:17825402).
{ECO:0000269|PubMed:17713478, ECO:0000269|PubMed:17825402,
ECO:0000269|PubMed:17851529, ECO:0000269|PubMed:18003914,
ECO:0000269|PubMed:28262558}.
-!- COFACTOR:
Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000269|PubMed:17825402};
-!- SUBUNIT: Interacts with TLE1 (By similarity). Component of the
MLL4 complex, at least composed of KMT2B/MLL4, ASH2L, RBBP5, WDR5,
and KDM6B. {ECO:0000250, ECO:0000269|PubMed:17825402,
ECO:0000269|Ref.13}.
-!- INTERACTION:
P03372:ESR1; NbExp=2; IntAct=EBI-2831260, EBI-78473;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:17825402}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2;
IsoId=O15054-2; Sequence=Displayed;
Note=Gene prediction based on similarity to mouse ortholog.;
Name=1;
IsoId=O15054-1; Sequence=VSP_040102;
-!- INDUCTION: By 12-O-tetradecanoylphorbol-13-acetate (TPA) in
myeloid leukemia cells. {ECO:0000269|PubMed:17193924}.
-!- SIMILARITY: Belongs to the UTX family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA21572.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB002344; BAA21572.2; ALT_INIT; mRNA.
EMBL; AC104581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC009994; AAH09994.1; -; mRNA.
CCDS; CCDS32552.1; -. [O15054-1]
RefSeq; NP_001073893.1; NM_001080424.2. [O15054-1]
RefSeq; NP_001335645.1; NM_001348716.1. [O15054-2]
RefSeq; XP_005256606.1; XM_005256549.3. [O15054-1]
RefSeq; XP_005256607.1; XM_005256550.4. [O15054-1]
RefSeq; XP_005256608.1; XM_005256551.3. [O15054-1]
RefSeq; XP_005256609.1; XM_005256552.4. [O15054-1]
RefSeq; XP_006721546.1; XM_006721483.3. [O15054-1]
RefSeq; XP_011522052.1; XM_011523750.2. [O15054-1]
RefSeq; XP_011522054.1; XM_011523752.2. [O15054-1]
UniGene; Hs.223678; -.
PDB; 2XUE; X-ray; 2.00 A; A/B=1141-1643.
PDB; 2XXZ; X-ray; 1.80 A; A/B=1176-1505.
PDB; 4ASK; X-ray; 1.86 A; A/B=1141-1643.
PDB; 5FP3; X-ray; 2.05 A; A/B=1141-1643.
PDBsum; 2XUE; -.
PDBsum; 2XXZ; -.
PDBsum; 4ASK; -.
PDBsum; 5FP3; -.
ProteinModelPortal; O15054; -.
SMR; O15054; -.
BioGrid; 116752; 13.
DIP; DIP-59912N; -.
IntAct; O15054; 6.
MINT; MINT-7002224; -.
STRING; 9606.ENSP00000254846; -.
BindingDB; O15054; -.
ChEMBL; CHEMBL1938211; -.
GuidetoPHARMACOLOGY; 2685; -.
iPTMnet; O15054; -.
PhosphoSitePlus; O15054; -.
BioMuta; KDM6B; -.
EPD; O15054; -.
PaxDb; O15054; -.
PeptideAtlas; O15054; -.
PRIDE; O15054; -.
Ensembl; ENST00000254846; ENSP00000254846; ENSG00000132510. [O15054-1]
Ensembl; ENST00000448097; ENSP00000412513; ENSG00000132510. [O15054-2]
GeneID; 23135; -.
KEGG; hsa:23135; -.
UCSC; uc002giw.2; human. [O15054-2]
CTD; 23135; -.
DisGeNET; 23135; -.
GeneCards; KDM6B; -.
HGNC; HGNC:29012; KDM6B.
HPA; HPA037988; -.
MIM; 611577; gene.
neXtProt; NX_O15054; -.
OpenTargets; ENSG00000132510; -.
eggNOG; KOG1124; Eukaryota.
eggNOG; KOG1246; Eukaryota.
eggNOG; ENOG410XR9J; LUCA.
GeneTree; ENSGT00410000025758; -.
HOGENOM; HOG000113217; -.
InParanoid; O15054; -.
KO; K11448; -.
OMA; AQPGLWE; -.
OrthoDB; EOG091G0OL6; -.
PhylomeDB; O15054; -.
TreeFam; TF317405; -.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-3214842; HDMs demethylate histones.
SIGNOR; O15054; -.
ChiTaRS; KDM6B; human.
EvolutionaryTrace; O15054; -.
GenomeRNAi; 23135; -.
PRO; PR:O15054; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000132510; -.
CleanEx; HS_JMJD3; -.
ExpressionAtlas; O15054; baseline and differential.
Genevisible; O15054; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
GO; GO:0032452; F:histone demethylase activity; TAS:Reactome.
GO; GO:0071558; F:histone demethylase activity (H3-K27 specific); IMP:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0055007; P:cardiac muscle cell differentiation; ISS:BHF-UCL.
GO; GO:0045165; P:cell fate commitment; IEA:Ensembl.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0045446; P:endothelial cell differentiation; ISS:BHF-UCL.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0071557; P:histone H3-K27 demethylation; IMP:UniProtKB.
GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0048333; P:mesodermal cell differentiation; ISS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:BHF-UCL.
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.
PANTHER; PTHR14017:SF22; PTHR14017:SF22; 1.
Pfam; PF02373; JmjC; 1.
SMART; SM00558; JmjC; 1.
PROSITE; PS51184; JMJC; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Complete proteome; Dioxygenase; Inflammatory response; Iron;
Isopeptide bond; Metal-binding; Nucleus; Oxidoreductase;
Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation;
Zinc.
CHAIN 1 1643 Lysine-specific demethylase 6B.
/FTId=PRO_0000292007.
DOMAIN 1339 1502 JmjC. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
COMPBIAS 32 85 Pro-rich.
COMPBIAS 195 906 Pro-rich.
COMPBIAS 738 764 Thr-rich.
COMPBIAS 1046 1082 Pro-rich.
METAL 1390 1390 Iron. {ECO:0000305}.
METAL 1392 1392 Iron. {ECO:0000305}.
METAL 1470 1470 Iron. {ECO:0000250|UniProtKB:O14607}.
METAL 1575 1575 Zinc. {ECO:0000250|UniProtKB:O14607}.
METAL 1578 1578 Zinc. {ECO:0000250|UniProtKB:O14607}.
METAL 1602 1602 Zinc. {ECO:0000250|UniProtKB:O14607}.
METAL 1605 1605 Zinc. {ECO:0000250|UniProtKB:O14607}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 1109 1109 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1636 1636 L -> LVRARRARGQRRRALGQAAGTGFGSPAAPFPEPPPA
FSPQ (in isoform 1).
{ECO:0000303|PubMed:9205841}.
/FTId=VSP_040102.
VARIANT 203 203 P -> A (in dbSNP:rs60738318).
/FTId=VAR_061670.
VARIANT 308 308 S -> L (in dbSNP:rs2270516).
/FTId=VAR_032927.
MUTAGEN 1390 1392 HQE->AQA: Abolishes lysine-specific
histone demethylase activity.
{ECO:0000269|PubMed:28262558}.
CONFLICT 252 254 Missing (in Ref. 1; BAA21572 and 3;
AAH09994). {ECO:0000305}.
HELIX 1178 1181 {ECO:0000244|PDB:4ASK}.
STRAND 1187 1189 {ECO:0000244|PDB:2XXZ}.
HELIX 1193 1195 {ECO:0000244|PDB:2XXZ}.
HELIX 1199 1206 {ECO:0000244|PDB:2XXZ}.
STRAND 1211 1217 {ECO:0000244|PDB:2XXZ}.
HELIX 1218 1222 {ECO:0000244|PDB:2XXZ}.
HELIX 1226 1229 {ECO:0000244|PDB:2XXZ}.
HELIX 1231 1238 {ECO:0000244|PDB:2XXZ}.
STRAND 1242 1249 {ECO:0000244|PDB:2XXZ}.
STRAND 1261 1264 {ECO:0000244|PDB:2XXZ}.
STRAND 1271 1276 {ECO:0000244|PDB:2XXZ}.
HELIX 1277 1289 {ECO:0000244|PDB:2XXZ}.
STRAND 1325 1333 {ECO:0000244|PDB:2XXZ}.
HELIX 1337 1347 {ECO:0000244|PDB:2XXZ}.
HELIX 1352 1354 {ECO:0000244|PDB:2XXZ}.
TURN 1356 1359 {ECO:0000244|PDB:2XXZ}.
STRAND 1363 1365 {ECO:0000244|PDB:2XXZ}.
STRAND 1366 1368 {ECO:0000244|PDB:4ASK}.
TURN 1371 1373 {ECO:0000244|PDB:4ASK}.
STRAND 1375 1381 {ECO:0000244|PDB:2XXZ}.
STRAND 1386 1390 {ECO:0000244|PDB:2XXZ}.
HELIX 1393 1395 {ECO:0000244|PDB:2XXZ}.
STRAND 1397 1406 {ECO:0000244|PDB:2XXZ}.
STRAND 1408 1413 {ECO:0000244|PDB:2XXZ}.
HELIX 1415 1417 {ECO:0000244|PDB:2XXZ}.
HELIX 1418 1427 {ECO:0000244|PDB:2XXZ}.
TURN 1432 1434 {ECO:0000244|PDB:2XXZ}.
HELIX 1441 1446 {ECO:0000244|PDB:2XXZ}.
STRAND 1452 1456 {ECO:0000244|PDB:2XXZ}.
STRAND 1461 1464 {ECO:0000244|PDB:2XXZ}.
STRAND 1469 1487 {ECO:0000244|PDB:2XXZ}.
HELIX 1491 1495 {ECO:0000244|PDB:2XXZ}.
HELIX 1497 1501 {ECO:0000244|PDB:2XXZ}.
HELIX 1514 1524 {ECO:0000244|PDB:4ASK}.
HELIX 1530 1557 {ECO:0000244|PDB:4ASK}.
STRAND 1561 1563 {ECO:0000244|PDB:4ASK}.
TURN 1576 1578 {ECO:0000244|PDB:4ASK}.
STRAND 1584 1590 {ECO:0000244|PDB:4ASK}.
STRAND 1592 1596 {ECO:0000244|PDB:5FP3}.
STRAND 1598 1601 {ECO:0000244|PDB:4ASK}.
HELIX 1603 1608 {ECO:0000244|PDB:4ASK}.
TURN 1610 1615 {ECO:0000244|PDB:4ASK}.
STRAND 1617 1622 {ECO:0000244|PDB:4ASK}.
HELIX 1624 1633 {ECO:0000244|PDB:4ASK}.
SEQUENCE 1643 AA; 176632 MW; 8CE32AE602683BA3 CRC64;
MHRAVDPPGA RAAREAFALG GLSCAGAWSS CPPHPPPRSA WLPGGRCSAS IGQPPLPAPL
PPSHGSSSGH PSKPYYAPGA PTPRPLHGKL ESLHGCVQAL LREPAQPGLW EQLGQLYESE
HDSEEATRCY HSALRYGGSF AELGPRIGRL QQAQLWNFHT GSCQHRAKVL PPLEQVWNLL
HLEHKRNYGA KRGGPPVKRA AEPPVVQPVP PAALSGPSGE EGLSPGGKRR RGCNSEQTGL
PPGLPLPPPP LPPPPPPPPP PPPPLPGLAT SPPFQLTKPG LWSTLHGDAW GPERKGSAPP
ERQEQRHSLP HPYPYPAPAY TAHPPGHRLV PAAPPGPGPR PPGAESHGCL PATRPPGSDL
RESRVQRSRM DSSVSPAATT ACVPYAPSRP PGLPGTTTSS SSSSSSNTGL RGVEPNPGIP
GADHYQTPAL EVSHHGRLGP SAHSSRKPFL GAPAATPHLS LPPGPSSPPP PPCPRLLRPP
PPPAWLKGPA CRAAREDGEI LEELFFGTEG PPRPAPPPLP HREGFLGPPA SRFSVGTQDS
HTPPTPPTPT TSSSNSNSGS HSSSPAGPVS FPPPPYLARS IDPLPRPPSP AQNPQDPPLV
PLTLALPPAP PSSCHQNTSG SFRRPESPRP RVSFPKTPEV GPGPPPGPLS KAPQPVPPGV
GELPARGPRL FDFPPTPLED QFEEPAEFKI LPDGLANIMK MLDESIRKEE EQQQHEAGVA
PQPPLKEPFA SLQSPFPTDT APTTTAPAVA VTTTTTTTTT TTATQEEEKK PPPALPPPPP
LAKFPPPSQP QPPPPPPPSP ASLLKSLASV LEGQKYCYRG TGAAVSTRPG PLPTTQYSPG
PPSGATALPP TSAAPSAQGS PQPSASSSSQ FSTSGGPWAR ERRAGEEPVP GPMTPTQPPP
PLSLPPARSE SEVLEEISRA CETLVERVGR SATDPADPVD TAEPADSGTE RLLPPAQAKE
EAGGVAAVSG SCKRRQKEHQ KEHRRHRRAC KDSVGRRPRE GRAKAKAKVP KEKSRRVLGN
LDLQSEEIQG REKSRPDLGG ASKAKPPTAP APPSAPAPSA QPTPPSASVP GKKAREEAPG
PPGVSRADML KLRSLSEGPP KELKIRLIKV ESGDKETFIA SEVEERRLRM ADLTISHCAA
DVVRASRNAK VKGKFRESYL SPAQSVKPKI NTEEKLPREK LNPPTPSIYL ESKRDAFSPV
LLQFCTDPRN PITVIRGLAG SLRLNLGLFS TKTLVEASGE HTVEVRTQVQ QPSDENWDLT
GTRQIWPCES SRSHTTIAKY AQYQASSFQE SLQEEKESED EESEEPDSTT GTPPSSAPDP
KNHHIIKFGT NIDLSDAKRW KPQLQELLKL PAFMRVTSTG NMLSHVGHTI LGMNTVQLYM
KVPGSRTPGH QENNNFCSVN INIGPGDCEW FAVHEHYWET ISAFCDRHGV DYLTGSWWPI
LDDLYASNIP VYRFVQRPGD LVWINAGTVH WVQATGWCNN IAWNVGPLTA YQYQLALERY
EWNEVKNVKS IVPMIHVSWN VARTVKISDP DLFKMIKFCL LQSMKHCQVQ RESLVRAGKK
IAYQGRVKDE PAYYCNECDV EVFNILFVTS ENGSRNTYLV HCEGCARRRS AGLQGVVVLE
QYRTEELAQA YDAFTLAPAS TSR


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U1916h CLIA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,Homo sapiens,Human,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6 96T
E1916h ELISA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,Homo sapiens,Human,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6,KIA 96T
E1916b ELISA 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,Lysy 96T
E1916h ELISA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,Homo sapiens,Human,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 96T
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
E1916b ELISA 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
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
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
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
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
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
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
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
ARP40101_P050 JMJD3(jumonji domain containing 3, histone lysine demethylase) 50 µg
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
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 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
18-003-43413 JmjC domain-containing histone demethylation protein 1A - EC 1.14.11.27; [Histone-H3]-lysine-36 demethylase 1A; F-box_LRR-repeat protein 11; F-box and leucine-rich repeat protein 11; F-box protein FBL 0.05 mg Aff Pur
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
27-137 JMJD5 is a histone lysine demethylase. Studies of a similar protein in mouse indicate a potential role for this protein as a tumor suppressor.JMJD5 is a putative histone lysine demethylase that contai 0.05 mg
KDM5C-1604H Protein Recombinant Human Lysine (K)-Specific Demethylase 5C, GST-tagged 20
KDM5C-1604H Protein: Recombinant Human Lysine (K)-Specific Demethylase 5C, GST-tagged 20


 

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