Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Lysine-specific demethylase 3A (EC 1.14.11.-) (JmjC domain-containing histone demethylation protein 2A) (Jumonji domain-containing protein 1A)

 KDM3A_HUMAN             Reviewed;        1321 AA.
Q9Y4C1; D6W5M3; Q53S72; Q68D47; Q68UT9; Q6N050; Q8IY08;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 4.
25-OCT-2017, entry version 138.
RecName: Full=Lysine-specific demethylase 3A;
EC=1.14.11.-;
AltName: Full=JmjC domain-containing histone demethylation protein 2A;
AltName: Full=Jumonji domain-containing protein 1A;
Name=KDM3A; Synonyms=JHDM2A, JMJD1, JMJD1A, KIAA0742, TSGA;
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], AND VARIANT VAL-212.
TISSUE=Brain;
PubMed=9872452; DOI=10.1093/dnares/5.5.277;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XI.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:277-286(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-212 AND
PRO-447.
TISSUE=Fetal kidney, Salivary gland, and Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-212.
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.
[5]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
COFACTOR, DOMAIN, AND MUTAGENESIS OF HIS-1120.
PubMed=16603237; DOI=10.1016/j.cell.2006.03.027;
Yamane K., Toumazou C., Tsukada Y.I., Erdjument-Bromage H., Tempst P.,
Wong J., Zhang Y.;
"JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription
activation by androgen receptor.";
Cell 125:483-495(2006).
[6]
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).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-895, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, 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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325; SER-445 AND
SER-766, 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).
[11]
FUNCTION, AND MUTAGENESIS OF HIS-1120.
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]
VARIANT [LARGE SCALE ANALYSIS] HIS-187.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-
9' of histone H3, thereby playing a central role in histone code.
Preferentially demethylates mono- and dimethylated H3 'Lys-9'
residue, with a preference for dimethylated residue, while it has
weak or no activity on trimethylated H3 'Lys-9'. Demethylation of
Lys residue generates formaldehyde and succinate. Involved in
hormone-dependent transcriptional activation, by participating in
recruitment to androgen-receptor target genes, resulting in H3
'Lys-9' demethylation and transcriptional activation. Involved in
spermatogenesis by regulating expression of target genes such as
PRM1 and TNP1 which are required for packaging and condensation of
sperm chromatin. Involved in obesity resistance through regulation
of metabolic genes such as PPARA and UCP1.
{ECO:0000269|PubMed:16603237, ECO:0000269|PubMed:28262558}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000269|PubMed:16603237};
Note=Binds 1 Fe(2+) ion per subunit.
{ECO:0000269|PubMed:16603237};
-!- INTERACTION:
O75582:RPS6KA5; NbExp=3; IntAct=EBI-2515339, EBI-73869;
O75582-1:RPS6KA5; NbExp=3; IntAct=EBI-2515339, EBI-16135973;
P42224-1:STAT1; NbExp=8; IntAct=EBI-2515339, EBI-15711971;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Note=Nuclear in round spermatids. When spermatids
start to elongate, localizes to the cytoplasm where it forms
distinct foci which disappear in mature spermatozoa (By
similarity). {ECO:0000250}.
-!- DOMAIN: The JmjC domain and the C6-type zinc-finger are required
for the demethylation activity. {ECO:0000269|PubMed:16603237}.
-!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate
the association with nuclear receptors. {ECO:0000250}.
-!- SIMILARITY: Belongs to the JHDM2 histone demethylase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA34462.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB018285; BAA34462.2; ALT_INIT; mRNA.
EMBL; AL832150; CAH18459.3; -; Transcribed_RNA.
EMBL; BX640698; CAE45820.1; -; mRNA.
EMBL; CR749581; CAH18373.1; -; mRNA.
EMBL; AC068288; AAY24210.1; -; Genomic_DNA.
EMBL; CH471053; EAW99453.1; -; Genomic_DNA.
EMBL; CH471053; EAW99456.1; -; Genomic_DNA.
CCDS; CCDS1990.1; -.
RefSeq; NP_001140160.1; NM_001146688.1.
RefSeq; NP_060903.2; NM_018433.5.
RefSeq; XP_016859982.1; XM_017004493.1.
UniGene; Hs.557425; -.
ProteinModelPortal; Q9Y4C1; -.
SMR; Q9Y4C1; -.
BioGrid; 120927; 27.
DIP; DIP-53661N; -.
IntAct; Q9Y4C1; 10.
MINT; MINT-6946055; -.
STRING; 9606.ENSP00000323659; -.
BindingDB; Q9Y4C1; -.
ChEMBL; CHEMBL1938209; -.
GuidetoPHARMACOLOGY; 2673; -.
iPTMnet; Q9Y4C1; -.
PhosphoSitePlus; Q9Y4C1; -.
SwissPalm; Q9Y4C1; -.
BioMuta; KDM3A; -.
DMDM; 308153659; -.
EPD; Q9Y4C1; -.
MaxQB; Q9Y4C1; -.
PaxDb; Q9Y4C1; -.
PeptideAtlas; Q9Y4C1; -.
PRIDE; Q9Y4C1; -.
Ensembl; ENST00000312912; ENSP00000323659; ENSG00000115548.
Ensembl; ENST00000409064; ENSP00000386516; ENSG00000115548.
Ensembl; ENST00000409556; ENSP00000386660; ENSG00000115548.
GeneID; 55818; -.
KEGG; hsa:55818; -.
UCSC; uc002sri.5; human.
CTD; 55818; -.
DisGeNET; 55818; -.
EuPathDB; HostDB:ENSG00000115548.16; -.
GeneCards; KDM3A; -.
H-InvDB; HIX0002238; -.
HGNC; HGNC:20815; KDM3A.
HPA; HPA055543; -.
HPA; HPA065162; -.
MIM; 611512; gene.
neXtProt; NX_Q9Y4C1; -.
OpenTargets; ENSG00000115548; -.
PharmGKB; PA164721293; -.
eggNOG; KOG1356; Eukaryota.
eggNOG; ENOG410XTAA; LUCA.
GeneTree; ENSGT00530000063039; -.
InParanoid; Q9Y4C1; -.
KO; K15601; -.
PhylomeDB; Q9Y4C1; -.
TreeFam; TF324723; -.
Reactome; R-HSA-3214842; HDMs demethylate histones.
ChiTaRS; KDM3A; human.
GenomeRNAi; 55818; -.
PRO; PR:Q9Y4C1; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115548; -.
CleanEx; HS_JMJD1A; -.
ExpressionAtlas; Q9Y4C1; baseline and differential.
Genevisible; Q9Y4C1; HS.
GO; GO:0000785; C:chromatin; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0050681; F:androgen receptor binding; IDA:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
GO; GO:0001047; F:core promoter binding; IEA:Ensembl.
GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
GO; GO:0032452; F:histone demethylase activity; TAS:Reactome.
GO; GO:0032454; F:histone demethylase activity (H3-K9 specific); IMP:UniProtKB.
GO; GO:0005506; F:iron ion binding; IMP:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0046293; P:formaldehyde biosynthetic process; IDA:UniProtKB.
GO; GO:0033169; P:histone H3-K9 demethylation; IDA:UniProtKB.
GO; GO:0036123; P:histone H3-K9 dimethylation; IEA:Ensembl.
GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:2000736; P:regulation of stem cell differentiation; IEA:Ensembl.
GO; GO:2000036; P:regulation of stem cell population maintenance; IEA:Ensembl.
GO; GO:0007290; P:spermatid nucleus elongation; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR003347; JmjC_dom.
Pfam; PF02373; JmjC; 1.
SMART; SM00558; JmjC; 1.
PROSITE; PS51184; JMJC; 1.
1: Evidence at protein level;
Acetylation; Activator; Chromatin regulator; Complete proteome;
Cytoplasm; Differentiation; Dioxygenase; Iron; Metal-binding; Nucleus;
Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome;
Spermatogenesis; Transcription; Transcription regulation; Zinc;
Zinc-finger.
CHAIN 1 1321 Lysine-specific demethylase 3A.
/FTId=PRO_0000084285.
DOMAIN 1058 1281 JmjC. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
ZN_FING 662 687 C6-type. {ECO:0000255}.
MOTIF 885 889 LXXLL motif.
METAL 1120 1120 Iron; catalytic.
{ECO:0000305|PubMed:16603237,
ECO:0000305|PubMed:28262558}.
METAL 1122 1122 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
METAL 1249 1249 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
MOD_RES 264 264 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 445 445 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 766 766 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 895 895 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VARIANT 187 187 D -> H (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035940.
VARIANT 194 194 E -> K (in dbSNP:rs13424350).
/FTId=VAR_030623.
VARIANT 212 212 I -> V (in dbSNP:rs2030259).
{ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:9872452,
ECO:0000269|Ref.4}.
/FTId=VAR_026220.
VARIANT 447 447 S -> P (in dbSNP:rs34605051).
{ECO:0000269|PubMed:17974005}.
/FTId=VAR_055977.
VARIANT 710 710 V -> E (in dbSNP:rs11677451).
/FTId=VAR_030624.
MUTAGEN 1120 1120 H->A: Abolishes lysine-specific histone
demethylase activity.
{ECO:0000269|PubMed:28262558}.
MUTAGEN 1120 1120 H->Y: Abolishes histone demethylase
activity. {ECO:0000269|PubMed:16603237}.
CONFLICT 24 24 D -> G (in Ref. 2; CAH18459/CAH18373).
{ECO:0000305}.
CONFLICT 51 51 V -> A (in Ref. 2; CAE45820).
{ECO:0000305}.
CONFLICT 500 500 S -> G (in Ref. 2; CAH18373).
{ECO:0000305}.
CONFLICT 698 698 G -> GG (in Ref. 2; CAH18459).
{ECO:0000305}.
CONFLICT 729 729 K -> KG (in Ref. 2; CAH18459).
{ECO:0000305}.
CONFLICT 767 767 K -> R (in Ref. 2; CAH18459).
{ECO:0000305}.
CONFLICT 773 773 T -> TQT (in Ref. 2; CAH18459).
{ECO:0000305}.
CONFLICT 980 980 G -> R (in Ref. 2; CAE45820).
{ECO:0000305}.
SEQUENCE 1321 AA; 147341 MW; 9689B3279F450C8A CRC64;
MVLTLGESWP VLVGRRFLSL SAADGSDGSH DSWDVERVAE WPWLSGTIRA VSHTDVTKKD
LKVCVEFDGE SWRKRRWIEV YSLLRRAFLV EHNLVLAERK SPEISERIVQ WPAITYKPLL
DKAGLGSITS VRFLGDQQRV FLSKDLLKPI QDVNSLRLSL TDNQIVSKEF QALIVKHLDE
SHLLKGDKNL VGSEVKIYSL DPSTQWFSAT VINGNPASKT LQVNCEEIPA LKIVDPSLIH
VEVVHDNLVT CGNSARIGAV KRKSSENNGT LVSKQAKSCS EASPSMCPVQ SVPTTVFKEI
LLGCTAATPP SKDPRQQSTP QAANSPPNLG AKIPQGCHKQ SLPEEISSCL NTKSEALRTK
PDVCKAGLLS KSSQIGTGDL KILTEPKGSC TQPKTNTDQE NRLESVPQAL TGLPKECLPT
KASSKAELEI ANPPELQKHL EHAPSPSDVS NAPEVKAGVN SDSPNNCSGK KVEPSALACR
SQNLKESSVK VDNESCCSRS NNKIQNAPSR KSVLTDPAKL KKLQQSGEAF VQDDSCVNIV
AQLPKCRECR LDSLRKDKEQ QKDSPVFCRF FHFRRLQFNK HGVLRVEGFL TPNKYDNEAI
GLWLPLTKNV VGIDLDTAKY ILANIGDHFC QMVISEKEAM STIEPHRQVA WKRAVKGVRE
MCDVCDTTIF NLHWVCPRCG FGVCVDCYRM KRKNCQQGAA YKTFSWLKCV KSQIHEPENL
MPTQIIPGKA LYDVGDIVHS VRAKWGIKAN CPCSNRQFKL FSKPASKEDL KQTSLAGEKP
TLGAVLQQNP SVLEPAAVGG EAASKPAGSM KPACPASTSP LNWLADLTSG NVNKENKEKQ
PTMPILKNEI KCLPPLPPLS KSSTVLHTFN STILTPVSNN NSGFLRNLLN SSTGKTENGL
KNTPKILDDI FASLVQNKTT SDLSKRPQGL TIKPSILGFD TPHYWLCDNR LLCLQDPNNK
SNWNVFRECW KQGQPVMVSG VHHKLNSELW KPESFRKEFG EQEVDLVNCR TNEIITGATV
GDFWDGFEDV PNRLKNEKEP MVLKLKDWPP GEDFRDMMPS RFDDLMANIP LPEYTRRDGK
LNLASRLPNY FVRPDLGPKM YNAYGLITPE DRKYGTTNLH LDVSDAANVM VYVGIPKGQC
EQEEEVLKTI QDGDSDELTI KRFIEGKEKP GALWHIYAAK DTEKIREFLK KVSEEQGQEN
PADHDPIHDQ SWYLDRSLRK RLHQEYGVQG WAIVQFLGDV VFIPAGAPHQ VHNLYSCIKV
AEDFVSPEHV KHCFWLTQEF RYLSQTHTNH EDKLQVKNVI YHAVKDAVAM LKASESSFGK
P


Related products :

Catalog number Product name Quantity
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
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
18-003-42721 JmjC domain-containing histone demethylation protein 3D - EC 1.14.11.-; Jumonji domain-containing protein 2D Polyclonal 0.1 mg Protein A
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
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
U1916h CLIA 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,KIAA 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
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 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
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
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
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
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
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
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
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
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


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur