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Lysine-specific demethylase 4D (EC 1.14.11.-) (JmjC domain-containing histone demethylation protein 3D) (Jumonji domain-containing protein 2D)

 KDM4D_HUMAN             Reviewed;         523 AA.
Q6B0I6; B3KPC4; Q0VF39; Q9NT41; Q9NW76;
16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 3.
22-NOV-2017, entry version 120.
RecName: Full=Lysine-specific demethylase 4D;
EC=1.14.11.-;
AltName: Full=JmjC domain-containing histone demethylation protein 3D;
AltName: Full=Jumonji domain-containing protein 2D;
Name=KDM4D; Synonyms=JHDM3D, JMJD2D;
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 GLN-408.
TISSUE=Embryo, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-408.
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 395-523.
TISSUE=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).
[6]
IDENTIFICATION.
PubMed=15138608;
Katoh M., Katoh M.;
"Identification and characterization of JMJD2 family genes in
silico.";
Int. J. Oncol. 24:1623-1628(2004).
[7]
FUNCTION, AND ENZYME ACTIVITY.
PubMed=16603238; DOI=10.1016/j.cell.2006.03.028;
Whetstine J.R., Nottke A., Lan F., Huarte M., Smolikov S., Chen Z.,
Spooner E., Li E., Zhang G., Colaiacovo M., Shi Y.;
"Reversal of histone lysine trimethylation by the JMJD2 family of
histone demethylases.";
Cell 125:467-481(2006).
[8]
ADP-RIBOSYLATION AT GLU-26 AND GLU-27.
PubMed=23102699; DOI=10.1016/j.molcel.2012.09.021;
Le May N., Iltis I., Ame J.C., Zhovmer A., Biard D., Egly J.M.,
Schreiber V., Coin F.;
"Poly (ADP-ribose) glycohydrolase regulates retinoic acid receptor-
mediated gene expression.";
Mol. Cell 48:785-798(2012).
[9]
X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) OF 11-340 IN COMPLEX WITH
INHIBITORS; ZINC AND NICKEL.
PubMed=26741168; DOI=10.1021/ACS.JMEDCHEM.5B01635;
Bavetsias V., Lanigan R.M., Ruda G.F., Atrash B., McLaughlin M.G.,
Tumber A., Mok N.Y., Le Bihan Y.V., Dempster S., Boxall K.J.,
Jeganathan F., Hatch S.B., Savitsky P., Velupillai S., Krojer T.,
England K.S., Sejberg J., Thai C., Donovan A., Pal A., Scozzafava G.,
Bennett J.M., Kawamura A., Johansson C., Szykowska A., Gileadi C.,
Burgess-Brown N.A., von Delft F., Oppermann U., Walters Z.,
Shipley J., Raynaud F.I., Westaway S.M., Prinjha R.K., Fedorov O.,
Burke R., Schofield C.J., Westwood I.M., Bountra C., Muller S.,
van Montfort R.L., Brennan P.E., Blagg J.;
"8-Substituted Pyrido[3,4-d]pyrimidin-4(3H)-one Derivatives As Potent,
Cell Permeable, KDM4 (JMJD2) and KDM5 (JARID1) Histone Lysine
Demethylase Inhibitors.";
J. Med. Chem. 59:1388-1409(2016).
-!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-
9' of histone H3, thereby playing a central role in histone code.
Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36'
nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys-
9' residue, while it has no activity on monomethylated residues.
Demethylation of Lys residue generates formaldehyde and succinate.
{ECO:0000269|PubMed:16603238}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00537}.
-!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
{ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA91508.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AK001113; BAA91508.1; ALT_INIT; mRNA.
EMBL; AK056162; BAG51636.1; -; mRNA.
EMBL; AP002383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471065; EAW66952.1; -; Genomic_DNA.
EMBL; BC074739; AAH74739.1; -; mRNA.
EMBL; BC119010; AAI19011.1; -; mRNA.
EMBL; BC122858; AAI22859.1; -; mRNA.
EMBL; AL137545; CAB70803.1; -; mRNA.
CCDS; CCDS8302.1; -.
PIR; T46388; T46388.
RefSeq; NP_060509.2; NM_018039.2.
UniGene; Hs.503598; -.
PDB; 3DXT; X-ray; 1.80 A; A=1-354.
PDB; 3DXU; X-ray; 2.20 A; A=11-341.
PDB; 4D6Q; X-ray; 1.29 A; A=1-342.
PDB; 4D6R; X-ray; 1.40 A; A=1-342.
PDB; 4D6S; X-ray; 1.40 A; A=1-342.
PDB; 4HON; X-ray; 1.80 A; A/B=12-341.
PDB; 4HOO; X-ray; 2.50 A; A/B=12-341.
PDB; 5F5A; X-ray; 1.41 A; A=1-342.
PDB; 5F5C; X-ray; 1.88 A; A=1-342.
PDB; 5FP4; X-ray; 2.00 A; A=11-341.
PDB; 5FP7; X-ray; 2.00 A; A=11-341.
PDB; 5FP8; X-ray; 1.98 A; A=11-341.
PDB; 5FP9; X-ray; 2.00 A; A=11-341.
PDB; 5FPA; X-ray; 1.96 A; A=11-341.
PDB; 5FPB; X-ray; 1.91 A; A=11-341.
PDB; 5PH0; X-ray; 1.34 A; A=1-342.
PDB; 5PH1; X-ray; 1.25 A; A=1-342.
PDB; 5PH2; X-ray; 1.45 A; A=1-342.
PDB; 5PH3; X-ray; 1.24 A; A=1-342.
PDB; 5PH4; X-ray; 1.27 A; A=1-342.
PDB; 5PH5; X-ray; 1.35 A; A=1-342.
PDB; 5PH6; X-ray; 1.74 A; A=1-342.
PDB; 5PH7; X-ray; 1.43 A; A=1-342.
PDB; 5PH8; X-ray; 1.40 A; A=1-342.
PDB; 5PH9; X-ray; 1.48 A; A=1-342.
PDB; 5PHA; X-ray; 1.45 A; A=1-342.
PDB; 5PHB; X-ray; 1.34 A; A=1-342.
PDB; 5PHC; X-ray; 1.29 A; A=1-342.
PDB; 5PHD; X-ray; 1.36 A; A=1-342.
PDB; 5PHE; X-ray; 1.35 A; A=1-342.
PDB; 5PHF; X-ray; 1.39 A; A=1-342.
PDB; 5PHG; X-ray; 1.40 A; A=1-342.
PDB; 5PHH; X-ray; 1.60 A; A=1-342.
PDB; 5PHI; X-ray; 1.97 A; A=1-342.
PDB; 5PHJ; X-ray; 1.15 A; A=1-342.
PDB; 5PHK; X-ray; 1.25 A; A=1-342.
PDB; 5PHL; X-ray; 1.14 A; A=1-342.
PDB; 5PHM; X-ray; 1.40 A; A=1-342.
PDB; 5PHN; X-ray; 1.29 A; A=1-342.
PDB; 5PHO; X-ray; 1.40 A; A=1-342.
PDB; 5PHP; X-ray; 1.72 A; A=1-342.
PDB; 5PHQ; X-ray; 2.23 A; A=1-342.
PDB; 5PHR; X-ray; 1.66 A; A=1-342.
PDB; 5PHS; X-ray; 2.54 A; A=1-342.
PDB; 5PHT; X-ray; 1.83 A; A=1-342.
PDB; 5PHU; X-ray; 1.79 A; A=1-342.
PDB; 5PHV; X-ray; 1.83 A; A=1-342.
PDB; 5PHW; X-ray; 1.31 A; A=1-342.
PDB; 5PHX; X-ray; 1.27 A; A=1-342.
PDB; 5PHY; X-ray; 1.34 A; A=1-342.
PDB; 5PHZ; X-ray; 1.47 A; A=1-342.
PDB; 5PI0; X-ray; 1.50 A; A=1-342.
PDB; 5PI1; X-ray; 1.34 A; A=1-342.
PDB; 5PI2; X-ray; 1.52 A; A=1-342.
PDB; 5PI3; X-ray; 1.29 A; A=1-342.
PDB; 5PI4; X-ray; 1.35 A; A=1-342.
PDB; 5PI5; X-ray; 1.42 A; A=1-342.
PDB; 5PI6; X-ray; 1.29 A; A=1-342.
PDB; 5PI7; X-ray; 1.61 A; A=1-342.
PDB; 5PI8; X-ray; 1.27 A; A=1-342.
PDB; 5PI9; X-ray; 1.45 A; A=1-342.
PDB; 5PIA; X-ray; 1.18 A; A=1-342.
PDB; 5PIB; X-ray; 1.64 A; A=1-342.
PDB; 5PIC; X-ray; 1.29 A; A=1-342.
PDB; 5PID; X-ray; 1.50 A; A=1-342.
PDB; 5PIE; X-ray; 1.42 A; A=1-342.
PDB; 5PIF; X-ray; 1.37 A; A=1-342.
PDB; 5PIG; X-ray; 1.44 A; A=1-342.
PDB; 5PIH; X-ray; 1.79 A; A=1-342.
PDB; 5PII; X-ray; 1.45 A; A=1-342.
PDB; 5PIJ; X-ray; 1.45 A; A=1-342.
PDB; 5PIK; X-ray; 1.80 A; A=1-342.
PDB; 5PIL; X-ray; 1.65 A; A=1-342.
PDB; 5PIM; X-ray; 1.25 A; A=1-342.
PDB; 5PIN; X-ray; 1.50 A; A=1-342.
PDB; 5PIO; X-ray; 1.72 A; A=1-342.
PDB; 5PIP; X-ray; 1.42 A; A=1-342.
PDB; 5PIQ; X-ray; 1.50 A; A=1-342.
PDB; 5PIR; X-ray; 1.45 A; A=1-342.
PDB; 5PIS; X-ray; 1.30 A; A=1-342.
PDB; 5PIT; X-ray; 1.79 A; A=1-342.
PDB; 5PIU; X-ray; 1.48 A; A=1-342.
PDB; 5PIV; X-ray; 1.43 A; A=1-342.
PDB; 5PIW; X-ray; 1.23 A; A=1-342.
PDB; 5PIX; X-ray; 1.35 A; A=1-342.
PDB; 5PIY; X-ray; 1.31 A; A=1-342.
PDB; 5PIZ; X-ray; 1.38 A; A=1-342.
PDB; 5PJ0; X-ray; 1.31 A; A=1-342.
PDB; 5PJ1; X-ray; 1.35 A; A=1-342.
PDB; 5PJ2; X-ray; 1.44 A; A=1-342.
PDB; 5PJ3; X-ray; 1.30 A; A=1-342.
PDB; 5PJ4; X-ray; 1.52 A; A=1-342.
PDB; 5PJ5; X-ray; 1.24 A; A=1-342.
PDB; 5PJ6; X-ray; 1.35 A; A=1-342.
PDB; 5PJ7; X-ray; 1.39 A; A=1-342.
PDB; 5PJ8; X-ray; 1.40 A; A=1-342.
PDB; 5PJ9; X-ray; 1.50 A; A=1-342.
PDB; 5PJA; X-ray; 1.89 A; A=1-342.
PDB; 5PJB; X-ray; 1.58 A; A=1-342.
PDB; 5PJC; X-ray; 1.40 A; A=1-342.
PDB; 5PJD; X-ray; 1.43 A; A=1-342.
PDB; 5PJE; X-ray; 1.37 A; A=1-342.
PDB; 5PJF; X-ray; 1.47 A; A=1-342.
PDB; 5PJG; X-ray; 1.40 A; A=1-342.
PDB; 5PJH; X-ray; 1.18 A; A=1-342.
PDB; 5PJI; X-ray; 1.34 A; A=1-342.
PDB; 5PJJ; X-ray; 1.67 A; A=1-342.
PDB; 5PJK; X-ray; 1.69 A; A=1-342.
PDB; 5PJL; X-ray; 1.52 A; A=1-342.
PDB; 5PJM; X-ray; 1.43 A; A=1-342.
PDB; 5PJN; X-ray; 1.48 A; A=1-342.
PDB; 5PJO; X-ray; 1.35 A; A=1-342.
PDB; 5PJP; X-ray; 1.39 A; A=1-342.
PDB; 5PJQ; X-ray; 1.38 A; A=1-342.
PDB; 5PJR; X-ray; 1.29 A; A=1-342.
PDB; 5PJS; X-ray; 1.64 A; A=1-342.
PDB; 5PJT; X-ray; 1.54 A; A=1-342.
PDB; 5PJU; X-ray; 1.27 A; A=1-342.
PDB; 5PJV; X-ray; 1.34 A; A=1-342.
PDB; 5PJW; X-ray; 1.56 A; A=1-342.
PDB; 5PJX; X-ray; 1.35 A; A=1-342.
PDB; 5PJY; X-ray; 1.34 A; A=1-342.
PDB; 5PJZ; X-ray; 1.29 A; A=1-342.
PDB; 5PK0; X-ray; 1.28 A; A=1-342.
PDB; 5PK1; X-ray; 1.35 A; A=1-342.
PDB; 5PK2; X-ray; 1.42 A; A=1-342.
PDB; 5PK3; X-ray; 1.42 A; A=1-342.
PDB; 5PK4; X-ray; 1.72 A; A=1-342.
PDB; 5PK5; X-ray; 1.39 A; A=1-342.
PDB; 5PK6; X-ray; 2.38 A; A=1-342.
PDB; 5PK7; X-ray; 1.29 A; A=1-342.
PDB; 5PK8; X-ray; 1.44 A; A=1-342.
PDB; 5PK9; X-ray; 1.34 A; A=1-342.
PDB; 5PKA; X-ray; 1.71 A; A=1-342.
PDB; 5PKB; X-ray; 1.40 A; A=1-342.
PDB; 5PKC; X-ray; 1.29 A; A=1-342.
PDB; 5PKD; X-ray; 1.55 A; A=1-342.
PDB; 5PKE; X-ray; 1.44 A; A=1-342.
PDB; 5PKF; X-ray; 1.34 A; A=1-342.
PDB; 5PKG; X-ray; 1.54 A; A=1-342.
PDB; 5PKH; X-ray; 1.19 A; A=1-342.
PDB; 5PKI; X-ray; 1.19 A; A=1-342.
PDB; 5PKJ; X-ray; 1.22 A; A=1-342.
PDB; 5PKK; X-ray; 1.50 A; A=1-342.
PDB; 5PKL; X-ray; 1.35 A; A=1-342.
PDB; 5PKM; X-ray; 1.37 A; A=1-342.
PDB; 5PKN; X-ray; 1.30 A; A=1-342.
PDB; 5PKO; X-ray; 2.38 A; A=1-342.
PDB; 5PKP; X-ray; 1.30 A; A=1-342.
PDB; 5PKQ; X-ray; 1.28 A; A=1-342.
PDB; 5PKR; X-ray; 1.31 A; A=1-342.
PDB; 5PKS; X-ray; 1.50 A; A=1-342.
PDB; 5PKT; X-ray; 1.50 A; A=1-342.
PDB; 5PKU; X-ray; 1.47 A; A=1-342.
PDB; 5PKV; X-ray; 1.35 A; A=1-342.
PDB; 5PKW; X-ray; 1.35 A; A=1-342.
PDB; 5PKX; X-ray; 1.45 A; A=1-342.
PDB; 5PKY; X-ray; 1.25 A; A=1-342.
PDB; 5PKZ; X-ray; 1.50 A; A=1-342.
PDB; 5PL0; X-ray; 1.27 A; A=1-342.
PDB; 5PL1; X-ray; 1.42 A; A=1-342.
PDB; 5PL2; X-ray; 1.34 A; A=1-342.
PDB; 5PL3; X-ray; 1.27 A; A=1-342.
PDB; 5PL4; X-ray; 1.21 A; A=1-342.
PDB; 5PL5; X-ray; 1.57 A; A=1-342.
PDB; 5PL6; X-ray; 1.29 A; A=1-342.
PDB; 5PL7; X-ray; 1.30 A; A=1-342.
PDB; 5PL8; X-ray; 1.54 A; A=1-342.
PDB; 5PL9; X-ray; 1.65 A; A=1-342.
PDB; 5PLA; X-ray; 1.37 A; A=1-342.
PDB; 5PLB; X-ray; 1.49 A; A=1-342.
PDB; 5PLC; X-ray; 1.49 A; A=1-342.
PDB; 5PLD; X-ray; 1.46 A; A=1-342.
PDB; 5PLE; X-ray; 1.45 A; A=1-342.
PDB; 5PLF; X-ray; 1.33 A; A=1-342.
PDB; 5PLG; X-ray; 1.31 A; A=1-342.
PDB; 5PLH; X-ray; 1.46 A; A=1-342.
PDB; 5PLI; X-ray; 1.39 A; A=1-342.
PDB; 5PLJ; X-ray; 1.49 A; A=1-342.
PDB; 5PLK; X-ray; 1.14 A; A=1-342.
PDB; 5PLL; X-ray; 1.28 A; A=1-342.
PDB; 5PLM; X-ray; 1.14 A; A=1-342.
PDB; 5PLN; X-ray; 1.14 A; A=1-342.
PDB; 5PLO; X-ray; 1.14 A; A=1-342.
PDB; 5PLP; X-ray; 1.46 A; A=1-342.
PDB; 5PLQ; X-ray; 1.36 A; A=1-342.
PDB; 5PLR; X-ray; 1.53 A; A=1-342.
PDB; 5PLS; X-ray; 1.70 A; A=1-342.
PDB; 5PLT; X-ray; 1.53 A; A=1-342.
PDB; 5PLU; X-ray; 1.47 A; A=1-342.
PDB; 5PLV; X-ray; 1.14 A; A=1-342.
PDB; 5PLW; X-ray; 1.31 A; A=1-342.
PDB; 5PLX; X-ray; 1.29 A; A=1-342.
PDB; 5PLY; X-ray; 1.38 A; A=1-342.
PDB; 5PLZ; X-ray; 1.71 A; A=1-342.
PDB; 5PM0; X-ray; 2.14 A; A=1-342.
PDB; 5PM1; X-ray; 1.54 A; A=1-342.
PDB; 5PM2; X-ray; 1.52 A; A=1-342.
PDB; 5PM3; X-ray; 1.46 A; A=1-342.
PDB; 5PM4; X-ray; 1.44 A; A=1-342.
PDB; 5PM5; X-ray; 1.76 A; A=1-342.
PDB; 5PM6; X-ray; 1.78 A; A=1-342.
PDB; 5PM7; X-ray; 1.43 A; A=1-342.
PDB; 5PM8; X-ray; 1.54 A; A=1-342.
PDB; 5PM9; X-ray; 1.50 A; A=1-342.
PDB; 5PMA; X-ray; 1.29 A; A=1-342.
PDB; 5PMB; X-ray; 1.63 A; A=1-342.
PDB; 5PMC; X-ray; 1.58 A; A=1-342.
PDB; 5PMD; X-ray; 1.63 A; A=1-342.
PDB; 5PME; X-ray; 1.39 A; A=1-342.
PDB; 5PMF; X-ray; 1.36 A; A=1-342.
PDB; 5PMG; X-ray; 1.51 A; A=1-342.
PDB; 5PMH; X-ray; 1.52 A; A=1-342.
PDB; 5PMI; X-ray; 1.71 A; A=1-342.
PDB; 5PMJ; X-ray; 1.37 A; A=1-342.
PDB; 5PMK; X-ray; 1.44 A; A=1-342.
PDB; 5PML; X-ray; 1.58 A; A=1-342.
PDB; 5PMM; X-ray; 1.39 A; A=1-342.
PDB; 5PMN; X-ray; 1.72 A; A=1-342.
PDB; 5PMO; X-ray; 1.53 A; A=1-342.
PDB; 5PMP; X-ray; 1.55 A; A=1-342.
PDB; 5PMQ; X-ray; 1.46 A; A=1-342.
PDB; 5PMR; X-ray; 1.51 A; A=1-342.
PDB; 5PMS; X-ray; 1.24 A; A=1-342.
PDB; 5PMT; X-ray; 1.22 A; A=1-342.
PDB; 5PMU; X-ray; 1.48 A; A=1-342.
PDB; 5PMV; X-ray; 1.34 A; A=1-342.
PDB; 5PMW; X-ray; 1.19 A; A=1-342.
PDB; 5PMX; X-ray; 1.14 A; A=1-342.
PDB; 5PMY; X-ray; 1.29 A; A=1-342.
PDB; 5PMZ; X-ray; 1.15 A; A=1-342.
PDB; 5PN0; X-ray; 1.14 A; A=1-342.
PDB; 5PN1; X-ray; 1.41 A; A=1-342.
PDB; 5PN2; X-ray; 1.41 A; A=1-342.
PDB; 5PN3; X-ray; 1.60 A; A=1-342.
PDB; 5PN4; X-ray; 1.37 A; A=1-342.
PDB; 5PN5; X-ray; 1.30 A; A=1-342.
PDB; 5PN6; X-ray; 1.42 A; A=1-342.
PDB; 5PN7; X-ray; 1.25 A; A=1-342.
PDB; 5PN8; X-ray; 1.34 A; A=1-342.
PDB; 5PN9; X-ray; 1.48 A; A=1-342.
PDB; 5PNA; X-ray; 1.78 A; A=1-342.
PDB; 5PNB; X-ray; 1.23 A; A=1-342.
PDB; 5PNC; X-ray; 1.35 A; A=1-342.
PDB; 5PND; X-ray; 1.49 A; A=1-342.
PDB; 5PNE; X-ray; 1.29 A; A=1-342.
PDB; 5PNF; X-ray; 1.24 A; A=1-342.
PDB; 5PNG; X-ray; 1.38 A; A=1-342.
PDB; 5PNH; X-ray; 1.14 A; A=1-342.
PDB; 5PNI; X-ray; 1.45 A; A=1-342.
PDB; 5PNJ; X-ray; 1.40 A; A=1-342.
PDB; 5PNK; X-ray; 1.27 A; A=1-342.
PDB; 5PNL; X-ray; 1.44 A; A=1-342.
PDB; 5PNM; X-ray; 1.25 A; A=1-342.
PDB; 5PNN; X-ray; 1.21 A; A=1-342.
PDB; 5PNO; X-ray; 1.55 A; A=1-342.
PDB; 5PNP; X-ray; 1.47 A; A=1-342.
PDB; 5PNQ; X-ray; 1.47 A; A=1-342.
PDB; 5PNR; X-ray; 1.14 A; A=1-342.
PDB; 5PNS; X-ray; 1.36 A; A=1-342.
PDB; 5PNU; X-ray; 1.14 A; A=1-342.
PDB; 5PNV; X-ray; 1.60 A; A=1-342.
PDB; 5PNW; X-ray; 1.40 A; A=1-342.
PDBsum; 3DXT; -.
PDBsum; 3DXU; -.
PDBsum; 4D6Q; -.
PDBsum; 4D6R; -.
PDBsum; 4D6S; -.
PDBsum; 4HON; -.
PDBsum; 4HOO; -.
PDBsum; 5F5A; -.
PDBsum; 5F5C; -.
PDBsum; 5FP4; -.
PDBsum; 5FP7; -.
PDBsum; 5FP8; -.
PDBsum; 5FP9; -.
PDBsum; 5FPA; -.
PDBsum; 5FPB; -.
PDBsum; 5PH0; -.
PDBsum; 5PH1; -.
PDBsum; 5PH2; -.
PDBsum; 5PH3; -.
PDBsum; 5PH4; -.
PDBsum; 5PH5; -.
PDBsum; 5PH6; -.
PDBsum; 5PH7; -.
PDBsum; 5PH8; -.
PDBsum; 5PH9; -.
PDBsum; 5PHA; -.
PDBsum; 5PHB; -.
PDBsum; 5PHC; -.
PDBsum; 5PHD; -.
PDBsum; 5PHE; -.
PDBsum; 5PHF; -.
PDBsum; 5PHG; -.
PDBsum; 5PHH; -.
PDBsum; 5PHI; -.
PDBsum; 5PHJ; -.
PDBsum; 5PHK; -.
PDBsum; 5PHL; -.
PDBsum; 5PHM; -.
PDBsum; 5PHN; -.
PDBsum; 5PHO; -.
PDBsum; 5PHP; -.
PDBsum; 5PHQ; -.
PDBsum; 5PHR; -.
PDBsum; 5PHS; -.
PDBsum; 5PHT; -.
PDBsum; 5PHU; -.
PDBsum; 5PHV; -.
PDBsum; 5PHW; -.
PDBsum; 5PHX; -.
PDBsum; 5PHY; -.
PDBsum; 5PHZ; -.
PDBsum; 5PI0; -.
PDBsum; 5PI1; -.
PDBsum; 5PI2; -.
PDBsum; 5PI3; -.
PDBsum; 5PI4; -.
PDBsum; 5PI5; -.
PDBsum; 5PI6; -.
PDBsum; 5PI7; -.
PDBsum; 5PI8; -.
PDBsum; 5PI9; -.
PDBsum; 5PIA; -.
PDBsum; 5PIB; -.
PDBsum; 5PIC; -.
PDBsum; 5PID; -.
PDBsum; 5PIE; -.
PDBsum; 5PIF; -.
PDBsum; 5PIG; -.
PDBsum; 5PIH; -.
PDBsum; 5PII; -.
PDBsum; 5PIJ; -.
PDBsum; 5PIK; -.
PDBsum; 5PIL; -.
PDBsum; 5PIM; -.
PDBsum; 5PIN; -.
PDBsum; 5PIO; -.
PDBsum; 5PIP; -.
PDBsum; 5PIQ; -.
PDBsum; 5PIR; -.
PDBsum; 5PIS; -.
PDBsum; 5PIT; -.
PDBsum; 5PIU; -.
PDBsum; 5PIV; -.
PDBsum; 5PIW; -.
PDBsum; 5PIX; -.
PDBsum; 5PIY; -.
PDBsum; 5PIZ; -.
PDBsum; 5PJ0; -.
PDBsum; 5PJ1; -.
PDBsum; 5PJ2; -.
PDBsum; 5PJ3; -.
PDBsum; 5PJ4; -.
PDBsum; 5PJ5; -.
PDBsum; 5PJ6; -.
PDBsum; 5PJ7; -.
PDBsum; 5PJ8; -.
PDBsum; 5PJ9; -.
PDBsum; 5PJA; -.
PDBsum; 5PJB; -.
PDBsum; 5PJC; -.
PDBsum; 5PJD; -.
PDBsum; 5PJE; -.
PDBsum; 5PJF; -.
PDBsum; 5PJG; -.
PDBsum; 5PJH; -.
PDBsum; 5PJI; -.
PDBsum; 5PJJ; -.
PDBsum; 5PJK; -.
PDBsum; 5PJL; -.
PDBsum; 5PJM; -.
PDBsum; 5PJN; -.
PDBsum; 5PJO; -.
PDBsum; 5PJP; -.
PDBsum; 5PJQ; -.
PDBsum; 5PJR; -.
PDBsum; 5PJS; -.
PDBsum; 5PJT; -.
PDBsum; 5PJU; -.
PDBsum; 5PJV; -.
PDBsum; 5PJW; -.
PDBsum; 5PJX; -.
PDBsum; 5PJY; -.
PDBsum; 5PJZ; -.
PDBsum; 5PK0; -.
PDBsum; 5PK1; -.
PDBsum; 5PK2; -.
PDBsum; 5PK3; -.
PDBsum; 5PK4; -.
PDBsum; 5PK5; -.
PDBsum; 5PK6; -.
PDBsum; 5PK7; -.
PDBsum; 5PK8; -.
PDBsum; 5PK9; -.
PDBsum; 5PKA; -.
PDBsum; 5PKB; -.
PDBsum; 5PKC; -.
PDBsum; 5PKD; -.
PDBsum; 5PKE; -.
PDBsum; 5PKF; -.
PDBsum; 5PKG; -.
PDBsum; 5PKH; -.
PDBsum; 5PKI; -.
PDBsum; 5PKJ; -.
PDBsum; 5PKK; -.
PDBsum; 5PKL; -.
PDBsum; 5PKM; -.
PDBsum; 5PKN; -.
PDBsum; 5PKO; -.
PDBsum; 5PKP; -.
PDBsum; 5PKQ; -.
PDBsum; 5PKR; -.
PDBsum; 5PKS; -.
PDBsum; 5PKT; -.
PDBsum; 5PKU; -.
PDBsum; 5PKV; -.
PDBsum; 5PKW; -.
PDBsum; 5PKX; -.
PDBsum; 5PKY; -.
PDBsum; 5PKZ; -.
PDBsum; 5PL0; -.
PDBsum; 5PL1; -.
PDBsum; 5PL2; -.
PDBsum; 5PL3; -.
PDBsum; 5PL4; -.
PDBsum; 5PL5; -.
PDBsum; 5PL6; -.
PDBsum; 5PL7; -.
PDBsum; 5PL8; -.
PDBsum; 5PL9; -.
PDBsum; 5PLA; -.
PDBsum; 5PLB; -.
PDBsum; 5PLC; -.
PDBsum; 5PLD; -.
PDBsum; 5PLE; -.
PDBsum; 5PLF; -.
PDBsum; 5PLG; -.
PDBsum; 5PLH; -.
PDBsum; 5PLI; -.
PDBsum; 5PLJ; -.
PDBsum; 5PLK; -.
PDBsum; 5PLL; -.
PDBsum; 5PLM; -.
PDBsum; 5PLN; -.
PDBsum; 5PLO; -.
PDBsum; 5PLP; -.
PDBsum; 5PLQ; -.
PDBsum; 5PLR; -.
PDBsum; 5PLS; -.
PDBsum; 5PLT; -.
PDBsum; 5PLU; -.
PDBsum; 5PLV; -.
PDBsum; 5PLW; -.
PDBsum; 5PLX; -.
PDBsum; 5PLY; -.
PDBsum; 5PLZ; -.
PDBsum; 5PM0; -.
PDBsum; 5PM1; -.
PDBsum; 5PM2; -.
PDBsum; 5PM3; -.
PDBsum; 5PM4; -.
PDBsum; 5PM5; -.
PDBsum; 5PM6; -.
PDBsum; 5PM7; -.
PDBsum; 5PM8; -.
PDBsum; 5PM9; -.
PDBsum; 5PMA; -.
PDBsum; 5PMB; -.
PDBsum; 5PMC; -.
PDBsum; 5PMD; -.
PDBsum; 5PME; -.
PDBsum; 5PMF; -.
PDBsum; 5PMG; -.
PDBsum; 5PMH; -.
PDBsum; 5PMI; -.
PDBsum; 5PMJ; -.
PDBsum; 5PMK; -.
PDBsum; 5PML; -.
PDBsum; 5PMM; -.
PDBsum; 5PMN; -.
PDBsum; 5PMO; -.
PDBsum; 5PMP; -.
PDBsum; 5PMQ; -.
PDBsum; 5PMR; -.
PDBsum; 5PMS; -.
PDBsum; 5PMT; -.
PDBsum; 5PMU; -.
PDBsum; 5PMV; -.
PDBsum; 5PMW; -.
PDBsum; 5PMX; -.
PDBsum; 5PMY; -.
PDBsum; 5PMZ; -.
PDBsum; 5PN0; -.
PDBsum; 5PN1; -.
PDBsum; 5PN2; -.
PDBsum; 5PN3; -.
PDBsum; 5PN4; -.
PDBsum; 5PN5; -.
PDBsum; 5PN6; -.
PDBsum; 5PN7; -.
PDBsum; 5PN8; -.
PDBsum; 5PN9; -.
PDBsum; 5PNA; -.
PDBsum; 5PNB; -.
PDBsum; 5PNC; -.
PDBsum; 5PND; -.
PDBsum; 5PNE; -.
PDBsum; 5PNF; -.
PDBsum; 5PNG; -.
PDBsum; 5PNH; -.
PDBsum; 5PNI; -.
PDBsum; 5PNJ; -.
PDBsum; 5PNK; -.
PDBsum; 5PNL; -.
PDBsum; 5PNM; -.
PDBsum; 5PNN; -.
PDBsum; 5PNO; -.
PDBsum; 5PNP; -.
PDBsum; 5PNQ; -.
PDBsum; 5PNR; -.
PDBsum; 5PNS; -.
PDBsum; 5PNU; -.
PDBsum; 5PNV; -.
PDBsum; 5PNW; -.
ProteinModelPortal; Q6B0I6; -.
SMR; Q6B0I6; -.
BioGrid; 120819; 7.
DIP; DIP-29606N; -.
IntAct; Q6B0I6; 4.
STRING; 9606.ENSP00000334181; -.
ChEMBL; CHEMBL6138; -.
iPTMnet; Q6B0I6; -.
PhosphoSitePlus; Q6B0I6; -.
BioMuta; KDM4D; -.
DMDM; 239938885; -.
EPD; Q6B0I6; -.
PaxDb; Q6B0I6; -.
PeptideAtlas; Q6B0I6; -.
PRIDE; Q6B0I6; -.
Ensembl; ENST00000335080; ENSP00000334181; ENSG00000186280.
Ensembl; ENST00000536741; ENSP00000460897; ENSG00000186280.
Ensembl; ENST00000610872; ENSP00000482224; ENSG00000186280.
GeneID; 55693; -.
KEGG; hsa:55693; -.
UCSC; uc001pfe.4; human.
CTD; 55693; -.
DisGeNET; 55693; -.
EuPathDB; HostDB:ENSG00000186280.6; -.
GeneCards; KDM4D; -.
HGNC; HGNC:25498; KDM4D.
HPA; HPA055854; -.
HPA; HPA064037; -.
MIM; 609766; gene.
neXtProt; NX_Q6B0I6; -.
OpenTargets; ENSG00000186280; -.
PharmGKB; PA164721552; -.
eggNOG; KOG0958; Eukaryota.
eggNOG; ENOG410XP0T; LUCA.
GeneTree; ENSGT00530000063342; -.
HOGENOM; HOG000231125; -.
InParanoid; Q6B0I6; -.
KO; K06709; -.
OMA; KNTKRMR; -.
OrthoDB; EOG091G01FR; -.
PhylomeDB; Q6B0I6; -.
TreeFam; TF106449; -.
BRENDA; 1.14.11.B1; 2681.
Reactome; R-HSA-3214842; HDMs demethylate histones.
EvolutionaryTrace; Q6B0I6; -.
GeneWiki; JMJD2D; -.
GenomeRNAi; 55693; -.
PRO; PR:Q6B0I6; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000186280; -.
CleanEx; HS_JMJD2D; -.
Genevisible; Q6B0I6; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0035861; C:site of double-strand break; IDA:MGI.
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); IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0071479; P:cellular response to ionizing radiation; IMP:MGI.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:MGI.
GO; GO:0033169; P:histone H3-K9 demethylation; IDA:UniProtKB.
GO; GO:0035563; P:positive regulation of chromatin binding; IMP:MGI.
GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IMP:MGI.
GO; GO:0001932; P:regulation of protein phosphorylation; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR003347; JmjC_dom.
InterPro; IPR003349; JmjN.
Pfam; PF02373; JmjC; 1.
Pfam; PF02375; JmjN; 1.
SMART; SM00558; JmjC; 1.
SMART; SM00545; JmjN; 1.
PROSITE; PS51184; JMJC; 1.
PROSITE; PS51183; JMJN; 1.
1: Evidence at protein level;
3D-structure; ADP-ribosylation; Chromatin regulator;
Complete proteome; Dioxygenase; Iron; Metal-binding; Nucleus;
Oxidoreductase; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Zinc.
CHAIN 1 523 Lysine-specific demethylase 4D.
/FTId=PRO_0000234376.
DOMAIN 18 60 JmjN. {ECO:0000255|PROSITE-
ProRule:PRU00537}.
DOMAIN 146 312 JmjC. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
COMPBIAS 91 94 Poly-Lys.
METAL 192 192 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538,
ECO:0000305|PubMed:26741168}.
METAL 194 194 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538,
ECO:0000305|PubMed:26741168}.
METAL 238 238 Zinc. {ECO:0000244|PDB:5F5A,
ECO:0000244|PDB:5F5C}.
METAL 244 244 Zinc; via tele nitrogen.
{ECO:0000244|PDB:5F5A,
ECO:0000244|PDB:5F5C}.
METAL 280 280 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538,
ECO:0000305|PubMed:26741168}.
METAL 310 310 Zinc. {ECO:0000244|PDB:5F5A,
ECO:0000244|PDB:5F5C}.
METAL 312 312 Zinc. {ECO:0000244|PDB:5F5A,
ECO:0000244|PDB:5F5C}.
BINDING 136 136 2-oxoglutarate.
{ECO:0000250|UniProtKB:B2RXH2}.
BINDING 202 202 2-oxoglutarate.
{ECO:0000250|UniProtKB:B2RXH2}.
BINDING 210 210 2-oxoglutarate.
{ECO:0000250|UniProtKB:B2RXH2}.
BINDING 245 245 2-oxoglutarate.
{ECO:0000250|UniProtKB:B2RXH2}.
MOD_RES 26 26 PolyADP-ribosyl glutamic acid.
{ECO:0000269|PubMed:23102699}.
MOD_RES 27 27 PolyADP-ribosyl glutamic acid.
{ECO:0000269|PubMed:23102699}.
VARIANT 355 355 S -> R (in dbSNP:rs35631512).
/FTId=VAR_057882.
VARIANT 408 408 R -> Q (in dbSNP:rs3740853).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_026225.
VARIANT 471 471 A -> S (in dbSNP:rs34366036).
/FTId=VAR_057883.
CONFLICT 510 510 H -> R (in Ref. 4; AAH74739).
{ECO:0000305}.
STRAND 19 21 {ECO:0000244|PDB:5PLK}.
TURN 25 28 {ECO:0000244|PDB:5PLK}.
HELIX 31 40 {ECO:0000244|PDB:5PLK}.
HELIX 43 46 {ECO:0000244|PDB:5PLK}.
STRAND 47 51 {ECO:0000244|PDB:5PLK}.
STRAND 59 61 {ECO:0000244|PDB:5PHO}.
HELIX 66 68 {ECO:0000244|PDB:5PIW}.
STRAND 70 73 {ECO:0000244|PDB:5PLK}.
STRAND 75 82 {ECO:0000244|PDB:5PLK}.
STRAND 85 92 {ECO:0000244|PDB:5PLK}.
HELIX 98 106 {ECO:0000244|PDB:5PLK}.
TURN 108 110 {ECO:0000244|PDB:5PLK}.
HELIX 118 128 {ECO:0000244|PDB:5PLK}.
HELIX 129 131 {ECO:0000244|PDB:5PLK}.
STRAND 135 141 {ECO:0000244|PDB:5PLK}.
HELIX 154 156 {ECO:0000244|PDB:5PK6}.
HELIX 160 168 {ECO:0000244|PDB:5PLK}.
TURN 173 175 {ECO:0000244|PDB:4HON}.
STRAND 179 183 {ECO:0000244|PDB:5PLK}.
STRAND 188 192 {ECO:0000244|PDB:5PLK}.
HELIX 195 197 {ECO:0000244|PDB:5PLK}.
STRAND 199 208 {ECO:0000244|PDB:5PLK}.
STRAND 210 215 {ECO:0000244|PDB:5PLK}.
HELIX 217 219 {ECO:0000244|PDB:5PLK}.
HELIX 220 230 {ECO:0000244|PDB:5PLK}.
HELIX 232 237 {ECO:0000244|PDB:5PLK}.
HELIX 241 244 {ECO:0000244|PDB:5PLK}.
STRAND 247 249 {ECO:0000244|PDB:5PLK}.
HELIX 251 256 {ECO:0000244|PDB:5PLK}.
STRAND 262 266 {ECO:0000244|PDB:5PLK}.
STRAND 271 274 {ECO:0000244|PDB:5PLK}.
STRAND 279 295 {ECO:0000244|PDB:5PLK}.
HELIX 300 306 {ECO:0000244|PDB:5PLK}.
STRAND 312 315 {ECO:0000244|PDB:5PLK}.
HELIX 321 328 {ECO:0000244|PDB:5PLK}.
HELIX 330 340 {ECO:0000244|PDB:5PLK}.
SEQUENCE 523 AA; 58603 MW; 5303A0846ECEBA58 CRC64;
METMKSKANC AQNPNCNIMI FHPTKEEFND FDKYIAYMES QGAHRAGLAK IIPPKEWKAR
ETYDNISEIL IATPLQQVAS GRAGVFTQYH KKKKAMTVGE YRHLANSKKY QTPPHQNFED
LERKYWKNRI YNSPIYGADI SGSLFDENTK QWNLGHLGTI QDLLEKECGV VIEGVNTPYL
YFGMWKTTFA WHTEDMDLYS INYLHLGEPK TWYVVPPEHG QRLERLAREL FPGSSRGCGA
FLRHKVALIS PTVLKENGIP FNRITQEAGE FMVTFPYGYH AGFNHGFNCA EAINFATPRW
IDYGKMASQC SCGEARVTFS MDAFVRILQP ERYDLWKRGQ DRAVVDHMEP RVPASQELST
QKEVQLPRRA ALGLRQLPSH WARHSPWPMA ARSGTRCHTL VCSSLPRRSA VSGTATQPRA
AAVHSSKKPS STPSSTPGPS AQIIHPSNGR RGRGRPPQKL RAQELTLQTP AKRPLLAGTT
CTASGPEPEP LPEDGALMDK PVPLSPGLQH PVKASGCSWA PVP


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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


 

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