KDM4D_HUMAN
ID KDM4D_HUMAN Reviewed; 523 AA.
AC Q6B0I6; B3KPC4; Q0VF39; Q9NT41; Q9NW76;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Lysine-specific demethylase 4D;
DE EC=1.14.11.66 {ECO:0000269|PubMed:16603238};
DE AltName: Full=JmjC domain-containing histone demethylation protein 3D;
DE AltName: Full=Jumonji domain-containing protein 2D;
DE AltName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase 4D {ECO:0000305};
GN Name=KDM4D; Synonyms=JHDM3D, JMJD2D;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-408.
RC TISSUE=Embryo, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-408.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 395-523.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP IDENTIFICATION.
RX PubMed=15138608;
RA Katoh M., Katoh M.;
RT "Identification and characterization of JMJD2 family genes in silico.";
RL Int. J. Oncol. 24:1623-1628(2004).
RN [7]
RP FUNCTION, AND ENZYME ACTIVITY.
RX PubMed=16603238; DOI=10.1016/j.cell.2006.03.028;
RA Whetstine J.R., Nottke A., Lan F., Huarte M., Smolikov S., Chen Z.,
RA Spooner E., Li E., Zhang G., Colaiacovo M., Shi Y.;
RT "Reversal of histone lysine trimethylation by the JMJD2 family of histone
RT demethylases.";
RL Cell 125:467-481(2006).
RN [8]
RP ADP-RIBOSYLATION AT GLU-26 AND GLU-27.
RX PubMed=23102699; DOI=10.1016/j.molcel.2012.09.021;
RA Le May N., Iltis I., Ame J.C., Zhovmer A., Biard D., Egly J.M.,
RA Schreiber V., Coin F.;
RT "Poly (ADP-ribose) glycohydrolase regulates retinoic acid receptor-mediated
RT gene expression.";
RL Mol. Cell 48:785-798(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) OF 11-340 IN COMPLEX WITH
RP INHIBITORS; ZINC AND NICKEL.
RX PubMed=26741168; DOI=10.1021/acs.jmedchem.5b01635;
RA Bavetsias V., Lanigan R.M., Ruda G.F., Atrash B., McLaughlin M.G.,
RA Tumber A., Mok N.Y., Le Bihan Y.V., Dempster S., Boxall K.J.,
RA Jeganathan F., Hatch S.B., Savitsky P., Velupillai S., Krojer T.,
RA England K.S., Sejberg J., Thai C., Donovan A., Pal A., Scozzafava G.,
RA Bennett J.M., Kawamura A., Johansson C., Szykowska A., Gileadi C.,
RA Burgess-Brown N.A., von Delft F., Oppermann U., Walters Z., Shipley J.,
RA Raynaud F.I., Westaway S.M., Prinjha R.K., Fedorov O., Burke R.,
RA Schofield C.J., Westwood I.M., Bountra C., Muller S., van Montfort R.L.,
RA Brennan P.E., Blagg J.;
RT "8-Substituted Pyrido[3,4-d]pyrimidin-4(3H)-one Derivatives As Potent, Cell
RT Permeable, KDM4 (JMJD2) and KDM5 (JARID1) Histone Lysine Demethylase
RT Inhibitors.";
RL J. Med. Chem. 59:1388-1409(2016).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of
CC histone H3, thereby playing a central role in histone code. Does not
CC demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-
CC 20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while
CC it has no activity on monomethylated residues. Demethylation of Lys
CC residue generates formaldehyde and succinate.
CC {ECO:0000269|PubMed:16603238}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-
CC COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC EC=1.14.11.66; Evidence={ECO:0000269|PubMed:16603238};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- INTERACTION:
CC Q6B0I6; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-4311651, EBI-742887;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537}.
CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91508.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK001113; BAA91508.1; ALT_INIT; mRNA.
DR EMBL; AK056162; BAG51636.1; -; mRNA.
DR EMBL; AP002383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW66952.1; -; Genomic_DNA.
DR EMBL; BC074739; AAH74739.1; -; mRNA.
DR EMBL; BC119010; AAI19011.1; -; mRNA.
DR EMBL; BC122858; AAI22859.1; -; mRNA.
DR EMBL; AL137545; CAB70803.1; -; mRNA.
DR CCDS; CCDS8302.1; -.
DR PIR; T46388; T46388.
DR RefSeq; NP_060509.2; NM_018039.2.
DR PDB; 3DXT; X-ray; 1.80 A; A=1-354.
DR PDB; 3DXU; X-ray; 2.20 A; A=11-341.
DR PDB; 4D6Q; X-ray; 1.29 A; A=1-342.
DR PDB; 4D6R; X-ray; 1.40 A; A=1-342.
DR PDB; 4D6S; X-ray; 1.40 A; A=1-342.
DR PDB; 4HON; X-ray; 1.80 A; A/B=12-341.
DR PDB; 4HOO; X-ray; 2.50 A; A/B=12-341.
DR PDB; 5F5A; X-ray; 1.41 A; A=1-342.
DR PDB; 5F5C; X-ray; 1.88 A; A=1-342.
DR PDB; 5FP4; X-ray; 2.00 A; A=11-341.
DR PDB; 5FP7; X-ray; 2.00 A; A=11-341.
DR PDB; 5FP8; X-ray; 1.98 A; A=11-341.
DR PDB; 5FP9; X-ray; 2.00 A; A=11-341.
DR PDB; 5FPA; X-ray; 1.96 A; A=11-341.
DR PDB; 5FPB; X-ray; 1.91 A; A=11-341.
DR PDB; 5PH0; X-ray; 1.34 A; A=1-342.
DR PDB; 5PH1; X-ray; 1.25 A; A=1-342.
DR PDB; 5PH2; X-ray; 1.45 A; A=1-342.
DR PDB; 5PH3; X-ray; 1.24 A; A=1-342.
DR PDB; 5PH4; X-ray; 1.27 A; A=1-342.
DR PDB; 5PH5; X-ray; 1.35 A; A=1-342.
DR PDB; 5PH6; X-ray; 1.74 A; A=1-342.
DR PDB; 5PH7; X-ray; 1.43 A; A=1-342.
DR PDB; 5PH8; X-ray; 1.40 A; A=1-342.
DR PDB; 5PH9; X-ray; 1.48 A; A=1-342.
DR PDB; 5PHA; X-ray; 1.45 A; A=1-342.
DR PDB; 5PHB; X-ray; 1.34 A; A=1-342.
DR PDB; 5PHC; X-ray; 1.29 A; A=1-342.
DR PDB; 5PHD; X-ray; 1.36 A; A=1-342.
DR PDB; 5PHE; X-ray; 1.35 A; A=1-342.
DR PDB; 5PHF; X-ray; 1.39 A; A=1-342.
DR PDB; 5PHG; X-ray; 1.40 A; A=1-342.
DR PDB; 5PHH; X-ray; 1.60 A; A=1-342.
DR PDB; 5PHI; X-ray; 1.97 A; A=1-342.
DR PDB; 5PHJ; X-ray; 1.15 A; A=1-342.
DR PDB; 5PHK; X-ray; 1.25 A; A=1-342.
DR PDB; 5PHL; X-ray; 1.14 A; A=1-342.
DR PDB; 5PHM; X-ray; 1.40 A; A=1-342.
DR PDB; 5PHN; X-ray; 1.29 A; A=1-342.
DR PDB; 5PHO; X-ray; 1.40 A; A=1-342.
DR PDB; 5PHP; X-ray; 1.72 A; A=1-342.
DR PDB; 5PHQ; X-ray; 2.23 A; A=1-342.
DR PDB; 5PHR; X-ray; 1.66 A; A=1-342.
DR PDB; 5PHS; X-ray; 2.54 A; A=1-342.
DR PDB; 5PHT; X-ray; 1.83 A; A=1-342.
DR PDB; 5PHU; X-ray; 1.79 A; A=1-342.
DR PDB; 5PHV; X-ray; 1.83 A; A=1-342.
DR PDB; 5PHW; X-ray; 1.31 A; A=1-342.
DR PDB; 5PHX; X-ray; 1.27 A; A=1-342.
DR PDB; 5PHY; X-ray; 1.34 A; A=1-342.
DR PDB; 5PHZ; X-ray; 1.47 A; A=1-342.
DR PDB; 5PI0; X-ray; 1.50 A; A=1-342.
DR PDB; 5PI1; X-ray; 1.34 A; A=1-342.
DR PDB; 5PI2; X-ray; 1.52 A; A=1-342.
DR PDB; 5PI3; X-ray; 1.29 A; A=1-342.
DR PDB; 5PI4; X-ray; 1.35 A; A=1-342.
DR PDB; 5PI5; X-ray; 1.42 A; A=1-342.
DR PDB; 5PI6; X-ray; 1.29 A; A=1-342.
DR PDB; 5PI7; X-ray; 1.61 A; A=1-342.
DR PDB; 5PI8; X-ray; 1.27 A; A=1-342.
DR PDB; 5PI9; X-ray; 1.45 A; A=1-342.
DR PDB; 5PIA; X-ray; 1.18 A; A=1-342.
DR PDB; 5PIB; X-ray; 1.64 A; A=1-342.
DR PDB; 5PIC; X-ray; 1.29 A; A=1-342.
DR PDB; 5PID; X-ray; 1.50 A; A=1-342.
DR PDB; 5PIE; X-ray; 1.42 A; A=1-342.
DR PDB; 5PIF; X-ray; 1.37 A; A=1-342.
DR PDB; 5PIG; X-ray; 1.44 A; A=1-342.
DR PDB; 5PIH; X-ray; 1.79 A; A=1-342.
DR PDB; 5PII; X-ray; 1.45 A; A=1-342.
DR PDB; 5PIJ; X-ray; 1.45 A; A=1-342.
DR PDB; 5PIK; X-ray; 1.80 A; A=1-342.
DR PDB; 5PIL; X-ray; 1.65 A; A=1-342.
DR PDB; 5PIM; X-ray; 1.25 A; A=1-342.
DR PDB; 5PIN; X-ray; 1.50 A; A=1-342.
DR PDB; 5PIO; X-ray; 1.72 A; A=1-342.
DR PDB; 5PIP; X-ray; 1.42 A; A=1-342.
DR PDB; 5PIQ; X-ray; 1.50 A; A=1-342.
DR PDB; 5PIR; X-ray; 1.45 A; A=1-342.
DR PDB; 5PIS; X-ray; 1.30 A; A=1-342.
DR PDB; 5PIT; X-ray; 1.79 A; A=1-342.
DR PDB; 5PIU; X-ray; 1.48 A; A=1-342.
DR PDB; 5PIV; X-ray; 1.43 A; A=1-342.
DR PDB; 5PIW; X-ray; 1.23 A; A=1-342.
DR PDB; 5PIX; X-ray; 1.35 A; A=1-342.
DR PDB; 5PIY; X-ray; 1.31 A; A=1-342.
DR PDB; 5PIZ; X-ray; 1.38 A; A=1-342.
DR PDB; 5PJ0; X-ray; 1.31 A; A=1-342.
DR PDB; 5PJ1; X-ray; 1.35 A; A=1-342.
DR PDB; 5PJ2; X-ray; 1.44 A; A=1-342.
DR PDB; 5PJ3; X-ray; 1.30 A; A=1-342.
DR PDB; 5PJ4; X-ray; 1.52 A; A=1-342.
DR PDB; 5PJ5; X-ray; 1.24 A; A=1-342.
DR PDB; 5PJ6; X-ray; 1.35 A; A=1-342.
DR PDB; 5PJ7; X-ray; 1.39 A; A=1-342.
DR PDB; 5PJ8; X-ray; 1.40 A; A=1-342.
DR PDB; 5PJ9; X-ray; 1.50 A; A=1-342.
DR PDB; 5PJA; X-ray; 1.89 A; A=1-342.
DR PDB; 5PJB; X-ray; 1.58 A; A=1-342.
DR PDB; 5PJC; X-ray; 1.40 A; A=1-342.
DR PDB; 5PJD; X-ray; 1.43 A; A=1-342.
DR PDB; 5PJE; X-ray; 1.37 A; A=1-342.
DR PDB; 5PJF; X-ray; 1.47 A; A=1-342.
DR PDB; 5PJG; X-ray; 1.40 A; A=1-342.
DR PDB; 5PJH; X-ray; 1.18 A; A=1-342.
DR PDB; 5PJI; X-ray; 1.34 A; A=1-342.
DR PDB; 5PJJ; X-ray; 1.67 A; A=1-342.
DR PDB; 5PJK; X-ray; 1.69 A; A=1-342.
DR PDB; 5PJL; X-ray; 1.52 A; A=1-342.
DR PDB; 5PJM; X-ray; 1.43 A; A=1-342.
DR PDB; 5PJN; X-ray; 1.48 A; A=1-342.
DR PDB; 5PJO; X-ray; 1.35 A; A=1-342.
DR PDB; 5PJP; X-ray; 1.39 A; A=1-342.
DR PDB; 5PJQ; X-ray; 1.38 A; A=1-342.
DR PDB; 5PJR; X-ray; 1.29 A; A=1-342.
DR PDB; 5PJS; X-ray; 1.64 A; A=1-342.
DR PDB; 5PJT; X-ray; 1.54 A; A=1-342.
DR PDB; 5PJU; X-ray; 1.27 A; A=1-342.
DR PDB; 5PJV; X-ray; 1.34 A; A=1-342.
DR PDB; 5PJW; X-ray; 1.56 A; A=1-342.
DR PDB; 5PJX; X-ray; 1.35 A; A=1-342.
DR PDB; 5PJY; X-ray; 1.34 A; A=1-342.
DR PDB; 5PJZ; X-ray; 1.29 A; A=1-342.
DR PDB; 5PK0; X-ray; 1.28 A; A=1-342.
DR PDB; 5PK1; X-ray; 1.35 A; A=1-342.
DR PDB; 5PK2; X-ray; 1.42 A; A=1-342.
DR PDB; 5PK3; X-ray; 1.42 A; A=1-342.
DR PDB; 5PK4; X-ray; 1.72 A; A=1-342.
DR PDB; 5PK5; X-ray; 1.39 A; A=1-342.
DR PDB; 5PK6; X-ray; 2.38 A; A=1-342.
DR PDB; 5PK7; X-ray; 1.29 A; A=1-342.
DR PDB; 5PK8; X-ray; 1.44 A; A=1-342.
DR PDB; 5PK9; X-ray; 1.34 A; A=1-342.
DR PDB; 5PKA; X-ray; 1.71 A; A=1-342.
DR PDB; 5PKB; X-ray; 1.40 A; A=1-342.
DR PDB; 5PKC; X-ray; 1.29 A; A=1-342.
DR PDB; 5PKD; X-ray; 1.55 A; A=1-342.
DR PDB; 5PKE; X-ray; 1.44 A; A=1-342.
DR PDB; 5PKF; X-ray; 1.34 A; A=1-342.
DR PDB; 5PKG; X-ray; 1.54 A; A=1-342.
DR PDB; 5PKH; X-ray; 1.19 A; A=1-342.
DR PDB; 5PKI; X-ray; 1.19 A; A=1-342.
DR PDB; 5PKJ; X-ray; 1.22 A; A=1-342.
DR PDB; 5PKK; X-ray; 1.50 A; A=1-342.
DR PDB; 5PKL; X-ray; 1.35 A; A=1-342.
DR PDB; 5PKM; X-ray; 1.37 A; A=1-342.
DR PDB; 5PKN; X-ray; 1.30 A; A=1-342.
DR PDB; 5PKO; X-ray; 2.38 A; A=1-342.
DR PDB; 5PKP; X-ray; 1.30 A; A=1-342.
DR PDB; 5PKQ; X-ray; 1.28 A; A=1-342.
DR PDB; 5PKR; X-ray; 1.31 A; A=1-342.
DR PDB; 5PKS; X-ray; 1.50 A; A=1-342.
DR PDB; 5PKT; X-ray; 1.50 A; A=1-342.
DR PDB; 5PKU; X-ray; 1.47 A; A=1-342.
DR PDB; 5PKV; X-ray; 1.35 A; A=1-342.
DR PDB; 5PKW; X-ray; 1.35 A; A=1-342.
DR PDB; 5PKX; X-ray; 1.45 A; A=1-342.
DR PDB; 5PKY; X-ray; 1.25 A; A=1-342.
DR PDB; 5PKZ; X-ray; 1.50 A; A=1-342.
DR PDB; 5PL0; X-ray; 1.27 A; A=1-342.
DR PDB; 5PL1; X-ray; 1.42 A; A=1-342.
DR PDB; 5PL2; X-ray; 1.34 A; A=1-342.
DR PDB; 5PL3; X-ray; 1.27 A; A=1-342.
DR PDB; 5PL4; X-ray; 1.21 A; A=1-342.
DR PDB; 5PL5; X-ray; 1.57 A; A=1-342.
DR PDB; 5PL6; X-ray; 1.29 A; A=1-342.
DR PDB; 5PL7; X-ray; 1.30 A; A=1-342.
DR PDB; 5PL8; X-ray; 1.54 A; A=1-342.
DR PDB; 5PL9; X-ray; 1.65 A; A=1-342.
DR PDB; 5PLA; X-ray; 1.37 A; A=1-342.
DR PDB; 5PLB; X-ray; 1.49 A; A=1-342.
DR PDB; 5PLC; X-ray; 1.49 A; A=1-342.
DR PDB; 5PLD; X-ray; 1.46 A; A=1-342.
DR PDB; 5PLE; X-ray; 1.45 A; A=1-342.
DR PDB; 5PLF; X-ray; 1.33 A; A=1-342.
DR PDB; 5PLG; X-ray; 1.31 A; A=1-342.
DR PDB; 5PLH; X-ray; 1.46 A; A=1-342.
DR PDB; 5PLI; X-ray; 1.39 A; A=1-342.
DR PDB; 5PLJ; X-ray; 1.49 A; A=1-342.
DR PDB; 5PLK; X-ray; 1.14 A; A=1-342.
DR PDB; 5PLL; X-ray; 1.28 A; A=1-342.
DR PDB; 5PLM; X-ray; 1.14 A; A=1-342.
DR PDB; 5PLN; X-ray; 1.14 A; A=1-342.
DR PDB; 5PLO; X-ray; 1.14 A; A=1-342.
DR PDB; 5PLP; X-ray; 1.46 A; A=1-342.
DR PDB; 5PLQ; X-ray; 1.36 A; A=1-342.
DR PDB; 5PLR; X-ray; 1.53 A; A=1-342.
DR PDB; 5PLS; X-ray; 1.70 A; A=1-342.
DR PDB; 5PLT; X-ray; 1.53 A; A=1-342.
DR PDB; 5PLU; X-ray; 1.47 A; A=1-342.
DR PDB; 5PLV; X-ray; 1.14 A; A=1-342.
DR PDB; 5PLW; X-ray; 1.31 A; A=1-342.
DR PDB; 5PLX; X-ray; 1.29 A; A=1-342.
DR PDB; 5PLY; X-ray; 1.38 A; A=1-342.
DR PDB; 5PLZ; X-ray; 1.71 A; A=1-342.
DR PDB; 5PM0; X-ray; 2.14 A; A=1-342.
DR PDB; 5PM1; X-ray; 1.54 A; A=1-342.
DR PDB; 5PM2; X-ray; 1.52 A; A=1-342.
DR PDB; 5PM3; X-ray; 1.46 A; A=1-342.
DR PDB; 5PM4; X-ray; 1.44 A; A=1-342.
DR PDB; 5PM5; X-ray; 1.76 A; A=1-342.
DR PDB; 5PM6; X-ray; 1.78 A; A=1-342.
DR PDB; 5PM7; X-ray; 1.43 A; A=1-342.
DR PDB; 5PM8; X-ray; 1.54 A; A=1-342.
DR PDB; 5PM9; X-ray; 1.50 A; A=1-342.
DR PDB; 5PMA; X-ray; 1.29 A; A=1-342.
DR PDB; 5PMB; X-ray; 1.63 A; A=1-342.
DR PDB; 5PMC; X-ray; 1.58 A; A=1-342.
DR PDB; 5PMD; X-ray; 1.63 A; A=1-342.
DR PDB; 5PME; X-ray; 1.39 A; A=1-342.
DR PDB; 5PMF; X-ray; 1.36 A; A=1-342.
DR PDB; 5PMG; X-ray; 1.51 A; A=1-342.
DR PDB; 5PMH; X-ray; 1.52 A; A=1-342.
DR PDB; 5PMI; X-ray; 1.71 A; A=1-342.
DR PDB; 5PMJ; X-ray; 1.37 A; A=1-342.
DR PDB; 5PMK; X-ray; 1.44 A; A=1-342.
DR PDB; 5PML; X-ray; 1.58 A; A=1-342.
DR PDB; 5PMM; X-ray; 1.39 A; A=1-342.
DR PDB; 5PMN; X-ray; 1.72 A; A=1-342.
DR PDB; 5PMO; X-ray; 1.53 A; A=1-342.
DR PDB; 5PMP; X-ray; 1.55 A; A=1-342.
DR PDB; 5PMQ; X-ray; 1.46 A; A=1-342.
DR PDB; 5PMR; X-ray; 1.51 A; A=1-342.
DR PDB; 5PMS; X-ray; 1.24 A; A=1-342.
DR PDB; 5PMT; X-ray; 1.22 A; A=1-342.
DR PDB; 5PMU; X-ray; 1.48 A; A=1-342.
DR PDB; 5PMV; X-ray; 1.34 A; A=1-342.
DR PDB; 5PMW; X-ray; 1.19 A; A=1-342.
DR PDB; 5PMX; X-ray; 1.14 A; A=1-342.
DR PDB; 5PMY; X-ray; 1.29 A; A=1-342.
DR PDB; 5PMZ; X-ray; 1.15 A; A=1-342.
DR PDB; 5PN0; X-ray; 1.14 A; A=1-342.
DR PDB; 5PN1; X-ray; 1.41 A; A=1-342.
DR PDB; 5PN2; X-ray; 1.41 A; A=1-342.
DR PDB; 5PN3; X-ray; 1.60 A; A=1-342.
DR PDB; 5PN4; X-ray; 1.37 A; A=1-342.
DR PDB; 5PN5; X-ray; 1.30 A; A=1-342.
DR PDB; 5PN6; X-ray; 1.42 A; A=1-342.
DR PDB; 5PN7; X-ray; 1.25 A; A=1-342.
DR PDB; 5PN8; X-ray; 1.34 A; A=1-342.
DR PDB; 5PN9; X-ray; 1.48 A; A=1-342.
DR PDB; 5PNA; X-ray; 1.78 A; A=1-342.
DR PDB; 5PNB; X-ray; 1.23 A; A=1-342.
DR PDB; 5PNC; X-ray; 1.35 A; A=1-342.
DR PDB; 5PND; X-ray; 1.49 A; A=1-342.
DR PDB; 5PNE; X-ray; 1.29 A; A=1-342.
DR PDB; 5PNF; X-ray; 1.24 A; A=1-342.
DR PDB; 5PNG; X-ray; 1.38 A; A=1-342.
DR PDB; 5PNH; X-ray; 1.14 A; A=1-342.
DR PDB; 5PNI; X-ray; 1.45 A; A=1-342.
DR PDB; 5PNJ; X-ray; 1.40 A; A=1-342.
DR PDB; 5PNK; X-ray; 1.27 A; A=1-342.
DR PDB; 5PNL; X-ray; 1.44 A; A=1-342.
DR PDB; 5PNM; X-ray; 1.25 A; A=1-342.
DR PDB; 5PNN; X-ray; 1.21 A; A=1-342.
DR PDB; 5PNO; X-ray; 1.55 A; A=1-342.
DR PDB; 5PNP; X-ray; 1.47 A; A=1-342.
DR PDB; 5PNQ; X-ray; 1.47 A; A=1-342.
DR PDB; 5PNR; X-ray; 1.14 A; A=1-342.
DR PDB; 5PNS; X-ray; 1.36 A; A=1-342.
DR PDB; 5PNU; X-ray; 1.14 A; A=1-342.
DR PDB; 5PNV; X-ray; 1.60 A; A=1-342.
DR PDB; 5PNW; X-ray; 1.40 A; A=1-342.
DR PDB; 6ETE; X-ray; 1.47 A; A=1-342.
DR PDB; 6ETG; X-ray; 1.28 A; A=1-342.
DR PDB; 6ETS; X-ray; 1.33 A; A=1-341.
DR PDB; 6ETT; X-ray; 1.26 A; A=1-342.
DR PDB; 6ETU; X-ray; 1.33 A; A=1-342.
DR PDB; 6ETV; X-ray; 1.18 A; A=1-342.
DR PDB; 6ETW; X-ray; 1.35 A; A=1-342.
DR PDB; 6F5Q; X-ray; 1.43 A; A=1-342.
DR PDB; 6F5R; X-ray; 1.61 A; A=11-337.
DR PDB; 6F5S; X-ray; 1.48 A; A=1-342.
DR PDB; 6F5T; X-ray; 1.58 A; A=11-340.
DR PDB; 6H0W; X-ray; 1.23 A; A=1-342.
DR PDB; 6H0X; X-ray; 1.64 A; A=1-342.
DR PDB; 6H0Y; X-ray; 1.21 A; A=1-342.
DR PDB; 6H0Z; X-ray; 1.34 A; A=1-342.
DR PDB; 6H10; X-ray; 1.10 A; A=1-342.
DR PDB; 6H11; X-ray; 1.52 A; A=1-342.
DR PDB; 7DYG; X-ray; 2.00 A; A=11-340.
DR PDB; 7DYQ; X-ray; 2.00 A; A=11-340.
DR PDBsum; 3DXT; -.
DR PDBsum; 3DXU; -.
DR PDBsum; 4D6Q; -.
DR PDBsum; 4D6R; -.
DR PDBsum; 4D6S; -.
DR PDBsum; 4HON; -.
DR PDBsum; 4HOO; -.
DR PDBsum; 5F5A; -.
DR PDBsum; 5F5C; -.
DR PDBsum; 5FP4; -.
DR PDBsum; 5FP7; -.
DR PDBsum; 5FP8; -.
DR PDBsum; 5FP9; -.
DR PDBsum; 5FPA; -.
DR PDBsum; 5FPB; -.
DR PDBsum; 5PH0; -.
DR PDBsum; 5PH1; -.
DR PDBsum; 5PH2; -.
DR PDBsum; 5PH3; -.
DR PDBsum; 5PH4; -.
DR PDBsum; 5PH5; -.
DR PDBsum; 5PH6; -.
DR PDBsum; 5PH7; -.
DR PDBsum; 5PH8; -.
DR PDBsum; 5PH9; -.
DR PDBsum; 5PHA; -.
DR PDBsum; 5PHB; -.
DR PDBsum; 5PHC; -.
DR PDBsum; 5PHD; -.
DR PDBsum; 5PHE; -.
DR PDBsum; 5PHF; -.
DR PDBsum; 5PHG; -.
DR PDBsum; 5PHH; -.
DR PDBsum; 5PHI; -.
DR PDBsum; 5PHJ; -.
DR PDBsum; 5PHK; -.
DR PDBsum; 5PHL; -.
DR PDBsum; 5PHM; -.
DR PDBsum; 5PHN; -.
DR PDBsum; 5PHO; -.
DR PDBsum; 5PHP; -.
DR PDBsum; 5PHQ; -.
DR PDBsum; 5PHR; -.
DR PDBsum; 5PHS; -.
DR PDBsum; 5PHT; -.
DR PDBsum; 5PHU; -.
DR PDBsum; 5PHV; -.
DR PDBsum; 5PHW; -.
DR PDBsum; 5PHX; -.
DR PDBsum; 5PHY; -.
DR PDBsum; 5PHZ; -.
DR PDBsum; 5PI0; -.
DR PDBsum; 5PI1; -.
DR PDBsum; 5PI2; -.
DR PDBsum; 5PI3; -.
DR PDBsum; 5PI4; -.
DR PDBsum; 5PI5; -.
DR PDBsum; 5PI6; -.
DR PDBsum; 5PI7; -.
DR PDBsum; 5PI8; -.
DR PDBsum; 5PI9; -.
DR PDBsum; 5PIA; -.
DR PDBsum; 5PIB; -.
DR PDBsum; 5PIC; -.
DR PDBsum; 5PID; -.
DR PDBsum; 5PIE; -.
DR PDBsum; 5PIF; -.
DR PDBsum; 5PIG; -.
DR PDBsum; 5PIH; -.
DR PDBsum; 5PII; -.
DR PDBsum; 5PIJ; -.
DR PDBsum; 5PIK; -.
DR PDBsum; 5PIL; -.
DR PDBsum; 5PIM; -.
DR PDBsum; 5PIN; -.
DR PDBsum; 5PIO; -.
DR PDBsum; 5PIP; -.
DR PDBsum; 5PIQ; -.
DR PDBsum; 5PIR; -.
DR PDBsum; 5PIS; -.
DR PDBsum; 5PIT; -.
DR PDBsum; 5PIU; -.
DR PDBsum; 5PIV; -.
DR PDBsum; 5PIW; -.
DR PDBsum; 5PIX; -.
DR PDBsum; 5PIY; -.
DR PDBsum; 5PIZ; -.
DR PDBsum; 5PJ0; -.
DR PDBsum; 5PJ1; -.
DR PDBsum; 5PJ2; -.
DR PDBsum; 5PJ3; -.
DR PDBsum; 5PJ4; -.
DR PDBsum; 5PJ5; -.
DR PDBsum; 5PJ6; -.
DR PDBsum; 5PJ7; -.
DR PDBsum; 5PJ8; -.
DR PDBsum; 5PJ9; -.
DR PDBsum; 5PJA; -.
DR PDBsum; 5PJB; -.
DR PDBsum; 5PJC; -.
DR PDBsum; 5PJD; -.
DR PDBsum; 5PJE; -.
DR PDBsum; 5PJF; -.
DR PDBsum; 5PJG; -.
DR PDBsum; 5PJH; -.
DR PDBsum; 5PJI; -.
DR PDBsum; 5PJJ; -.
DR PDBsum; 5PJK; -.
DR PDBsum; 5PJL; -.
DR PDBsum; 5PJM; -.
DR PDBsum; 5PJN; -.
DR PDBsum; 5PJO; -.
DR PDBsum; 5PJP; -.
DR PDBsum; 5PJQ; -.
DR PDBsum; 5PJR; -.
DR PDBsum; 5PJS; -.
DR PDBsum; 5PJT; -.
DR PDBsum; 5PJU; -.
DR PDBsum; 5PJV; -.
DR PDBsum; 5PJW; -.
DR PDBsum; 5PJX; -.
DR PDBsum; 5PJY; -.
DR PDBsum; 5PJZ; -.
DR PDBsum; 5PK0; -.
DR PDBsum; 5PK1; -.
DR PDBsum; 5PK2; -.
DR PDBsum; 5PK3; -.
DR PDBsum; 5PK4; -.
DR PDBsum; 5PK5; -.
DR PDBsum; 5PK6; -.
DR PDBsum; 5PK7; -.
DR PDBsum; 5PK8; -.
DR PDBsum; 5PK9; -.
DR PDBsum; 5PKA; -.
DR PDBsum; 5PKB; -.
DR PDBsum; 5PKC; -.
DR PDBsum; 5PKD; -.
DR PDBsum; 5PKE; -.
DR PDBsum; 5PKF; -.
DR PDBsum; 5PKG; -.
DR PDBsum; 5PKH; -.
DR PDBsum; 5PKI; -.
DR PDBsum; 5PKJ; -.
DR PDBsum; 5PKK; -.
DR PDBsum; 5PKL; -.
DR PDBsum; 5PKM; -.
DR PDBsum; 5PKN; -.
DR PDBsum; 5PKO; -.
DR PDBsum; 5PKP; -.
DR PDBsum; 5PKQ; -.
DR PDBsum; 5PKR; -.
DR PDBsum; 5PKS; -.
DR PDBsum; 5PKT; -.
DR PDBsum; 5PKU; -.
DR PDBsum; 5PKV; -.
DR PDBsum; 5PKW; -.
DR PDBsum; 5PKX; -.
DR PDBsum; 5PKY; -.
DR PDBsum; 5PKZ; -.
DR PDBsum; 5PL0; -.
DR PDBsum; 5PL1; -.
DR PDBsum; 5PL2; -.
DR PDBsum; 5PL3; -.
DR PDBsum; 5PL4; -.
DR PDBsum; 5PL5; -.
DR PDBsum; 5PL6; -.
DR PDBsum; 5PL7; -.
DR PDBsum; 5PL8; -.
DR PDBsum; 5PL9; -.
DR PDBsum; 5PLA; -.
DR PDBsum; 5PLB; -.
DR PDBsum; 5PLC; -.
DR PDBsum; 5PLD; -.
DR PDBsum; 5PLE; -.
DR PDBsum; 5PLF; -.
DR PDBsum; 5PLG; -.
DR PDBsum; 5PLH; -.
DR PDBsum; 5PLI; -.
DR PDBsum; 5PLJ; -.
DR PDBsum; 5PLK; -.
DR PDBsum; 5PLL; -.
DR PDBsum; 5PLM; -.
DR PDBsum; 5PLN; -.
DR PDBsum; 5PLO; -.
DR PDBsum; 5PLP; -.
DR PDBsum; 5PLQ; -.
DR PDBsum; 5PLR; -.
DR PDBsum; 5PLS; -.
DR PDBsum; 5PLT; -.
DR PDBsum; 5PLU; -.
DR PDBsum; 5PLV; -.
DR PDBsum; 5PLW; -.
DR PDBsum; 5PLX; -.
DR PDBsum; 5PLY; -.
DR PDBsum; 5PLZ; -.
DR PDBsum; 5PM0; -.
DR PDBsum; 5PM1; -.
DR PDBsum; 5PM2; -.
DR PDBsum; 5PM3; -.
DR PDBsum; 5PM4; -.
DR PDBsum; 5PM5; -.
DR PDBsum; 5PM6; -.
DR PDBsum; 5PM7; -.
DR PDBsum; 5PM8; -.
DR PDBsum; 5PM9; -.
DR PDBsum; 5PMA; -.
DR PDBsum; 5PMB; -.
DR PDBsum; 5PMC; -.
DR PDBsum; 5PMD; -.
DR PDBsum; 5PME; -.
DR PDBsum; 5PMF; -.
DR PDBsum; 5PMG; -.
DR PDBsum; 5PMH; -.
DR PDBsum; 5PMI; -.
DR PDBsum; 5PMJ; -.
DR PDBsum; 5PMK; -.
DR PDBsum; 5PML; -.
DR PDBsum; 5PMM; -.
DR PDBsum; 5PMN; -.
DR PDBsum; 5PMO; -.
DR PDBsum; 5PMP; -.
DR PDBsum; 5PMQ; -.
DR PDBsum; 5PMR; -.
DR PDBsum; 5PMS; -.
DR PDBsum; 5PMT; -.
DR PDBsum; 5PMU; -.
DR PDBsum; 5PMV; -.
DR PDBsum; 5PMW; -.
DR PDBsum; 5PMX; -.
DR PDBsum; 5PMY; -.
DR PDBsum; 5PMZ; -.
DR PDBsum; 5PN0; -.
DR PDBsum; 5PN1; -.
DR PDBsum; 5PN2; -.
DR PDBsum; 5PN3; -.
DR PDBsum; 5PN4; -.
DR PDBsum; 5PN5; -.
DR PDBsum; 5PN6; -.
DR PDBsum; 5PN7; -.
DR PDBsum; 5PN8; -.
DR PDBsum; 5PN9; -.
DR PDBsum; 5PNA; -.
DR PDBsum; 5PNB; -.
DR PDBsum; 5PNC; -.
DR PDBsum; 5PND; -.
DR PDBsum; 5PNE; -.
DR PDBsum; 5PNF; -.
DR PDBsum; 5PNG; -.
DR PDBsum; 5PNH; -.
DR PDBsum; 5PNI; -.
DR PDBsum; 5PNJ; -.
DR PDBsum; 5PNK; -.
DR PDBsum; 5PNL; -.
DR PDBsum; 5PNM; -.
DR PDBsum; 5PNN; -.
DR PDBsum; 5PNO; -.
DR PDBsum; 5PNP; -.
DR PDBsum; 5PNQ; -.
DR PDBsum; 5PNR; -.
DR PDBsum; 5PNS; -.
DR PDBsum; 5PNU; -.
DR PDBsum; 5PNV; -.
DR PDBsum; 5PNW; -.
DR PDBsum; 6ETE; -.
DR PDBsum; 6ETG; -.
DR PDBsum; 6ETS; -.
DR PDBsum; 6ETT; -.
DR PDBsum; 6ETU; -.
DR PDBsum; 6ETV; -.
DR PDBsum; 6ETW; -.
DR PDBsum; 6F5Q; -.
DR PDBsum; 6F5R; -.
DR PDBsum; 6F5S; -.
DR PDBsum; 6F5T; -.
DR PDBsum; 6H0W; -.
DR PDBsum; 6H0X; -.
DR PDBsum; 6H0Y; -.
DR PDBsum; 6H0Z; -.
DR PDBsum; 6H10; -.
DR PDBsum; 6H11; -.
DR PDBsum; 7DYG; -.
DR PDBsum; 7DYQ; -.
DR AlphaFoldDB; Q6B0I6; -.
DR SMR; Q6B0I6; -.
DR BioGRID; 120819; 41.
DR DIP; DIP-29606N; -.
DR IntAct; Q6B0I6; 37.
DR MINT; Q6B0I6; -.
DR STRING; 9606.ENSP00000334181; -.
DR BindingDB; Q6B0I6; -.
DR ChEMBL; CHEMBL6138; -.
DR iPTMnet; Q6B0I6; -.
DR PhosphoSitePlus; Q6B0I6; -.
DR BioMuta; KDM4D; -.
DR DMDM; 239938885; -.
DR MassIVE; Q6B0I6; -.
DR PaxDb; Q6B0I6; -.
DR PeptideAtlas; Q6B0I6; -.
DR PRIDE; Q6B0I6; -.
DR ProteomicsDB; 66206; -.
DR ABCD; Q6B0I6; 2 sequenced antibodies.
DR Antibodypedia; 17907; 250 antibodies from 32 providers.
DR DNASU; 55693; -.
DR Ensembl; ENST00000335080.6; ENSP00000334181.5; ENSG00000186280.7.
DR Ensembl; ENST00000536741.1; ENSP00000460897.1; ENSG00000186280.7.
DR Ensembl; ENST00000610872.1; ENSP00000482224.1; ENSG00000186280.7.
DR GeneID; 55693; -.
DR KEGG; hsa:55693; -.
DR MANE-Select; ENST00000335080.6; ENSP00000334181.5; NM_018039.3; NP_060509.2.
DR UCSC; uc001pfe.4; human.
DR CTD; 55693; -.
DR DisGeNET; 55693; -.
DR GeneCards; KDM4D; -.
DR HGNC; HGNC:25498; KDM4D.
DR HPA; ENSG00000186280; Tissue enriched (testis).
DR MIM; 609766; gene.
DR neXtProt; NX_Q6B0I6; -.
DR OpenTargets; ENSG00000186280; -.
DR PharmGKB; PA164721552; -.
DR VEuPathDB; HostDB:ENSG00000186280; -.
DR eggNOG; KOG0958; Eukaryota.
DR GeneTree; ENSGT00940000162152; -.
DR HOGENOM; CLU_001442_6_1_1; -.
DR InParanoid; Q6B0I6; -.
DR OMA; RASICKC; -.
DR OrthoDB; 1186832at2759; -.
DR PhylomeDB; Q6B0I6; -.
DR TreeFam; TF106449; -.
DR BioCyc; MetaCyc:MON66-43295; -.
DR BRENDA; 1.14.11.27; 2681.
DR BRENDA; 1.14.11.66; 2681.
DR PathwayCommons; Q6B0I6; -.
DR Reactome; R-HSA-3214842; HDMs demethylate histones.
DR SignaLink; Q6B0I6; -.
DR BioGRID-ORCS; 55693; 8 hits in 1080 CRISPR screens.
DR ChiTaRS; KDM4D; human.
DR EvolutionaryTrace; Q6B0I6; -.
DR GeneWiki; JMJD2D; -.
DR GenomeRNAi; 55693; -.
DR Pharos; Q6B0I6; Tchem.
DR PRO; PR:Q6B0I6; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6B0I6; protein.
DR Bgee; ENSG00000186280; Expressed in buccal mucosa cell and 122 other tissues.
DR Genevisible; Q6B0I6; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IDA:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
DR GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; IDA:UniProtKB.
DR GO; GO:0140684; F:histone H3-tri/dimethyl-lysine-9 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IMP:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:MGI.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IDA:UniProtKB.
DR GO; GO:1900113; P:negative regulation of histone H3-K9 trimethylation; IEA:Ensembl.
DR GO; GO:0035563; P:positive regulation of chromatin binding; IMP:MGI.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IMP:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:MGI.
DR IDEAL; IID00481; -.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Chromatin regulator; Dioxygenase; Iron;
KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..523
FT /note="Lysine-specific demethylase 4D"
FT /id="PRO_0000234376"
FT DOMAIN 18..60
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 146..312
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 407..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:B2RXH2"
FT BINDING 192
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538,
FT ECO:0000305|PubMed:26741168"
FT BINDING 194
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538,
FT ECO:0000305|PubMed:26741168"
FT BINDING 202
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:B2RXH2"
FT BINDING 210
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:B2RXH2"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:5F5A, ECO:0007744|PDB:5F5C"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:5F5A, ECO:0007744|PDB:5F5C"
FT BINDING 245
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:B2RXH2"
FT BINDING 280
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538,
FT ECO:0000305|PubMed:26741168"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:5F5A, ECO:0007744|PDB:5F5C"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:5F5A, ECO:0007744|PDB:5F5C"
FT MOD_RES 26
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000269|PubMed:23102699"
FT MOD_RES 27
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000269|PubMed:23102699"
FT VARIANT 355
FT /note="S -> R (in dbSNP:rs35631512)"
FT /id="VAR_057882"
FT VARIANT 408
FT /note="R -> Q (in dbSNP:rs3740853)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_026225"
FT VARIANT 471
FT /note="A -> S (in dbSNP:rs34366036)"
FT /id="VAR_057883"
FT CONFLICT 510
FT /note="H -> R (in Ref. 4; AAH74739)"
FT /evidence="ECO:0000305"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:6H10"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:6H10"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:6H10"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:6H10"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:6H10"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:6H10"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:5PIW"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:6H10"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:6H10"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:6H10"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:6H10"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:6H10"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:6H10"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:6H10"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:6H10"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:5PK6"
FT HELIX 160..168
FT /evidence="ECO:0007829|PDB:6H10"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:4HON"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:6H10"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:6H10"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:6H10"
FT STRAND 199..208
FT /evidence="ECO:0007829|PDB:6H10"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:6H10"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:6H10"
FT HELIX 220..230
FT /evidence="ECO:0007829|PDB:6H10"
FT HELIX 232..237
FT /evidence="ECO:0007829|PDB:6H10"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:6H10"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:6H10"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:6H10"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:6H10"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:6H10"
FT STRAND 279..295
FT /evidence="ECO:0007829|PDB:6H10"
FT HELIX 300..306
FT /evidence="ECO:0007829|PDB:6H10"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:6H10"
FT HELIX 321..328
FT /evidence="ECO:0007829|PDB:6H10"
FT HELIX 330..339
FT /evidence="ECO:0007829|PDB:6H10"
SQ 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
