ID KDM7A_HUMAN Reviewed; 941 AA.
AC Q6ZMT4; A4D1S9; C9JJH9; C9JQU2; Q6MZL8; Q9C0E5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 24-JAN-2024, entry version 155.
DE RecName: Full=Lysine-specific demethylase 7A;
DE AltName: Full=JmjC domain-containing histone demethylation protein 1D;
DE AltName: Full=Lysine-specific demethylase 7;
DE AltName: Full=[histone H3]-dimethyl-L-lysine9 demethylase 7A;
DE EC=1.14.11.65 {ECO:0000269|PubMed:20023638, ECO:0000269|PubMed:20622853};
GN Name=KDM7A; Synonyms=JHDM1D, KDM7, KIAA1718;
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] (ISOFORM 1).
RC TISSUE=Trachea;
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=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 565-941 (ISOFORM 1), AND VARIANT
RP SER-644.
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 407-941 (ISOFORM 2).
RC TISSUE=Fetal kidney;
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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20622853; DOI=10.1038/nature09261;
RA Qi H.H., Sarkissian M., Hu G.Q., Wang Z., Bhattacharjee A., Gordon D.B.,
RA Gonzales M., Lan F., Ongusaha P.P., Huarte M., Yaghi N.K., Lim H.,
RA Garcia B.A., Brizuela L., Zhao K., Roberts T.M., Shi Y.;
RT "Histone H4K20/H3K9 demethylase PHF8 regulates zebrafish brain and
RT craniofacial development.";
RL Nature 466:503-507(2010).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-488 IN COMPLEX WITH IRON AND
RP N-OXALYLGLYCINE, ZINC-BINDING, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND DOMAIN LINKER AND PHD-FINGER.
RX PubMed=20023638; DOI=10.1038/nsmb.1753;
RA Horton J.R., Upadhyay A.K., Qi H.H., Zhang X., Shi Y., Cheng X.;
RT "Enzymatic and structural insights for substrate specificity of a family of
RT jumonji histone lysine demethylases.";
RL Nat. Struct. Mol. Biol. 17:38-43(2010).
CC -!- FUNCTION: Histone demethylase required for brain development.
CC Specifically demethylates dimethylated 'Lys-9', 'Lys-27' and 'Lys-36'
CC (H3K9me2, H3K27me2, H3K36me2, respectively) of histone H3 and
CC monomethylated histone H4 'Lys-20' residue (H4K20Me1), thereby playing
CC a central role in histone code (PubMed:20023638, PubMed:20622853).
CC Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3),
CC affecting histone demethylase specificity: in presence of H3K4me3, it
CC has no demethylase activity toward H3K9me2, while it has high activity
CC toward H3K27me2. Demethylates H3K9me2 in absence of H3K4me3
CC (PubMed:20023638). Has activity toward H4K20Me1 only when nucleosome is
CC used as a substrate and when not histone octamer is used as substrate
CC (PubMed:20622853). {ECO:0000269|PubMed:20023638,
CC ECO:0000269|PubMed:20622853}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(9)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:60188, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.65;
CC Evidence={ECO:0000269|PubMed:20023638, ECO:0000269|PubMed:20622853};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60189;
CC Evidence={ECO:0000305|PubMed:20023638, ECO:0000305|PubMed:20622853};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(27)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(27)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:67800, Rhea:RHEA-COMP:15539, Rhea:RHEA-
CC COMP:15548, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:20023638};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67801;
CC Evidence={ECO:0000305|PubMed:20023638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] +
CC O2 = CO2 + formaldehyde + N(6)-methyl-L-lysyl(36)-[histone H3] +
CC succinate; Xref=Rhea:RHEA:21788, Rhea:RHEA-COMP:9786, Rhea:RHEA-
CC COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929,
CC ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:20023638,
CC ECO:0000269|PubMed:20622853};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21789;
CC Evidence={ECO:0000305|PubMed:20023638, ECO:0000305|PubMed:20622853};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(6)-methyl-L-lysyl(20)-[histone H4] + O2 =
CC CO2 + formaldehyde + L-lysyl(20)-[histone H4] + succinate;
CC Xref=Rhea:RHEA:67804, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15555,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61929; Evidence={ECO:0000269|PubMed:20622853};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67805;
CC Evidence={ECO:0000305|PubMed:20622853};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:20023638};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:20023638};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 uM for histone H3 H3K9Me2 {ECO:0000269|PubMed:20023638};
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZMT4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZMT4-2; Sequence=VSP_017458, VSP_017459;
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC Binding to H3K4me3 prevents its access to H3K9me2.
CC {ECO:0000269|PubMed:20023638}.
CC -!- DOMAIN: The linker region is a critical determinant of demethylase
CC specificity. It prevents the active site of JmjC to reach the target
CC H3K9me2 when the PHD-type zinc finger binds to H3K4me3, while it favors
CC selectivity toward H3K27me2. {ECO:0000269|PubMed:20023638}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. JHDM1D
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD18641.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=EAL24032.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK131497; BAD18641.1; ALT_FRAME; mRNA.
DR EMBL; AC004849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236950; EAL24032.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB051505; BAB21809.1; -; mRNA.
DR EMBL; BX641017; CAE46011.1; -; mRNA.
DR CCDS; CCDS43658.1; -. [Q6ZMT4-1]
DR RefSeq; NP_085150.1; NM_030647.1. [Q6ZMT4-1]
DR PDB; 3KV5; X-ray; 2.39 A; A/D=1-488.
DR PDB; 3KV6; X-ray; 2.89 A; A/D=1-488.
DR PDB; 3KV9; X-ray; 2.29 A; A=92-488.
DR PDB; 3KVA; X-ray; 2.79 A; A=92-488.
DR PDB; 3KVB; X-ray; 2.69 A; A=92-488.
DR PDB; 3U78; X-ray; 2.69 A; A=92-488.
DR PDBsum; 3KV5; -.
DR PDBsum; 3KV6; -.
DR PDBsum; 3KV9; -.
DR PDBsum; 3KVA; -.
DR PDBsum; 3KVB; -.
DR PDBsum; 3U78; -.
DR AlphaFoldDB; Q6ZMT4; -.
DR SMR; Q6ZMT4; -.
DR BioGRID; 123331; 4.
DR IntAct; Q6ZMT4; 3.
DR MINT; Q6ZMT4; -.
DR STRING; 9606.ENSP00000380692; -.
DR BindingDB; Q6ZMT4; -.
DR ChEMBL; CHEMBL2163177; -.
DR GuidetoPHARMACOLOGY; 2686; -.
DR iPTMnet; Q6ZMT4; -.
DR PhosphoSitePlus; Q6ZMT4; -.
DR BioMuta; KDM7A; -.
DR DMDM; 90111764; -.
DR EPD; Q6ZMT4; -.
DR jPOST; Q6ZMT4; -.
DR MassIVE; Q6ZMT4; -.
DR MaxQB; Q6ZMT4; -.
DR PaxDb; 9606-ENSP00000380692; -.
DR PeptideAtlas; Q6ZMT4; -.
DR ProteomicsDB; 67913; -. [Q6ZMT4-1]
DR ProteomicsDB; 67914; -. [Q6ZMT4-2]
DR Antibodypedia; 2004; 141 antibodies from 20 providers.
DR DNASU; 80853; -.
DR Ensembl; ENST00000397560.7; ENSP00000380692.2; ENSG00000006459.11. [Q6ZMT4-1]
DR GeneID; 80853; -.
DR KEGG; hsa:80853; -.
DR MANE-Select; ENST00000397560.7; ENSP00000380692.2; NM_030647.2; NP_085150.1.
DR UCSC; uc003vvm.4; human. [Q6ZMT4-1]
DR AGR; HGNC:22224; -.
DR CTD; 80853; -.
DR DisGeNET; 80853; -.
DR GeneCards; KDM7A; -.
DR HGNC; HGNC:22224; KDM7A.
DR HPA; ENSG00000006459; Low tissue specificity.
DR MIM; 619640; gene.
DR neXtProt; NX_Q6ZMT4; -.
DR OpenTargets; ENSG00000006459; -.
DR PharmGKB; PA162392512; -.
DR VEuPathDB; HostDB:ENSG00000006459; -.
DR eggNOG; KOG1632; Eukaryota.
DR eggNOG; KOG1633; Eukaryota.
DR GeneTree; ENSGT00940000158039; -.
DR HOGENOM; CLU_003540_2_1_1; -.
DR InParanoid; Q6ZMT4; -.
DR OMA; PWEEDIT; -.
DR OrthoDB; 2784357at2759; -.
DR PhylomeDB; Q6ZMT4; -.
DR TreeFam; TF106480; -.
DR BioCyc; MetaCyc:ENSG00000006459-MONOMER; -.
DR BRENDA; 1.14.11.65; 2681.
DR PathwayCommons; Q6ZMT4; -.
DR Reactome; R-HSA-3214842; HDMs demethylate histones.
DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions.
DR SABIO-RK; Q6ZMT4; -.
DR SignaLink; Q6ZMT4; -.
DR SIGNOR; Q6ZMT4; -.
DR BioGRID-ORCS; 80853; 12 hits in 1171 CRISPR screens.
DR ChiTaRS; KDM7A; human.
DR EvolutionaryTrace; Q6ZMT4; -.
DR GenomeRNAi; 80853; -.
DR Pharos; Q6ZMT4; Tchem.
DR PRO; PR:Q6ZMT4; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q6ZMT4; Protein.
DR Bgee; ENSG00000006459; Expressed in cartilage tissue and 209 other cell types or tissues.
DR ExpressionAtlas; Q6ZMT4; baseline and differential.
DR Genevisible; Q6ZMT4; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0071558; F:histone H3K27me2/H3K27me3 demethylase activity; IDA:UniProtKB.
DR GO; GO:0051864; F:histone H3K36 demethylase activity; IDA:UniProtKB.
DR GO; GO:0032454; F:histone H3K9 demethylase activity; IDA:UniProtKB.
DR GO; GO:0140683; F:histone H3K9me/H3K9me2 demethylase activity; IEA:RHEA.
DR GO; GO:0035575; F:histone H4K20 demethylase activity; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0030901; P:midbrain development; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd15640; PHD_KDM7; 1.
DR Gene3D; 1.20.58.1360; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23123:SF15; LYSINE-SPECIFIC DEMETHYLASE 7A; 1.
DR PANTHER; PTHR23123; PHD/F-BOX CONTAINING PROTEIN; 1.
DR Pfam; PF17811; JHD; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Dioxygenase; Iron;
KW Metal-binding; Neurogenesis; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..941
FT /note="Lysine-specific demethylase 7A"
FT /id="PRO_0000226771"
FT DOMAIN 230..386
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 37..88
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 97..114
FT /note="Linker"
FT REGION 597..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538,
FT ECO:0000269|PubMed:20023638"
FT BINDING 284
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538,
FT ECO:0000269|PubMed:20023638"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538,
FT ECO:0000269|PubMed:20023638"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 792..809
FT /note="GYHVKTEDPDLRTSSWIK -> ETRSHLCCPDWSPTPELK (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_017458"
FT VAR_SEQ 810..941
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_017459"
FT VARIANT 644
FT /note="R -> S (in dbSNP:rs6950119)"
FT /evidence="ECO:0000269|PubMed:11214970"
FT /id="VAR_049653"
FT CONFLICT 677
FT /note="T -> I (in Ref. 5; CAE46011)"
FT /evidence="ECO:0000305"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:3KV5"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:3KV5"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:3KV5"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:3KV5"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:3KV5"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:3KV5"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:3KV5"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:3KV5"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:3KV5"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:3KV9"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:3KV9"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:3KV9"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:3KV9"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:3KV9"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:3KV5"
FT HELIX 179..186
FT /evidence="ECO:0007829|PDB:3KV9"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:3KV9"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:3KV9"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:3KV9"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:3KV9"
FT HELIX 207..215
FT /evidence="ECO:0007829|PDB:3KV9"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:3KV5"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:3KV9"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:3U78"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:3KV9"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:3KV9"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:3KV9"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:3KV9"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:3KV9"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:3KV9"
FT STRAND 289..304
FT /evidence="ECO:0007829|PDB:3KV9"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:3KV9"
FT HELIX 321..325
FT /evidence="ECO:0007829|PDB:3KV9"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:3KV9"
FT STRAND 336..341
FT /evidence="ECO:0007829|PDB:3KV9"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:3KV9"
FT STRAND 353..369
FT /evidence="ECO:0007829|PDB:3KV9"
FT HELIX 375..388
FT /evidence="ECO:0007829|PDB:3KV9"
FT HELIX 391..395
FT /evidence="ECO:0007829|PDB:3KV9"
FT HELIX 399..418
FT /evidence="ECO:0007829|PDB:3KV9"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:3KV9"
FT HELIX 426..442
FT /evidence="ECO:0007829|PDB:3KV9"
FT TURN 445..447
FT /evidence="ECO:0007829|PDB:3KV9"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:3KV9"
FT HELIX 452..454
FT /evidence="ECO:0007829|PDB:3KV9"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:3KV5"
FT HELIX 461..477
FT /evidence="ECO:0007829|PDB:3KV9"
SQ SEQUENCE 941 AA; 106557 MW; AB8161020D157F11 CRC64;
MAGAAAAVAA GAAAGAAAAA VSVAAPGRAS APPPPPPVYC VCRQPYDVNR FMIECDICKD
WFHGSCVGVE EHHAVDIDLY HCPNCAVLHG SSLMKKRRNW HRHDYTEIDD GSKPVQAGTR
TFIKELRSRV FPSADEIIIK MHGSQLTQRY LEKHGFDVPI MVPKLDDLGL RLPSPTFSVM
DVERYVGGDK VIDVIDVARQ ADSKMTLHNY VKYFMNPNRP KVLNVISLEF SDTKMSELVE
VPDIAKKLSW VENYWPDDSV FPKPFVQKYC LMGVQDSYTD FHIDFGGTSV WYHVLWGEKI
FYLIKPTDEN LARYESWSSS VTQSEVFFGD KVDKCYKCVV KQGHTLFVPT GWIHAVLTSQ
DCMAFGGNFL HNLNIGMQLR CYEMEKRLKT PDLFKFPFFE AICWFVAKNL LETLKELRED
GFQPQTYLVQ GVKALHTALK LWMKKELVSE HAFEIPDNVR PGHLIKELSK VIRAIEEENG
KPVKSQGIPI VCPVSRSSNE ATSPYHSRRK MRKLRDHNVR TPSNLDILEL HTREVLKRLE
MCPWEEDILS SKLNGKFNKH LQPSSTVPEW RAKDNDLRLL LTNGRIIKDE RQPFADQSLY
TADSENEEDK RRTKKAKMKI EESSGVEGVE HEESQKPLNG FFTRVKSELR SRSSGYSDIS
ESEDSGPECT ALKSIFTTEE SESSGDEKKQ EITSNFKEES NVMRNFLQKS QKPSRSEIPI
KRECPTSTST EEEAIQGMLS MAGLHYSTCL QRQIQSTDCS GERNSLQDPS SCHGSNHEVR
QLYRYDKPVE CGYHVKTEDP DLRTSSWIKQ FDTSRFHPQD LSRSQKCIRK EGSSEISQRV
QSRNYVDSSG SSLQNGKYMQ NSNLTSGACQ ISNGSLSPER PVGETSFSVP LHPTKRPASN
PPPISNQATK GKRPKKGMAT AKQRLGKILK LNRNGHARFF V
//
