KDM4C_HUMAN
ID KDM4C_HUMAN Reviewed; 1056 AA.
AC Q9H3R0; B4E1Y4; B7ZL46; F5H347; F5H7P0; O94877; Q2M3M0; Q5JUC9; Q5VYJ2;
AC Q5VYJ3;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Lysine-specific demethylase 4C;
DE EC=1.14.11.66 {ECO:0000269|PubMed:16603238};
DE AltName: Full=Gene amplified in squamous cell carcinoma 1 protein;
DE Short=GASC-1 protein;
DE AltName: Full=JmjC domain-containing histone demethylation protein 3C;
DE AltName: Full=Jumonji domain-containing protein 2C;
DE AltName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase 4C {ECO:0000305};
GN Name=KDM4C; Synonyms=GASC1, JHDM3C, JMJD2C, KIAA0780;
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS
RP THR-492 AND ARG-772.
RX PubMed=10987278;
RA Yang Z.Q., Imoto I., Fukuda Y., Pimkhaokham A., Shimada Y., Imamura M.,
RA Sugano S., Nakamura Y., Inazawa J.;
RT "Identification of a novel gene, GASC1, within an amplicon at 9p23-24
RT frequently detected in esophageal cancer cell lines.";
RL Cancer Res. 60:4735-4739(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-492.
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT
RP THR-492.
RC TISSUE=Testis, and 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-1039.
RC TISSUE=Liver;
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 [6]
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 [7]
RP FUNCTION, AND MUTAGENESIS OF 190-HIS--GLU-192.
RX PubMed=28262558; DOI=10.1016/j.chembiol.2017.02.006;
RA Tumber A., Nuzzi A., Hookway E.S., Hatch S.B., Velupillai S., Johansson C.,
RA Kawamura A., Savitsky P., Yapp C., Szykowska A., Wu N., Bountra C.,
RA Strain-Damerell C., Burgess-Brown N.A., Ruda G.F., Fedorov O., Munro S.,
RA England K.S., Nowak R.P., Schofield C.J., La Thangue N.B., Pawlyn C.,
RA Davies F., Morgan G., Athanasou N., Muller S., Oppermann U., Brennan P.E.;
RT "Potent and Selective KDM5 Inhibitor Stops Cellular Demethylation of
RT H3K4me3 at Transcription Start Sites and Proliferation of MM1S Myeloma
RT Cells.";
RL Cell Chem. Biol. 24:371-380(2017).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 1-347 IN COMPLEX WITH ZINC AND
RP NICKEL ION, COFACTOR, AND SUBSTRATE SPECIFICITY.
RX PubMed=21914792; DOI=10.1074/jbc.m111.283689;
RA Hillringhaus L., Yue W.W., Rose N.R., Ng S.S., Gileadi C., Loenarz C.,
RA Bello S.H., Bray J.E., Schofield C.J., Oppermann U.;
RT "Structural and evolutionary basis for the dual substrate selectivity of
RT human KDM4 histone demethylase family.";
RL J. Biol. Chem. 286:41616-41625(2011).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-9'
CC and 'Lys-36' residues of histone H3, thereby playing a central role in
CC histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor
CC H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36'
CC residue, while it has no activity on mono- and dimethylated residues.
CC Demethylation of Lys residue generates formaldehyde and succinate.
CC {ECO:0000269|PubMed:16603238, ECO:0000269|PubMed:28262558}.
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;
CC Evidence={ECO:0000269|PubMed:21914792};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:21914792};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9H3R0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H3R0-2; Sequence=VSP_018311;
CC Name=3;
CC IsoId=Q9H3R0-3; Sequence=VSP_045462, VSP_045463;
CC Name=4;
CC IsoId=Q9H3R0-4; Sequence=VSP_046113, VSP_045462, VSP_045463;
CC -!- TISSUE SPECIFICITY: Overexpressed in several esophageal squamous cell
CC carcinomas (ESCs). {ECO:0000269|PubMed:10987278}.
CC -!- DOMAIN: The 2 Tudor domains recognize and bind methylated histones.
CC Double Tudor domain has an interdigitated structure and the unusual
CC fold is required for its ability to bind methylated histone tails (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34500.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/GASC1ID432.html";
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DR EMBL; AB037901; BAB16102.1; -; mRNA.
DR EMBL; AB018323; BAA34500.1; ALT_INIT; mRNA.
DR EMBL; AK304032; BAG64946.1; -; mRNA.
DR EMBL; AK310439; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL137020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC104859; AAI04860.1; -; mRNA.
DR EMBL; BC104861; AAI04862.1; -; mRNA.
DR EMBL; BC143571; AAI43572.1; -; mRNA.
DR CCDS; CCDS55285.1; -. [Q9H3R0-4]
DR CCDS; CCDS55286.1; -. [Q9H3R0-3]
DR CCDS; CCDS6471.1; -. [Q9H3R0-1]
DR RefSeq; NP_001140167.1; NM_001146695.1. [Q9H3R0-3]
DR RefSeq; NP_001140168.1; NM_001146696.1. [Q9H3R0-4]
DR RefSeq; NP_055876.2; NM_015061.3. [Q9H3R0-1]
DR PDB; 2XDP; X-ray; 1.56 A; A=875-995.
DR PDB; 2XML; X-ray; 2.55 A; A/B=1-347.
DR PDB; 4XDO; X-ray; 1.97 A; A/B=10-347.
DR PDB; 4XDP; X-ray; 2.07 A; A/B=10-347.
DR PDB; 5FJH; X-ray; 2.10 A; A/B=3-347.
DR PDB; 5FJK; X-ray; 1.66 A; A=3-347.
DR PDB; 5KR7; X-ray; 1.90 A; A/B=1-350.
DR PDBsum; 2XDP; -.
DR PDBsum; 2XML; -.
DR PDBsum; 4XDO; -.
DR PDBsum; 4XDP; -.
DR PDBsum; 5FJH; -.
DR PDBsum; 5FJK; -.
DR PDBsum; 5KR7; -.
DR AlphaFoldDB; Q9H3R0; -.
DR SMR; Q9H3R0; -.
DR BioGRID; 116712; 66.
DR DIP; DIP-60098N; -.
DR IntAct; Q9H3R0; 41.
DR MINT; Q9H3R0; -.
DR STRING; 9606.ENSP00000370710; -.
DR BindingDB; Q9H3R0; -.
DR ChEMBL; CHEMBL6175; -.
DR GuidetoPHARMACOLOGY; 2677; -.
DR iPTMnet; Q9H3R0; -.
DR PhosphoSitePlus; Q9H3R0; -.
DR BioMuta; KDM4C; -.
DR DMDM; 97536525; -.
DR EPD; Q9H3R0; -.
DR jPOST; Q9H3R0; -.
DR MassIVE; Q9H3R0; -.
DR MaxQB; Q9H3R0; -.
DR PaxDb; Q9H3R0; -.
DR PeptideAtlas; Q9H3R0; -.
DR PRIDE; Q9H3R0; -.
DR ProteomicsDB; 26163; -.
DR ProteomicsDB; 27544; -.
DR ProteomicsDB; 80741; -. [Q9H3R0-1]
DR ProteomicsDB; 80742; -. [Q9H3R0-2]
DR Antibodypedia; 24299; 354 antibodies from 28 providers.
DR DNASU; 23081; -.
DR Ensembl; ENST00000381306.7; ENSP00000370707.3; ENSG00000107077.19. [Q9H3R0-2]
DR Ensembl; ENST00000381309.8; ENSP00000370710.3; ENSG00000107077.19. [Q9H3R0-1]
DR Ensembl; ENST00000536108.5; ENSP00000440656.3; ENSG00000107077.19. [Q9H3R0-4]
DR Ensembl; ENST00000543771.5; ENSP00000445427.1; ENSG00000107077.19. [Q9H3R0-3]
DR GeneID; 23081; -.
DR KEGG; hsa:23081; -.
DR MANE-Select; ENST00000381309.8; ENSP00000370710.3; NM_015061.6; NP_055876.2.
DR UCSC; uc003zkg.4; human. [Q9H3R0-1]
DR CTD; 23081; -.
DR DisGeNET; 23081; -.
DR GeneCards; KDM4C; -.
DR HGNC; HGNC:17071; KDM4C.
DR HPA; ENSG00000107077; Low tissue specificity.
DR MIM; 605469; gene.
DR neXtProt; NX_Q9H3R0; -.
DR OpenTargets; ENSG00000107077; -.
DR PharmGKB; PA164721503; -.
DR VEuPathDB; HostDB:ENSG00000107077; -.
DR eggNOG; KOG0958; Eukaryota.
DR GeneTree; ENSGT00940000154930; -.
DR HOGENOM; CLU_001442_0_0_1; -.
DR InParanoid; Q9H3R0; -.
DR OMA; VPSHEIC; -.
DR OrthoDB; 1186832at2759; -.
DR PhylomeDB; Q9H3R0; -.
DR TreeFam; TF106449; -.
DR BioCyc; MetaCyc:ENSG00000107077-MON; -.
DR BRENDA; 1.14.11.27; 2681.
DR BRENDA; 1.14.11.66; 2681.
DR BRENDA; 1.14.11.69; 2681.
DR PathwayCommons; Q9H3R0; -.
DR Reactome; R-HSA-3214842; HDMs demethylate histones.
DR Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR SignaLink; Q9H3R0; -.
DR SIGNOR; Q9H3R0; -.
DR BioGRID-ORCS; 23081; 14 hits in 1094 CRISPR screens.
DR ChiTaRS; KDM4C; human.
DR EvolutionaryTrace; Q9H3R0; -.
DR GeneWiki; JMJD2C; -.
DR GenomeRNAi; 23081; -.
DR Pharos; Q9H3R0; Tchem.
DR PRO; PR:Q9H3R0; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9H3R0; protein.
DR Bgee; ENSG00000107077; Expressed in right hemisphere of cerebellum and 170 other tissues.
DR ExpressionAtlas; Q9H3R0; baseline and differential.
DR Genevisible; Q9H3R0; HS.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
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:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0032452; F:histone demethylase activity; EXP:Reactome.
DR GO; GO:0051864; F:histone H3-methyl-lysine-36 demethylase activity; IDA:UniProtKB.
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:0050681; F:nuclear androgen receptor binding; IPI:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0001825; P:blastocyst formation; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0070544; P:histone H3-K36 demethylation; IDA:UniProtKB.
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:0008284; P:positive regulation of cell population proliferation; IMP:BHF-UCL.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; TAS:Reactome.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR040477; KDM4_Tudor_2.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF18104; Tudor_2; 2.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Dioxygenase; Iron;
KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1056
FT /note="Lysine-specific demethylase 4C"
FT /id="PRO_0000183177"
FT DOMAIN 16..58
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 144..310
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT DOMAIN 877..934
FT /note="Tudor 1"
FT DOMAIN 935..991
FT /note="Tudor 2"
FT ZN_FING 689..747
FT /note="PHD-type 1"
FT ZN_FING 752..785
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 808..865
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 370..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:B2RXH2"
FT BINDING 190
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT BINDING 192
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT BINDING 200
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:B2RXH2"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:21914792"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:21914792"
FT BINDING 243
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:B2RXH2"
FT BINDING 278
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:21914792"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:21914792"
FT VAR_SEQ 1
FT /note="M -> MKHYGLPWKRTEEAAADTALTIM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046113"
FT VAR_SEQ 809..813
FT /note="KCIFC -> GRLGI (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045462"
FT VAR_SEQ 814..1056
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045463"
FT VAR_SEQ 999..1056
FT /note="STASDMRFEDTFYGADIIQGERKRQRVLSSRFKNEYVADPVYRTFLKSSFQK
FT KCQKRQ -> VSAGRCHLGTCQVNSLSSPHVSQAQQETYLGFWINSKKSQCNIFLSGTY
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9872452"
FT /id="VSP_018311"
FT VARIANT 206
FT /note="E -> D (in dbSNP:rs7864351)"
FT /id="VAR_049660"
FT VARIANT 396
FT /note="D -> N (in dbSNP:rs2296067)"
FT /id="VAR_020340"
FT VARIANT 492
FT /note="S -> T (in dbSNP:rs35826653)"
FT /evidence="ECO:0000269|PubMed:10987278,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:9872452"
FT /id="VAR_049661"
FT VARIANT 697
FT /note="N -> S (in dbSNP:rs35389625)"
FT /id="VAR_049662"
FT VARIANT 767
FT /note="Q -> E (in dbSNP:rs1407856)"
FT /id="VAR_024681"
FT VARIANT 772
FT /note="K -> R (in dbSNP:rs1417290)"
FT /evidence="ECO:0000269|PubMed:10987278"
FT /id="VAR_049663"
FT VARIANT 1039
FT /note="V -> I (in dbSNP:rs913588)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_024682"
FT MUTAGEN 190..192
FT /note="HTE->ATA: Abolishes lysine-specific histone
FT demethylase activity."
FT /evidence="ECO:0000269|PubMed:28262558"
FT CONFLICT 155
FT /note="L -> I (in Ref. 1; BAB16102)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="C -> S (in Ref. 3; BAG64946)"
FT /evidence="ECO:0000305"
FT CONFLICT 807
FT /note="K -> R (in Ref. 3; BAG64946)"
FT /evidence="ECO:0000305"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:5FJK"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:5FJK"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:5FJK"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:5FJK"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:5FJK"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:5FJK"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:5FJK"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:5FJK"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:5FJK"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:5FJK"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:5FJK"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:5FJK"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:5FJK"
FT HELIX 158..166
FT /evidence="ECO:0007829|PDB:5FJK"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:5FJK"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:5FJK"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:5FJK"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:5FJK"
FT STRAND 197..206
FT /evidence="ECO:0007829|PDB:5FJK"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:5FJK"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:5FJK"
FT HELIX 218..228
FT /evidence="ECO:0007829|PDB:5FJK"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:5FJK"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:5FJK"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:5FJK"
FT HELIX 249..255
FT /evidence="ECO:0007829|PDB:5FJK"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:5FJK"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:5FJK"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:5FJK"
FT STRAND 284..293
FT /evidence="ECO:0007829|PDB:5FJK"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:5FJK"
FT HELIX 299..304
FT /evidence="ECO:0007829|PDB:5FJK"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:5FJH"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:4XDP"
FT HELIX 320..326
FT /evidence="ECO:0007829|PDB:5FJK"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:5FJK"
FT HELIX 331..335
FT /evidence="ECO:0007829|PDB:5FJK"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:5KR7"
FT STRAND 898..912
FT /evidence="ECO:0007829|PDB:2XDP"
FT STRAND 917..921
FT /evidence="ECO:0007829|PDB:2XDP"
FT HELIX 923..925
FT /evidence="ECO:0007829|PDB:2XDP"
FT HELIX 931..934
FT /evidence="ECO:0007829|PDB:2XDP"
FT STRAND 942..946
FT /evidence="ECO:0007829|PDB:2XDP"
FT STRAND 952..969
FT /evidence="ECO:0007829|PDB:2XDP"
FT STRAND 975..979
FT /evidence="ECO:0007829|PDB:2XDP"
FT HELIX 980..982
FT /evidence="ECO:0007829|PDB:2XDP"
FT STRAND 986..988
FT /evidence="ECO:0007829|PDB:2XDP"
SQ SEQUENCE 1056 AA; 119982 MW; CBE871D4FAADD06D CRC64;
MEVAEVESPL NPSCKIMTFR PSMEEFREFN KYLAYMESKG AHRAGLAKVI PPKEWKPRQC
YDDIDNLLIP APIQQMVTGQ SGLFTQYNIQ KKAMTVKEFR QLANSGKYCT PRYLDYEDLE
RKYWKNLTFV APIYGADING SIYDEGVDEW NIARLNTVLD VVEEECGISI EGVNTPYLYF
GMWKTTFAWH TEDMDLYSIN YLHFGEPKSW YAIPPEHGKR LERLAQGFFP SSSQGCDAFL
RHKMTLISPS VLKKYGIPFD KITQEAGEFM ITFPYGYHAG FNHGFNCAES TNFATVRWID
YGKVAKLCTC RKDMVKISMD IFVRKFQPDR YQLWKQGKDI YTIDHTKPTP ASTPEVKAWL
QRRRKVRKAS RSFQCARSTS KRPKADEEEE VSDEVDGAEV PNPDSVTDDL KVSEKSEAAV
KLRNTEASSE EESSASRMQV EQNLSDHIKL SGNSCLSTSV TEDIKTEDDK AYAYRSVPSI
SSEADDSIPL SSGYEKPEKS DPSELSWPKS PESCSSVAES NGVLTEGEES DVESHGNGLE
PGEIPAVPSG ERNSFKVPSI AEGENKTSKS WRHPLSRPPA RSPMTLVKQQ APSDEELPEV
LSIEEEVEET ESWAKPLIHL WQTKSPNFAA EQEYNATVAR MKPHCAICTL LMPYHKPDSS
NEENDARWET KLDEVVTSEG KTKPLIPEMC FIYSEENIEY SPPNAFLEED GTSLLISCAK
CCVRVHASCY GIPSHEICDG WLCARCKRNA WTAECCLCNL RGGALKQTKN NKWAHVMCAV
AVPEVRFTNV PERTQIDVGR IPLQRLKLKC IFCRHRVKRV SGACIQCSYG RCPASFHVTC
AHAAGVLMEP DDWPYVVNIT CFRHKVNPNV KSKACEKVIS VGQTVITKHR NTRYYSCRVM
AVTSQTFYEV MFDDGSFSRD TFPEDIVSRD CLKLGPPAEG EVVQVKWPDG KLYGAKYFGS
NIAHMYQVEF EDGSQIAMKR EDIYTLDEEL PKRVKARFST ASDMRFEDTF YGADIIQGER
KRQRVLSSRF KNEYVADPVY RTFLKSSFQK KCQKRQ
