KDM5C_HUMAN
ID KDM5C_HUMAN Reviewed; 1560 AA.
AC P41229; B0QZ44; B4E3I2; F5H3T1; Q5JUX3; Q5JUX4; Q5JUX5; Q7Z5S5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Lysine-specific demethylase 5C;
DE EC=1.14.11.67 {ECO:0000269|PubMed:26645689};
DE AltName: Full=Histone demethylase JARID1C;
DE AltName: Full=Jumonji/ARID domain-containing protein 1C {ECO:0000303|PubMed:19636912};
DE AltName: Full=Protein SmcX {ECO:0000303|PubMed:19636912};
DE AltName: Full=Protein Xe169;
DE AltName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase 5C {ECO:0000305};
GN Name=KDM5C {ECO:0000312|HGNC:HGNC:11114};
GN Synonyms=DXS1272E, JARID1C {ECO:0000303|PubMed:19636912},
GN SMCX {ECO:0000303|PubMed:19636912}, XE169;
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).
RC TISSUE=Fibroblast;
RX PubMed=8162017; DOI=10.1093/hmg/3.1.153;
RA Wu J., Ellison J., Salido E., Yen P., Mohandas T., Shapiro L.J.;
RT "Isolation and characterization of XE169, a novel human gene that escapes
RT X-inactivation.";
RL Hum. Mol. Genet. 3:153-160(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Uterus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Eye;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 280-344.
RC TISSUE=Blood;
RX PubMed=7951230; DOI=10.1093/hmg/3.6.879;
RA Agulnik A.I., Mitchell M.J., Mattei M.-G., Borsani G., Avner P.A.,
RA Lerner J.L., Bishop C.E.;
RT "A novel X gene with a widely transcribed Y-linked homologue escapes X-
RT inactivation in mouse and human.";
RL Hum. Mol. Genet. 3:879-884(1994).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1359, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP FUNCTION.
RX PubMed=17320161; DOI=10.1016/j.cell.2007.02.003;
RA Christensen J., Agger K., Cloos P.A.C., Pasini D., Rose S., Sennels L.,
RA Rappsilber J., Hansen K.H., Salcini A.E., Helin K.;
RT "RBP2 belongs to a family of demethylases, specific for tri-and
RT dimethylated lysine 4 on histone 3.";
RL Cell 128:1063-1076(2007).
RN [9]
RP FUNCTION, MUTAGENESIS OF HIS-514, AND CHARACTERIZATION OF VARIANTS MRXSCJ
RP PRO-388; LEU-642; PHE-731 AND CYS-751.
RX PubMed=17320160; DOI=10.1016/j.cell.2007.02.017;
RA Iwase S., Lan F., Bayliss P., de la Torre-Ubieta L., Huarte M., Qi H.H.,
RA Whetstine J.R., Bonni A., Roberts T.M., Shi Y.;
RT "The X-linked mental retardation gene SMCX/JARID1C defines a family of
RT histone H3 lysine 4 demethylases.";
RL Cell 128:1077-1088(2007).
RN [10]
RP FUNCTION, SUBUNIT, MUTAGENESIS OF HIS-514, SUBCELLULAR LOCATION, AND
RP CHARACTERIZATION OF VARIANTS MRXSCJ GLY-87; TYR-402 AND CYS-751.
RX PubMed=17468742; DOI=10.1038/nature05823;
RA Tahiliani M., Mei P., Fang R., Leonor T., Rutenberg M., Shimizu F., Li J.,
RA Rao A., Shi Y.;
RT "The histone H3K4 demethylase SMCX links REST target genes to X-linked
RT mental retardation.";
RL Nature 447:601-605(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1359, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1359, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1359, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287; SER-301; SER-317;
RP SER-897 AND SER-1359, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [17]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=26645689; DOI=10.1074/jbc.m115.698449;
RA Horton J.R., Engstrom A., Zoeller E.L., Liu X., Shanks J.R., Zhang X.,
RA Johns M.A., Vertino P.M., Fu H., Cheng X.;
RT "Characterization of a Linked Jumonji Domain of the KDM5/JARID1 Family of
RT Histone H3 Lysine 4 Demethylases.";
RL J. Biol. Chem. 291:2631-2646(2016).
RN [18]
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF 514-HIS--GLU-516.
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 [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-205; LYS-229; LYS-244; LYS-274;
RP LYS-295 AND LYS-1127, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [20]
RP STRUCTURE BY NMR OF 73-188.
RX PubMed=19636912; DOI=10.1007/s12104-007-9071-7;
RA Koehler C., Bishop S., Dowler E.F., Schmieder P., Diehl A., Oschkinat H.,
RA Ball L.J.;
RT "Backbone and sidechain 1H, 13C and 15N resonance assignments of the
RT Bright/ARID domain from the human JARID1C (SMCX) protein.";
RL Biomol. NMR. Assign. 2:9-11(2008).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 384-772 IN COMPLEX WITH MANGANESE
RP AND ZINC.
RX PubMed=27214403; DOI=10.1038/nchembio.2087;
RA Johansson C., Velupillai S., Tumber A., Szykowska A., Hookway E.S.,
RA Nowak R.P., Strain-Damerell C., Gileadi C., Philpott M., Burgess-Brown N.,
RA Wu N., Kopec J., Nuzzi A., Steuber H., Egner U., Badock V., Munro S.,
RA LaThangue N.B., Westaway S., Brown J., Athanasou N., Prinjha R.,
RA Brennan P.E., Oppermann U.;
RT "Structural analysis of human KDM5B guides histone demethylase inhibitor
RT development.";
RL Nat. Chem. Biol. 12:539-545(2016).
RN [22]
RP VARIANTS MRXSCJ PRO-388; TYR-402; LYS-698 AND PHE-731, AND TISSUE
RP SPECIFICITY.
RX PubMed=15586325; DOI=10.1086/427563;
RA Jensen L.R., Amende M., Gurok U., Moser B., Gimmel V., Tzschach A.,
RA Janecke A.R., Tariverdian G., Chelly J., Fryns J.-P., Van Esch H.,
RA Kleefstra T., Hamel B.C.J., Moraine C., Gecz J., Turner G., Reinhardt R.,
RA Kalscheuer V.M., Ropers H.-H., Lenzner S.;
RT "Mutations in the JARID1C gene, which is involved in transcriptional
RT regulation and chromatin remodeling, cause X-linked mental retardation.";
RL Am. J. Hum. Genet. 76:227-236(2005).
RN [23]
RP VARIANT MRXSCJ ARG-451.
RX PubMed=16538222; DOI=10.1038/sj.ejhg.5201608;
RA Santos C., Rodriguez-Revenga L., Madrigal I., Badenas C., Pineda M.,
RA Mila M.;
RT "A novel mutation in JARID1C gene associated with mental retardation.";
RL Eur. J. Hum. Genet. 14:583-586(2006).
RN [24]
RP VARIANTS MRXSCJ GLY-87; LEU-642; TRP-750 AND CYS-751.
RX PubMed=16541399; DOI=10.1002/humu.9420;
RA Tzschach A., Lenzner S., Moser B., Reinhardt R., Chelly J., Fryns J.-P.,
RA Kleefstra T., Raynaud M., Turner G., Ropers H.-H., Kuss A., Jensen L.R.;
RT "Novel JARID1C/SMCX mutations in patients with X-linked mental
RT retardation.";
RL Hum. Mutat. 27:389-389(2006).
RN [25]
RP VARIANT TYR-640.
RX PubMed=21076407; DOI=10.1038/ng.712;
RA Vissers L.E., de Ligt J., Gilissen C., Janssen I., Steehouwer M.,
RA de Vries P., van Lier B., Arts P., Wieskamp N., del Rosario M.,
RA van Bon B.W., Hoischen A., de Vries B.B., Brunner H.G., Veltman J.A.;
RT "A de novo paradigm for mental retardation.";
RL Nat. Genet. 42:1109-1112(2010).
RN [26]
RP VARIANT MRXSCJ LEU-480.
RX PubMed=23356856; DOI=10.1186/1755-8794-6-1;
RA Grafodatskaya D., Chung B.H., Butcher D.T., Turinsky A.L., Goodman S.J.,
RA Choufani S., Chen Y.A., Lou Y., Zhao C., Rajendram R., Abidi F.E.,
RA Skinner C., Stavropoulos J., Bondy C.A., Hamilton J., Wodak S.,
RA Scherer S.W., Schwartz C.E., Weksberg R.;
RT "Multilocus loss of DNA methylation in individuals with mutations in the
RT histone H3 lysine 4 demethylase KDM5C.";
RL BMC Med. Genomics 6:1-1(2013).
RN [27]
RP CHARACTERIZATION OF VARIANTS MRXSCJ TYR-402 AND LEU-480.
RX PubMed=25666439; DOI=10.1093/hmg/ddv046;
RA Brookes E., Laurent B., Ounap K., Carroll R., Moeschler J.B., Field M.,
RA Schwartz C.E., Gecz J., Shi Y.;
RT "Mutations in the intellectual disability gene KDM5C reduce protein
RT stability and demethylase activity.";
RL Hum. Mol. Genet. 24:2861-2872(2015).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-4' of
CC histone H3, thereby playing a central role in histone code
CC (PubMed:28262558). Does not demethylate histone H3 'Lys-9', H3 'Lys-
CC 27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates
CC trimethylated and dimethylated but not monomethylated H3 'Lys-4'.
CC Participates in transcriptional repression of neuronal genes by
CC recruiting histone deacetylases and REST at neuron-restrictive silencer
CC elements. Represses the CLOCK-ARNTL/BMAL1 heterodimer-mediated
CC transcriptional activation of the core clock component PER2 (By
CC similarity). {ECO:0000250|UniProtKB:P41230,
CC ECO:0000269|PubMed:17320160, ECO:0000269|PubMed:17320161,
CC ECO:0000269|PubMed:17468742, ECO:0000269|PubMed:26645689,
CC ECO:0000269|PubMed:28262558}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC Evidence={ECO:0000269|PubMed:26645689};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:17320160};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:17320160};
CC -!- ACTIVITY REGULATION: The inhibitor KDOAM-25 and others inhibit its
CC demethylase activity, resulting to cell cycle arrest in myeloma cells.
CC {ECO:0000269|PubMed:28262558}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 uM for 2-oxoglutarate {ECO:0000269|PubMed:26645689};
CC KM=3.3 uM for histone H3K4me3 {ECO:0000269|PubMed:26645689};
CC Note=kcat is 1.92 min(-1) and 2.71 min(-1) for 2-oxoglutarate and
CC histone H3K4me3, respectively. {ECO:0000269|PubMed:26645689};
CC -!- SUBUNIT: Part of two distinct complexes, one containing E2F6, and the
CC other containing REST. {ECO:0000269|PubMed:17468742}.
CC -!- INTERACTION:
CC P41229; Q13127: REST; NbExp=3; IntAct=EBI-1246541, EBI-926706;
CC P41229; P03122: E2; Xeno; NbExp=2; IntAct=EBI-1246541, EBI-7028618;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:17468742}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P41229-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P41229-2; Sequence=VSP_000315;
CC Name=3;
CC IsoId=P41229-3; Sequence=VSP_026410, VSP_000315;
CC Name=4;
CC IsoId=P41229-4; Sequence=VSP_043752, VSP_026410, VSP_000315,
CC VSP_043753;
CC Name=5;
CC IsoId=P41229-5; Sequence=VSP_053420;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined. Highest levels
CC found in brain and skeletal muscle. {ECO:0000269|PubMed:15586325}.
CC -!- DOMAIN: The first PHD-type zinc finger domain recognizes and binds H3-
CC K9Me3.
CC -!- DOMAIN: Both the JmjC domain and the JmjN domain are required for
CC enzymatic activity.
CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic,
CC Claes-Jensen type (MRXSCJ) [MIM:300534]: A disorder characterized by
CC significantly below average general intellectual functioning associated
CC with impairments in adaptive behavior and manifested during the
CC developmental period. MRXSCJ patients manifest intellectual disability
CC associated with variable features such as slowly progressive spastic
CC paraplegia, seizures, facial dysmorphism. {ECO:0000269|PubMed:15586325,
CC ECO:0000269|PubMed:16538222, ECO:0000269|PubMed:16541399,
CC ECO:0000269|PubMed:17320160, ECO:0000269|PubMed:17468742,
CC ECO:0000269|PubMed:23356856, ECO:0000269|PubMed:25666439}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Escapes X-inactivation.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000305}.
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DR EMBL; L25270; AAA61302.1; -; mRNA.
DR EMBL; AK304732; BAG65494.1; -; mRNA.
DR EMBL; AL139396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471154; EAW93145.1; -; Genomic_DNA.
DR EMBL; BC054499; AAH54499.1; -; mRNA.
DR EMBL; Z29650; CAA82758.1; -; mRNA.
DR CCDS; CCDS14351.1; -. [P41229-1]
DR CCDS; CCDS55417.1; -. [P41229-4]
DR CCDS; CCDS65269.1; -. [P41229-5]
DR CCDS; CCDS87747.1; -. [P41229-2]
DR PIR; I54361; I54361.
DR RefSeq; NP_001140174.1; NM_001146702.1. [P41229-4]
DR RefSeq; NP_001269551.1; NM_001282622.1. [P41229-5]
DR RefSeq; NP_004178.2; NM_004187.3. [P41229-1]
DR RefSeq; XP_005262092.1; XM_005262035.4.
DR RefSeq; XP_011529128.1; XM_011530826.2.
DR PDB; 2JRZ; NMR; -; A=73-188.
DR PDB; 5FWJ; X-ray; 2.10 A; A/B=8-83, A/B=384-772.
DR PDBsum; 2JRZ; -.
DR PDBsum; 5FWJ; -.
DR AlphaFoldDB; P41229; -.
DR BMRB; P41229; -.
DR SMR; P41229; -.
DR BioGRID; 113870; 122.
DR DIP; DIP-39663N; -.
DR IntAct; P41229; 56.
DR MINT; P41229; -.
DR STRING; 9606.ENSP00000364550; -.
DR BindingDB; P41229; -.
DR ChEMBL; CHEMBL2163176; -.
DR GuidetoPHARMACOLOGY; 2682; -.
DR GlyGen; P41229; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P41229; -.
DR PhosphoSitePlus; P41229; -.
DR BioMuta; KDM5C; -.
DR DMDM; 117949812; -.
DR EPD; P41229; -.
DR jPOST; P41229; -.
DR MassIVE; P41229; -.
DR MaxQB; P41229; -.
DR PaxDb; P41229; -.
DR PeptideAtlas; P41229; -.
DR PRIDE; P41229; -.
DR ProteomicsDB; 2727; -.
DR ProteomicsDB; 55436; -. [P41229-1]
DR ProteomicsDB; 55437; -. [P41229-2]
DR ProteomicsDB; 55438; -. [P41229-3]
DR ProteomicsDB; 55439; -. [P41229-4]
DR ABCD; P41229; 1 sequenced antibody.
DR Antibodypedia; 26540; 218 antibodies from 31 providers.
DR DNASU; 8242; -.
DR Ensembl; ENST00000375379.7; ENSP00000364528.3; ENSG00000126012.13. [P41229-2]
DR Ensembl; ENST00000375383.7; ENSP00000364532.3; ENSG00000126012.13. [P41229-3]
DR Ensembl; ENST00000375401.8; ENSP00000364550.4; ENSG00000126012.13. [P41229-1]
DR Ensembl; ENST00000404049.7; ENSP00000385394.3; ENSG00000126012.13. [P41229-5]
DR Ensembl; ENST00000452825.7; ENSP00000445176.1; ENSG00000126012.13. [P41229-4]
DR GeneID; 8242; -.
DR KEGG; hsa:8242; -.
DR MANE-Select; ENST00000375401.8; ENSP00000364550.4; NM_004187.5; NP_004178.2.
DR UCSC; uc004drz.4; human. [P41229-1]
DR CTD; 8242; -.
DR DisGeNET; 8242; -.
DR GeneCards; KDM5C; -.
DR HGNC; HGNC:11114; KDM5C.
DR HPA; ENSG00000126012; Low tissue specificity.
DR MalaCards; KDM5C; -.
DR MIM; 300534; phenotype.
DR MIM; 314690; gene.
DR neXtProt; NX_P41229; -.
DR OpenTargets; ENSG00000126012; -.
DR Orphanet; 85279; KDM5C-related syndromic X-linked intellectual disability.
DR PharmGKB; PA35964; -.
DR VEuPathDB; HostDB:ENSG00000126012; -.
DR eggNOG; KOG1246; Eukaryota.
DR GeneTree; ENSGT00940000161236; -.
DR HOGENOM; CLU_000991_2_2_1; -.
DR InParanoid; P41229; -.
DR OMA; ASAHSWK; -.
DR OrthoDB; 664180at2759; -.
DR PhylomeDB; P41229; -.
DR TreeFam; TF106476; -.
DR BioCyc; MetaCyc:ENSG00000126012-MON; -.
DR BRENDA; 1.14.11.67; 2681.
DR PathwayCommons; P41229; -.
DR Reactome; R-HSA-3214842; HDMs demethylate histones.
DR SignaLink; P41229; -.
DR SIGNOR; P41229; -.
DR BioGRID-ORCS; 8242; 64 hits in 744 CRISPR screens.
DR ChiTaRS; KDM5C; human.
DR EvolutionaryTrace; P41229; -.
DR GeneWiki; JARID1C; -.
DR GenomeRNAi; 8242; -.
DR Pharos; P41229; Tchem.
DR PRO; PR:P41229; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P41229; protein.
DR Bgee; ENSG00000126012; Expressed in sural nerve and 196 other tissues.
DR ExpressionAtlas; P41229; baseline and differential.
DR Genevisible; P41229; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0032453; F:histone H3-methyl-lysine-4 demethylase activity; IDA:MGI.
DR GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0034720; P:histone H3-K4 demethylation; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.60; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
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 Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF46774; SSF46774; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Biological rhythms;
KW Chromatin regulator; Dioxygenase; Disease variant; Intellectual disability;
KW Iron; Isopeptide bond; Metal-binding; Nucleus; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1560
FT /note="Lysine-specific demethylase 5C"
FT /id="PRO_0000200586"
FT DOMAIN 14..55
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 79..169
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 468..634
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 326..372
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 707..759
FT /note="C5HC2"
FT /evidence="ECO:0000269|PubMed:27214403"
FT ZN_FING 1187..1248
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 197..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1444..1560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1461..1489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1515..1541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 440
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT BINDING 514
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:27214403"
FT BINDING 516
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:27214403"
FT BINDING 522
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT BINDING 524
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT BINDING 532
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT BINDING 602
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:27214403"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41230"
FT MOD_RES 897
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 205
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 229
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 244
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 295
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 51..76
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043752"
FT VAR_SEQ 77..117
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026410"
FT VAR_SEQ 175
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053420"
FT VAR_SEQ 1370..1372
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_000315"
FT VAR_SEQ 1420..1560
FT /note="WQLLQAGQPPDLERIRTLLELEKAERHGSRARGRALERRRRRKVDRGGEGDD
FT PAREELEPKRVRSSGPEAEEVQEEEELEEETGGEGPPAPIPTTGSPSTQENQNGLEPAE
FT GTTSGPSAPFSTLTPRLHLPCPQQPPQQQL -> PESLDFCILTPRYCSDLSSWGPAPG
FT VFPPW (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043753"
FT VARIANT 87
FT /note="D -> G (in MRXSCJ; no effect on subcellular location
FT and enzymatic activity)"
FT /evidence="ECO:0000269|PubMed:16541399,
FT ECO:0000269|PubMed:17468742"
FT /id="VAR_032986"
FT VARIANT 388
FT /note="A -> P (in MRXSCJ; impairs enzymatic activity and
FT binding to H3-K9Me3; dbSNP:rs199422235)"
FT /evidence="ECO:0000269|PubMed:15586325,
FT ECO:0000269|PubMed:17320160"
FT /id="VAR_022730"
FT VARIANT 402
FT /note="D -> Y (in MRXSCJ; decreases enzymatic activity)"
FT /evidence="ECO:0000269|PubMed:15586325,
FT ECO:0000269|PubMed:17468742, ECO:0000269|PubMed:25666439"
FT /id="VAR_022731"
FT VARIANT 451
FT /note="S -> R (in MRXSCJ; dbSNP:rs199422237)"
FT /evidence="ECO:0000269|PubMed:16538222"
FT /id="VAR_032987"
FT VARIANT 480
FT /note="P -> L (in MRXSCJ; patient fibroblasts show
FT decreased enzymatic activity; dbSNP:rs1057518697)"
FT /evidence="ECO:0000269|PubMed:23356856,
FT ECO:0000269|PubMed:25666439"
FT /id="VAR_074308"
FT VARIANT 640
FT /note="C -> Y (de novo mutation found in a patient with
FT intellectual disability)"
FT /evidence="ECO:0000269|PubMed:21076407"
FT /id="VAR_065091"
FT VARIANT 642
FT /note="F -> L (in MRXSCJ; impairs enzymatic activity)"
FT /evidence="ECO:0000269|PubMed:16541399,
FT ECO:0000269|PubMed:17320160"
FT /id="VAR_032988"
FT VARIANT 698
FT /note="E -> K (in MRXSCJ; dbSNP:rs1057517955)"
FT /evidence="ECO:0000269|PubMed:15586325"
FT /id="VAR_022732"
FT VARIANT 731
FT /note="L -> F (in MRXSCJ; impairs enzymatic activity;
FT dbSNP:rs199422234)"
FT /evidence="ECO:0000269|PubMed:15586325,
FT ECO:0000269|PubMed:17320160"
FT /id="VAR_022733"
FT VARIANT 750
FT /note="R -> W (in MRXSCJ)"
FT /evidence="ECO:0000269|PubMed:16541399"
FT /id="VAR_032989"
FT VARIANT 751
FT /note="Y -> C (in MRXSCJ; impairs enzymatic activity)"
FT /evidence="ECO:0000269|PubMed:16541399,
FT ECO:0000269|PubMed:17320160, ECO:0000269|PubMed:17468742"
FT /id="VAR_032990"
FT MUTAGEN 514..516
FT /note="HIE->AIA: Abolishes lysine-specific histone
FT demethylase activity."
FT /evidence="ECO:0000269|PubMed:28262558"
FT MUTAGEN 514
FT /note="H->A: Abolishes lysine-specific histone demethylase
FT activity."
FT /evidence="ECO:0000269|PubMed:17320160,
FT ECO:0000269|PubMed:17468742"
FT CONFLICT 16
FT /note="V -> L (in Ref. 2; BAG65494)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="E -> G (in Ref. 2; BAG65494)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="C -> Y (in Ref. 6; CAA82758)"
FT /evidence="ECO:0000305"
FT CONFLICT 1199
FT /note="A -> R (in Ref. 1; AAA61302)"
FT /evidence="ECO:0000305"
FT CONFLICT 1419
FT /note="I -> T (in Ref. 2; BAG65494)"
FT /evidence="ECO:0000305"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:2JRZ"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:2JRZ"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:2JRZ"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2JRZ"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:2JRZ"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:2JRZ"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:2JRZ"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:2JRZ"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:2JRZ"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:2JRZ"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:2JRZ"
FT HELIX 181..185
FT /evidence="ECO:0007829|PDB:2JRZ"
FT HELIX 394..409
FT /evidence="ECO:0007829|PDB:5FWJ"
FT HELIX 418..429
FT /evidence="ECO:0007829|PDB:5FWJ"
FT STRAND 437..445
FT /evidence="ECO:0007829|PDB:5FWJ"
FT HELIX 446..449
FT /evidence="ECO:0007829|PDB:5FWJ"
FT HELIX 464..471
FT /evidence="ECO:0007829|PDB:5FWJ"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:5FWJ"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:5FWJ"
FT HELIX 486..489
FT /evidence="ECO:0007829|PDB:5FWJ"
FT TURN 495..497
FT /evidence="ECO:0007829|PDB:5FWJ"
FT STRAND 501..505
FT /evidence="ECO:0007829|PDB:5FWJ"
FT STRAND 510..514
FT /evidence="ECO:0007829|PDB:5FWJ"
FT HELIX 517..519
FT /evidence="ECO:0007829|PDB:5FWJ"
FT STRAND 521..530
FT /evidence="ECO:0007829|PDB:5FWJ"
FT STRAND 532..536
FT /evidence="ECO:0007829|PDB:5FWJ"
FT HELIX 539..541
FT /evidence="ECO:0007829|PDB:5FWJ"
FT HELIX 542..552
FT /evidence="ECO:0007829|PDB:5FWJ"
FT HELIX 573..577
FT /evidence="ECO:0007829|PDB:5FWJ"
FT TURN 578..580
FT /evidence="ECO:0007829|PDB:5FWJ"
FT STRAND 584..588
FT /evidence="ECO:0007829|PDB:5FWJ"
FT STRAND 593..596
FT /evidence="ECO:0007829|PDB:5FWJ"
FT STRAND 602..617
FT /evidence="ECO:0007829|PDB:5FWJ"
FT HELIX 620..622
FT /evidence="ECO:0007829|PDB:5FWJ"
FT HELIX 623..636
FT /evidence="ECO:0007829|PDB:5FWJ"
FT HELIX 644..652
FT /evidence="ECO:0007829|PDB:5FWJ"
FT HELIX 655..657
FT /evidence="ECO:0007829|PDB:5FWJ"
FT HELIX 660..687
FT /evidence="ECO:0007829|PDB:5FWJ"
FT STRAND 692..694
FT /evidence="ECO:0007829|PDB:5FWJ"
FT HELIX 697..699
FT /evidence="ECO:0007829|PDB:5FWJ"
FT HELIX 702..704
FT /evidence="ECO:0007829|PDB:5FWJ"
FT TURN 708..710
FT /evidence="ECO:0007829|PDB:5FWJ"
FT STRAND 716..723
FT /evidence="ECO:0007829|PDB:5FWJ"
FT HELIX 731..733
FT /evidence="ECO:0007829|PDB:5FWJ"
FT HELIX 742..744
FT /evidence="ECO:0007829|PDB:5FWJ"
FT STRAND 745..751
FT /evidence="ECO:0007829|PDB:5FWJ"
FT HELIX 755..767
FT /evidence="ECO:0007829|PDB:5FWJ"
SQ SEQUENCE 1560 AA; 175720 MW; 5DC673D0091E7C87 CRC64;
MEPGSDDFLP PPECPVFEPS WAEFRDPLGY IAKIRPIAEK SGICKIRPPA DWQPPFAVEV
DNFRFTPRIQ RLNELEAQTR VKLNYLDQIA KFWEIQGSSL KIPNVERRIL DLYSLSKIVV
EEGGYEAICK DRRWARVAQR LNYPPGKNIG SLLRSHYERI VYPYEMYQSG ANLVQCNTRP
FDNEEKDKEY KPHSIPLRQS VQPSKFNSYG RRAKRLQPDP EPTEEDIEKN PELKKLQIYG
AGPKMMGLGL MAKDKTLRKK DKEGPECPPT VVVKEELGGD VKVESTSPKT FLESKEELSH
SPEPCTKMTM RLRRNHSNAQ FIESYVCRMC SRGDEDDKLL LCDGCDDNYH IFCLLPPLPE
IPKGVWRCPK CVMAECKRPP EAFGFEQATR EYTLQSFGEM ADSFKADYFN MPVHMVPTEL
VEKEFWRLVN SIEEDVTVEY GADIHSKEFG SGFPVSDSKR HLTPEEEEYA TSGWNLNVMP
VLEQSVLCHI NADISGMKVP WLYVGMVFSA FCWHIEDHWS YSINYLHWGE PKTWYGVPSL
AAEHLEEVMK KLTPELFDSQ PDLLHQLVTL MNPNTLMSHG VPVVRTNQCA GEFVITFPRA
YHSGFNQGYN FAEAVNFCTA DWLPAGRQCI EHYRRLRRYC VFSHEELICK MAACPEKLDL
NLAAAVHKEM FIMVQEERRL RKALLEKGIT EAEREAFELL PDDERQCIKC KTTCFLSALA
CYDCPDGLVC LSHINDLCKC SSSRQYLRYR YTLDELPAML HKLKVRAESF DTWANKVRVA
LEVEDGRKRS LEELRALESE ARERRFPNSE LLQQLKNCLS EAEACVSRAL GLVSGQEAGP
HRVAGLQMTL TELRAFLDQM NNLPCAMHQI GDVKGVLEQV EAYQAEAREA LASLPSSPGL
LQSLLERGRQ LGVEVPEAQQ LQRQVEQARW LDEVKRTLAP SARRGTLAVM RGLLVAGASV
APSPAVDKAQ AELQELLTIA ERWEEKAHLC LEARQKHPPA TLEAIIREAE NIPVHLPNIQ
ALKEALAKAR AWIADVDEIQ NGDHYPCLDD LEGLVAVGRD LPVGLEELRQ LELQVLTAHS
WREKASKTFL KKNSCYTLLE VLCPCADAGS DSTKRSRWME KELGLYKSDT ELLGLSAQDL
RDPGSVIVAF KEGEQKEKEG ILQLRRTNSA KPSPLASSST ASSTTSICVC GQVLAGAGAL
QCDLCQDWFH GRCVSVPRLL SSPRPNPTSS PLLAWWEWDT KFLCPLCMRS RRPRLETILA
LLVALQRLPV RLPEGEALQC LTERAISWQG RARQALASED VTALLGRLAE LRQRLQAEPR
PEEPPNYPAA PASDPLREGS GKDMPKVQGL LENGDSVTSP EKVAPEEGSG KRDLELLSSL
LPQLTGPVLE LPEATRAPLE ELMMEGDLLE VTLDENHSIW QLLQAGQPPD LERIRTLLEL
EKAERHGSRA RGRALERRRR RKVDRGGEGD DPAREELEPK RVRSSGPEAE EVQEEEELEE
ETGGEGPPAP IPTTGSPSTQ ENQNGLEPAE GTTSGPSAPF STLTPRLHLP CPQQPPQQQL
