HAIR_HUMAN
ID HAIR_HUMAN Reviewed; 1189 AA.
AC O43593; Q6GS30; Q96H33; Q9NPE1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 5.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Lysine-specific demethylase hairless;
DE EC=1.14.11.65 {ECO:0000269|PubMed:24334705};
DE AltName: Full=[histone H3]-dimethyl-L-lysine(9) demethylase hairless {ECO:0000305};
GN Name=HR;
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), VARIANT ASP-337, AND VARIANT ALUNC
RP ALA-1022.
RX PubMed=9445480; DOI=10.1126/science.279.5351.720;
RA Ahmad W., ul Haque M.F., Brancolini V., Tsou H.C., Ul Haque S., Lam H.,
RA Aita V.M., Owen J., Deblaquiere M., Frank J., Cserhalmi-Friedman P.B.,
RA Leask A., McGrath J.A., Peacocke M., Ahmad M., Ott J., Christiano A.M.;
RT "Alopecia universalis associated with a mutation in the human hairless
RT gene.";
RL Science 279:720-724(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SEQUENCE REVISION TO 572 AND 774,
RP TISSUE SPECIFICITY, AND VARIANT ASP-337.
RC TISSUE=Peripheral blood leukocyte, and Skin fibroblast;
RX PubMed=10051399; DOI=10.1006/geno.1998.5699;
RA Ahmad W., Zlotogorski A., Panteleyev A.A., Lam H., Ahmad M., ul Haque M.F.,
RA Abdallah H.M., Dragan L., Christiano A.M.;
RT "Genomic organization of the human hairless gene (HR) and identification of
RT a mutation underlying congenital atrichia in an Arab Palestinian family.";
RL Genomics 56:141-148(1999).
RN [3]
RP SEQUENCE REVISION TO 446 AND 584.
RA Christiano A.M.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), VARIANT
RP ASP-337, VARIANT ALUNC ASP-1136, AND TISSUE SPECIFICITY.
RC TISSUE=Brain, Fetal brain, and Peripheral blood leukocyte;
RX PubMed=9736769; DOI=10.1093/hmg/7.11.1671;
RA Cichon S., Anker M., Vogt I.R., Rohleder H., Putzstuck M., Hillmer A.,
RA Farooq S.A., Al-Dhafri K.S., Ahmad M., Haque S., Rietschel M., Propping P.,
RA Kruse R., Noethen M.M.;
RT "Cloning, genomic organization, alternative transcripts and mutational
RT analysis of the gene responsible for autosomal recessive universal
RT congenital alopecia.";
RL Hum. Mol. Genet. 7:1671-1679(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 INVOLVEMENT IN HYPT4.
RX PubMed=19122663; DOI=10.1038/ng.276;
RA Wen Y., Liu Y., Xu Y., Zhao Y., Hua R., Wang K., Sun M., Li Y., Yang S.,
RA Zhang X.J., Kruse R., Cichon S., Betz R.C., Nothen M.M., van Steensel M.A.,
RA van Geel M., Steijlen P.M., Hohl D., Huber M., Dunnill G.S., Kennedy C.,
RA Messenger A., Munro C.S., Terrinoni A., Hovnanian A., Bodemer C.,
RA de Prost Y., Paller A.S., Irvine A.D., Sinclair R., Green J., Shang D.,
RA Liu Q., Luo Y., Jiang L., Chen H.D., Lo W.H., McLean W.H., He C.D.,
RA Zhang X.;
RT "Loss-of-function mutations of an inhibitory upstream ORF in the human
RT hairless transcript cause Marie Unna hereditary hypotrichosis.";
RL Nat. Genet. 41:228-233(2009).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANT ALUNC ASN-1012,
RP AND MUTAGENESIS OF VAL-1056.
RX PubMed=24334705; DOI=10.1096/fj.13-237677;
RA Liu L., Kim H., Casta A., Kobayashi Y., Shapiro L.S., Christiano A.M.;
RT "Hairless is a histone H3K9 demethylase.";
RL FASEB J. 28:1534-1542(2014).
RN [8]
RP VARIANT GLN-620.
RX PubMed=9758627; DOI=10.1086/302069;
RA Ahmad W., Irvine A.D., Lam H., Buckley C., Bingham E.A., Panteleyev A.A.,
RA Ahmad M., McGrath J.A., Christiano A.M.;
RT "A missense mutation in the zinc-finger domain of the human hairless gene
RT underlies congenital atrichia in a family of Irish travellers.";
RL Am. J. Hum. Genet. 63:984-991(1998).
RN [9]
RP VARIANT GLN-620.
RX PubMed=11410842; DOI=10.1086/321273;
RA Hillmer A.M., Kruse R., Betz R.C., Schumacher J., Heyn U., Propping P.,
RA Noethen M.M., Cichon S.;
RT "Variant 1859G-->A (Arg620Gln) of the 'hairless' gene: absence of
RT association with papular atrichia or androgenic alopecia.";
RL Am. J. Hum. Genet. 69:235-237(2001).
RN [10]
RP VARIANT ALUNC ASN-1012.
RX PubMed=12406339; DOI=10.1046/j.1523-1747.2002.00268.x;
RA Klein I., Bergman R., Indelman M., Sprecher E.;
RT "A novel missense mutation affecting the human hairless thyroid receptor
RT interacting domain 2 causes congenital atrichia.";
RL J. Invest. Dermatol. 119:920-922(2002).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-633.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [12]
RP INVOLVEMENT IN HYPT4.
RX PubMed=24961381; DOI=10.1111/ijd.12545;
RA Yun S.K., Cho Y.G., Song K.H., Hwang S.R., Kim Yoon S.J., Choi K.W.,
RA Kim H.U., Park J.;
RT "Identification of a novel U2HR mutation in a Korean woman with Marie Unna
RT hereditary hypotrichosis.";
RL Int. J. Dermatol. 53:1358-1361(2014).
CC -!- FUNCTION: Histone demethylase that specifically demethylates both
CC mono- and dimethylated 'Lys-9' of histone H3. May act as a
CC transcription regulator controlling hair biology (via targeting of
CC collagens), neural activity, and cell cycle.
CC {ECO:0000269|PubMed:24334705}.
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:24334705};
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 O43593; Q8NFV4-4: ABHD11; NbExp=3; IntAct=EBI-2880706, EBI-12318443;
CC O43593; Q9Y4X0-3: AMMECR1; NbExp=3; IntAct=EBI-2880706, EBI-12823597;
CC O43593; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-2880706, EBI-12811889;
CC O43593; Q9H5F2: C11orf1; NbExp=3; IntAct=EBI-2880706, EBI-718615;
CC O43593; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-2880706, EBI-11976299;
CC O43593; Q9BYD5: CNFN; NbExp=3; IntAct=EBI-2880706, EBI-12819063;
CC O43593; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2880706, EBI-3867333;
CC O43593; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-2880706, EBI-11978259;
CC O43593; P57678: GEMIN4; NbExp=3; IntAct=EBI-2880706, EBI-356700;
CC O43593; P49639: HOXA1; NbExp=3; IntAct=EBI-2880706, EBI-740785;
CC O43593; Q0VD86: INCA1; NbExp=3; IntAct=EBI-2880706, EBI-6509505;
CC O43593; Q9BS75: KLHL20; NbExp=3; IntAct=EBI-2880706, EBI-10693436;
CC O43593; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-2880706, EBI-1052037;
CC O43593; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-2880706, EBI-11953846;
CC O43593; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-2880706, EBI-11992140;
CC O43593; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-2880706, EBI-9996449;
CC O43593; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-2880706, EBI-3957694;
CC O43593; O15496: PLA2G10; NbExp=3; IntAct=EBI-2880706, EBI-726466;
CC O43593; P10745: RBP3; NbExp=3; IntAct=EBI-2880706, EBI-12806054;
CC O43593; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-2880706, EBI-11959123;
CC O43593; O43610: SPRY3; NbExp=3; IntAct=EBI-2880706, EBI-12290641;
CC O43593; Q86WV8: TSC1; NbExp=3; IntAct=EBI-2880706, EBI-12806590;
CC O43593; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-2880706, EBI-12030590;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Long;
CC IsoId=O43593-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=O43593-2; Sequence=VSP_004276;
CC -!- TISSUE SPECIFICITY: Strongest expression of isoforms 1 and 2 is seen in
CC the small intestine, weaker expression in brain and colon, and trace
CC expression is found in liver, pancreas, spleen, thymus, stomach,
CC salivary gland, appendix and trachea. Isoform 1 is always the most
CC abundant. Isoform 1 is exclusively expressed at low levels in kidney
CC and testis. Isoform 2 is exclusively expressed at high levels in the
CC skin. {ECO:0000269|PubMed:10051399, ECO:0000269|PubMed:9736769}.
CC -!- DOMAIN: Contains two Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. The LXXLL
CC motifs are essential for the association with nuclear receptors (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The JmjC domain and the C6-type zinc-finger are required for
CC the demethylation activity. {ECO:0000250}.
CC -!- DISEASE: Alopecia universalis congenita (ALUNC) [MIM:203655]: A rare
CC disorder characterized by loss of hair from the entire body. No hair
CC are present in hair follicles on skin biopsy.
CC {ECO:0000269|PubMed:12406339, ECO:0000269|PubMed:24334705,
CC ECO:0000269|PubMed:9445480, ECO:0000269|PubMed:9736769}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Atrichia with papular lesions (APL) [MIM:209500]: An autosomal
CC recessive disease characterized by papillary lesions over most of the
CC body and almost complete absence of hair. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Hypotrichosis 4 (HYPT4) [MIM:146550]: An autosomal dominant
CC condition characterized by reduced amount of hair, alopecia, little or
CC no eyebrows, eyelashes or body hair, and coarse, wiry, twisted hair in
CC early childhood. {ECO:0000269|PubMed:19122663,
CC ECO:0000269|PubMed:24961381}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AF039196; AAC32258.3; -; mRNA.
DR EMBL; AJ277249; CAB87577.2; -; Genomic_DNA.
DR EMBL; AJ277250; CAB87577.2; JOINED; Genomic_DNA.
DR EMBL; AJ277251; CAB87577.2; JOINED; Genomic_DNA.
DR EMBL; AJ277252; CAB87577.2; JOINED; Genomic_DNA.
DR EMBL; AJ277253; CAB87577.2; JOINED; Genomic_DNA.
DR EMBL; AJ400825; CAB87577.2; JOINED; Genomic_DNA.
DR EMBL; AJ400826; CAB87577.2; JOINED; Genomic_DNA.
DR EMBL; AJ400827; CAB87577.2; JOINED; Genomic_DNA.
DR EMBL; AJ400828; CAB87577.2; JOINED; Genomic_DNA.
DR EMBL; AJ400829; CAB87577.2; JOINED; Genomic_DNA.
DR EMBL; AJ400830; CAB87577.2; JOINED; Genomic_DNA.
DR EMBL; AJ400831; CAB87577.2; JOINED; Genomic_DNA.
DR EMBL; AJ400832; CAB87577.2; JOINED; Genomic_DNA.
DR EMBL; AJ400833; CAB87577.2; JOINED; Genomic_DNA.
DR EMBL; AJ400834; CAB87577.2; JOINED; Genomic_DNA.
DR EMBL; AJ400835; CAB87577.2; JOINED; Genomic_DNA.
DR EMBL; AJ400836; CAB87577.2; JOINED; Genomic_DNA.
DR EMBL; AJ400837; CAB87577.2; JOINED; Genomic_DNA.
DR EMBL; AJ277165; CAB86602.1; -; mRNA.
DR EMBL; BC067128; AAH67128.1; -; mRNA.
DR CCDS; CCDS6022.1; -. [O43593-1]
DR CCDS; CCDS6023.1; -. [O43593-2]
DR RefSeq; NP_005135.2; NM_005144.4. [O43593-1]
DR RefSeq; NP_060881.2; NM_018411.4. [O43593-2]
DR AlphaFoldDB; O43593; -.
DR SMR; O43593; -.
DR BioGRID; 120917; 46.
DR ELM; O43593; -.
DR IntAct; O43593; 36.
DR MINT; O43593; -.
DR STRING; 9606.ENSP00000370826; -.
DR iPTMnet; O43593; -.
DR PhosphoSitePlus; O43593; -.
DR BioMuta; HR; -.
DR EPD; O43593; -.
DR jPOST; O43593; -.
DR MassIVE; O43593; -.
DR PaxDb; O43593; -.
DR PeptideAtlas; O43593; -.
DR PRIDE; O43593; -.
DR ProteomicsDB; 49067; -. [O43593-1]
DR ProteomicsDB; 49068; -. [O43593-2]
DR Antibodypedia; 9297; 190 antibodies from 27 providers.
DR DNASU; 55806; -.
DR Ensembl; ENST00000312841.9; ENSP00000326765.8; ENSG00000168453.16. [O43593-2]
DR Ensembl; ENST00000381418.9; ENSP00000370826.4; ENSG00000168453.16. [O43593-1]
DR Ensembl; ENST00000680789.1; ENSP00000505181.1; ENSG00000168453.16. [O43593-1]
DR GeneID; 55806; -.
DR KEGG; hsa:55806; -.
DR MANE-Select; ENST00000381418.9; ENSP00000370826.4; NM_005144.5; NP_005135.2.
DR UCSC; uc003xas.4; human. [O43593-1]
DR CTD; 55806; -.
DR DisGeNET; 55806; -.
DR GeneCards; HR; -.
DR HGNC; HGNC:5172; HR.
DR HPA; ENSG00000168453; Tissue enhanced (esophagus, skin).
DR MalaCards; HR; -.
DR MIM; 146550; phenotype.
DR MIM; 203655; phenotype.
DR MIM; 209500; phenotype.
DR MIM; 602302; gene.
DR neXtProt; NX_O43593; -.
DR OpenTargets; ENSG00000168453; -.
DR Orphanet; 701; Alopecia universalis.
DR Orphanet; 86819; Atrichia with papular lesions.
DR Orphanet; 444; Marie Unna hereditary hypotrichosis.
DR PharmGKB; PA29443; -.
DR VEuPathDB; HostDB:ENSG00000168453; -.
DR eggNOG; KOG1356; Eukaryota.
DR GeneTree; ENSGT00940000161687; -.
DR HOGENOM; CLU_294677_0_0_1; -.
DR InParanoid; O43593; -.
DR OMA; LACHSQE; -.
DR OrthoDB; 1324479at2759; -.
DR PhylomeDB; O43593; -.
DR TreeFam; TF324723; -.
DR BioCyc; MetaCyc:ENSG00000168453-MON; -.
DR BRENDA; 1.14.11.65; 2681.
DR PathwayCommons; O43593; -.
DR SignaLink; O43593; -.
DR SIGNOR; O43593; -.
DR BioGRID-ORCS; 55806; 14 hits in 1087 CRISPR screens.
DR GeneWiki; HR_(gene); -.
DR GenomeRNAi; 55806; -.
DR Pharos; O43593; Tbio.
DR PRO; PR:O43593; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O43593; protein.
DR Bgee; ENSG00000168453; Expressed in skin of abdomen and 169 other tissues.
DR ExpressionAtlas; O43593; baseline and differential.
DR Genevisible; O43593; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0140683; F:histone H3-di/monomethyl-lysine-9 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR PANTHER; PTHR12549; PTHR12549; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; DNA-binding; Hypotrichosis; Iron;
KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1189
FT /note="Lysine-specific demethylase hairless"
FT /id="PRO_0000083890"
FT DOMAIN 946..1157
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 600..625
FT /note="C6-type"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 566..570
FT /note="LXXLL motif 1"
FT MOTIF 758..762
FT /note="LXXLL motif 2"
FT COMPBIAS 453..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1007
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 1009
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 1125
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT VAR_SEQ 1072..1126
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9736769"
FT /id="VSP_004276"
FT VARIANT 337
FT /note="G -> D (in dbSNP:rs12675375)"
FT /evidence="ECO:0000269|PubMed:10051399,
FT ECO:0000269|PubMed:9445480, ECO:0000269|PubMed:9736769"
FT /id="VAR_027806"
FT VARIANT 526
FT /note="L -> P (in dbSNP:rs56140348)"
FT /id="VAR_061664"
FT VARIANT 620
FT /note="R -> Q (in dbSNP:rs117197822)"
FT /evidence="ECO:0000269|PubMed:11410842,
FT ECO:0000269|PubMed:9758627"
FT /id="VAR_005265"
FT VARIANT 633
FT /note="R -> Q (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035927"
FT VARIANT 924
FT /note="P -> L (in dbSNP:rs11990421)"
FT /id="VAR_027807"
FT VARIANT 1012
FT /note="D -> N (in ALUNC; affects binding to thyroid hormone
FT receptor; Markedly diminished histone demethylase activity;
FT dbSNP:rs121434451)"
FT /evidence="ECO:0000269|PubMed:12406339,
FT ECO:0000269|PubMed:24334705"
FT /id="VAR_016222"
FT VARIANT 1022
FT /note="T -> A (in ALUNC; dbSNP:rs7014851)"
FT /evidence="ECO:0000269|PubMed:9445480"
FT /id="VAR_005266"
FT VARIANT 1136
FT /note="V -> D (in ALUNC; dbSNP:rs121434448)"
FT /evidence="ECO:0000269|PubMed:9736769"
FT /id="VAR_005267"
FT MUTAGEN 1056
FT /note="V->M: Markedly diminishes histone demethylase
FT activity."
FT /evidence="ECO:0000269|PubMed:24334705"
SQ SEQUENCE 1189 AA; 127495 MW; 67A4B95A01063387 CRC64;
MESTPSFLKG TPTWEKTAPE NGIVRQEPGS PPRDGLHHGP LCLGEPAPFW RGVLSTPDSW
LPPGFPQGPK DMLPLVEGEG PQNGERKVNW LGSKEGLRWK EAMLTHPLAF CGPACPPRCG
PLMPEHSGGH LKSDPVAFRP WHCPFLLETK ILERAPFWVP TCLPPYLVSG LPPEHPCDWP
LTPHPWVYSG GQPKVPSAFS LGSKGFYYKD PSIPRLAKEP LAAAEPGLFG LNSGGHLQRA
GEAERPSLHQ RDGEMGAGRQ QNPCPLFLGQ PDTVPWTSWP ACPPGLVHTL GNVWAGPGDG
NLGYQLGPPA TPRCPSPEPP VTQRGCCSSY PPTKGGGLGP CGKCQEGLEG GASGASEPSE
EVNKASGPRA CPPSHHTKLK KTWLTRHSEQ FECPRGCPEV EERPVARLRA LKRAGSPEVQ
GAMGSPAPKR PPDPFPGTAE QGAGGWQEVR DTSIGNKDVD SGQHDEQKGP QDGQASLQDP
GLQDIPCLAL PAKLAQCQSC AQAAGEGGGH ACHSQQVRRS PLGGELQQEE DTATNSSSEE
GPGSGPDSRL STGLAKHLLS GLGDRLCRLL RREREALAWA QREGQGPAVT EDSPGIPRCC
SRCHHGLFNT HWRCPRCSHR LCVACGRVAG TGRAREKAGF QEQSAEECTQ EAGHAACSLM
LTQFVSSQAL AELSTAMHQV WVKFDIRGHC PCQADARVWA PGDAGQQKES TQKTPPTPQP
SCNGDTHRTK SIKEETPDSA ETPAEDRAGR GPLPCPSLCE LLASTAVKLC LGHERIHMAF
APVTPALPSD DRITNILDSI IAQVVERKIQ EKALGPGLRA GPGLRKGLGL PLSPVRPRLP
PPGALLWLQE PQPCPRRGFH LFQEHWRQGQ PVLVSGIQRT LQGNLWGTEA LGALGGQVQA
LSPLGPPQPS SLGSTTFWEG FSWPELRPKS DEGSVLLLHR ALGDEDTSRV ENLAASLPLP
EYCALHGKLN LASYLPPGLA LRPLEPQLWA AYGVSPHRGH LGTKNLCVEV ADLVSILVHA
DTPLPAWHRA QKDFLSGLDG EGLWSPGSQV STVWHVFRAQ DAQRIRRFLQ MVCPAGAGAL
EPGAPGSCYL DAGLRRRLRE EWGVSCWTLL QAPGEAVLVP AGAPHQVQGL VSTVSVTQHF
LSPETSALSA QLCHQGPSLP PDCHLLYAQM DWAVFQAVKV AVGTLQEAK
