ID KDM1B_HUMAN Reviewed; 822 AA. AC Q8NB78; A2A2C5; A2A2C6; Q5TGV3; Q6AI15; Q6ZUU4; Q8N258; Q96EL7; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 3. DT 27-MAR-2024, entry version 171. DE RecName: Full=Lysine-specific histone demethylase 2 {ECO:0000305}; DE EC=1.14.99.66 {ECO:0000269|PubMed:23260659, ECO:0000269|PubMed:23357850, ECO:0000269|PubMed:30970244}; DE AltName: Full=Flavin-containing amine oxidase domain-containing protein 1; DE AltName: Full=Lysine-specific histone demethylase 1B {ECO:0000305}; GN Name=KDM1B {ECO:0000312|HGNC:HGNC:21577}; GN Synonyms=AOF1, C6orf193, LSD2 {ECO:0000303|PubMed:30970244}; 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] (ISOFORMS 2 AND 4), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 185-822 (ISOFORM 1). RC TISSUE=Brain, and Tongue; 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=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 624-822 (ISOFORM 1). RC TISSUE=Cervix; 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-247, AND RP IDENTIFICATION BY 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-17; SER-26 AND RP SER-247, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 30-822 IN COMPLEX WITH HISTONE H3 RP ANALOG PEPTIDE; FAD AND ZINC, AND MUTAGENESIS OF 48-LYS-LYS-49; RP 51-ARG-LYS-52; CYS-53; TRP-82; HIS-84; HIS-90; ARG-101; 114-LYS-LYS-115; RP TRP-139; TRP-150; ARG-151; CYS-185; 318-TRP-TYR-319; 340-LEU-VAL-341; RP 361-LEU-ILE-362; 443-ILE-ASN-444; ASN-542; LEU-543; CYS-547; TRP-559 AND RP TYR-767. RX PubMed=23266887; DOI=10.1038/cr.2012.177; RA Zhang Q., Qi S., Xu M., Yu L., Tao Y., Deng Z., Wu W., Li J., Chen Z., RA Wong J.; RT "Structure-function analysis reveals a novel mechanism for regulation of RT histone demethylase LSD2/AOF1/KDM1b."; RL Cell Res. 23:225-241(2013). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 51-822 IN COMPLEX WITH FAD AND RP ZINC, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 273-TYR--CYS-278; RP 285-ARG--ASP-287; GLU-563 AND LYS-661. RX PubMed=23357850; DOI=10.1038/cr.2013.17; RA Chen F., Yang H., Dong Z., Fang J., Wang P., Zhu T., Gong W., Fang R., RA Shi Y.G., Li Z., Xu Y.; RT "Structural insight into substrate recognition by histone demethylase RT LSD2/KDM1b."; RL Cell Res. 23:306-309(2013). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 51-822 IN COMPLEX WITH GLYR1; RP HISTONE H3 PEPTIDE; FAD; ZINC AND FAD ANALOG, FUNCTION, CATALYTIC ACTIVITY, RP INTERACTION WITH GLYR1, AND ACTIVITY REGULATION. RX PubMed=23260659; DOI=10.1016/j.molcel.2012.11.019; RA Fang R., Chen F., Dong Z., Hu D., Barbera A.J., Clark E.A., Fang J., RA Yang Y., Mei P., Rutenberg M., Li Z., Zhang Y., Xu Y., Yang H., Wang P., RA Simon M.D., Zhou Q., Li J., Marynick M.P., Li X., Lu H., Kaiser U.B., RA Kingston R.E., Xu Y., Shi Y.G.; RT "LSD2/KDM1B and its cofactor NPAC/GLYR1 endow a structural and molecular RT model for regulation of H3K4 demethylation."; RL Mol. Cell 49:558-570(2013). RN [13] {ECO:0007744|PDB:6R1U, ECO:0007744|PDB:6R25} RP STRUCTURE BY ELECTRON MICROSCOPY (4.36 ANGSTROMS) OF 51-822 IN COMPLEX WIH RP NUCLEOSOMES AND GLYR1, CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL RP PROPERTIES, ACTIVITY REGULATION, INTERACTION WITH GLYR1, COFACTOR, AND RP MUTAGENESIS OF HIS-103; LYS-104; LYS-109; LYS-114; LYS-115; LYS-122; RP ARG-302 AND 481-LYS-ARG-482. RX PubMed=30970244; DOI=10.1016/j.celrep.2019.03.061; RA Marabelli C., Marrocco B., Pilotto S., Chittori S., Picaud S., Marchese S., RA Ciossani G., Forneris F., Filippakopoulos P., Schoehn G., Rhodes D., RA Subramaniam S., Mattevi A.; RT "A Tail-Based Mechanism Drives Nucleosome Demethylation by the LSD2/NPAC RT Multimeric Complex."; RL Cell Rep. 27:387-399.e7(2019). CC -!- FUNCTION: Histone demethylase that demethylates 'Lys-4' of histone H3, CC a specific tag for epigenetic transcriptional activation, thereby CC acting as a corepressor. Required for de novo DNA methylation of a CC subset of imprinted genes during oogenesis. Acts by oxidizing the CC substrate by FAD to generate the corresponding imine that is CC subsequently hydrolyzed. Demethylates both mono- and di-methylated CC 'Lys-4' of histone H3. Has no effect on tri-methylated 'Lys-4', mono-, CC di- or tri-methylated 'Lys-9', mono-, di- or tri-methylated 'Lys-27', CC mono-, di- or tri-methylated 'Lys-36' of histone H3, or on mono-, CC di- or tri-methylated 'Lys-20' of histone H4. Alone, it is unable to CC demethylate H3K4me on nucleosomes and requires the presence of GLYR1 to CC achieve such activity, they form a multifunctional enzyme complex that CC modifies transcribed chromatin and facilitates Pol II transcription CC through nucleosomes (PubMed:30970244). {ECO:0000269|PubMed:23260659, CC ECO:0000269|PubMed:23357850, ECO:0000269|PubMed:30970244}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 A + 2 H2O + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] = 2 CC AH2 + 2 formaldehyde + L-lysyl(4)-[histone H3]; Xref=Rhea:RHEA:60244, CC Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:13193, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499, CC ChEBI:CHEBI:29969, ChEBI:CHEBI:61976; EC=1.14.99.66; CC Evidence={ECO:0000269|PubMed:23260659, ECO:0000269|PubMed:23357850, CC ECO:0000269|PubMed:30970244}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60245; CC Evidence={ECO:0000305|PubMed:30970244}; CC -!- CATALYTIC ACTIVITY: CC Reaction=A + H2O + N(6)-methyl-L-lysyl(4)-[histone H3] = AH2 + CC formaldehyde + L-lysyl(4)-[histone H3]; Xref=Rhea:RHEA:60256, CC Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:13193, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499, CC ChEBI:CHEBI:29969, ChEBI:CHEBI:61929; CC Evidence={ECO:0000269|PubMed:30970244}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60257; CC Evidence={ECO:0000305|PubMed:30970244}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000269|PubMed:23260659, ECO:0000269|PubMed:23266887, CC ECO:0000269|PubMed:23357850, ECO:0000269|PubMed:30970244}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:23260659, ECO:0000269|PubMed:23266887, CC ECO:0000269|PubMed:23357850, ECO:0000269|PubMed:30970244}; CC Note=Binds 3 Zn(2+) ions per subunit. {ECO:0000269|PubMed:23260659, CC ECO:0000269|PubMed:23266887, ECO:0000269|PubMed:23357850, CC ECO:0000269|PubMed:30970244}; CC -!- ACTIVITY REGULATION: Histone H3K4me1 and H3K4me2 demethylase activity CC is inhibited by DNA, this inhibition is released in complex with GLYR1. CC {ECO:0000269|PubMed:23260659, ECO:0000269|PubMed:30970244}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.34 uM for N(6)-methyl-L-lysyl-[histone H3] CC {ECO:0000269|PubMed:30970244}; CC KM=0.99 uM for N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] CC {ECO:0000269|PubMed:30970244}; CC Note=Kcat is 0.56 min(-1) for N(6)-methyl-L-lysyl(4)-[histone H3] and CC 1.30 min(-1) for N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] as CC substrates. {ECO:0000269|PubMed:30970244}; CC -!- SUBUNIT: Interacts with its cofactor GLYR1 at nucleosomes; this CC interaction stimulates H3K4me1 and H3K4me2 demethylation CC (PubMed:30970244, PubMed:23260659). In contrast to KDM1A, does not form CC a complex with RCOR1/CoREST (Probable). {ECO:0000269|PubMed:23260659, CC ECO:0000269|PubMed:30970244, ECO:0000305|PubMed:30970244}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:30970244}. Chromosome CC {ECO:0000305|PubMed:30970244}. Note=Found in actively RNAPolII- CC transcribed gene bodies. {ECO:0000305|PubMed:30970244}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8NB78-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8NB78-2; Sequence=VSP_019964, VSP_019965; CC Name=4; CC IsoId=Q8NB78-4; Sequence=VSP_019963; CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC03663.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK091217; BAC03612.1; -; mRNA. DR EMBL; AK091428; BAC03663.1; ALT_INIT; mRNA. DR EMBL; AK125318; BAC86124.1; -; mRNA. DR EMBL; AL031774; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL589723; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471087; EAW55401.1; -; Genomic_DNA. DR EMBL; CR627410; CAH10499.1; -; mRNA. DR CCDS; CCDS34343.1; -. [Q8NB78-2] DR CCDS; CCDS93866.1; -. [Q8NB78-1] DR RefSeq; NP_694587.3; NM_153042.3. [Q8NB78-2] DR RefSeq; XP_005248983.1; XM_005248926.1. DR PDB; 4FWE; X-ray; 2.13 A; A=30-822. DR PDB; 4FWF; X-ray; 2.70 A; A=30-822. DR PDB; 4FWJ; X-ray; 2.90 A; A/B=30-822. DR PDB; 4GU0; X-ray; 3.10 A; A/B/C/D=51-822. DR PDB; 4GU1; X-ray; 2.94 A; A/B=51-822. DR PDB; 4GUR; X-ray; 2.51 A; A=51-822. DR PDB; 4GUS; X-ray; 2.23 A; A=51-822. DR PDB; 4GUT; X-ray; 2.00 A; A=51-822. DR PDB; 4GUU; X-ray; 2.30 A; A=51-822. DR PDB; 4HSU; X-ray; 1.99 A; A=51-822. DR PDB; 6R1U; EM; 4.36 A; K=51-822. DR PDB; 6R25; EM; 4.61 A; K=51-822. DR PDB; 7XE1; X-ray; 2.07 A; A/B=30-822. DR PDB; 7XE2; X-ray; 2.05 A; A/B=30-822. DR PDB; 7XE3; X-ray; 2.82 A; A/B=30-822. DR PDBsum; 4FWE; -. DR PDBsum; 4FWF; -. DR PDBsum; 4FWJ; -. DR PDBsum; 4GU0; -. DR PDBsum; 4GU1; -. DR PDBsum; 4GUR; -. DR PDBsum; 4GUS; -. DR PDBsum; 4GUT; -. DR PDBsum; 4GUU; -. DR PDBsum; 4HSU; -. DR PDBsum; 6R1U; -. DR PDBsum; 6R25; -. DR PDBsum; 7XE1; -. DR PDBsum; 7XE2; -. DR PDBsum; 7XE3; -. DR AlphaFoldDB; Q8NB78; -. DR EMDB; EMD-4705; -. DR EMDB; EMD-4710; -. DR SASBDB; Q8NB78; -. DR SMR; Q8NB78; -. DR BioGRID; 128743; 58. DR IntAct; Q8NB78; 26. DR MINT; Q8NB78; -. DR BindingDB; Q8NB78; -. DR ChEMBL; CHEMBL1938208; -. DR DrugCentral; Q8NB78; -. DR GlyGen; Q8NB78; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8NB78; -. DR PhosphoSitePlus; Q8NB78; -. DR SwissPalm; Q8NB78; -. DR BioMuta; KDM1B; -. DR DMDM; 317373434; -. DR EPD; Q8NB78; -. DR jPOST; Q8NB78; -. DR MassIVE; Q8NB78; -. DR MaxQB; Q8NB78; -. DR PeptideAtlas; Q8NB78; -. DR ProteomicsDB; 72745; -. [Q8NB78-1] DR ProteomicsDB; 72746; -. [Q8NB78-2] DR ProteomicsDB; 72747; -. [Q8NB78-4] DR Pumba; Q8NB78; -. DR Antibodypedia; 25190; 178 antibodies from 26 providers. DR DNASU; 221656; -. DR Ensembl; ENST00000297792.9; ENSP00000297792.5; ENSG00000165097.16. [Q8NB78-2] DR Ensembl; ENST00000650836.2; ENSP00000499208.1; ENSG00000165097.16. [Q8NB78-1] DR GeneID; 221656; -. DR KEGG; hsa:221656; -. DR MANE-Select; ENST00000650836.2; ENSP00000499208.1; NM_001364614.2; NP_001351543.1. DR UCSC; uc003ncn.2; human. [Q8NB78-1] DR AGR; HGNC:21577; -. DR CTD; 221656; -. DR DisGeNET; 221656; -. DR GeneCards; KDM1B; -. DR HGNC; HGNC:21577; KDM1B. DR HPA; ENSG00000165097; Low tissue specificity. DR MIM; 613081; gene. DR neXtProt; NX_Q8NB78; -. DR OpenTargets; ENSG00000165097; -. DR PharmGKB; PA162379723; -. DR PharmGKB; PA165617946; -. DR VEuPathDB; HostDB:ENSG00000165097; -. DR eggNOG; KOG0029; Eukaryota. DR GeneTree; ENSGT00940000157751; -. DR InParanoid; Q8NB78; -. DR OrthoDB; 5402444at2759; -. DR PhylomeDB; Q8NB78; -. DR TreeFam; TF352593; -. DR BioCyc; MetaCyc:ENSG00000165097-MONOMER; -. DR PathwayCommons; Q8NB78; -. DR Reactome; R-HSA-3214842; HDMs demethylate histones. DR Reactome; R-HSA-5689603; UCH proteinases. DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux. DR SignaLink; Q8NB78; -. DR BioGRID-ORCS; 221656; 22 hits in 1176 CRISPR screens. DR ChiTaRS; KDM1B; human. DR GenomeRNAi; 221656; -. DR Pharos; Q8NB78; Tbio. DR PRO; PR:Q8NB78; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q8NB78; Protein. DR Bgee; ENSG00000165097; Expressed in secondary oocyte and 174 other cell types or tissues. DR ExpressionAtlas; Q8NB78; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:UniProt. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0000786; C:nucleosome; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central. DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB. DR GO; GO:0140682; F:FAD-dependent H3K4me/H3K4me3 demethylase activity; IDA:UniProtKB. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central. DR GO; GO:0042393; F:histone binding; IDA:UniProtKB. DR GO; GO:0032452; F:histone demethylase activity; TAS:Reactome. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0044726; P:epigenetic programing of female pronucleus; IEA:Ensembl. DR GO; GO:0071514; P:genomic imprinting; ISS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IDA:UniProt. DR Gene3D; 3.30.40.100; -; 1. DR Gene3D; 3.90.660.10; -; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR IDEAL; IID00487; -. DR InterPro; IPR002937; Amino_oxidase. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR007526; SWIRM. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR011124; Znf_CW. DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1. DR PANTHER; PTHR10742:SF413; LYSINE-SPECIFIC HISTONE DEMETHYLASE 1B; 1. DR Pfam; PF01593; Amino_oxidase; 1. DR Pfam; PF04433; SWIRM; 1. DR Pfam; PF07496; zf-CW; 1. DR PRINTS; PR00419; ADXRDTASE. DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR SUPFAM; SSF46689; Homeodomain-like; 1. DR PROSITE; PS50934; SWIRM; 1. DR PROSITE; PS51050; ZF_CW; 1. DR Genevisible; Q8NB78; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromatin regulator; Chromosome; KW Developmental protein; FAD; Flavoprotein; Metal-binding; Nucleus; KW Oxidoreductase; Phosphoprotein; Reference proteome; Repressor; KW Transcription; Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..822 FT /note="Lysine-specific histone demethylase 2" FT /id="PRO_0000247336" FT DOMAIN 275..373 FT /note="SWIRM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247" FT ZN_FING 133..193 FT /note="CW-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454" FT REGION 1..47 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 273..292 FT /note="GLYR1-binding" FT /evidence="ECO:0000269|PubMed:23260659, FT ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS, FT ECO:0007744|PDB:4GUT, ECO:0007744|PDB:4GUU" FT REGION 438..467 FT /note="Histone H3-binding" FT /evidence="ECO:0000269|PubMed:23260659, FT ECO:0000269|PubMed:23266887, ECO:0007744|PDB:4FWF, FT ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS" FT REGION 487..498 FT /note="Histone H3-binding" FT /evidence="ECO:0000269|PubMed:23260659, FT ECO:0000269|PubMed:23266887, ECO:0007744|PDB:4FWF, FT ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS" FT REGION 538..572 FT /note="Histone H3-binding" FT /evidence="ECO:0000269|PubMed:23260659, FT ECO:0000269|PubMed:23266887, ECO:0007744|PDB:4FWF, FT ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS" FT REGION 564..566 FT /note="GLYR1-binding" FT /evidence="ECO:0000269|PubMed:23260659, FT ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS, FT ECO:0007744|PDB:4GUT, ECO:0007744|PDB:4GUU" FT REGION 798..814 FT /note="GLYR1-binding" FT /evidence="ECO:0000269|PubMed:23260659, FT ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS, FT ECO:0007744|PDB:4GUT, ECO:0007744|PDB:4GUU" FT COMPBIAS 29..47 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 53 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:23260659, FT ECO:0000269|PubMed:23266887, ECO:0000269|PubMed:23357850, FT ECO:0000269|PubMed:30970244, ECO:0007744|PDB:4FWE, FT ECO:0007744|PDB:4FWF, ECO:0007744|PDB:4FWJ, FT ECO:0007744|PDB:4GU0, ECO:0007744|PDB:4GU1, FT ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS, FT ECO:0007744|PDB:4GUT, ECO:0007744|PDB:4GUU, FT ECO:0007744|PDB:4HSU, ECO:0007744|PDB:6R1U, FT ECO:0007744|PDB:6R25" FT BINDING 58 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:23260659, FT ECO:0000269|PubMed:23266887, ECO:0000269|PubMed:23357850, FT ECO:0000269|PubMed:30970244, ECO:0007744|PDB:4FWE, FT ECO:0007744|PDB:4FWF, ECO:0007744|PDB:4FWJ, FT ECO:0007744|PDB:4GU0, ECO:0007744|PDB:4GU1, FT ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS, FT ECO:0007744|PDB:4GUT, ECO:0007744|PDB:4GUU, FT ECO:0007744|PDB:4HSU, ECO:0007744|PDB:6R1U, FT ECO:0007744|PDB:6R25" FT BINDING 65 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:23260659, FT ECO:0000269|PubMed:23266887, ECO:0000269|PubMed:23357850, FT ECO:0000269|PubMed:30970244, ECO:0007744|PDB:4FWE, FT ECO:0007744|PDB:4FWF, ECO:0007744|PDB:4FWJ, FT ECO:0007744|PDB:4GU0, ECO:0007744|PDB:4GU1, FT ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS, FT ECO:0007744|PDB:4GUT, ECO:0007744|PDB:4GUU, FT ECO:0007744|PDB:4HSU, ECO:0007744|PDB:6R1U, FT ECO:0007744|PDB:6R25" FT BINDING 73 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:23260659, FT ECO:0000269|PubMed:23266887, ECO:0000269|PubMed:23357850, FT ECO:0000269|PubMed:30970244, ECO:0007744|PDB:4FWE, FT ECO:0007744|PDB:4FWF, ECO:0007744|PDB:4FWJ, FT ECO:0007744|PDB:4GU0, ECO:0007744|PDB:4GU1, FT ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS, FT ECO:0007744|PDB:4GUT, ECO:0007744|PDB:4GUU, FT ECO:0007744|PDB:4HSU, ECO:0007744|PDB:6R1U, FT ECO:0007744|PDB:6R25" FT BINDING 84 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:23260659, FT ECO:0000269|PubMed:23266887, ECO:0000269|PubMed:23357850, FT ECO:0000269|PubMed:30970244, ECO:0007744|PDB:4FWE, FT ECO:0007744|PDB:4FWF, ECO:0007744|PDB:4FWJ, FT ECO:0007744|PDB:4GU0, ECO:0007744|PDB:4GU1, FT ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS, FT ECO:0007744|PDB:4GUT, ECO:0007744|PDB:4GUU, FT ECO:0007744|PDB:4HSU, ECO:0007744|PDB:6R1U, FT ECO:0007744|PDB:6R25" FT BINDING 90 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:23260659, FT ECO:0000269|PubMed:23266887, ECO:0000269|PubMed:23357850, FT ECO:0000269|PubMed:30970244, ECO:0007744|PDB:4FWE, FT ECO:0007744|PDB:4FWF, ECO:0007744|PDB:4FWJ, FT ECO:0007744|PDB:4GU0, ECO:0007744|PDB:4GU1, FT ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS, FT ECO:0007744|PDB:4GUT, ECO:0007744|PDB:4GUU, FT ECO:0007744|PDB:4HSU, ECO:0007744|PDB:6R1U, FT ECO:0007744|PDB:6R25" FT BINDING 92 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:23260659, FT ECO:0000269|PubMed:23266887, ECO:0000269|PubMed:23357850, FT ECO:0000269|PubMed:30970244, ECO:0007744|PDB:4FWE, FT ECO:0007744|PDB:4FWF, ECO:0007744|PDB:4FWJ, FT ECO:0007744|PDB:4GU0, ECO:0007744|PDB:4GU1, FT ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS, FT ECO:0007744|PDB:4GUT, ECO:0007744|PDB:4GUU, FT ECO:0007744|PDB:4HSU, ECO:0007744|PDB:6R1U, FT ECO:0007744|PDB:6R25" FT BINDING 95 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:23260659, FT ECO:0000269|PubMed:23266887, ECO:0000269|PubMed:23357850, FT ECO:0000269|PubMed:30970244, ECO:0007744|PDB:4FWE, FT ECO:0007744|PDB:4FWF, ECO:0007744|PDB:4FWJ, FT ECO:0007744|PDB:4GU0, ECO:0007744|PDB:4GU1, FT ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS, FT ECO:0007744|PDB:4GUT, ECO:0007744|PDB:4GUU, FT ECO:0007744|PDB:4HSU, ECO:0007744|PDB:6R1U, FT ECO:0007744|PDB:6R25" FT BINDING 142 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454, FT ECO:0000269|PubMed:23260659, ECO:0000269|PubMed:23266887, FT ECO:0000269|PubMed:23357850, ECO:0000269|PubMed:30970244, FT ECO:0007744|PDB:4FWE, ECO:0007744|PDB:4FWF, FT ECO:0007744|PDB:4FWJ, ECO:0007744|PDB:4GU0, FT ECO:0007744|PDB:4GU1, ECO:0007744|PDB:4GUR, FT ECO:0007744|PDB:4GUS, ECO:0007744|PDB:4GUT, FT ECO:0007744|PDB:4GUU, ECO:0007744|PDB:4HSU, FT ECO:0007744|PDB:6R1U, ECO:0007744|PDB:6R25" FT BINDING 147 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454, FT ECO:0000269|PubMed:23260659, ECO:0000269|PubMed:23266887, FT ECO:0000269|PubMed:23357850, ECO:0000269|PubMed:30970244, FT ECO:0007744|PDB:4FWE, ECO:0007744|PDB:4FWF, FT ECO:0007744|PDB:4FWJ, ECO:0007744|PDB:4GU0, FT ECO:0007744|PDB:4GU1, ECO:0007744|PDB:4GUR, FT ECO:0007744|PDB:4GUS, ECO:0007744|PDB:4GUT, FT ECO:0007744|PDB:4GUU, ECO:0007744|PDB:4HSU, FT ECO:0007744|PDB:6R1U, ECO:0007744|PDB:6R25" FT BINDING 169 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454, FT ECO:0000269|PubMed:23260659, ECO:0000269|PubMed:23266887, FT ECO:0000269|PubMed:23357850, ECO:0000269|PubMed:30970244, FT ECO:0007744|PDB:4FWE, ECO:0007744|PDB:4FWF, FT ECO:0007744|PDB:4FWJ, ECO:0007744|PDB:4GU0, FT ECO:0007744|PDB:4GU1, ECO:0007744|PDB:4GUR, FT ECO:0007744|PDB:4GUS, ECO:0007744|PDB:4GUT, FT ECO:0007744|PDB:4GUU, ECO:0007744|PDB:4HSU, FT ECO:0007744|PDB:6R1U, ECO:0007744|PDB:6R25" FT BINDING 185 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454, FT ECO:0000269|PubMed:23260659, ECO:0000269|PubMed:23266887, FT ECO:0000269|PubMed:23357850, ECO:0000269|PubMed:30970244, FT ECO:0007744|PDB:4FWE, ECO:0007744|PDB:4FWF, FT ECO:0007744|PDB:4FWJ, ECO:0007744|PDB:4GU0, FT ECO:0007744|PDB:4GU1, ECO:0007744|PDB:4GUR, FT ECO:0007744|PDB:4GUS, ECO:0007744|PDB:4GUT, FT ECO:0007744|PDB:4GUU, ECO:0007744|PDB:4HSU, FT ECO:0007744|PDB:6R1U, ECO:0007744|PDB:6R25" FT BINDING 383..439 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255, ECO:0000269|PubMed:23260659, FT ECO:0000269|PubMed:23266887, ECO:0000269|PubMed:23357850, FT ECO:0000269|PubMed:30970244, ECO:0007744|PDB:4FWE, FT ECO:0007744|PDB:4FWF, ECO:0007744|PDB:4FWJ, FT ECO:0007744|PDB:4GU0, ECO:0007744|PDB:4GU1, FT ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS, FT ECO:0007744|PDB:4GUT, ECO:0007744|PDB:4GUU, FT ECO:0007744|PDB:4HSU, ECO:0007744|PDB:6R1U, FT ECO:0007744|PDB:6R25" FT BINDING 598 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:23260659, FT ECO:0000269|PubMed:23266887, ECO:0000269|PubMed:23357850, FT ECO:0000269|PubMed:30970244, ECO:0007744|PDB:4FWE, FT ECO:0007744|PDB:4FWF, ECO:0007744|PDB:4FWJ, FT ECO:0007744|PDB:4GU0, ECO:0007744|PDB:4GU1, FT ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS, FT ECO:0007744|PDB:4GUT, ECO:0007744|PDB:4GUU, FT ECO:0007744|PDB:4HSU, ECO:0007744|PDB:6R1U, FT ECO:0007744|PDB:6R25" FT BINDING 795 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:23260659, FT ECO:0000269|PubMed:23266887, ECO:0000269|PubMed:30970244, FT ECO:0007744|PDB:4FWE, ECO:0007744|PDB:4FWF, FT ECO:0007744|PDB:4FWJ, ECO:0007744|PDB:4GU1, FT ECO:0007744|PDB:4GUS, ECO:0007744|PDB:4GUT, FT ECO:0007744|PDB:4GUU, ECO:0007744|PDB:6R1U, FT ECO:0007744|PDB:6R25" FT BINDING 803..805 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:23260659, FT ECO:0000269|PubMed:23266887, ECO:0000269|PubMed:23357850, FT ECO:0000269|PubMed:30970244, ECO:0007744|PDB:4FWE, FT ECO:0007744|PDB:4FWF, ECO:0007744|PDB:4FWJ, FT ECO:0007744|PDB:4GU0, ECO:0007744|PDB:4GU1, FT ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS, FT ECO:0007744|PDB:4GUT, ECO:0007744|PDB:4GUU, FT ECO:0007744|PDB:4HSU, ECO:0007744|PDB:6R1U, FT ECO:0007744|PDB:6R25" FT MOD_RES 13 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 17 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 26 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 247 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..647 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_019963" FT VAR_SEQ 192..323 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_019964" FT VAR_SEQ 453..552 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_019965" FT MUTAGEN 48..49 FT /note="KK->AA: Normal demethylase activity." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 51..52 FT /note="RK->AA: Reduced demethylase activity." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 53 FT /note="C->A: Loss of demethylase activity." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 82 FT /note="W->A: Loss of demethylase activity." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 84 FT /note="H->A: Loss of demethylase activity. Defective in the FT binding of FAD." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 90 FT /note="H->A: Loss of demethylase activity. Defective in the FT binding of FAD." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 101 FT /note="R->A: Reduced demethylase activity." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 103 FT /note="H->D: No effect on DNA or nucleosome binding." FT /evidence="ECO:0000269|PubMed:30970244" FT MUTAGEN 104 FT /note="K->E: No effect on DNA or nucleosome binding." FT /evidence="ECO:0000269|PubMed:30970244" FT MUTAGEN 109 FT /note="K->E: No effect on DNA or nucleosome binding." FT /evidence="ECO:0000269|PubMed:30970244" FT MUTAGEN 114..115 FT /note="KK->AA: Reduced demethylase activity." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 114 FT /note="K->E: No effect on DNA or nucleosome binding." FT /evidence="ECO:0000269|PubMed:30970244" FT MUTAGEN 115 FT /note="K->E: No effect on DNA or nucleosome binding." FT /evidence="ECO:0000269|PubMed:30970244" FT MUTAGEN 122 FT /note="K->E: No effect on DNA or nucleosome binding." FT /evidence="ECO:0000269|PubMed:30970244" FT MUTAGEN 139 FT /note="W->A: Loss of demethylase activity." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 150 FT /note="W->A: Loss of demethylase activity. Defective in the FT binding of FAD." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 151 FT /note="R->A: Loss of demethylase activity." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 185 FT /note="C->A: Loss of demethylase activity." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 273..278 FT /note="YQPNEC->GSGSGS: Strongly reduced demethylase FT activity. Loss of enzymatic activity; when associated with FT 285-A--A-287." FT /evidence="ECO:0000269|PubMed:23357850" FT MUTAGEN 285..287 FT /note="RPD->APA: Strongly reduced demethylase activity. FT Loss of enzymatic activity; when associated with FT 273-G--S-278." FT /evidence="ECO:0000269|PubMed:23357850" FT MUTAGEN 302 FT /note="R->D: No effect on DNA or nucleosome binding." FT /evidence="ECO:0000269|PubMed:30970244" FT MUTAGEN 318..319 FT /note="WY->AA: Loss of demethylase activity." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 340..341 FT /note="LV->AA: Loss of demethylase activity. Defective in FT the binding of FAD." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 361..362 FT /note="LI->AA: Loss of demethylase activity. Defective in FT the binding of FAD." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 443..444 FT /note="IN->GG: Loss of demethylase activity. Defective in FT the binding of FAD." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 481..482 FT /note="KR->ED: No effect on DNA or nucleosome binding." FT /evidence="ECO:0000269|PubMed:30970244" FT MUTAGEN 542 FT /note="N->A: Loss of demethylase activity." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 543 FT /note="L->A: Reduced demethylase activity." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 547 FT /note="C->A: Reduced demethylase activity." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 559 FT /note="W->A: Loss of demethylase activity." FT /evidence="ECO:0000269|PubMed:23266887" FT MUTAGEN 563 FT /note="E->A: Loss of demethylase activity." FT /evidence="ECO:0000269|PubMed:23357850" FT MUTAGEN 661 FT /note="K->A: Normal demethylase activity." FT /evidence="ECO:0000269|PubMed:23357850" FT MUTAGEN 767 FT /note="Y->A: Loss of demethylase activity." FT /evidence="ECO:0000269|PubMed:23266887" FT CONFLICT 651 FT /note="I -> T (in Ref. 1; BAC86124)" FT /evidence="ECO:0000305" FT CONFLICT 794..795 FT /note="Missing (in Ref. 4; CAH10499)" FT /evidence="ECO:0000305" FT STRAND 51..55 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 70..72 FT /evidence="ECO:0007829|PDB:4FWF" FT STRAND 75..77 FT /evidence="ECO:0007829|PDB:4FWJ" FT STRAND 82..86 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 89..92 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 93..100 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:4FWJ" FT HELIX 107..116 FT /evidence="ECO:0007829|PDB:4HSU" FT TURN 117..120 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 127..134 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 139..141 FT /evidence="ECO:0007829|PDB:4HSU" FT TURN 145..147 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 150..152 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 161..166 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 173..175 FT /evidence="ECO:0007829|PDB:4GU0" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:4FWE" FT HELIX 184..186 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 192..195 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 199..203 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 217..219 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 225..227 FT /evidence="ECO:0007829|PDB:4HSU" FT TURN 235..238 FT /evidence="ECO:0007829|PDB:7XE2" FT HELIX 267..269 FT /evidence="ECO:0007829|PDB:4GU1" FT STRAND 286..288 FT /evidence="ECO:0007829|PDB:4GU1" FT HELIX 291..296 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 298..300 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 305..320 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 328..331 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 332..334 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 341..358 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 361..363 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 371..373 FT /evidence="ECO:0007829|PDB:4GUT" FT HELIX 378..380 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 384..388 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 392..404 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 407..411 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 413..417 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 427..430 FT /evidence="ECO:0007829|PDB:4FWF" FT STRAND 432..435 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 438..440 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 446..454 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 458..460 FT /evidence="ECO:0007829|PDB:4FWF" FT STRAND 467..469 FT /evidence="ECO:0007829|PDB:7XE1" FT HELIX 477..497 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 498..500 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 503..505 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 509..523 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 530..547 FT /evidence="ECO:0007829|PDB:4HSU" FT TURN 551..553 FT /evidence="ECO:0007829|PDB:4HSU" FT TURN 556..560 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 561..564 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 572..574 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 580..587 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 592..595 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 598..602 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 604..612 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 617..625 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 629..634 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 637..641 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 645..653 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 654..657 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 660..665 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 672..675 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 679..683 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 686..688 FT /evidence="ECO:0007829|PDB:4HSU" FT TURN 689..692 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 693..700 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 708..713 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 716..720 FT /evidence="ECO:0007829|PDB:4HSU" FT TURN 721..723 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 726..740 FT /evidence="ECO:0007829|PDB:4HSU" FT TURN 741..743 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 750..754 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 757..759 FT /evidence="ECO:0007829|PDB:4HSU" FT TURN 761..763 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 766..771 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 777..783 FT /evidence="ECO:0007829|PDB:4HSU" FT TURN 787..789 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 790..792 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 795..797 FT /evidence="ECO:0007829|PDB:4HSU" FT STRAND 799..801 FT /evidence="ECO:0007829|PDB:4HSU" FT HELIX 805..821 FT /evidence="ECO:0007829|PDB:4HSU" SQ SEQUENCE 822 AA; 92098 MW; 6C0A9BD6B2CEA2EA CRC64; MATPRGRTKK KASFDHSPDS LPLRSSGRQA KKKATETTDE DEDGGSEKKY RKCEKAGCTA TCPVCFASAS ERCAKNGYTS RWYHLSCGEH FCNECFDHYY RSHKDGYDKY TTWKKIWTSN GKTEPSPKAF MADQQLPYWV QCTKPECRKW RQLTKEIQLT PQIAKTYRCG MKPNTAIKPE TSDHCSLPED LRVLEVSNHW WYSMLILPPL LKDSVAAPLL SAYYPDCVGM SPSCTSTNRA AATGNASPGK LEHSKAALSV HVPGMNRYFQ PFYQPNECGK ALCVRPDVME LDELYEFPEY SRDPTMYLAL RNLILALWYT NCKEALTPQK CIPHIIVRGL VRIRCVQEVE RILYFMTRKG LINTGVLSVG ADQYLLPKDY HNKSVIIIGA GPAGLAAARQ LHNFGIKVTV LEAKDRIGGR VWDDKSFKGV TVGRGAQIVN GCINNPVALM CEQLGISMHK FGERCDLIQE GGRITDPTID KRMDFHFNAL LDVVSEWRKD KTQLQDVPLG EKIEEIYKAF IKESGIQFSE LEGQVLQFHL SNLEYACGSN LHQVSARSWD HNEFFAQFAG DHTLLTPGYS VIIEKLAEGL DIQLKSPVQC IDYSGDEVQV TTTDGTGYSA QKVLVTVPLA LLQKGAIQFN PPLSEKKMKA INSLGAGIIE KIALQFPYRF WDSKVQGADF FGHVPPSASK RGLFAVFYDM DPQKKHSVLM SVIAGEAVAS VRTLDDKQVL QQCMATLREL FKEQEVPDPT KYFVTRWSTD PWIQMAYSFV KTGGSGEAYD IIAEDIQGTV FFAGEATNRH FPQTVTGAYL SGVREASKIA AF //