KDM1B_HUMAN
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 03-AUG-2022, entry version 162.
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};
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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 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 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 AlphaFoldDB; Q8NB78; -.
DR SASBDB; Q8NB78; -.
DR SMR; Q8NB78; -.
DR BioGRID; 128743; 48.
DR IntAct; Q8NB78; 25.
DR MINT; Q8NB78; -.
DR BindingDB; Q8NB78; -.
DR ChEMBL; CHEMBL1938208; -.
DR DrugCentral; Q8NB78; -.
DR iPTMnet; Q8NB78; -.
DR PhosphoSitePlus; Q8NB78; -.
DR BioMuta; KDM1B; -.
DR DMDM; 317373434; -.
DR EPD; Q8NB78; -.
DR jPOST; Q8NB78; -.
DR MassIVE; Q8NB78; -.
DR MaxQB; Q8NB78; -.
DR PaxDb; Q8NB78; -.
DR PeptideAtlas; Q8NB78; -.
DR PRIDE; Q8NB78; -.
DR ProteomicsDB; 72745; -. [Q8NB78-1]
DR ProteomicsDB; 72746; -. [Q8NB78-2]
DR ProteomicsDB; 72747; -. [Q8NB78-4]
DR Antibodypedia; 25190; 158 antibodies from 25 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 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; 1034142at2759; -.
DR PhylomeDB; Q8NB78; -.
DR TreeFam; TF352593; -.
DR BioCyc; MetaCyc:ENSG00000165097-MON; -.
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; 21 hits in 1095 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 tissues.
DR ExpressionAtlas; Q8NB78; baseline and differential.
DR Genevisible; Q8NB78; HS.
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: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:0140682; F:histone H3-di/monomethyl-lysine-4 FAD-dependent demethylase activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; IEA:Ensembl.
DR GO; GO:0034720; P:histone H3-K4 demethylation; IDA: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:0044030; P:regulation of DNA methylation; ISS:UniProtKB.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.50.50.60; -; 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 Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF04433; SWIRM; 1.
DR Pfam; PF07496; zf-CW; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS50934; SWIRM; 1.
DR PROSITE; PS51050; ZF_CW; 1.
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 273-G--S-
FT 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 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:4FWF"
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
