ID KDM3B_HUMAN Reviewed; 1761 AA. AC Q7LBC6; A6H8X7; Q9BVH6; Q9BW93; Q9BZ52; Q9NYF4; Q9UPS0; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 2. DT 29-MAY-2024, entry version 157. DE RecName: Full=Lysine-specific demethylase 3B; DE EC=1.14.11.65 {ECO:0000269|PubMed:16603237}; DE AltName: Full=JmjC domain-containing histone demethylation protein 2B; DE AltName: Full=Jumonji domain-containing protein 1B; DE AltName: Full=Nuclear protein 5qNCA; DE AltName: Full=[histone H3]-dimethyl-L-lysine(9) demethylase 3B {ECO:0000305}; GN Name=KDM3B; Synonyms=C5orf7, JHDM2B, JMJD1B, KIAA1082; 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 2), AND TISSUE SPECIFICITY. RC TISSUE=Bone marrow; RX PubMed=11087669; DOI=10.1006/geno.2000.6345; RA Lai F., Godley L.A., Fernald A.A., Orelli B.J., Pamintuan L., Zhao N., RA Le Beau M.M.; RT "cDNA cloning and genomic structure of three genes localized to human RT chromosome band 5q31 encoding potential nuclear proteins."; RL Genomics 70:123-130(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT RP THR-256. RX PubMed=11687974; DOI=10.1038/sj.onc.1204850; RA Hu Z., Gomes I., Horrigan S.K., Kravarusic J., Mar B., Arbieva Z., RA Chyna B., Fulton N., Edassery S., Raza A., Westbrook C.A.; RT "A novel nuclear protein, 5qNCA (LOC51780) is a candidate for the myeloid RT leukemia tumor suppressor gene on chromosome 5 band q31."; RL Oncogene 20:6946-6954(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-256. RC TISSUE=Brain; RX PubMed=10470851; DOI=10.1093/dnares/6.3.197; RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIV. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:197-205(1999). RN [4] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-256. RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT RP THR-256. RC TISSUE=Brain, and 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 [8] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=16603237; DOI=10.1016/j.cell.2006.03.027; RA Yamane K., Toumazou C., Tsukada Y.I., Erdjument-Bromage H., Tempst P., RA Wong J., Zhang Y.; RT "JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription RT activation by androgen receptor."; RL Cell 125:483-495(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-798, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-773 AND SER-779, AND RP IDENTIFICATION BY 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-361, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-773; SER-779 AND SER-798, 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 [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492; SER-560; THR-614; RP SER-766; SER-773; SER-778; SER-779; SER-1253 AND SER-1259, AND RP 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 [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-788, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [19] RP INVOLVEMENT IN DIJOS, AND VARIANTS DIJOS 45-ARG--SER-1761 DEL; RP 93-GLU--SER-1761 DEL; ARG-117; GLY-336; 827-GLN--SER-1761 DEL; GLN-943; RP TRP-943; GLN-1028; VAL-1032; PRO-1509; 1517-ARG--SER-1761 DEL; CYS-1544; RP LYS-1731 AND ARG-1734. RX PubMed=30929739; DOI=10.1016/j.ajhg.2019.02.023; RA Diets I.J., van der Donk R., Baltrunaite K., Waanders E., Reijnders M.R.F., RA Dingemans A.J.M., Pfundt R., Vulto-van Silfhout A.T., Wiel L., Gilissen C., RA Thevenon J., Perrin L., Afenjar A., Nava C., Keren B., Bartz S., Peri B., RA Beunders G., Verbeek N., van Gassen K., Thiffault I., Cadieux-Dion M., RA Huerta-Saenz L., Wagner M., Konstantopoulou V., Vodopiutz J., Griese M., RA Boel A., Callewaert B., Brunner H.G., Kleefstra T., Hoogerbrugge N., RA de Vries B.B.A., Hwa V., Dauber A., Hehir-Kwa J.Y., Kuiper R.P., RA Jongmans M.C.J.; RT "De Novo and Inherited Pathogenic Variants in KDM3B Cause Intellectual RT Disability, Short Stature, and Facial Dysmorphism."; RL Am. J. Hum. Genet. 104:758-766(2019). CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of CC histone H3, thereby playing a central role in histone code. CC Demethylation of Lys residue generates formaldehyde and succinate. May CC have tumor suppressor activity. {ECO:0000269|PubMed:16603237}. 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:16603237}; 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q7LBC6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q7LBC6-2; Sequence=VSP_018299, VSP_018300; CC Name=3; CC IsoId=Q7LBC6-3; Sequence=VSP_018298; CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in placenta, skeletal CC muscle, kidney, heart and liver. {ECO:0000269|PubMed:11087669, CC ECO:0000269|PubMed:11687974}. CC -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate the CC association with nuclear receptors. {ECO:0000250}. CC -!- DISEASE: Diets-Jongmans syndrome (DIJOS) [MIM:618846]: An autosomal CC dominant disorder characterized by varying degrees of intellectual CC disability, developmental delay, short stature, and characteristic CC facial features such as a wide mouth, a pointed chin, long ears and a CC low columella. {ECO:0000269|PubMed:30929739}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Its gene is located in the 5q region of the genome which CC is deleted in del(5q) interstitial deletion, a frequent deletion found CC in myeloid leukemias and myelodysplasias, suggesting that it may be a CC good candidate for the del(5q) tumor suppressor gene. CC -!- SIMILARITY: Belongs to the JHDM2 histone demethylase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA83034.2; Type=Erroneous initiation; Note=Extended 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; AF251039; AAF63765.1; -; mRNA. DR EMBL; AF338242; AAK13499.1; -; mRNA. DR EMBL; AB029005; BAA83034.2; ALT_INIT; mRNA. DR EMBL; AC104116; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC113403; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471062; EAW62141.1; -; Genomic_DNA. DR EMBL; BC000539; AAH00539.2; -; mRNA. DR EMBL; BC001202; AAH01202.1; -; mRNA. DR EMBL; BC146788; AAI46789.1; -; mRNA. DR CCDS; CCDS34242.1; -. [Q7LBC6-1] DR RefSeq; NP_057688.2; NM_016604.3. [Q7LBC6-1] DR PDB; 4C8D; X-ray; 2.18 A; A=1380-1720. DR PDB; 5R7X; X-ray; 1.44 A; A/B=1380-1728. DR PDB; 5RAA; X-ray; 1.57 A; A/B=1380-1728. DR PDB; 5RAB; X-ray; 1.52 A; A/B=1380-1728. DR PDB; 5RAC; X-ray; 1.73 A; A/B=1380-1728. DR PDB; 5RAD; X-ray; 1.90 A; A/B=1380-1728. DR PDB; 5RAE; X-ray; 1.88 A; A/B=1380-1728. DR PDB; 5RAF; X-ray; 1.62 A; A/B=1380-1728. DR PDB; 5RAG; X-ray; 1.52 A; A/B=1380-1728. DR PDB; 5RAH; X-ray; 1.66 A; A/B=1380-1728. DR PDB; 5RAI; X-ray; 1.54 A; A/B=1380-1728. DR PDB; 5RAJ; X-ray; 1.61 A; A/B=1380-1728. DR PDB; 5RAK; X-ray; 1.69 A; A/B=1380-1728. DR PDB; 5RAL; X-ray; 1.68 A; A/B=1380-1728. DR PDB; 5RAM; X-ray; 2.05 A; A/B=1380-1728. DR PDB; 5RAN; X-ray; 1.95 A; A/B=1380-1728. DR PDB; 5RAO; X-ray; 1.59 A; A/B=1380-1728. DR PDB; 5RAP; X-ray; 1.90 A; A/B=1380-1728. DR PDB; 5RAQ; X-ray; 1.85 A; A/B=1380-1728. DR PDB; 5RAR; X-ray; 1.47 A; A/B=1380-1728. DR PDB; 5RAS; X-ray; 1.58 A; A/B=1380-1728. DR PDB; 5RAU; X-ray; 1.73 A; A/B=1380-1728. DR PDB; 5RAV; X-ray; 1.77 A; A/B=1380-1728. DR PDB; 5RAW; X-ray; 1.55 A; A/B=1380-1728. DR PDB; 5RAX; X-ray; 2.01 A; A/B=1380-1728. DR PDB; 5RAY; X-ray; 1.63 A; A/B=1380-1728. DR PDB; 5RAZ; X-ray; 1.81 A; A/B=1380-1728. DR PDB; 5RB0; X-ray; 1.95 A; A/B=1380-1728. DR PDB; 5RB1; X-ray; 1.76 A; A/B=1380-1728. DR PDB; 5RB2; X-ray; 1.52 A; A/B=1380-1728. DR PDB; 5RB3; X-ray; 1.53 A; A/B=1380-1728. DR PDB; 5RB4; X-ray; 1.55 A; A/B=1380-1728. DR PDB; 5RB5; X-ray; 1.51 A; A/B=1380-1728. DR PDB; 5RB6; X-ray; 1.63 A; A/B=1380-1728. DR PDB; 5RB7; X-ray; 1.57 A; A/B=1380-1728. DR PDB; 6RBJ; X-ray; 2.09 A; A/B=1380-1728. DR PDBsum; 4C8D; -. DR PDBsum; 5R7X; -. DR PDBsum; 5RAA; -. DR PDBsum; 5RAB; -. DR PDBsum; 5RAC; -. DR PDBsum; 5RAD; -. DR PDBsum; 5RAE; -. DR PDBsum; 5RAF; -. DR PDBsum; 5RAG; -. DR PDBsum; 5RAH; -. DR PDBsum; 5RAI; -. DR PDBsum; 5RAJ; -. DR PDBsum; 5RAK; -. DR PDBsum; 5RAL; -. DR PDBsum; 5RAM; -. DR PDBsum; 5RAN; -. DR PDBsum; 5RAO; -. DR PDBsum; 5RAP; -. DR PDBsum; 5RAQ; -. DR PDBsum; 5RAR; -. DR PDBsum; 5RAS; -. DR PDBsum; 5RAU; -. DR PDBsum; 5RAV; -. DR PDBsum; 5RAW; -. DR PDBsum; 5RAX; -. DR PDBsum; 5RAY; -. DR PDBsum; 5RAZ; -. DR PDBsum; 5RB0; -. DR PDBsum; 5RB1; -. DR PDBsum; 5RB2; -. DR PDBsum; 5RB3; -. DR PDBsum; 5RB4; -. DR PDBsum; 5RB5; -. DR PDBsum; 5RB6; -. DR PDBsum; 5RB7; -. DR PDBsum; 6RBJ; -. DR AlphaFoldDB; Q7LBC6; -. DR SMR; Q7LBC6; -. DR BioGRID; 119727; 101. DR IntAct; Q7LBC6; 30. DR MINT; Q7LBC6; -. DR STRING; 9606.ENSP00000326563; -. DR BindingDB; Q7LBC6; -. DR ChEMBL; CHEMBL3784906; -. DR GlyCosmos; Q7LBC6; 22 sites, 2 glycans. DR GlyGen; Q7LBC6; 28 sites, 2 O-linked glycans (28 sites). DR iPTMnet; Q7LBC6; -. DR PhosphoSitePlus; Q7LBC6; -. DR BioMuta; KDM3B; -. DR DMDM; 308153456; -. DR EPD; Q7LBC6; -. DR jPOST; Q7LBC6; -. DR MassIVE; Q7LBC6; -. DR MaxQB; Q7LBC6; -. DR PaxDb; 9606-ENSP00000326563; -. DR PeptideAtlas; Q7LBC6; -. DR ProteomicsDB; 68846; -. [Q7LBC6-1] DR ProteomicsDB; 68847; -. [Q7LBC6-2] DR ProteomicsDB; 68848; -. [Q7LBC6-3] DR Pumba; Q7LBC6; -. DR Antibodypedia; 14936; 396 antibodies from 38 providers. DR DNASU; 51780; -. DR Ensembl; ENST00000314358.10; ENSP00000326563.5; ENSG00000120733.15. [Q7LBC6-1] DR GeneID; 51780; -. DR KEGG; hsa:51780; -. DR MANE-Select; ENST00000314358.10; ENSP00000326563.5; NM_016604.4; NP_057688.3. DR UCSC; uc003lcy.1; human. [Q7LBC6-1] DR AGR; HGNC:1337; -. DR CTD; 51780; -. DR DisGeNET; 51780; -. DR GeneCards; KDM3B; -. DR HGNC; HGNC:1337; KDM3B. DR HPA; ENSG00000120733; Low tissue specificity. DR MalaCards; KDM3B; -. DR MIM; 609373; gene. DR MIM; 618846; phenotype. DR neXtProt; NX_Q7LBC6; -. DR OpenTargets; ENSG00000120733; -. DR Orphanet; 633004; KDM3B-related intellectual disability-facial dysmorphism-short stature syndrome. DR PharmGKB; PA25918; -. DR VEuPathDB; HostDB:ENSG00000120733; -. DR eggNOG; KOG1356; Eukaryota. DR GeneTree; ENSGT00940000158095; -. DR HOGENOM; CLU_002991_0_0_1; -. DR InParanoid; Q7LBC6; -. DR OMA; ENSWVSA; -. DR OrthoDB; 3473445at2759; -. DR PhylomeDB; Q7LBC6; -. DR TreeFam; TF324723; -. DR BioCyc; MetaCyc:ENSG00000120733-MONOMER; -. DR BRENDA; 1.14.11.65; 2681. DR PathwayCommons; Q7LBC6; -. DR Reactome; R-HSA-3214842; HDMs demethylate histones. DR SignaLink; Q7LBC6; -. DR SIGNOR; Q7LBC6; -. DR BioGRID-ORCS; 51780; 42 hits in 1196 CRISPR screens. DR ChiTaRS; KDM3B; human. DR GeneWiki; JMJD1B; -. DR GenomeRNAi; 51780; -. DR Pharos; Q7LBC6; Tbio. DR PRO; PR:Q7LBC6; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q7LBC6; Protein. DR Bgee; ENSG00000120733; Expressed in ventricular zone and 213 other cell types or tissues. DR ExpressionAtlas; Q7LBC6; baseline and differential. 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:0016209; F:antioxidant activity; IEA:Ensembl. DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central. DR GO; GO:0032454; F:histone H3K9 demethylase activity; IBA:GO_Central. DR GO; GO:0140683; F:histone H3K9me/H3K9me2 demethylase activity; IEA:UniProtKB-EC. 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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR Gene3D; 2.60.120.650; Cupin; 1. DR InterPro; IPR045109; JHDM2-like. DR InterPro; IPR003347; JmjC_dom. DR PANTHER; PTHR12549; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN; 1. DR PANTHER; PTHR12549:SF8; LYSINE-SPECIFIC DEMETHYLASE 3B; 1. DR Pfam; PF02373; JmjC; 1. DR SMART; SM00558; JmjC; 1. DR SUPFAM; SSF51197; Clavaminate synthase-like; 1. DR PROSITE; PS51184; JMJC; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator; KW Dioxygenase; Disease variant; Dwarfism; Intellectual disability; Iron; KW Isopeptide bond; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation; KW Ubl conjugation; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..1761 FT /note="Lysine-specific demethylase 3B" FT /id="PRO_0000234373" FT DOMAIN 1498..1721 FT /note="JmjC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538" FT ZN_FING 1031..1056 FT /note="C6-type" FT /evidence="ECO:0000255" FT REGION 253..346 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 370..394 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 438..496 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 572..603 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 714..762 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 805..828 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1142..1220 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 1293..1297 FT /note="LXXLL motif" FT COMPBIAS 273..312 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 449..496 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 808..828 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1142..1166 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1178..1192 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1560 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538" FT BINDING 1562 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538" FT BINDING 1689 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT MOD_RES 361 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 492 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 546 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6ZPY7" FT MOD_RES 556 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6ZPY7" FT MOD_RES 560 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 614 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 766 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 773 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 778 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 779 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 798 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231" FT MOD_RES 1253 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1259 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 788 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..1002 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_018298" FT VAR_SEQ 1..344 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11087669" FT /id="VSP_018299" FT VAR_SEQ 345..349 FT /note="TFVPQ -> MGAME (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11087669" FT /id="VSP_018300" FT VARIANT 45..1761 FT /note="Missing (in DIJOS)" FT /evidence="ECO:0000269|PubMed:30929739" FT /id="VAR_083997" FT VARIANT 93..1761 FT /note="Missing (in DIJOS)" FT /evidence="ECO:0000269|PubMed:30929739" FT /id="VAR_083998" FT VARIANT 117 FT /note="W -> R (in DIJOS)" FT /evidence="ECO:0000269|PubMed:30929739" FT /id="VAR_083999" FT VARIANT 256 FT /note="A -> T (in dbSNP:rs6865472)" FT /evidence="ECO:0000269|PubMed:10470851, FT ECO:0000269|PubMed:11687974, ECO:0000269|PubMed:15489334, FT ECO:0000269|Ref.6" FT /id="VAR_026221" FT VARIANT 336 FT /note="D -> G (in DIJOS; uncertain significance; FT dbSNP:rs1762257015)" FT /evidence="ECO:0000269|PubMed:30929739" FT /id="VAR_084000" FT VARIANT 827..1761 FT /note="Missing (in DIJOS)" FT /evidence="ECO:0000269|PubMed:30929739" FT /id="VAR_084001" FT VARIANT 943 FT /note="R -> Q (in DIJOS; dbSNP:rs1334033128)" FT /evidence="ECO:0000269|PubMed:30929739" FT /id="VAR_084002" FT VARIANT 943 FT /note="R -> W (in DIJOS)" FT /evidence="ECO:0000269|PubMed:30929739" FT /id="VAR_084003" FT VARIANT 1028 FT /note="R -> Q (in DIJOS)" FT /evidence="ECO:0000269|PubMed:30929739" FT /id="VAR_084004" FT VARIANT 1032 FT /note="D -> V (in DIJOS; dbSNP:rs1762639635)" FT /evidence="ECO:0000269|PubMed:30929739" FT /id="VAR_084005" FT VARIANT 1201 FT /note="S -> N (in dbSNP:rs7706614)" FT /id="VAR_026222" FT VARIANT 1509 FT /note="L -> P (in DIJOS)" FT /evidence="ECO:0000269|PubMed:30929739" FT /id="VAR_084006" FT VARIANT 1517..1761 FT /note="Missing (in DIJOS)" FT /evidence="ECO:0000269|PubMed:30929739" FT /id="VAR_084007" FT VARIANT 1544 FT /note="Y -> C (in DIJOS; uncertain significance)" FT /evidence="ECO:0000269|PubMed:30929739" FT /id="VAR_084008" FT VARIANT 1731 FT /note="E -> K (in DIJOS; uncertain significance; FT dbSNP:rs1763530961)" FT /evidence="ECO:0000269|PubMed:30929739" FT /id="VAR_084009" FT VARIANT 1734 FT /note="L -> R (in DIJOS)" FT /evidence="ECO:0000269|PubMed:30929739" FT /id="VAR_084010" FT CONFLICT 569 FT /note="C -> R (in Ref. 1; AAF63765)" FT /evidence="ECO:0000305" FT STRAND 1381..1385 FT /evidence="ECO:0007829|PDB:5R7X" FT HELIX 1386..1388 FT /evidence="ECO:0007829|PDB:5R7X" FT STRAND 1390..1394 FT /evidence="ECO:0007829|PDB:5R7X" FT HELIX 1401..1410 FT /evidence="ECO:0007829|PDB:5R7X" FT STRAND 1415..1417 FT /evidence="ECO:0007829|PDB:5R7X" FT HELIX 1420..1423 FT /evidence="ECO:0007829|PDB:5R7X" FT HELIX 1426..1429 FT /evidence="ECO:0007829|PDB:5R7X" FT HELIX 1431..1438 FT /evidence="ECO:0007829|PDB:5R7X" FT STRAND 1441..1447 FT /evidence="ECO:0007829|PDB:5R7X" FT TURN 1448..1450 FT /evidence="ECO:0007829|PDB:5R7X" FT STRAND 1453..1458 FT /evidence="ECO:0007829|PDB:5R7X" FT HELIX 1459..1463 FT /evidence="ECO:0007829|PDB:5R7X" FT STRAND 1466..1468 FT /evidence="ECO:0007829|PDB:5R7X" FT HELIX 1469..1471 FT /evidence="ECO:0007829|PDB:5R7X" FT STRAND 1483..1485 FT /evidence="ECO:0007829|PDB:5R7X" FT STRAND 1487..1489 FT /evidence="ECO:0007829|PDB:5R7X" FT TURN 1491..1493 FT /evidence="ECO:0007829|PDB:5R7X" FT HELIX 1494..1497 FT /evidence="ECO:0007829|PDB:5R7X" FT HELIX 1499..1506 FT /evidence="ECO:0007829|PDB:5R7X" FT HELIX 1512..1515 FT /evidence="ECO:0007829|PDB:5R7X" FT HELIX 1524..1526 FT /evidence="ECO:0007829|PDB:5R7X" FT STRAND 1539..1543 FT /evidence="ECO:0007829|PDB:5R7X" FT HELIX 1550..1553 FT /evidence="ECO:0007829|PDB:5R7X" FT STRAND 1556..1560 FT /evidence="ECO:0007829|PDB:5R7X" FT STRAND 1563..1574 FT /evidence="ECO:0007829|PDB:5R7X" FT STRAND 1577..1579 FT /evidence="ECO:0007829|PDB:5R7X" FT TURN 1580..1582 FT /evidence="ECO:0007829|PDB:5RAH" FT HELIX 1583..1592 FT /evidence="ECO:0007829|PDB:5R7X" FT HELIX 1597..1604 FT /evidence="ECO:0007829|PDB:5R7X" FT STRAND 1610..1616 FT /evidence="ECO:0007829|PDB:5R7X" FT HELIX 1619..1621 FT /evidence="ECO:0007829|PDB:5R7X" FT HELIX 1622..1635 FT /evidence="ECO:0007829|PDB:5R7X" FT HELIX 1646..1649 FT /evidence="ECO:0007829|PDB:5R7X" FT HELIX 1656..1666 FT /evidence="ECO:0007829|PDB:5R7X" FT STRAND 1671..1676 FT /evidence="ECO:0007829|PDB:5R7X" FT STRAND 1680..1683 FT /evidence="ECO:0007829|PDB:5R7X" FT STRAND 1689..1704 FT /evidence="ECO:0007829|PDB:5R7X" FT HELIX 1707..1713 FT /evidence="ECO:0007829|PDB:5R7X" FT HELIX 1718..1724 FT /evidence="ECO:0007829|PDB:5R7X" SQ SEQUENCE 1761 AA; 191581 MW; FB900FCBF0675CD8 CRC64; MADAAASPVG KRLLLLFADT AASASASAPA AAAASGDPGP ALRTRAWRAG TVRAMSGAVP QDLAIFVEFD GCNWKQHSWV KVHAEEVIVL LLEGSLVWAP REDPVLLQGI RVSIAQWPAL TFTPLVDKLG LGSVVPVEYL LDRELRFLSD ANGLHLFQMG TDSQNQILLE HAALRETVNA LISDQKLQEI FSRGPYSVQG HRVKIYQPEG EEGWLYGVVS HQDSITRLME VSVTESGEIK SVDPRLIHVM LMDNSAPQSE GGTLKAVKSS KGKKKRESIE GKDGRRRKSA SDSGCDPASK KLKGDRGEVD SNGSDGGEAS RGPWKGGNAS GEPGLDQRAK QPPSTFVPQI NRNIRFATYT KENGRTLVVQ DEPVGGDTPA SFTPYSTATG QTPLAPEVGG AENKEAGKTL EQVGQGIVAS AAVVTTASST PNTVRISDTG LAAGTVPEKQ KGSRSQASGE NSRNSILASS GFGAPLPSSS QPLTFGSGRS QSNGVLATEN KPLGFSFGCS SAQEAQKDTD LSKNLFFQCM SQTLPTSNYF TTVSESLADD SSSRDSFKQS LESLSSGLCK GRSVLGTDTK PGSKAGSSVD RKVPAESMPT LTPAFPRSLL NARTPENHEN LFLQPPKLSR EEPSNPFLAF VEKVEHSPFS SFASQASGSS SSATTVTSKV APSWPESHSS ADSASLAKKK PLFITTDSSK LVSGVLGSAL TSGGPSLSAM GNGRSSSPTS SLTQPIEMPT LSSSPTEERP TVGPGQQDNP LLKTFSNVFG RHSGGFLSSP ADFSQENKAP FEAVKRFSLD ERSLACRQDS DSSTNSDLSD LSDSEEQLQA KTGLKGIPEH LMGKLGPNGE RSAELLLGKS KGKQAPKGRP RTAPLKVGQS VLKDVSKVKK LKQSGEPFLQ DGSCINVAPH LHKCRECRLE RYRKFKEQEQ DDSTVACRFF HFRRLIFTRK GVLRVEGFLS PQQSDPDAMN LWIPSSSLAE GIDLETSKYI LANVGDQFCQ LVMSEKEAMM MVEPHQKVAW KRAVRGVREM CDVCETTLFN IHWVCRKCGF GVCLDCYRLR KSRPRSETEE MGDEEVFSWL KCAKGQSHEP ENLMPTQIIP GTALYNIGDM VHAARGKWGI KANCPCISRQ NKSVLRPAVT NGMSQLPSIN PSASSGNETT FSGGGGPAPV TTPEPDHVPK ADSTDIRSEE PLKTDSSASN SNSELKAIRP PCPDTAPPSS ALHWLADLAT QKAKEETKEA GSLRSVLNKE SHSPFGLDSF NSTAKVSPLT PKLFNSLLLG PTASNNKTEG SSLRDLLHSG PGKLPQTPLD TGIPFPPVFS TSSAGVKSKA SLPNFLDHII ASVVENKKTS DASKRACNLT DTQKEVKEMV MGLNVLDPHT SHSWLCDGRL LCLHDPSNKN NWKIFRECWK QGQPVLVSGV HKKLKSELWK PEAFSQEFGD QDVDLVNCRN CAIISDVKVR DFWDGFEIIC KRLRSEDGQP MVLKLKDWPP GEDFRDMMPT RFEDLMENLP LPEYTKRDGR LNLASRLPSY FVRPDLGPKM YNAYGLITAE DRRVGTTNLH LDVSDAVNVM VYVGIPIGEG AHDEEVLKTI DEGDADEVTK QRIHDGKEKP GALWHIYAAK DAEKIRELLR KVGEEQGQEN PPDHDPIHDQ SWYLDQTLRK RLYEEYGVQG WAIVQFLGDA VFIPAGAPHQ VHNLYSCIKV AEDFVSPEHV KHCFRLTQEF RHLSNTHTNH EDKLQVKNII YHAVKDAVGT LKAHESKLAR S //