KDM3B

KDM3B
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4C8D
Identifiers
Aliases	KDM3B, 5qNCA, C5orf7, JMJD1B, NET22, lysine demethylase 3B, DIJOS
External IDs	OMIM: 609373 MGI: 1923356 HomoloGene: 41145 GeneCards: KDM3B
Gene location (Human)
Chr.	Chromosome 5 (human)
End	138,437,028 bp
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• oxidoreductase activity; • antioxidant activity; • dioxygenase activity; • metal ion binding; • histone demethylase activity; • GO:0000975 transcription cis-regulatory region binding; • chromatin DNA binding; • histone H3-methyl-lysine-9 demethylase activity;
Cellular component	• chromatin; • nucleus; • nucleoplasm;
Biological process	• cellular oxidant detoxification; • response to cisplatin; • transcription, DNA-templated; • regulation of transcription, DNA-templated; • histone H3-K9 demethylation; • chromatin organization;
	Sources:Amigo / QuickGO
Orthologs
	51780
	277250
	ENSG00000120733
	ENSMUSG00000038773
	Q7LBC6
	Q6ZPY7
	NM_016604
	NM_001081256; NM_029518
	NP_057688
	NP_001074725
	Wikidata
View/Edit Human	View/Edit Mouse

Lysine-specific demethylase 3B is an enzyme that in humans is encoded by the KDM3B gene.^[4]^[5] KDM3B belongs to the alpha-ketoglutarate-dependent hydroxylase superfamily.

References[]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000120733 - Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Katoh M, Katoh M (Jun 2004). "Identification and characterization of JMJD2 family genes in silico". International Journal of Oncology. 24 (6): 1623–8. doi:10.3892/ijo.25.3.759. PMID 15138608.
^ "Entrez Gene: JMJD1B jumonji domain containing 1B".

Further reading[]

Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T (Jun 2002). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Research. 9 (3): 99–106. CiteSeerX 10.1.1.500.923. doi:10.1093/dnares/9.3.99. PMID 12168954.
Dias Neto E, Correa RG, Verjovski-Almeida S, Briones MR, Nagai MA, da Silva W, Zago MA, Bordin S, Costa FF, Goldman GH, Carvalho AF, Matsukuma A, Baia GS, Simpson DH, Brunstein A, de Oliveira PS, Bucher P, Jongeneel CV, O'Hare MJ, Soares F, Brentani RR, Reis LF, de Souza SJ, Simpson AJ (Mar 2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags". Proceedings of the National Academy of Sciences of the United States of America. 97 (7): 3491–6. Bibcode:2000PNAS...97.3491D. doi:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800.
Lai F, Godley LA, Fernald AA, Orelli BJ, Pamintuan L, Zhao N, Le Beau MM (Nov 2000). "cDNA cloning and genomic structure of three genes localized to human chromosome band 5q31 encoding potential nuclear proteins". Genomics. 70 (1): 123–30. doi:10.1006/geno.2000.6345. PMID 11087669.
Lai F, Godley LA, Joslin J, Fernald AA, Liu J, Espinosa R, Zhao N, Pamintuan L, Till BG, Larson RA, Qian Z, Le Beau MM (Jan 2001). "Transcript map and comparative analysis of the 1.5-Mb commonly deleted segment of human 5q31 in malignant myeloid diseases with a del(5q)". Genomics. 71 (2): 235–45. doi:10.1006/geno.2000.6414. PMID 11161817.
Hu Z, Gomes I, Horrigan SK, Kravarusic J, Mar B, Arbieva Z, Chyna B, Fulton N, Edassery S, Raza A, Westbrook CA (Oct 2001). "A novel nuclear protein, 5qNCA (LOC51780) is a candidate for the myeloid leukemia tumor suppressor gene on chromosome 5 band q31". Oncogene. 20 (47): 6946–54. doi:10.1038/sj.onc.1204850. PMID 11687974.
Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (Aug 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (Jan 2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
Yamane K, Toumazou C, Tsukada Y, Erdjument-Bromage H, Tempst P, Wong J, Zhang Y (May 2006). "JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor". Cell. 125 (3): 483–95. doi:10.1016/j.cell.2006.03.027. PMID 16603237. S2CID 6643329.
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.

External links[]

JMJD1B+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

This article on a gene on human chromosome 5 is a stub. You can help Wikipedia by .

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000120733 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid15138608-4] Katoh M, Katoh M (Jun 2004). "Identification and characterization of JMJD2 family genes in silico". International Journal of Oncology. 24 (6): 1623–8. doi:10.3892/ijo.25.3.759. PMID 15138608.

[entrez-5] "Entrez Gene: JMJD1B jumonji domain containing 1B".

[1]

[2]

[3]

[4]

[5]

v t Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
1.14.11: 2-oxoglutarate	Prolyl hydroxylase HIF prolyl-hydroxylase EGLN1 EGLN2 EGLN3 P4HTM Lysyl hydroxylase AlkB ALKBH1 FTO
1.14.13: NADH or NADPH	Flavin-containing monooxygenase FMO1 FMO2 FMO3 FMO4 FMO5 Nitric oxide synthase NOS1 NOS2 NOS3 Cholesterol 7 alpha-hydroxylase Methane monooxygenase 3A4 14α-demethylase 24-hydroxycholesterol 7α-hydroxylase
1.14.14: reduced flavin or flavoprotein	19A1 2D6 2E1
1.14.15: reduced iron-sulfur protein	11B1 11B2 11A1
1.14.16: reduced pteridine (BH4 dependent)	Phenylalanine hydroxylase Tyrosine hydroxylase Tryptophan hydroxylase
1.14.17: reduced ascorbate	Dopamine beta-hydroxylase
1.14.18-19: other	Tyrosinase Stearoyl-CoA desaturase-1
1.14.99 - miscellaneous	Cyclooxygenase Heme oxygenase (HMOX1) Squalene monooxygenase 17A1 21A2 Ecdysone 20-monooxygenase Deoxyhypusine monooxygenase

v t Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)