KDM1B

KDM1B
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	4FWE, 4FWF, 4FWJ, 4GU0, 4GU1, 4GUR, 4GUS, 4GUT, 4GUU, 4HSU
Identifiers
Aliases	KDM1B, AOF1, C6orf193, LSD2, bA204B7.3, dJ298J15.2, lysine demethylase 1B
External IDs	OMIM: 613081 HomoloGene: 131158 GeneCards: KDM1B
Gene location (Human)
Chr.	Chromosome 6 (human)[1]
End	18,223,854 bp[1]
Gene ontology
Molecular function	• metal ion binding; • DNA binding; • oxidoreductase activity; • flavin adenine dinucleotide binding; • histone demethylase activity; • GO:0001948 protein binding; • zinc ion binding; • histone demethylase activity (H3-dimethyl-K4 specific); • histone demethylase activity (H3-monomethyl-K4 specific); • histone binding; • FAD binding;
Cellular component	• cell nucleus; • nucleoplasm; • nucleosome;
Biological process	• multicellular organism development; • regulation of transcription, DNA-templated; • regulation of gene expression by genetic imprinting; • regulation of DNA methylation; • transcription, DNA-templated; • DNA methylation involved in gamete generation; • oxidation-reduction process; • protein deubiquitination; • histone H3-K4 demethylation; • chromatin organization;
	Sources:Amigo / QuickGO
Orthologs
	221656
	n/a
	ENSG00000165097
	n/a
	Q8NB78
	n/a
	NM_153042; NM_001364614
	n/a
	NP_694587; NP_001351543
	n/a
	Wikidata
View/Edit Human

Lysine (K)-specific demethylase 1B is a protein that in humans is encoded by the KDM1B gene.[3]

Function

Flavin-dependent histone demethylases, such as KDM1B, regulate histone lysine methylation, an epigenetic mark that regulates gene expression and chromatin function.[3][4]

GRCh38: Ensembl release 89: ENSG00000165097 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Entrez Gene: Lysine (K)-specific demethylase 1B".
Karytinos A, Forneris F, Profumo A, Ciossani G, Battaglioli E, Binda C, Mattevi A (Jun 2009). "A novel mammalian flavin-dependent histone demethylase". The Journal of Biological Chemistry. 284 (26): 17775–82. doi:10.1074/jbc.M109.003087. PMC 2719416. PMID 19407342.

Yu H, Mashtalir N, Daou S, Hammond-Martel I, Ross J, Sui G, Hart GW, Rauscher FJ, Drobetsky E, Milot E, Shi Y, Affar el B (Nov 2010). "The ubiquitin carboxyl hydrolase BAP1 forms a ternary complex with YY1 and HCF-1 and is a critical regulator of gene expression". Molecular and Cellular Biology. 30 (21): 5071–85. doi:10.1128/MCB.00396-10. PMC 2953049. PMID 20805357.
Fang R, Barbera AJ, Xu Y, Rutenberg M, Leonor T, Bi Q, Lan F, Mei P, Yuan GC, Lian C, Peng J, Cheng D, Sui G, Kaiser UB, Shi Y, Shi YG (Jul 2010). "Human LSD2/KDM1b/AOF1 regulates gene transcription by modulating intragenic H3K4me2 methylation". Molecular Cell. 39 (2): 222–33. doi:10.1016/j.molcel.2010.07.008. PMC 3518444. PMID 20670891.
Ciccone DN, Su H, Hevi S, Gay F, Lei H, Bajko J, Xu G, Li E, Chen T (Sep 2009). "KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints". Nature. 461 (7262): 415–8. Bibcode:2009Natur.461..415C. doi:10.1038/nature08315. PMID 19727073. S2CID 1143128.
Machida YJ, Machida Y, Vashisht AA, Wohlschlegel JA, Dutta A (Dec 2009). "The deubiquitinating enzyme BAP1 regulates cell growth via interaction with HCF-1". The Journal of Biological Chemistry. 284 (49): 34179–88. doi:10.1074/jbc.M109.046755. PMC 2797188. PMID 19815555.

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