KDM1B

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

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] Band 6p22.3 Start 18,155,329 bp[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
Species	Human	Mouse
Entrez	221656	n/a
Ensembl	ENSG00000165097	n/a
UniProt	Q8NB78	n/a
RefSeq (mRNA)	NM_153042 NM_001364614	n/a
RefSeq (protein)	NP_694587 NP_001351543	n/a
Location (UCSC)	Chr 6: 18.16 – 18.22 Mb	n/a
PubMed search	[2]	n/a
Wikidata
View/Edit Human

Function

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

References

1. GRCh38: Ensembl release 89: ENSG00000165097 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Entrez Gene: Lysine (K)-specific demethylase 1B".
4. 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.

Further reading

• 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.

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