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KDM1B
Available structures PDB Ortholog 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; MGI: 2145261; HomoloGene: 131158; GeneCards: KDM1B; OMA:KDM1B - orthologs
Gene location (Human) Chr. Chromosome 6 (human) Band 6p22.3 Start 18,155,329 bp End 18,223,854 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13|13 A5 Start 47,196,975 bp End 47,238,755 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in secondary oocyte monocyte skin of arm testicle bronchial epithelial cell islet of Langerhans mucosa of ileum bone marrow ganglionic eminence right lobe of thyroid gland Top expressed in primary oocyte zygote secondary oocyte parotid gland transitional epithelium of urinary bladder lacrimal gland lobe of prostate Gonadal ridge skin of external ear seminal vesicula More reference expression data BioGPS n/a
Gene ontology Molecular function metal ion binding DNA binding oxidoreductase activity flavin adenine dinucleotide binding histone demethylase activity protein binding zinc ion binding histone binding FAD binding Cellular component 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 protein deubiquitination histone H3-K4 demethylation chromatin organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 221656 218214 Ensembl ENSG00000165097 ENSMUSG00000038080 UniProt Q8NB78 Q8CIG3 RefSeq (mRNA) NM_153042 NM_001364614 NM_172262 RefSeq (protein) NP_694587 NP_001351543 NP_758466 NP_001389837 NP_001389838 Location (UCSC) Chr 6: 18.16 – 18.22 Mb Chr 13: 47.2 – 47.24 Mb PubMed search
Wikidata
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Lysine (K)-specific demethylase 1B is a protein that in humans is encoded by the KDM1B gene.

Function

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

References

1. ^ GRCh38: Ensembl release 89: ENSG00000165097 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000038080 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ "Entrez Gene: Lysine (K)-specific demethylase 1B".
6. 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.

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