KDM1A information

KDM1A
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2COM, 2DW4, 2EJR, 2H94, 2HKO, 2IW5, 2L3D, 2UXN, 2UXX, 2V1D, 2X0L, 2XAF, 2XAG, 2XAH, 2XAJ, 2XAQ, 2XAS, 2Y48, 2Z3Y, 2Z5U, 3ABT, 3ZMS, 3ZMT, 3ZMU, 3ZMV, 3ZMZ, 3ZN0, 3ZN1, 4BAY, 4CZZ, 4KUM, 4UV8, 4UV9, 4UVA, 4UVB, 4UVC, 4UXN, 5AFW, 5L3D, 5L3B, 5IT3, 5L3C, 4XBF
Identifiers
Aliases	KDM1A, AOF2, BHC110, KDM1, LSD1, CPRF, lysine demethylase 1A
External IDs	OMIM: 609132 MGI: 1196256 HomoloGene: 32240 GeneCards: KDM1A
Gene location (Human)
Chr.	Chromosome 1 (human)
End	23,083,689 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	136,330,034 bp
RNA expression pattern
	Top expressed in
	ganglionic eminence; ; stromal cell of endometrium; ; anterior pituitary; ; right uterine tube; ; canal of the cervix; ; minor salivary glands; ; left uterine tube; ; cerebellar hemisphere; ; skin of abdomen; ; smooth muscle tissue;
	Top expressed in
	urethra; ; epithelium of urethra; ; male urethra; ; ganglionic eminence; ; female urethra; ; abdominal wall; ; medial ganglionic eminence; ; vagina; ; primitive streak; ; cloaca;
	More reference expression data
	n/a
Gene ontology
Molecular function	DNA binding; telomeric repeat-containing RNA binding; demethylase activity; telomeric DNA binding; flavin adenine dinucleotide binding; p53 binding; protein binding; androgen receptor binding; nuclear receptor coactivator activity; histone H3-methyl-lysine-4 demethylase activity; oxidoreductase activity; chromatin binding; histone deacetylase activity; histone demethylase activity; enzyme binding; MRF binding; transcription factor binding; histone H3-methyl-lysine-9 demethylase activity;
Cellular component	DNA repair complex; nucleoplasm; nucleus; transcription regulator complex; protein-containing complex;
Biological process	regulation of transcription, DNA-templated; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; regulation of double-strand break repair via homologous recombination; cellular response to UV; histone H3-K4 demethylation; regulation of transcription by RNA polymerase II; negative regulation of DNA binding; protein demethylation; positive regulation of DNA-binding transcription factor activity; blood coagulation; negative regulation of protein binding; negative regulation of DNA-binding transcription factor activity; transcription, DNA-templated; multicellular organism development; negative regulation of DNA damage response, signal transduction by p53 class mediator; positive regulation of histone ubiquitination; cellular response to gamma radiation; negative regulation of transcription, DNA-templated; positive regulation of transcription by RNA polymerase II; alternative mRNA splicing, via spliceosome; cerebral cortex development; positive regulation of cell size; response to organic cyclic compound; guanine metabolic process; cellular response to cAMP; positive regulation of chromatin binding; histone deacetylation; positive regulation of neuron projection development; neuron maturation; response to fungicide; negative regulation of transcription by RNA polymerase II; histone H3-K9 demethylation; muscle cell development; chromatin organization; positive regulation of neuroblast proliferation; negative regulation of histone H3-K4 methylation; negative regulation of histone H3-K9 methylation; positive regulation of cold-induced thermogenesis; positive regulation of neural precursor cell proliferation; positive regulation of stem cell proliferation;
	Sources:Amigo / QuickGO
Orthologs
	23028
	99982
	ENSG00000004487
	ENSMUSG00000036940
	O60341
	Q6ZQ88
	NM_001009999; NM_015013; NM_001363654
	NM_133872; NM_001347221; NM_001356567
	NP_001009999; NP_055828; NP_001350583
	NP_001334150; NP_598633; NP_001343496
	Wikidata
View/Edit Human	View/Edit Mouse

Lysine-specific histone demethylase 1A (LSD1) also known as lysine (K)-specific demethylase 1A (KDM1A) is a protein that in humans is encoded by the KDM1A gene.^[5] LSD1 is a flavin-dependent monoamine oxidase, which can demethylate mono- and di-methylated lysines, specifically histone 3, lysine 4 (H3K4). Other reported methylated lysine substrates such as histone H3K9 and TP53 have not been biochemically validated.^[6] This enzyme plays a critical role in oocyte growth, embryogenesis, hematopoiesis and tissue-specific differentiation.^[7] LSD1 was the first histone demethylase to be discovered though more than 30 have since been described.^[8]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000004487 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000036940 – 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.
^ "Entrez Gene: Lysine (K)-specific demethylase 1A".
^ Rudolph T, Beuch S, Reuter G (August 2013). "Lysine-specific histone demethylase LSD1 and the dynamic control of chromatin". (review). Biological Chemistry. 394 (8): 1019–1028. doi:10.1515/hsz-2013-0119. PMID 23612539. S2CID 41459906.
^ Pedersen MT, Helin K (November 2010). "Histone demethylases in development and disease". (review). Trends in Cell Biology. 20 (11): 662–671. doi:10.1016/j.tcb.2010.08.011. PMID 20863703.
^ Shi Y, Lan F, Matson C, Mulligan P, Whetstine JR, Cole PA, et al. (December 2004). "Histone demethylation mediated by the nuclear amine oxidase homolog LSD1". Cell. 119 (7): 941–953. doi:10.1016/j.cell.2004.12.012. PMID 15620353. S2CID 10847230.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000004487 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000036940 – 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.

[entrez-5] "Entrez Gene: Lysine (K)-specific demethylase 1A".

[6] Rudolph T, Beuch S, Reuter G (August 2013). "Lysine-specific histone demethylase LSD1 and the dynamic control of chromatin". (review). Biological Chemistry. 394 (8): 1019–1028. doi:10.1515/hsz-2013-0119. PMID 23612539. S2CID 41459906.

[7] Pedersen MT, Helin K (November 2010). "Histone demethylases in development and disease". (review). Trends in Cell Biology. 20 (11): 662–671. doi:10.1016/j.tcb.2010.08.011. PMID 20863703.

[8] Shi Y, Lan F, Matson C, Mulligan P, Whetstine JR, Cole PA, et al. (December 2004). "Histone demethylation mediated by the nuclear amine oxidase homolog LSD1". Cell. 119 (7): 941–953. doi:10.1016/j.cell.2004.12.012. PMID 15620353. S2CID 10847230.

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