EHMT1

EHMT1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2IGQ, 2RFI, 3B7B, 3B95, 3FPD, 3HNA, 3MO0, 3MO2, 3MO5, 3SW9, 3SWC, 4I51
Identifiers
Aliases	EHMT1, EUHMTASE1, Eu-HMTase1, FP13812, GLP, GLP1, KMT1D, bA188C12.1, euchromatic histone lysine methyltransferase 1
External IDs	MGI: 1924933 HomoloGene: 11698 GeneCards: EHMT1
Gene ontology Molecular function • methyltransferase activity • transferase activity • histone methyltransferase activity (H3-K9 specific) • zinc ion binding • p53 binding • C2H2 zinc finger domain binding • histone-lysine N-methyltransferase activity • metal ion binding • histone methyltransferase activity (H3-K27 specific) • protein-lysine N-methyltransferase activity • protein binding Cellular component • nucleoplasm • chromosome • nucleus Biological process • response to fungicide • embryo development • negative regulation of transcription from RNA polymerase II promoter • peptidyl-lysine monomethylation • histone H3-K27 methylation • DNA methylation • methylation • histone H3-K9 methylation • peptidyl-lysine dimethylation • histone lysine methylation • histone methylation • negative regulation of transcription, DNA-templated • chromatin modification • regulation of signal transduction by p53 class mediator • covalent chromatin modification Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	79813	77683
Ensembl	ENSG00000181090	ENSMUSG00000036893
UniProt	Q9H9B1	Q5DW34
RefSeq (mRNA)	NM_001145527 NM_024757	NM_001012518 NM_001109686 NM_001109687 NM_172545
RefSeq (protein)	NP_001138999.1 NP_079033.4	NP_001012536.2 NP_001103156.1 NP_001103157.1
Location (UCSC)	Chr 9: 137.62 – 137.87 Mb	Chr 2: 24.79 – 24.92 Mb
PubMed search	[1]	[2]
Wikidata

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Euchromatic histone-lysine N-methyltransferase 1, also known as G9a-like protein (GLP), is a protein that in humans is encoded by the EHMT1 gene.^[3]

Function

The protein encoded by this gene is a histone methyltransferase that is part of the E2F6 complex, which represses transcription. The encoded protein methylates the Lys-9 position of histone H3, which tags it for transcriptional repression. This protein may be involved in the silencing of MYC- and E2F-responsive genes and therefore could play a role in the G0/G1 cell cycle transition.^[3]

Clinical significance

Defects in this gene are a cause of chromosome 9q subtelomeric deletion syndrome (9q-syndrome).^[3]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. "Entrez Gene: Euchromatic histone-lysine N-methyltransferase 1". Retrieved 2012-03-04.

Further reading

• Ogawa H, Ishiguro K, Gaubatz S, Livingston DM, Nakatani Y (May 2002). "A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells". Science. 296 (5570): 1132–1136. doi:10.1126/science.1069861. PMID 12004135.
• Kleefstra T, Smidt M, Banning MJ, Oudakker AR, Van Esch H, de Brouwer AP, Nillesen W, Sistermans EA, Hamel BC, de Bruijn D, Fryns JP, Yntema HG, Brunner HG, de Vries BB, van Bokhoven H (Apr 2005). "Disruption of the gene Euchromatin Histone Methyl Transferase1 (Eu-HMTase1) is associated with the 9q34 subtelomeric deletion syndrome". Journal of Medical Genetics. 42 (4): 299–306. doi:10.1136/jmg.2004.028464. PMC 1736026. PMID 15805155.
• Cebrian A, Pharoah PD, Ahmed S, Ropero S, Fraga MF, Smith PL, Conroy D, Luben R, Perkins B, Easton DF, Dunning AM, Esteller M, Ponder BA (Aug 2006). "Genetic variants in epigenetic genes and breast cancer risk". Carcinogenesis. 27 (8): 1661–1669. doi:10.1093/carcin/bgi375. PMID 16501248.
• Ueda J, Tachibana M, Ikura T, Shinkai Y (Jul 2006). "Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the co-repressor molecule CtBP". The Journal of Biological Chemistry. 281 (29): 20120–20128. doi:10.1074/jbc.M603087200. PMID 16702210.
• Kleefstra T, Brunner HG, Amiel J, Oudakker AR, Nillesen WM, Magee A, Geneviève D, Cormier-Daire V, van Esch H, Fryns JP, Hamel BC, Sistermans EA, de Vries BB, van Bokhoven H (Aug 2006). "Loss-of-function mutations in euchromatin histone methyl transferase 1 (EHMT1) cause the 9q34 subtelomeric deletion syndrome". American Journal of Human Genetics. 79 (2): 370–377. doi:10.1086/505693. PMC 1559478. PMID 16826528.
• Heo K, Kim B, Kim K, Choi J, Kim H, Zhan Y, Ranish JA, An W (May 2007). "Isolation and characterization of proteins associated with histone H3 tails in vivo". The Journal of Biological Chemistry. 282 (21): 15476–15483. doi:10.1074/jbc.M610270200. PMID 17403666.
• Collins RE, Northrop JP, Horton JR, Lee DY, Zhang X, Stallcup MR, Cheng X (Mar 2008). "The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules". Nature Structural & Molecular Biology. 15 (3): 245–250. doi:10.1038/nsmb.1384. PMC 2586904. PMID 18264113.
• Shirato H, Ogawa S, Nakajima K, Inagawa M, Kojima M, Tachibana M, Shinkai Y, Takeuchi T (Jan 2009). "A jumonji (Jarid2) protein complex represses cyclin D1 expression by methylation of histone H3-K9". The Journal of Biological Chemistry. 284 (2): 733–739. doi:10.1074/jbc.M804994200. PMID 19010785.
• Biron VL, Dort JC (Jun 2008). "Epigenetic perspective into head and neck cancer through in silico gene expression profiling of histone lysine methyltransferases". Journal of Otolaryngology - Head & Neck Surgery = Le Journal D'oto-Rhino-Laryngologie Et De Chirurgie Cervico-Faciale. 37 (3): 366–372. PMID 19128641.
• Kleefstra T, van Zelst-Stams WA, Nillesen WM, Cormier-Daire V, Houge G, Foulds N, van Dooren M, Willemsen MH, Pfundt R, Turner A, Wilson M, McGaughran J, Rauch A, Zenker M, Adam MP, Innes M, Davies C, López AG, Casalone R, Weber A, Brueton LA, Navarro AD, Bralo MP, Venselaar H, Stegmann SP, Yntema HG, van Bokhoven H, Brunner HG (Sep 2009). "Further clinical and molecular delineation of the 9q subtelomeric deletion syndrome supports a major contribution of EHMT1 haploinsufficiency to the core phenotype". Journal of Medical Genetics. 46 (9): 598–606. doi:10.1136/jmg.2008.062950. PMID 19264732.
• Ohno H, Shinoda K, Ohyama K, Sharp LZ, Kajimura S (Dec 2013). "EHMT1 controls brown adipose cell fate and thermogenesis through the PRDM16 complex". Nature. 504 (7478): 163–7. doi:10.1038/nature12652. PMC 3855638. PMID 24196706.