EHMT1
entrez
79813
canonical
uniprot
Q9H9B1
canonical
ensembl
ENSG00000181090
resolver
ensp
ENSP00000417328
resolver
ensp
ENSP00000417980
resolver
ensp
ENSP00000485900
resolver
ensp
ENSP00000489961
resolver
ensp
ENSP00000490056
resolver
ensp
ENSP00000490328
resolver
ensp
ENSP00000566822
resolver
ensp
ENSP00000689109
resolver
ensp
ENSP00000777008
resolver
enst
ENST00000629335
resolver
enst
ENST00000637161
resolver
genesymbol
EHMT1
resolver
genesymbol_syn
EUHMTASE1
resolver
genesymbol_syn
GLP
resolver
genesymbol_syn
KIAA1876
resolver
genesymbol_syn
KMT1D
resolver
hgnc
HGNC:24650
resolver
uniprot
A0A1B0GUD1
resolver
uniprot
A0A1B0GV09
resolver
uniprot
B1AQ58
resolver
uniprot
B1AQ59
resolver
uniprot
Q86X08
resolver
uniprot
Q8TCN7
resolver
uniprot
Q96F53
resolver
uniprot
Q96JF1
resolver
uniprot
Q96KH4
resolver
uniprot_entry
A0A1B0GUD1_HUMAN
resolver
uniprot_entry
A0A1B0GV09_HUMAN
resolver
uniprot_entry
EHMT1_HUMAN
resolver
uniprot_sec
B1AQ58
resolver
uniprot_sec
B1AQ59
resolver
uniprot_sec
Q86X08
resolver
uniprot_sec
Q8TCN7
resolver
uniprot_sec
Q96F53
resolver
uniprot_sec
Q96JF1
resolver
uniprot_sec
Q96KH4
resolver
activity_regulation
ACTIVITY REGULATION: Methyltransferase activity is inhibited by BIX-01294. Efficiently inhibited by compound E72, a BIX-01294 derivative in which the diazepane ring and the benzyl are replaced with a 3-dimethylaminopropyl and a 5-aminopentyl group at sites B and C, respectively. {ECO:0000269|PubMed:20434463}.
uniprot
proteins
amino_acid_sequence
MAAADAEAVPARGEPQQDCCVKTELLGEETPMAADEGSAEKQAGEAHMAADGETNGSCENSDASSHANAAKHTQDSARVNPQDGTNTLTRIAENGVSERDSEAAKQNHVTADDFVQTSVIGSNGYILNKPALQAQPLRTTSTLASSLPGHAAKTLPGGAGKGRTPSAFPQTPAAPPATLGEGSADTEDRKLPAPGADVKVHRARKTMPKSVVGLHAASKDPREVREARDHKEPKEEINKNISDFGRQQLLPPFPSLHQSLPQNQCYMATTKSQTACLPFVLAAAVSRKKKRRMGTYSLVPKKKTKVLKQRTVIEMFKSITHSTVGSKGEKDLGASSLHVNGESLEMDSDEDDSEELEEDDGHGAEQAAAFPTEDSRTSKESMSEADRAQKMDGESEEEQESVDTGEEEEGGDESDLSSESSIKKKFLKRKGKTDSPWIKPARKRRRRSRKKPSGALGSESYKSSAGSAEQTAPGDSTGYMEVSLDSLDLRVKGILSSQAEGLANGPDVLETDGLQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTNSVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCGYFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESSKAKEVTIAKADTTSTVTPVPGQEKGSALEGRADTTTGSAAGPPLSEDDKLQGAASHVPEGFDPTGPAGLGRPTPGLSQGPGKETLESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSQVWSALQMSKALQDSAPDRPSPVERIVSRDIARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHSSAALAQRQASAAQEAQEDGLPDTSSAAAADPL
uniprot
proteins
disease_involvement
DISEASE: Kleefstra syndrome 1 (KLEFS1) [MIM:610253]: A form of Kleefstra syndrome, an autosomal dominant disease characterized by variable intellectual disability, psychomotor developmental delay, seizures, behavioral abnormalities, and facial dysmorphisms. KLEFS1 patients additionally manifest brachy(micro)cephaly, congenital heart defects, and urogenital defects. {ECO:0000269|PubMed:16826528, ECO:0000269|PubMed:19264732}. Note=The disease is caused by variants affecting the gene represented in this entry. The syndrome can be either caused by intragenic EHMT1 mutations leading to haploinsufficiency of the EHMT1 gene or by a submicroscopic 9q34.3 deletion. Although it is not known if and to what extent other genes in the 9q34.3 region contribute to the syndrome observed in deletion cases, EHMT1 seems to be the major determinant of the core disease phenotype (PubMed:19264732). {ECO:0000269|PubMed:16826528, ECO:0000269|PubMed:19264732}.
uniprot
proteins
ec_number
2.1.1.-
uniprot
proteins
ec_number
2.1.1.367
uniprot
proteins
function
FUNCTION: Histone methyltransferase that specifically mono-, di- and trimethylates 'Lys-9' of histone H3 (H3K9me1, H3K9me2 and H3K9me3, respectively) in euchromatin (PubMed:12004135). H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones (PubMed:12004135). Also weakly methylates 'Lys-27' of histone H3 (H3K27me) (PubMed:12004135). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently (By similarity). Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1 (PubMed:12004135). During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle (PubMed:12004135). Involved in the differentiation of myoblastic precursors into brown adipose cells: following recruitment to chromatin by PRDM16, mediates formation of H3K9me2 and H3K9me3, inhibiting the expression of white adipose-selective genes (By similarity). Also involved in the differentiation of beige adipocytes from white adipose cells following recruitment by PRDM16 (By similarity). EHMT1 also promotes protein stabilization of PRDM16, by preventing PRDM16 ubiquitination and degradation (By similarity). In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53 (PubMed:20118233). Represses the expression of mitochondrial function-related genes, perhaps by occupying their promoter regions, working in concert with probable chromatin reader BAZ2B (By similarity). {ECO:0000250|UniProtKB:Q5DW34, ECO:0000269|PubMed:12004135, ECO:0000269|PubMed:20118233}.
uniprot
proteins
mass_dalton
141466
uniprot
proteins
mutagenesis
MUTAGEN 874; /note="W->A: Abolishes binding to methylated RELAK310me1, histone H3K9me1 and H3K9me2."; /evidence="ECO:0000269|PubMed:21515635"; MUTAGEN 882; /note="E->A: Abolishes binding to methylated RELAK310me1, histone H3K9me1 and H3K9me2."; /evidence="ECO:0000269|PubMed:21515635"; MUTAGEN 905; /note="E->A: Abolishes binding to histone H3K9me."; /evidence="ECO:0000269|PubMed:18264113"; MUTAGEN 912; /note="W->A: Abolishes binding to methylated RELAK310me1, histone H3K9me1 and H3K9me2."; /evidence="ECO:0000269|PubMed:21515635
uniprot
proteins
protein_family
Class V-like SAM-binding methyltransferase superfamily
uniprot
proteins
pubmed
11347906
uniprot
proteins
pubmed
12004135
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16702210
uniprot
proteins
pubmed
16826528
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18264113
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19061646
uniprot
proteins
pubmed
19264732
uniprot
proteins
pubmed
20084102
uniprot
proteins
pubmed
20118233
uniprot
proteins
pubmed
20434463
uniprot
proteins
pubmed
20871592
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21515635
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25489052
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
28112733
uniprot
proteins
sequence_length
1298
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5DW34}. Chromosome {ECO:0000250|UniProtKB:Q5DW34}. Note=Associates with euchromatic regions. {ECO:0000250|UniProtKB:Q5DW34}.
uniprot
proteins