Search Results
Overview
| Uniprot ID | P26358 |
|---|---|
| Protein Name | DNA (cytosine-5)-methyltransferase 1 |
| Gene Name | DNMT1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1121 | GKGKGKPKSQACEPS |
| 142 | PRTPRRSKSDGEAKP |
| 173 | TITSHFAKGPAKRKP |
| 291 | KKHRSQPKDLAAKRR |
| 323 | DEDEKEEKRRKTTPK |
| 330 | KRRKTTPKEPTEKKM |
| 341 | EKKMARAKTVMNSKT |
| 347 | AKTVMNSKTHPPKCI |
| 961 | SPVKRPRKEPVDEDL |
Function
DNA methyltransferase that methylates CpG residues (PubMed:17200670, PubMed:18754681, PubMed:21745816, PubMed:26070743). Preferentially methylates hemimethylated DNA (PubMed:21745816, PubMed:26070743). Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance (PubMed:17200670, PubMed:21745816). Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication (PubMed:21745816). It is responsible for maintaining methylation patterns established in development (PubMed:21745816). DNA methylation is coordinated with methylation of histones (PubMed:16357870). Mediates transcriptional repression by direct binding to HDAC2 (PubMed:10888872). In association with DNMT3B and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9 (PubMed:18413740). Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells (PubMed:24623306). Also required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (PubMed:24623306). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing (PubMed:24623306)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000792 | heterochromatin |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005721 | pericentric heterochromatin |
| Cellular Component | GO:0005657 | replication fork |
| Molecular Function | GO:0003886 | DNA (cytosine-5-)-methyltransferase activity |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0009008 | DNA-methyltransferase activity |
| Molecular Function | GO:0140258 | histone H3K14ub reader activity |
| Molecular Function | GO:0140254 | histone H3K18ub reader activity |
| Molecular Function | GO:0140257 | histone H3K23ub reader activity |
| Molecular Function | GO:0106222 | lncRNA binding |
| Molecular Function | GO:0008327 | methyl-CpG binding |
| Molecular Function | GO:1990841 | promoter-specific chromatin binding |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0141119 | chromosomal DNA methylation maintenance following DNA replication |
| Biological Process | GO:0006346 | DNA methylation-dependent constitutive heterochromatin formation |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0032259 | methylation |
| Biological Process | GO:0010629 | negative regulation of gene expression |
| Biological Process | GO:0044027 | negative regulation of gene expression via chromosomal CpG island methylation |
| Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
| Biological Process | GO:1905460 | negative regulation of vascular associated smooth muscle cell apoptotic process |
| Biological Process | GO:1905931 | negative regulation of vascular associated smooth muscle cell differentiation involved in phenotypic switching |
| Biological Process | GO:0010628 | positive regulation of gene expression |
| Biological Process | GO:1904707 | positive regulation of vascular associated smooth muscle cell proliferation |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.