※ PTMD 2.0 database Online Browse Options
Browse result for Up-regulation in Decrotonylation
※ introduction Lysine crotonylation has been discovered in histone and non-histone proteins and found to be involved in diverse diseases and biological processes, such as neuropsychiatric disease, carcinogenesis, spermatogenesis, tissue injury, and inflammation. The unique carbon¨Ccarbon ¦Ð-bond structure indicates that lysine crotonylation may use distinct regulatory mechanisms from the widely studied other types of lysine acylation.
Reference
Pubmed: Jiang G, Li C, Lu M, Lu K, Li H. Protein lysine crotonylation: past, present, perspective. Cell Death Dis. 2021 Jul 14;12(7):703. doi: 10.1038/s41419-021-03987-z.
Reference
Pubmed: Jiang G, Li C, Lu M, Lu K, Li H. Protein lysine crotonylation: past, present, perspective. Cell Death Dis. 2021 Jul 14;12(7):703. doi: 10.1038/s41419-021-03987-z.
| PTMD ID | UniProt Accession | Entrez ID | Gene Name | Protein Name | Organism |
|---|---|---|---|---|---|
| PTMD00532 | P11586 | 4522 | MTHFD1 | C-1-tetrahydrofolate synthase, cytoplasmic [Cleaved into: C-1-tetrahydrofolate synthase, cytoplasmic, N-terminally processed] [Includes: Methylenetetrahydrofolate dehydrogenase ; Methenyltetrahydrofolate cyclohydrolase ; Formyltetrahydrofolate synthetase ] | Homo sapiens |
| PTMD01091 | P36776 | 9361 | LONP1 | Lon protease homolog, mitochondrial | Homo sapiens |
