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Browse result for Down-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.



PTMD IDUniProt AccessionEntrez IDGene NameProtein NameOrganism
PTMD00225P6843183508
H3C1
Histone H3.1
Homo sapiens
PTMD00307A0A0U1RQF0
FASN
Fatty acid synthase
Homo sapiens
PTMD00314P067332023
ENO1
Alpha-enolase
Homo sapiens
PTMD00481O758743417
IDH1
Isocitrate dehydrogenase [NADP] cytoplasmic -specific ICDH)
Homo sapiens
PTMD00532P115864522
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
PTMD00692Q150194735
SEPTIN2
Septin-2
Homo sapiens
PTMD00469O5514311938
Atp2a2
Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 -ATPase 2) ATPase)
Mus musculus