Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to lysine residues of substrate proteins as a monomer or a lysine-linked polymer (PubMed:15071506, PubMed:20018847, PubMed:27653677, PubMed:29868776, PubMed:30626644, PubMed:38377992, PubMed:38383785). The so-called ufmylation, requires the UFM1-activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme UFC1, and the UFM1-ligase E3 enzyme UFL1 (PubMed:15071506, PubMed:20018847, PubMed:27653677, PubMed:29868776). Ufmylation is involved in various processes, such as ribosome recycling, response to DNA damage, transcription or reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress (PubMed:25219498, PubMed:32160526, PubMed:38383785).
Leukodystrophy, hypomyelinating, 14
HLD14
An autosomal recessive, severe disorder characterized by atrophy of the basal ganglia and cerebellum, hypomyelination, severe developmental delay, typically without intentional movements and language development, and microcephaly. Almost all patients exhibit spasticity, extrapyramidal movement abnormalities, and severe drug-resistant epilepsy. Disease onset is early in infancy, and most patients die in the first years of life.
None
The disease is caused by variants affecting the gene represented in this entry. The disease-causing variant may be a homozygous 3-bp deletion in the promoter region of the UFM1 gene, which segregates with the disorder in affected families. In vitro expression studies in different cell lines showed that the mutation significantly reduces transcriptional activity in certain neuronal cell lines (SY5Y and U373), but not in other cell lines, including HeLa and HOF-F2.
UFM1 precursor is cleaved by UFSP1, promoting its maturation: processing of the C-terminal Ser-Cys dipeptide is required to expose its C-terminal conserved Gly residue.
Belongs to the UFM1 family.
C13orf20, BM-002, UFM1, Ubiquitin-fold modifier 1
Proteins
Oncology
9118Da
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ab104461