Primary Information |
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BoMiProt ID | Bomi377 |
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Protein Name | Ubiquitin-fold modifier 1 |
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Organism | Bos taurus |
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Uniprot ID | Q2KJG2 |
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Milk Fraction | Exosome |
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Ref Sequence ID | NP_001039779.1 |
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Aminoacid Length | 85 |
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Molecular Weight | 9168 |
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FASTA Sequence |
Download |
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Gene Name | UFM1 |
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Gene ID | 530547 |
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Protein Existence Status | Reviewed: Protein inferred from homology |
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Secondary Information |
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Presence in other biological fluids/tissue/cells | ocalized in both the nucleus and the cytoplasm |
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Protein Function | Ubiquitin-like protein; small Ubl modifier; Ufm1 conjugation to its
target proteins, a process termed as ufmylation, is
accomplished in multi-step biochemical reactions that are
catalyzed by a set of Ufm1-specific enzymes |
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Biochemical Properties | Expressed in human cells as a precursor with a C-terminal Ser-Cys dipeptide extension, which needs to be processed by UFSPs prior to conjugation to target proteins; Matured UFM1 has a single glycine residue at the C-terminus, which also is required for conjugation to its target proteins, unlike ubiquitin and most other ubiquitin-like proteins, such as SUMO and NEDD8, which have a conserved C-terminal di-glycine; adopts an ubiquitin-like α + β fold with ordered β−β−α−β−β−α−β secondary structure along the sequence; a special feature in UFM1 structure is the absence of the cluster of the acidic residues in the α1 surface, which is displayed by ubiquitin; employs the uncharged surface for binding to its putative partners |
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Significance in milk | play an important role during the inflammatory response and thereby acts as a potential therapeutic target for bovine mastitis |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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Predicted Disorder Regions | NA |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Bibliography | 1. Li, C. et al. (2019) ‘UFL1 Alleviates Lipopolysaccharide-Induced Cell Damage and Inflammation via Regulation of the TLR4/NF- κ B Pathway in Bovine Mammary Epithelial Cells’, Oxidative Medicine and Cellular Longevity. Hindawi, 2019, pp. 1–17. doi: 10.1155/2019/6505373. |