Ubiquitin-fold modifier-conjugating enzyme 1 (UFC1)
The protein contains 167 amino acids for an estimated molecular weight of 19458 Da.
E1-like enzyme which specifically catalyzes the second step in ufmylation (PubMed:15071506, PubMed:29868776). Accepts the ubiquitin-like modifier UFM1 from the E1 enzyme UBA5 and forms an intermediate with UFM1 via a thioester linkage (PubMed:15071506, PubMed:29868776). Ufmylation is involved in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress (PubMed:32160526). (updated: Aug. 12, 2020)
Protein identification was indicated in the following studies:
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs17849932 | |
| NEDSG | |
| NEDSG |
The reference OMIM entry for this protein is 610554
Ubiquitin-fold modifier-conjugating enzyme 1; ufc1
Ufm1-conjugating enzyme 1
DESCRIPTION
UFC1 is an E2-like conjugating enzyme for ubiquitin-fold modifier-1 (UFM1; 610553) (Komatsu et al., 2004).CLONING
Using coimmunoprecipitation with FLAG-tagged UBE1DC1/UBE5 (610552) expressed in HEK293 cells, Komatsu et al. (2004) purified fragments of proteins physically associated with UBE1DC1. By database analysis with these fragments followed by PCR of human liver cDNA, they cloned UFC1 and UFM1. The deduced 167-amino acid UFC1 protein has a predicted molecular mass of 19.4 kD and contains a potential active site cysteine residue that shares similarity with ubiquitin E2 conjugating enzymes (Komatsu et al., 2004).GENE FUNCTION
Using FLAG-tagged UFC1 and mutant constructs coexpressed with Myc-tagged UFM1 in HEK293 cells as well as an in vitro UFM1 conjugation assay, Komatsu et al. (2004) showed that UFC1 acts as an E2-like enzyme that conjugates with UFM1 via a thioester linkage, with the active site at cys116. ... More on the omim web site
Aug. 24, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 610554 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).