UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1)
The protein contains 1555 amino acids for an estimated molecular weight of 177190 Da.
Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation. (updated: March 4, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- 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.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- 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.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
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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Biological Process
'de novo' posttranslational protein folding
Cellular protein metabolic process
Endoplasmic reticulum mannose trimming
Endoplasmic reticulum unfolded protein response
ER-associated misfolded protein catabolic process
Post-translational protein modification
Protein folding
Protein N-linked glycosylation via asparagine
UDP-glucosylation
The reference OMIM entry for this protein is 605897
Udp-glucose:glycoprotein glucosyltransferase 1; uggt1
Hugt1
DESCRIPTION
UDP-glucose:glycoprotein glucosyltransferase (UGT) is a soluble protein of the endoplasmic reticulum (ER) that selectively reglucosylates unfolded glycoproteins, thus providing quality control for protein transport out of the ER.CLONING
Using a portion of Drosophila UGT to screen a human fetal liver cDNA library, Arnold et al. (2000) isolated HUGT1. The assembled full-length HUGT1 cDNA encodes a deduced 1,555-amino acid protein with a predicted ER-targeting signal sequence, ER retrieval signal, 3 N-glycosylation sites, and 2 disulfide loops. HUGT1 shares 55% sequence identity with HUGT2 (605898) and 31 to 45% identity with Drosophila, C. elegans, and S. pombe homologs. Northern blot analysis detected 3 HUGT1 transcripts of 5.7, 8, and 10.6 kb in pancreas, heart, brain, placenta, lung, liver, skeletal muscle, and kidney. Arnold et al. (2000) noted that HUGT1 and HUGT2 differ slightly in their tissue distribution.GENE FUNCTION
Using cell culture experiments, Arnold et al. (2000) demonstrated that HUGT1 expression was induced upon disruption of protein folding in the ER, whereas HUGT2 was not. By immunofluorescence microscopy, they localized HUGT1 to the ER. Arnold et al. (2000) expressed HUGT1 in transient transfection experiments and demonstrated UGT activity. Using site-directed mutagenesis, they identified 4 residues of HUGT1 that are essential for catalytic function.MAPPING
Scott (2001) mapped the HUGT1 gene to chromosome 2 based on sequence similarity between the HUGT1 sequence (GenBank GENBANK AF227905) and a chromosome 2 clone (GenBank GENBANK AC017079). ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 605897 was added.