SUMO-conjugating enzyme UBC9 (UBE2I)
The protein contains 158 amino acids for an estimated molecular weight of 18007 Da.
Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3, SUMO4 and SUMO1P1/SUMO5 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451. Can catalyze the formation of poly-SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation. Sumoylates p53/TP53 at 'Lys-386'. Mediates sumoylation of ERCC6 which is essential for its transcription-coupled nucleotide excision repair activity (PubMed:26620705). (updated: Oct. 16, 2019)
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.
- 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.
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
Cell cycle
Cell division
Cellular protein metabolic process
Cellular protein modification process
Chromosome segregation
Global genome nucleotide-excision repair
Mitotic nuclear division
Mitotic nuclear membrane reassembly
Negative regulation of transcription by RNA polymerase II
Negative regulation of transcription, DNA-templated
Positive regulation of DNA-binding transcription factor activity
Positive regulation of I-kappaB kinase/NF-kappaB signaling
Positive regulation of intracellular steroid hormone receptor signaling pathway
Positive regulation of SUMO transferase activity
Post-translational protein modification
Proteasome-mediated ubiquitin-dependent protein catabolic process
Protein sumoylation
Protein ubiquitination
Regulation of signaling receptor activity
Ubiquitin-dependent protein catabolic process
Viral process
Viral protein processing
Vitamin D metabolic process
Cellular Component
Cytoplasm
Cytosol
Dendrite
Fibrillar center
Nuclear envelope
Nucleoplasm
Nucleus
PML body
Sumoylated E2 ligase complex
Synapse
Synaptonemal complex
Transferase complex
Molecular Function
ATP binding
BHLH transcription factor binding
Enzyme binding
HLH domain binding
Ligase activity
Poly(A) RNA binding
Protein C-terminus binding
RING-like zinc finger domain binding
RNA binding
Small protein activating enzyme binding
SUMO conjugating enzyme activity
SUMO transferase activity
Transcription coregulator binding
Transcription factor binding
Ubiquitin-protein transferase activity
The reference OMIM entry for this protein is 601661
Ubiquitin-conjugating enzyme e2i; ube2i
Ubiquitin-conjugating enzyme ubc9, yeast, homolog of; ubc9
CLONING
The ubiquitin-conjugating enzymes (E2s) are a family of proteins involved in the ubiquitin-dependent protein degradation system. In yeast, at least 10 different E2s have been identified; they are involved in essential cellular processes such as DNA repair, cell cycle control, and stress responses. Using the yeast 2-hybrid system with the repressor domain of the Wilms tumor gene product (WT1; 607102) as bait, Wang et al. (1996) isolated a cDNA encoding a human homolog of the yeast ubiquitin-conjugating enzyme-9 (UBC9). Human UBC9 has 56% identity with yeast ubc9 and contains the active site cysteine necessary for the ubiquitin-conjugating activity of all E2 enzymes. Northern blot analysis revealed human UBC9 transcripts of 4.4, 2.4, and 1.3 kb in all of the tissues examined. Watanabe et al. (1996) likewise cloned UBE2I, a human homolog of yeast ubc9. The deduced protein contains 158 amino acids. Yasugi and Howley (1996) independently isolated the human UBC9 gene. Nacerddine et al. (2005) stated that the human and mouse UBC9 proteins are 100% identical. Rajan et al. (2005) stated that the human and Xenopus UBC9 proteins are identical.GENE FUNCTION
Wang et al. (1996) found that human UBC9 could fully complement the mutant phenotype of a yeast ubc9 mutant strain. In yeast, ubc9 is involved in cell cycle progression via degradation of cyclins (see 123835). Wang et al. (1996) suggested that human UBC9 may play a similar role via interaction with WT1, which is able to impose a block to cell cycle progression in eukaryotic cells. Yasugi and Howley (1996) found that human UBC9 could support the growth of yeast ubc9 temperature-sensitive mutants at nonpermissive temperatures, indicating that the gene is a functional homolog of yeast ubc9. A sumoylated form of RANGAP1 (602362) associates with the nuclear pore complex and is required for import of proteins into the nucleus. Okuma et al. (1999) showed that SUA1 (SAE1; 613294), UBA2 (613295), and UBC9 catalyzed in vitro sumoylation of RANGAP1. Faint RANGAP1 modification was observed in the absence of UBC9. Okuma et al. (1999) concluded that, in contrast to the 3-step ubiquitination reaction, which requires an E1 ubiquitin-activating enzyme, an E2 ubiquitin-conjugating enzyme, and an E3 ubiquitin ligase, sumoylation is a 2-step reaction in which the SUA1/UBA2 dimer functions as an E1 enzyme and UBC9 functions as an E2 enzyme. Fragile histidine triad (FHIT; 601153), a candidate tumor suppressor gene located on 3p14.2, is deleted in many types of human cancer. Using a yeast 2-hybrid screen to search for proteins that interact with the FHIT protein in vivo, Shi et al. (2000) found that UBC9 is specifically associated with FHIT. The last 21 amino acids at the C terminus of UBC9 appear to be unimportant for its biologic activity, since a UBC9 mutant harboring a deletion of these amino acids could still restore normal growth of yeast containing a temperature-sensitive mutation in the homolog UBC9 gene. Mutational analysis indicated that UBC9 was associated with the C-terminal portion of FHIT. The interaction between FHIT and UBC9 appeared to be independent of the enzymatic activity of FHIT. Given that yeast UBC9 is involved in the degradation of S- and M-phase cyclins, Shi et al. (2000) concluded that FHIT may be involved in cell cycle control through its interaction with UBC9. The RAD6 (179095) pathway is central to postreplicative DNA repair in eukaryotic cells. Two principa ... More on the omim web site
Oct. 27, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.
Nov. 16, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
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 601661 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed