UBE2I

From Wikipedia, the free encyclopedia

Ubiquitin-conjugating enzyme E2I (UBC9 homolog, yeast)

PDB rendering based on 1a3s.

Available structures: 1a3s, 1kps, 1u9a, 1u9b, 1z5s, 2grn, 2gro, 2grp, 2grq, 2grr, 2o25, 2pe6

Identifiers

Symbol(s)

UBE2I; C358B7.1; P18; UBC9

External IDs

OMIM: 601661 MGI: 107365 HomoloGene: 55737

Gene ontology
Molecular Function:	• ubiquitin-protein ligase activity • protein binding • ligase activity
Cellular Component:	• synaptonemal complex • nucleus
Biological Process:	• ubiquitin-dependent protein catabolic process • ubiquitin cycle • cell cycle • chromosome segregation • mitosis • cell division

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003345 (mRNA)
NP_003336 (protein)

NM_011665 (mRNA)
NP_035795 (protein)

Location

Chr 16: 1.3 - 1.32 Mb

Chr 17: 24.99 - 25 Mb

Pubmed search

[1]

[2]

Ubiquitin-conjugating enzyme E2I (UBC9 homolog, yeast), also known as UBE2I, is a human gene.

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. Four alternatively spliced transcript variants encoding the same protein have been found for this gene.^[1]

[edit] References

^ Entrez Gene: UBE2I ubiquitin-conjugating enzyme E2I (UBC9 homolog, yeast).

Watanabe TK, Fujiwara T, Kawai A, et al. (1996). "Cloning, expression, and mapping of UBE2I, a novel gene encoding a human homologue of yeast ubiquitin-conjugating enzymes which are critical for regulating the cell cycle.". Cytogenet. Cell Genet. 72 (1): 86–9. PMID 8565643.
Kovalenko OV, Plug AW, Haaf T, et al. (1996). "Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes.". Proc. Natl. Acad. Sci. U.S.A. 93 (7): 2958–63. PMID 8610150.
Jiang W, Koltin Y (1996). "Two-hybrid interaction of a human UBC9 homolog with centromere proteins of Saccharomyces cerevisiae.". Mol. Gen. Genet. 251 (2): 153–60. PMID 8668125.
Yasugi T, Howley PM (1996). "Identification of the structural and functional human homolog of the yeast ubiquitin conjugating enzyme UBC9.". Nucleic Acids Res. 24 (11): 2005–10. PMID 8668529.
Göttlicher M, Heck S, Doucas V, et al. (1996). "Interaction of the Ubc9 human homologue with c-Jun and with the glucocorticoid receptor.". Steroids 61 (4): 257–62. PMID 8733011.
Schneikert J, Peterziel H, Defossez PA, et al. (1996). "Androgen receptor-Ets protein interaction is a novel mechanism for steroid hormone-mediated down-modulation of matrix metalloproteinase expression.". J. Biol. Chem. 271 (39): 23907–13. PMID 8798622.
Wang ZY, Qiu QQ, Seufert W, et al. (1996). "Molecular cloning of the cDNA and chromosome localization of the gene for human ubiquitin-conjugating enzyme 9.". J. Biol. Chem. 271 (40): 24811–6. PMID 8798754.
Hateboer G, Hijmans EM, Nooij JB, et al. (1996). "mUBC9, a novel adenovirus E1A-interacting protein that complements a yeast cell cycle defect.". J. Biol. Chem. 271 (42): 25906–11. PMID 8824223.
Shen Z, Pardington-Purtymun PE, Comeaux JC, et al. (1997). "Associations of UBE2I with RAD52, UBL1, p53, and RAD51 proteins in a yeast two-hybrid system.". Genomics 37 (2): 183–6. doi:10.1006/geno.1996.0540. PMID 8921390.
Tachibana M, Iwata N, Watanabe A, et al. (1997). "Assignment of the gene for a ubiquitin-conjugating enzyme (UBE2I) to human chromosome band 16p13.3 by in situ hybridization.". Cytogenet. Cell Genet. 75 (4): 222–3. PMID 9067428.
Masson M, Menissier-de Murcia J, Mattei MG, et al. (1997). "Poly(ADP-ribose) polymerase interacts with a novel human ubiquitin conjugating enzyme: hUbc9.". Gene 190 (2): 287–96. PMID 9197546.
Yasugi T, Vidal M, Sakai H, et al. (1997). "Two classes of human papillomavirus type 16 E1 mutants suggest pleiotropic conformational constraints affecting E1 multimerization, E2 interaction, and interaction with cellular proteins.". J. Virol. 71 (8): 5942–51. PMID 9223484.
Becker K, Schneider P, Hofmann K, et al. (1997). "Interaction of Fas(Apo-1/CD95) with proteins implicated in the ubiquitination pathway.". FEBS Lett. 412 (1): 102–6. PMID 9257699.
Tong H, Hateboer G, Perrakis A, et al. (1997). "Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating system.". J. Biol. Chem. 272 (34): 21381–7. PMID 9261152.
Hahn SL, Wasylyk B, Criqui-Filipe P, Criqui P (1997). "Modulation of ETS-1 transcriptional activity by huUBC9, a ubiquitin-conjugating enzyme.". Oncogene 15 (12): 1489–95. doi:10.1038/sj.onc.1201301. PMID 9333025.
Hu G, Zhang S, Vidal M, et al. (1997). "Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-proteasome pathway.". Genes Dev. 11 (20): 2701–14. PMID 9334332.
Firestein R, Feuerstein N (1998). "Association of activating transcription factor 2 (ATF2) with the ubiquitin-conjugating enzyme hUBC9. Implication of the ubiquitin/proteasome pathway in regulation of ATF2 in T cells.". J. Biol. Chem. 273 (10): 5892–902. PMID 9488727.
Joanisse DR, Inaguma Y, Tanguay RM (1998). "Cloning and developmental expression of a nuclear ubiquitin-conjugating enzyme (DmUbc9) that interacts with small heat shock proteins in Drosophila melanogaster.". Biochem. Biophys. Res. Commun. 244 (1): 102–9. doi:10.1006/bbrc.1998.8214. PMID 9514881.
Saltzman A, Searfoss G, Marcireau C, et al. (1998). "hUBC9 associates with MEKK1 and type I TNF-alpha receptor and stimulates NFkappaB activity.". FEBS Lett. 425 (3): 431–5. PMID 9563508.
Koldamova RP, Lefterov IM, DiSabella MT, Lazo JS (1999). "An evolutionarily conserved cysteine protease, human bleomycin hydrolase, binds to the human homologue of ubiquitin-conjugating enzyme 9.". Mol. Pharmacol. 54 (6): 954–61. PMID 9855622.