UBE2E1

Ubiquitin-conjugating enzyme E2E 1
PDB rendering based on 1y6l.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1XR9​, 3BZH​, 4JJQ​
Identifiers
Symbols	UBE2E1 ; UBCH6
External IDs	OMIM: 602916 MGI: 107411 HomoloGene: 84372 GeneCards: UBE2E1 Gene
EC number	6.3.2.19
Gene ontology Molecular function • ubiquitin-protein transferase activity • protein binding • ATP binding • ligase activity • ISG15 transferase activity • ubiquitin conjugating enzyme activity Cellular component • ubiquitin ligase complex • nucleus • nucleoplasm • cytosol Biological process • protein polyubiquitination • mitotic cell cycle • ubiquitin-dependent protein catabolic process • mitotic spindle assembly checkpoint • histone monoubiquitination • protein ubiquitination • cytokine-mediated signaling pathway • anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process • ISG15-protein conjugation • histone H2B ubiquitination • negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle • positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition • regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle • protein K48-linked ubiquitination Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	7324	22194
Ensembl	ENSG00000170142	ENSMUSG00000021774
UniProt	P51965	P52482
RefSeq (mRNA)	NM_001202476	NM_009455
RefSeq (protein)	NP_001189405	NP_033481
Location (UCSC)	Chr 3: 23.81 – 23.89 Mb	Chr 14: 18.28 – 18.33 Mb
PubMed search

Ubiquitin-conjugating enzyme E2 E1 is a protein that in humans is encoded by the UBE2E1 gene.^[1][2]

Function

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. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.^[2]

Interactions

UBE2E1 has been shown to interact with Ataxin 1^[3] and NEDD4.^[4][5]

References

1. Nuber U, Schwarz S, Kaiser P, Schneider R, Scheffner M (Mar 1996). "Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5". J. Biol. Chem. 271 (5): 2795–800. doi:10.1074/jbc.271.5.2795. PMID 8576257.
2. "Entrez Gene: UBE2E1 ubiquitin-conjugating enzyme E2E 1 (UBC4/5 homolog, yeast)".
3. Hong S, Lee S, Cho SG, Kang S (Jun 2008). "UbcH6 interacts with and ubiquitinates the SCA1 gene product ataxin-1". Biochem. Biophys. Res. Commun. 371 (2): 256–60. doi:10.1016/j.bbrc.2008.04.066. PMID 18439907.
4. Anan T, Nagata Y, Koga H, Honda Y, Yabuki N, Miyamoto C, Kuwano A, Matsuda I, Endo F, Saya H, Nakao M (Nov 1998). "Human ubiquitin-protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin-conjugating enzymes". Genes Cells 3 (11): 751–63. doi:10.1046/j.1365-2443.1998.00227.x. PMID 9990509.
5. Malakhova OA, Zhang DE (Apr 2008). "ISG15 inhibits Nedd4 ubiquitin E3 activity and enhances the innate antiviral response". J. Biol. Chem. 283 (14): 8783–7. doi:10.1074/jbc.C800030200. PMC 2276364. PMID 18287095.

Further reading

• Pickart CM (2001). "Mechanisms underlying ubiquitination". Annu. Rev. Biochem. 70: 503–33. doi:10.1146/annurev.biochem.70.1.503. PMID 11395416.
• Chen P, Johnson P, Sommer T, Jentsch S, Hochstrasser M (1993). "Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor". Cell 74 (2): 357–69. doi:10.1016/0092-8674(93)90426-Q. PMID 8393731.
• Anan T, Nagata Y, Koga H, Honda Y, Yabuki N, Miyamoto C, Kuwano A, Matsuda I, Endo F, Saya H, Nakao M (1998). "Human ubiquitin-protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin-conjugating enzymes". Genes Cells 3 (11): 751–63. doi:10.1046/j.1365-2443.1998.00227.x. PMID 9990509.
• Nyman TA, Matikainen S, Sareneva T, Julkunen I, Kalkkinen N (2000). "Proteome analysis reveals ubiquitin-conjugating enzymes to be a new family of interferon-alpha-regulated genes". Eur. J. Biochem. 267 (13): 4011–9. doi:10.1046/j.1432-1327.2000.01433.x. PMID 10866800.
• Lenk U, Sommer T (2000). "Ubiquitin-mediated proteolysis of a short-lived regulatory protein depends on its cellular localization". J. Biol. Chem. 275 (50): 39403–10. doi:10.1074/jbc.M006949200. PMID 10991948.
• Pringa E, Martinez-Noel G, Muller U, Harbers K (2001). "Interaction of the ring finger-related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymes". J. Biol. Chem. 276 (22): 19617–23. doi:10.1074/jbc.M100192200. PMID 11274149.
• Ito K, Adachi S, Iwakami R, Yasuda H, Muto Y, Seki N, Okano Y (2001). "N-Terminally extended human ubiquitin-conjugating enzymes (E2s) mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8". Eur. J. Biochem. 268 (9): 2725–32. doi:10.1046/j.1432-1327.2001.02169.x. PMID 11322894.
• Lehner B, Semple JI, Brown SE, Counsell D, Campbell RD, Sanderson CM (2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819.
• Takeuchi T, Iwahara S, Saeki Y, Sasajima H, Yokosawa H (2005). "Link between the ubiquitin conjugation system and the ISG15 conjugation system: ISG15 conjugation to the UbcH6 ubiquitin E2 enzyme". J. Biochem. 138 (6): 711–9. doi:10.1093/jb/mvi172. PMID 16428300.