UBE2E1

Ubiquitin-conjugating enzyme E2E 1
PDB rendering based on 1y6l.
Available structures PDB 1XR9, 3BZH
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 • nucleotide binding • ubiquitin-protein ligase activity • protein binding • ATP binding • ligase activity • acid-amino acid ligase activity • ISG15 ligase activity Cellular component • ubiquitin ligase complex • nucleus • nucleoplasm • nucleoplasm • cytosol • cytosol Biological process • cell cycle checkpoint • protein polyubiquitination • mitotic cell cycle • ubiquitin-dependent protein catabolic process • mitotic cell cycle spindle assembly checkpoint • histone monoubiquitination • protein ubiquitination • protein ubiquitination • anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process • 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 mitotic cell cycle • 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_001202476.1	NM_009455.3
RefSeq (protein)	NP_001189405.1	NP_033481.1
Location (UCSC)	Chr 3: 23.85 – 23.93 Mb	Chr 14: 19.12 – 19.16 Mb
PubMed search	[1]	[2]

Ubiquitin-conjugating enzyme E2 E1 is a protein that in humans is encoded by the UBE2E1 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. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

Interactions

UBE2E1 has been shown to interact with Ataxin 1 and NEDD4.

Further reading

• Pickart CM (2002). "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 et al (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 et al (1999). "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 et al (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 (2001). "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 et al (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. 
• Strausberg RL, Feingold EA, Grouse LH et al (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Lehner B, Semple JI, Brown SE et al (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. 
• Gerhard DS, Wagner L, Feingold EA et al (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Takeuchi T, Iwahara S, Saeki Y et al (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.