UBE2G1

UBE2G1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2AWF
Identifiers
Aliases	UBE2G1, E217K, UBC7, UBE2G, ubiquitin conjugating enzyme E2 G1
External IDs	OMIM: 601569; MGI: 1914378; HomoloGene: 2508; GeneCards: UBE2G1; OMA:UBE2G1 - orthologs
Gene location (Human) Chr. Chromosome 17 (human) Band 17p13.2 Start 4,269,259 bp End 4,366,675 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11|11 B4 Start 72,498,109 bp End 72,577,307 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sperm secondary oocyte biceps brachii vastus lateralis muscle Skeletal muscle tissue of rectus abdominis Skeletal muscle tissue of biceps brachii glutes deltoid muscle muscle of thigh tibialis anterior muscle Top expressed in primary oocyte otic placode otic vesicle saccule triceps brachii muscle sternocleidomastoid muscle extensor digitorum longus muscle temporal muscle medial ganglionic eminence plantaris muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding ATP binding ubiquitin conjugating enzyme activity ubiquitin protein ligase binding ubiquitin protein ligase activity ubiquitin-protein transferase activity Cellular component cytoplasm extracellular exosome cytosol Biological process protein K63-linked ubiquitination protein K48-linked ubiquitination ubiquitin-dependent protein catabolic process protein ubiquitination protein polyubiquitination proteasome-mediated ubiquitin-dependent protein catabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 7326 67128 Ensembl ENSG00000132388 ENSMUSG00000020794 UniProt P62253 P62254 RefSeq (mRNA) NM_182682 NM_003342 NM_025985 RefSeq (protein) NP_003333 NP_080261 Location (UCSC) Chr 17: 4.27 – 4.37 Mb Chr 11: 72.5 – 72.58 Mb PubMed search
Wikidata
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Ubiquitin-conjugating enzyme E2 G1 is a protein that in humans is encoded by the UBE2G1 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 and catalyzes the covalent attachment of ubiquitin to other proteins. The protein may be involved in degradation of muscle-specific proteins.

Further reading

• 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. S2CID 205020910.
• Katsanis N, Fisher EM (1998). "Identification, expression, and chromosomal localization of ubiquitin conjugating enzyme 7 (UBE2G2), a human homologue of the Saccharomyces cerevisiae ubc7 gene". Genomics. 51 (1): 128–31. doi:10.1006/geno.1998.5263. PMID 9693041.
• Moynihan TP, Ardley HC, Nuber U, et al. (1999). "The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING finger/IBR motif-containing domains of HHARI and H7-AP1". J. Biol. Chem. 274 (43): 30963–8. doi:10.1074/jbc.274.43.30963. PMID 10521492.
• Huang L, Kinnucan E, Wang G, et al. (1999). "Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade". Science. 286 (5443): 1321–6. doi:10.1126/science.286.5443.1321. PMID 10558980.
• Joazeiro CA, Hunter T (2000). "Biochemistry. Ubiquitination--more than two to tango". Science. 289 (5487): 2061–2. doi:10.1126/science.289.5487.2061. PMID 11032556. S2CID 83324199.
• Tiwari S, Weissman AM (2001). "Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s)". J. Biol. Chem. 276 (19): 16193–200. doi:10.1074/jbc.M007640200. PMID 11278356.
• Imai Y, Soda M, Inoue H, et al. (2001). "An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin". Cell. 105 (7): 891–902. doi:10.1016/S0092-8674(01)00407-X. PMID 11439185. S2CID 721363.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
• Kim BW, Zavacki AM, Curcio-Morelli C, et al. (2004). "Endoplasmic reticulum-associated degradation of the human type 2 iodothyronine deiodinase (D2) is mediated via an association between mammalian UBC7 and the carboxyl region of D2". Mol. Endocrinol. 17 (12): 2603–12. doi:10.1210/me.2003-0082. PMID 12933904.
• 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.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.