UBE2G1

Ubiquitin-conjugating enzyme E2G 1 (UBC7 homolog, yeast), also known as UBE2G1, is a human gene.cite web | title = Entrez Gene: UBE2G1 ubiquitin-conjugating enzyme E2G 1 (UBC7 homolog, yeast)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7326| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: UBE2G1 ubiquitin-conjugating enzyme E2G 1 (UBC7 homolog, yeast)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7326| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Chen P, Johnson P, Sommer T, "et al." |title=Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor. |journal=Cell |volume=74 |issue= 2 |pages= 357–69 |year= 1993 |pmid= 8393731 |doi=
*cite journal | author=Watanabe TK, Kawai A, Fujiwara T, "et al." |title=Molecular cloning of UBE2G, encoding a human skeletal muscle-specific ubiquitin-conjugating enzyme homologous to UBC7 of C. elegans. |journal=Cytogenet. Cell Genet. |volume=74 |issue= 1-2 |pages= 146–8 |year= 1996 |pmid= 8893823 |doi=
*cite journal | author=Katsanis N, Fisher EM |title=Identification, expression, and chromosomal localization of ubiquitin conjugating enzyme 7 (UBE2G2), a human homologue of the Saccharomyces cerevisiae ubc7 gene. |journal=Genomics |volume=51 |issue= 1 |pages= 128–31 |year= 1998 |pmid= 9693041 |doi= 10.1006/geno.1998.5263
*cite journal | author=Moynihan TP, Ardley HC, Nuber U, "et al." |title=The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING finger/IBR motif-containing domains of HHARI and H7-AP1. |journal=J. Biol. Chem. |volume=274 |issue= 43 |pages= 30963–8 |year= 1999 |pmid= 10521492 |doi=
*cite journal | author=Huang L, Kinnucan E, Wang G, "et al." |title=Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. |journal=Science |volume=286 |issue= 5443 |pages= 1321–6 |year= 1999 |pmid= 10558980 |doi=
*cite journal | author=Joazeiro CA, Hunter T |title=Biochemistry. Ubiquitination--more than two to tango. |journal=Science |volume=289 |issue= 5487 |pages= 2061–2 |year= 2000 |pmid= 11032556 |doi=
*cite journal | author=Tiwari S, Weissman AM |title=Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s). |journal=J. Biol. Chem. |volume=276 |issue= 19 |pages= 16193–200 |year= 2001 |pmid= 11278356 |doi= 10.1074/jbc.M007640200
*cite journal | author=Imai Y, Soda M, Inoue H, "et al." |title=An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. |journal=Cell |volume=105 |issue= 7 |pages= 891–902 |year= 2001 |pmid= 11439185 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Gevaert K, Goethals M, Martens L, "et al." |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566–9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810
*cite journal | author=Kim BW, Zavacki AM, Curcio-Morelli C, "et al." |title=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. |journal=Mol. Endocrinol. |volume=17 |issue= 12 |pages= 2603–12 |year= 2004 |pmid= 12933904 |doi= 10.1210/me.2003-0082
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes