UBE2G1: Difference between revisions

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'''Ubiquitin-conjugating enzyme E2 G1''' is a [[protein]] that in humans is encoded by the ''UBE2G1'' [[gene]].<ref name="pmid8893823">{{cite journal | vauthors = Watanabe TK, Kawai A, Fujiwara T, Maekawa H, Hirai Y, Nakamura Y, Takahashi E | 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 |date=Dec 1996 | pmid = 8893823 | pmc =  | doi =10.1159/000134403 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: UBE2G1 ubiquitin-conjugating enzyme E2G 1 (UBC7 homolog, yeast)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7326| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_UBE2G1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2awf.
| PDB = {{PDB2|2awf}}
| Name = Ubiquitin-conjugating enzyme E2G 1 (UBC7 homolog, yeast)
| HGNCid = 12482
| Symbol = UBE2G1
| AltSymbols =; E217K; UBC7; UBE2G
| OMIM = 601569
| ECnumber = 
| Homologene = 2508
| MGIid = 1914378
| GeneAtlas_image1 = PBB_GE_UBE2G1_209141_at_tn.png
| GeneAtlas_image2 = PBB_GE_UBE2G1_209142_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004842 |text = ubiquitin-protein ligase activity}} {{GNF_GO|id=GO:0016874 |text = ligase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}} {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7326
    | Hs_Ensembl = ENSG00000132388
    | Hs_RefseqProtein = NP_872623
    | Hs_RefseqmRNA = NM_182682
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 4119261
    | Hs_GenLoc_end = 4216718
    | Hs_Uniprot = P62253
    | Mm_EntrezGene = 67128
    | Mm_Ensembl = ENSMUSG00000020794
    | Mm_RefseqmRNA = NM_025985
    | Mm_RefseqProtein = NP_080261
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 72423478
    | Mm_GenLoc_end = 72502675
    | Mm_Uniprot = Q5SPX0
  }}
}}
'''Ubiquitin-conjugating enzyme E2G 1 (UBC7 homolog, yeast)''', also known as '''UBE2G1''', is a human [[gene]].<ref name="entrez">{{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 = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| 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.<ref name="entrez">{{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 = }}</ref>
| 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.<ref name="entrez">{{cite web | title = Entrez Gene: UBE2G1 ubiquitin-conjugating enzyme E2G 1 (UBC7 homolog, yeast)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7326| accessdate = }}</ref>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| 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   |vauthors=Chen P, Johnson P, Sommer T, etal |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=10.1016/0092-8674(93)90426-Q }}
*{{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  | vauthors=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=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   |vauthors=Moynihan TP, Ardley HC, Nuber U, etal |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=10.1074/jbc.274.43.30963 }}
*{{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   |vauthors=Huang L, Kinnucan E, Wang G, etal |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=10.1126/science.286.5443.1321 }}
*{{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  | vauthors=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=10.1126/science.289.5487.2061 }}
*{{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  | vauthors=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=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   |vauthors=Imai Y, Soda M, Inoue H, etal |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=10.1016/S0092-8674(01)00407-X }}
*{{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   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 | pmc=139241 }}
*{{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   |vauthors=Gevaert K, Goethals M, Martens L, etal |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=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   |vauthors=Kim BW, Zavacki AM, Curcio-Morelli C, etal |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=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   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |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 | pmc=528928 }}
*{{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   |vauthors=Rual JF, Venkatesan K, Hao T, etal |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 }}
*{{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 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=7326}}
{{Ubiquitin-conjugating enzymes}}
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Revision as of 09:31, 17 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Ubiquitin-conjugating enzyme E2 G1 is a protein that in humans is encoded by the UBE2G1 gene.[1][2]

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.[2]

References

  1. ↑ Watanabe TK, Kawai A, Fujiwara T, Maekawa H, Hirai Y, Nakamura Y, Takahashi E (Dec 1996). "Molecular cloning of UBE2G, encoding a human skeletal muscle-specific ubiquitin-conjugating enzyme homologous to UBC7 of C. elegans". Cytogenet Cell Genet. 74 (1–2): 146–8. doi:10.1159/000134403. PMID 8893823.
  2. ↑ 2.0 2.1 "Entrez Gene: UBE2G1 ubiquitin-conjugating enzyme E2G 1 (UBC7 homolog, yeast)".

Further reading



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