UBE2G1

Protein-coding gene in the species Homo sapiens
UBE2G1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2AWF

Identifiers
AliasesUBE2G1, E217K, UBC7, UBE2G, ubiquitin conjugating enzyme E2 G1
External IDsOMIM: 601569; MGI: 1914378; HomoloGene: 2508; GeneCards: UBE2G1; OMA:UBE2G1 - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for UBE2G1
Genomic location for UBE2G1
Band17p13.2Start4,269,259 bp[1]
End4,366,675 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for UBE2G1
Genomic location for UBE2G1
Band11|11 B4Start72,498,109 bp[2]
End72,577,307 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 11: 72.5 – 72.58 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ubiquitin-conjugating enzyme E2 G1 is a protein that in humans is encoded by the UBE2G1 gene.[5][6]

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.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000132388 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020794 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ a b "Entrez Gene: UBE2G1 ubiquitin-conjugating enzyme E2G 1 (UBC7 homolog, yeast)".

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.
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  • 2awf: Structure of human Ubiquitin-conjugating enzyme E2 G1
    2awf: Structure of human Ubiquitin-conjugating enzyme E2 G1
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Chaperones/
protein folding
Heat shock proteins/
Chaperonins
Other
Protein targeting
Ubiquitin
(ubiquitylation)
Ubiquitin-like proteins
(UBL)
SUMO protein
(SUMOylation)
  • E1 SUMO-activating enzyme
  • E2 SUMO-conjugating enzyme
Other


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