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Protein

Ubiquitin-conjugating enzyme E2 G1

Gene

UBE2G1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. May be involved in degradation of muscle-specific proteins. Mediates polyubiquitination of CYP3A4.2 Publications

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei90 – 901Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ligase activity Source: UniProtKB-KW
  3. ubiquitin conjugating enzyme activity Source: MGI
  4. ubiquitin-like protein transferase activity Source: GO_Central
  5. ubiquitin protein ligase activity Source: GO_Central
  6. ubiquitin protein ligase binding Source: UniProtKB
  7. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. cellular protein catabolic process Source: MGI
  2. protein K48-linked ubiquitination Source: UniProtKB
  3. protein K63-linked ubiquitination Source: UniProtKB
  4. ubiquitin-dependent protein catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.3.2.B6. 2681.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiP62253.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 G1 (EC:6.3.2.19)
Alternative name(s):
E217K
UBC7
Ubiquitin carrier protein G1
Ubiquitin-protein ligase G1
Cleaved into the following chain:
Gene namesi
Name:UBE2G1
Synonyms:UBE2G
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:12482. UBE2G1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37131.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 170170Ubiquitin-conjugating enzyme E2 G1PRO_0000424514Add
BLAST
Initiator methioninei1 – 11Removed; alternate3 Publications
Chaini2 – 170169Ubiquitin-conjugating enzyme E2 G1, N-terminally processedPRO_0000082480Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei2 – 21N-acetylthreonine; in Ubiquitin-conjugating enzyme E2 G1, N-terminally processed3 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP62253.
PaxDbiP62253.
PeptideAtlasiP62253.
PRIDEiP62253.

PTM databases

PhosphoSiteiP62253.

Expressioni

Tissue specificityi

Widely expressed, mainly in skeletal muscle.1 Publication

Gene expression databases

BgeeiP62253.
CleanExiHS_UBE2G1.
ExpressionAtlasiP62253. baseline and differential.
GenevestigatoriP62253.

Organism-specific databases

HPAiHPA045681.
HPA050551.

Interactioni

Protein-protein interaction databases

BioGridi113174. 18 interactions.
IntActiP62253. 1 interaction.
STRINGi9606.ENSP00000380178.

Structurei

Secondary structure

1
170
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 1912Combined sources
Beta strandi25 – 317Combined sources
Beta strandi37 – 437Combined sources
Turni49 – 524Combined sources
Beta strandi54 – 607Combined sources
Turni63 – 664Combined sources
Beta strandi71 – 744Combined sources
Helixi92 – 943Combined sources
Helixi117 – 12812Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AWFX-ray2.10A8-160[»]
ProteinModelPortaliP62253.
SMRiP62253. Positions 5-166.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62253.

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110436.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiP62253.
KOiK10575.
OMAiEWREDRH.
OrthoDBiEOG7VB2HT.
PhylomeDBiP62253.
TreeFamiTF101118.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62253-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTELQSALLL RRQLAELNKN PVEGFSAGLI DDNDLYRWEV LIIGPPDTLY
60 70 80 90 100
EGGVFKAHLT FPKDYPLRPP KMKFITEIWH PNVDKNGDVC ISILHEPGED
110 120 130 140 150
KYGYEKPEER WLPIHTVETI MISVISMLAD PNGDSPANVD AAKEWREDRN
160 170
GEFKRKVARC VRKSQETAFE
Length:170
Mass (Da):19,509
Last modified:January 22, 2007 - v3
Checksum:i36B61766D995B332
GO

Sequence cautioni

The sequence AAH26288.2 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78514 mRNA. Translation: BAA11410.1.
BT007416 mRNA. Translation: AAP36084.1.
AK313059 mRNA. Translation: BAG35889.1.
CH471108 Genomic DNA. Translation: EAW90445.1.
CH471108 Genomic DNA. Translation: EAW90446.1.
BC002775 mRNA. Translation: AAH02775.1.
BC026288 mRNA. Translation: AAH26288.2. Different initiation.
CCDSiCCDS32532.1.
RefSeqiNP_003333.1. NM_003342.4.
UniGeneiHs.741319.

Genome annotation databases

EnsembliENST00000396981; ENSP00000380178; ENSG00000132388.
GeneIDi7326.
KEGGihsa:7326.
UCSCiuc002fxs.3. human.

Polymorphism databases

DMDMi51338681.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78514 mRNA. Translation: BAA11410.1.
BT007416 mRNA. Translation: AAP36084.1.
AK313059 mRNA. Translation: BAG35889.1.
CH471108 Genomic DNA. Translation: EAW90445.1.
CH471108 Genomic DNA. Translation: EAW90446.1.
BC002775 mRNA. Translation: AAH02775.1.
BC026288 mRNA. Translation: AAH26288.2. Different initiation.
CCDSiCCDS32532.1.
RefSeqiNP_003333.1. NM_003342.4.
UniGeneiHs.741319.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AWFX-ray2.10A8-160[»]
ProteinModelPortaliP62253.
SMRiP62253. Positions 5-166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113174. 18 interactions.
IntActiP62253. 1 interaction.
STRINGi9606.ENSP00000380178.

PTM databases

PhosphoSiteiP62253.

Polymorphism databases

DMDMi51338681.

Proteomic databases

MaxQBiP62253.
PaxDbiP62253.
PeptideAtlasiP62253.
PRIDEiP62253.

Protocols and materials databases

DNASUi7326.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000396981; ENSP00000380178; ENSG00000132388.
GeneIDi7326.
KEGGihsa:7326.
UCSCiuc002fxs.3. human.

Organism-specific databases

CTDi7326.
GeneCardsiGC17M004120.
HGNCiHGNC:12482. UBE2G1.
HPAiHPA045681.
HPA050551.
MIMi601569. gene.
neXtProtiNX_P62253.
PharmGKBiPA37131.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110436.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiP62253.
KOiK10575.
OMAiEWREDRH.
OrthoDBiEOG7VB2HT.
PhylomeDBiP62253.
TreeFamiTF101118.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B6. 2681.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiP62253.

Miscellaneous databases

ChiTaRSiUBE2G1. human.
EvolutionaryTraceiP62253.
GeneWikiiUBE2G1.
GenomeRNAii7326.
NextBioi28666.
PROiP62253.
SOURCEiSearch...

Gene expression databases

BgeeiP62253.
CleanExiHS_UBE2G1.
ExpressionAtlasiP62253. baseline and differential.
GenevestigatoriP62253.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of UBE2G, encoding a human skeletal muscle-specific ubiquitin-conjugating enzyme homologous to UBC7 of C. elegans."
    Watanabe T.K., Kawai A., Fujiwara T., Maekawa H., Hirai Y., Nakamura Y., Takahashi E.
    Cytogenet. Cell Genet. 74:146-148(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Caudate nucleus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lymph and Prostate.
  6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11, ACETYLATION AT THR-2.
    Tissue: Platelet.
  7. "CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases."
    Pabarcus M.K., Hoe N., Sadeghi S., Patterson C., Wiertz E., Correia M.A.
    Arch. Biochem. Biophys. 483:66-74(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines."
    David Y., Ziv T., Admon A., Navon A.
    J. Biol. Chem. 285:8595-8604(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUB2G1_HUMAN
AccessioniPrimary (citable) accession number: P62253
Secondary accession number(s): B2R7P2, D3DTK0, Q99462
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 4, 2004
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 114 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.