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P62253

- UB2G1_HUMAN

UniProt

P62253 - UB2G1_HUMAN

Protein

Ubiquitin-conjugating enzyme E2 G1

Gene

UBE2G1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. ubiquitin protein ligase binding Source: UniProtKB
    4. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. protein K48-linked ubiquitination Source: UniProtKB
    2. protein K63-linked ubiquitination Source: UniProtKB
    3. ubiquitin-dependent protein catabolic process Source: ProtInc

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    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: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:12482. UBE2G1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt

    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; alternate2 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

    ArrayExpressiP62253.
    BgeeiP62253.
    CleanExiHS_UBE2G1.
    GenevestigatoriP62253.

    Organism-specific databases

    HPAiHPA045681.
    HPA050551.

    Interactioni

    Protein-protein interaction databases

    BioGridi113174. 16 interactions.
    IntActiP62253. 1 interaction.
    STRINGi9606.ENSP00000380178.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MTELQSALLL RRQLAELNKN PVEGFSAGLI DDNDLYRWEV LIIGPPDTLY    50
    EGGVFKAHLT FPKDYPLRPP KMKFITEIWH PNVDKNGDVC ISILHEPGED 100
    KYGYEKPEER WLPIHTVETI MISVISMLAD PNGDSPANVD AAKEWREDRN 150
    GEFKRKVARC VRKSQETAFE 170
    Length:170
    Mass (Da):19,509
    Last modified:January 23, 2007 - v3
    Checksum:i36B61766D995B332
    GO

    Sequence cautioni

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS32532.1.
    RefSeqi NP_003333.1. NM_003342.4.
    UniGenei Hs.741319.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AWF X-ray 2.10 A 8-160 [» ]
    ProteinModelPortali P62253.
    SMRi P62253. Positions 5-166.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113174. 16 interactions.
    IntActi P62253. 1 interaction.
    STRINGi 9606.ENSP00000380178.

    PTM databases

    PhosphoSitei P62253.

    Polymorphism databases

    DMDMi 51338681.

    Proteomic databases

    MaxQBi P62253.
    PaxDbi P62253.
    PeptideAtlasi P62253.
    PRIDEi P62253.

    Protocols and materials databases

    DNASUi 7326.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000396981 ; ENSP00000380178 ; ENSG00000132388 .
    GeneIDi 7326.
    KEGGi hsa:7326.
    UCSCi uc002fxs.3. human.

    Organism-specific databases

    CTDi 7326.
    GeneCardsi GC17M004120.
    HGNCi HGNC:12482. UBE2G1.
    HPAi HPA045681.
    HPA050551.
    MIMi 601569. gene.
    neXtProti NX_P62253.
    PharmGKBi PA37131.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5078.
    HOGENOMi HOG000233454.
    HOVERGENi HBG063308.
    InParanoidi P62253.
    KOi K10575.
    OMAi EWREDRH.
    OrthoDBi EOG7VB2HT.
    PhylomeDBi P62253.
    TreeFami TF101118.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki P62253.

    Miscellaneous databases

    ChiTaRSi UBE2G1. human.
    EvolutionaryTracei P62253.
    GeneWikii UBE2G1.
    GenomeRNAii 7326.
    NextBioi 28666.
    PROi P62253.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62253.
    Bgeei P62253.
    CleanExi HS_UBE2G1.
    Genevestigatori P62253.

    Family and domain databases

    Gene3Di 3.10.110.10. 1 hit.
    InterProi IPR000608. UBQ-conjugat_E2.
    IPR023313. UBQ-conjugating_AS.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view ]
    Pfami PF00179. UQ_con. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54495. SSF54495. 1 hit.
    PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
    PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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(1996) [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 (MAY-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(2004) [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(2004) [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(2003) [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(2009) [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(2010) [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(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [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 5, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 109 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