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O00762

- UBE2C_HUMAN

UniProt

O00762 - UBE2C_HUMAN

Protein

Ubiquitin-conjugating enzyme E2 C

Gene

UBE2C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      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-11'- and 'Lys-48'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by initiating 'Lys-11'-linked polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit.5 Publications

    Catalytic activityi

    ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.1 PublicationPROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei114 – 1141Glycyl thioester intermediate

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. activation of anaphase-promoting complex activity Source: UniProtKB
    2. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
    3. cell cycle Source: UniProtKB
    4. cyclin catabolic process Source: UniProtKB
    5. exit from mitosis Source: UniProtKB
    6. free ubiquitin chain polymerization Source: UniProtKB
    7. mitotic cell cycle Source: Reactome
    8. mitotic spindle assembly checkpoint Source: Reactome
    9. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    10. phosphatidylinositol-mediated signaling Source: UniProtKB
    11. positive regulation of exit from mitosis Source: UniProtKB
    12. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    13. protein K11-linked ubiquitination Source: UniProtKB
    14. protein K48-linked ubiquitination Source: UniProtKB
    15. protein ubiquitination Source: UniProtKB
    16. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    17. spindle organization Source: UniProtKB
    18. ubiquitin-dependent protein catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
    REACT_150471. Separation of Sister Chromatids.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_6904. Phosphorylation of the APC/C.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiO00762.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 C (EC:6.3.2.19)
    Alternative name(s):
    UbcH10
    Ubiquitin carrier protein C
    Ubiquitin-protein ligase C
    Gene namesi
    Name:UBE2C
    Synonyms:UBCH10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:15937. UBE2C.

    Subcellular locationi

    GO - Cellular componenti

    1. anaphase-promoting complex Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleoplasm Source: Reactome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi114 – 1141C → S: Loss of function; inhibition of cyclin-B degradation. 2 Publications

    Organism-specific databases

    PharmGKBiPA38057.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 179178Ubiquitin-conjugating enzyme E2 CPRO_0000082560Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei3 – 31Phosphoserine1 Publication

    Post-translational modificationi

    Autoubiquitinated by the APC/C complex, leading to its degradation by the proteasome. Its degradation plays a central role in APC/C regulation, allowing cyclin-A accumulation before S phase entry. APC/C substrates inhibit the autoubiquitination of UBE2C/UBCH10 but not its E2 function, hence APC/C remaining active until its substrates have been destroyed.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO00762.
    PaxDbiO00762.
    PRIDEiO00762.

    PTM databases

    PhosphoSiteiO00762.

    Expressioni

    Gene expression databases

    ArrayExpressiO00762.
    BgeeiO00762.
    CleanExiHS_UBE2C.
    GenevestigatoriO00762.

    Organism-specific databases

    HPAiCAB011464.
    CAB035990.
    HPA054975.

    Interactioni

    Subunit structurei

    Component of the APC/C complex.

    Protein-protein interaction databases

    BioGridi116249. 66 interactions.
    DIPiDIP-52725N.
    IntActiO00762. 8 interactions.
    STRINGi9606.ENSP00000348838.

    Structurei

    Secondary structure

    1
    179
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi31 – 4515
    Beta strandi50 – 556
    Beta strandi58 – 6811
    Beta strandi78 – 847
    Turni87 – 915
    Beta strandi95 – 1006
    Helixi116 – 1183
    Turni119 – 1213
    Helixi128 – 14013
    Helixi150 – 1556
    Helixi159 – 17113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1I7KX-ray1.95A/B1-179[»]
    ProteinModelPortaliO00762.
    SMRiO00762. Positions 30-175.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00762.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5078.
    HOGENOMiHOG000233454.
    HOVERGENiHBG063308.
    InParanoidiO00762.
    KOiK06688.
    OMAiAELWDKD.
    OrthoDBiEOG7M0NTH.
    PhylomeDBiO00762.
    TreeFamiTF101116.

    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]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O00762-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASQNRDPAA TSVAAARKGA EPSGGAARGP VGKRLQQELM TLMMSGDKGI    50
    SAFPESDNLF KWVGTIHGAA GTVYEDLRYK LSLEFPSGYP YNAPTVKFLT 100
    PCYHPNVDTQ GNICLDILKE KWSALYDVRT ILLSIQSLLG EPNIDSPLNT 150
    HAAELWKNPT AFKKYLQETY SKQVTSQEP 179
    Length:179
    Mass (Da):19,652
    Last modified:July 1, 1997 - v1
    Checksum:i0B6F58A1F0665D9A
    GO
    Isoform 2 (identifier: O00762-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-39: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:140
    Mass (Da):15,765
    Checksum:i194F276AD75D5168
    GO
    Isoform 3 (identifier: O00762-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         44-72: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:150
    Mass (Da):16,676
    Checksum:i5410B7BA11DFC35E
    GO
    Isoform 4 (identifier: O00762-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         73-140: VYEDLRYKLS...ILLSIQSLLG → AVGSIRTSST...LTLQLFLQMP

    Note: No experimental confirmation available.

    Show »
    Length:161
    Mass (Da):17,373
    Checksum:iD8F52001401888DA
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251G → D.
    VAR_007694

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3939Missing in isoform 2. 1 PublicationVSP_045647Add
    BLAST
    Alternative sequencei44 – 7229Missing in isoform 3. 1 PublicationVSP_045648Add
    BLAST
    Alternative sequencei73 – 14068VYEDL…QSLLG → AVGSIRTSSTVCLLSGPRET QDSSKPLVWGLGWDMRLLLE LTLQLFLQMP in isoform 4. 1 PublicationVSP_045649Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U73379 mRNA. Translation: AAB53362.1.
    BT007300 mRNA. Translation: AAP35964.1.
    AL050348 Genomic DNA. No translation available.
    CH471077 Genomic DNA. Translation: EAW75804.1.
    CH471077 Genomic DNA. Translation: EAW75805.1.
    CH471077 Genomic DNA. Translation: EAW75806.1.
    CH471077 Genomic DNA. Translation: EAW75807.1.
    BC007656 mRNA. Translation: AAH07656.1.
    BC016292 mRNA. Translation: AAH16292.1.
    BC050736 mRNA. Translation: AAH50736.1.
    BI858659 mRNA. No translation available.
    BM556795 mRNA. No translation available.
    BU844974 mRNA. No translation available.
    CCDSiCCDS13370.1. [O00762-1]
    CCDS13371.1. [O00762-4]
    CCDS13372.1. [O00762-3]
    CCDS13374.1. [O00762-2]
    RefSeqiNP_001268670.1. NM_001281741.1.
    NP_001268671.1. NM_001281742.1.
    NP_008950.1. NM_007019.3. [O00762-1]
    NP_861515.1. NM_181799.2. [O00762-4]
    NP_861516.1. NM_181800.2. [O00762-3]
    NP_861517.1. NM_181801.3. [O00762-2]
    UniGeneiHs.93002.

    Genome annotation databases

    EnsembliENST00000335046; ENSP00000335674; ENSG00000175063. [O00762-4]
    ENST00000352551; ENSP00000333975; ENSG00000175063. [O00762-3]
    ENST00000356455; ENSP00000348838; ENSG00000175063. [O00762-1]
    ENST00000372568; ENSP00000361649; ENSG00000175063. [O00762-2]
    ENST00000405520; ENSP00000385878; ENSG00000175063. [O00762-2]
    GeneIDi11065.
    KEGGihsa:11065.
    UCSCiuc002xpl.3. human.
    uc002xpm.3. human. [O00762-1]
    uc002xpo.3. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U73379 mRNA. Translation: AAB53362.1 .
    BT007300 mRNA. Translation: AAP35964.1 .
    AL050348 Genomic DNA. No translation available.
    CH471077 Genomic DNA. Translation: EAW75804.1 .
    CH471077 Genomic DNA. Translation: EAW75805.1 .
    CH471077 Genomic DNA. Translation: EAW75806.1 .
    CH471077 Genomic DNA. Translation: EAW75807.1 .
    BC007656 mRNA. Translation: AAH07656.1 .
    BC016292 mRNA. Translation: AAH16292.1 .
    BC050736 mRNA. Translation: AAH50736.1 .
    BI858659 mRNA. No translation available.
    BM556795 mRNA. No translation available.
    BU844974 mRNA. No translation available.
    CCDSi CCDS13370.1. [O00762-1 ]
    CCDS13371.1. [O00762-4 ]
    CCDS13372.1. [O00762-3 ]
    CCDS13374.1. [O00762-2 ]
    RefSeqi NP_001268670.1. NM_001281741.1.
    NP_001268671.1. NM_001281742.1.
    NP_008950.1. NM_007019.3. [O00762-1 ]
    NP_861515.1. NM_181799.2. [O00762-4 ]
    NP_861516.1. NM_181800.2. [O00762-3 ]
    NP_861517.1. NM_181801.3. [O00762-2 ]
    UniGenei Hs.93002.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1I7K X-ray 1.95 A/B 1-179 [» ]
    ProteinModelPortali O00762.
    SMRi O00762. Positions 30-175.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116249. 66 interactions.
    DIPi DIP-52725N.
    IntActi O00762. 8 interactions.
    STRINGi 9606.ENSP00000348838.

    PTM databases

    PhosphoSitei O00762.

    Proteomic databases

    MaxQBi O00762.
    PaxDbi O00762.
    PRIDEi O00762.

    Protocols and materials databases

    DNASUi 11065.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000335046 ; ENSP00000335674 ; ENSG00000175063 . [O00762-4 ]
    ENST00000352551 ; ENSP00000333975 ; ENSG00000175063 . [O00762-3 ]
    ENST00000356455 ; ENSP00000348838 ; ENSG00000175063 . [O00762-1 ]
    ENST00000372568 ; ENSP00000361649 ; ENSG00000175063 . [O00762-2 ]
    ENST00000405520 ; ENSP00000385878 ; ENSG00000175063 . [O00762-2 ]
    GeneIDi 11065.
    KEGGi hsa:11065.
    UCSCi uc002xpl.3. human.
    uc002xpm.3. human. [O00762-1 ]
    uc002xpo.3. human.

    Organism-specific databases

    CTDi 11065.
    GeneCardsi GC20P044442.
    HGNCi HGNC:15937. UBE2C.
    HPAi CAB011464.
    CAB035990.
    HPA054975.
    MIMi 605574. gene.
    neXtProti NX_O00762.
    PharmGKBi PA38057.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5078.
    HOGENOMi HOG000233454.
    HOVERGENi HBG063308.
    InParanoidi O00762.
    KOi K06688.
    OMAi AELWDKD.
    OrthoDBi EOG7M0NTH.
    PhylomeDBi O00762.
    TreeFami TF101116.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
    REACT_150471. Separation of Sister Chromatids.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_6904. Phosphorylation of the APC/C.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki O00762.

    Miscellaneous databases

    EvolutionaryTracei O00762.
    GeneWikii UBE2C.
    GenomeRNAii 11065.
    NextBioi 42051.
    PROi O00762.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00762.
    Bgeei O00762.
    CleanExi HS_UBE2C.
    Genevestigatori O00762.

    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. "Dominant-negative cyclin-selective ubiquitin carrier protein E2-C/UbcH10 blocks cells in metaphase."
      Townsley F.M., Aristarkhov A., Beck S., Hershko A., Ruderman J.V.
      Proc. Natl. Acad. Sci. U.S.A. 94:2362-2367(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF CYS-114.
    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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORMS 1; 2; 3 AND 4).
      Tissue: Lung adenocarcinoma, Lymph, Melanoma, Teratocarcinoma and Uterus.
    6. "Autonomous regulation of the anaphase-promoting complex couples mitosis to S-phase entry."
      Rape M., Kirschner M.W.
      Nature 432:588-595(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, UBIQUITINATION, MUTAGENESIS OF CYS-114.
    7. "Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex."
      Jin L., Williamson A., Banerjee S., Philipp I., Rape M.
      Cell 133:653-665(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    9. "UBE2S elongates ubiquitin chains on APC/C substrates to promote mitotic exit."
      Garnett M.J., Mansfeld J., Godwin C., Matsusaka T., Wu J., Russell P., Pines J., Venkitaraman A.R.
      Nat. Cell Biol. 11:1363-1369(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Identification of a physiological E2 module for the human anaphase-promoting complex."
      Williamson A., Wickliffe K.E., Mellone B.G., Song L., Karpen G.H., Rape M.
      Proc. Natl. Acad. Sci. U.S.A. 106:18213-18218(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "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.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Structural and functional analysis of the human mitotic-specific ubiquitin-conjugating enzyme, UbcH10."
      Lin Y., Hwang W.C., Basavappa R.
      J. Biol. Chem. 277:21913-21921(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).

    Entry informationi

    Entry nameiUBE2C_HUMAN
    AccessioniPrimary (citable) accession number: O00762
    Secondary accession number(s): A6NP33, E1P5N7, G3XAB7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 151 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3