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O00762

- UBE2C_HUMAN

UniProt

O00762 - UBE2C_HUMAN

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Protein
Ubiquitin-conjugating enzyme E2 C
Gene
UBE2C, UBCH10
Organism
Homo sapiens (Human)
Status
Reviewed - 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-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 Publication

Pathwayi

Sites

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

GO - Molecular functioni

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

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
Complete GO annotation...

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
Complete GO annotation...

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 – 11Removed1 Publication
Chaini2 – 179178Ubiquitin-conjugating enzyme E2 C
PRO_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.

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. 65 interactions.
DIPiDIP-52725N.
IntActiO00762. 8 interactions.
STRINGi9606.ENSP00000348838.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiO00762.

Family & Domainsi

Sequence similaritiesi

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.
VSP_045647Add
BLAST
Alternative sequencei44 – 7229Missing in isoform 3.
VSP_045648Add
BLAST
Alternative sequencei73 – 14068VYEDL…QSLLG → AVGSIRTSSTVCLLSGPRET QDSSKPLVWGLGWDMRLLLE LTLQLFLQMP in isoform 4.
VSP_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...

Protein-protein interaction databases

BioGridi 116249. 65 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 150 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

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