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Protein

Ubiquitin-conjugating enzyme E2 C

Gene

UBE2C

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-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.PROSITE-ProRule annotation1 Publication

Pathway:iprotein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.PROSITE-ProRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

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

GO - Molecular functioni

GO - Biological processi

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

BRENDAi2.3.2.B6. 2681.
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_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
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.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
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 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15937. UBE2C.

Subcellular locationi

GO - Cellular componenti

  • anaphase-promoting complex Source: UniProtKB
  • cytoplasm Source: GO_Central
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • nucleus Source: GO_Central
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 – 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

BgeeiO00762.
CleanExiHS_UBE2C.
ExpressionAtlasiO00762. baseline and differential.
GenevisibleiO00762. HS.

Organism-specific databases

HPAiCAB011464.
CAB035990.
HPA034569.
HPA054975.

Interactioni

Subunit structurei

Component of the APC/C complex.

Protein-protein interaction databases

BioGridi116249. 60 interactions.
DIPiDIP-52725N.
IntActiO00762. 9 interactions.
STRINGi9606.ENSP00000348838.

Structurei

Secondary structure

1
179
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 4516Combined sources
Beta strandi50 – 545Combined sources
Beta strandi61 – 688Combined sources
Beta strandi78 – 847Combined sources
Turni87 – 915Combined sources
Beta strandi95 – 1006Combined sources
Beta strandi111 – 1133Combined sources
Helixi116 – 1183Combined sources
Turni119 – 1213Combined sources
Helixi128 – 14013Combined sources
Helixi150 – 1556Combined sources
Helixi159 – 17214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I7KX-ray1.95A/B1-179[»]
4YIIX-ray1.80U27-179[»]
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.
GeneTreeiENSGT00760000119350.
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. AlignAdd to basket

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

        10         20         30         40         50
MASQNRDPAA TSVAAARKGA EPSGGAARGP VGKRLQQELM TLMMSGDKGI
60 70 80 90 100
SAFPESDNLF KWVGTIHGAA GTVYEDLRYK LSLEFPSGYP YNAPTVKFLT
110 120 130 140 150
PCYHPNVDTQ GNICLDILKE KWSALYDVRT ILLSIQSLLG EPNIDSPLNT
160 170
HAAELWKNPT AFKKYLQETY SKQVTSQEP
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:
EMBLi
GenBanki
DDBJi
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.
ENST00000372568; ENSP00000361649; 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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I7KX-ray1.95A/B1-179[»]
4YIIX-ray1.80U27-179[»]
ProteinModelPortaliO00762.
SMRiO00762. Positions 30-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116249. 60 interactions.
DIPiDIP-52725N.
IntActiO00762. 9 interactions.
STRINGi9606.ENSP00000348838.

PTM databases

PhosphoSiteiO00762.

Proteomic databases

MaxQBiO00762.
PaxDbiO00762.
PRIDEiO00762.

Protocols and materials databases

DNASUi11065.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi11065.
GeneCardsiGC20P044442.
HGNCiHGNC:15937. UBE2C.
HPAiCAB011464.
CAB035990.
HPA034569.
HPA054975.
MIMi605574. gene.
neXtProtiNX_O00762.
PharmGKBiPA38057.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00760000119350.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiO00762.
KOiK06688.
OMAiAELWDKD.
OrthoDBiEOG7M0NTH.
PhylomeDBiO00762.
TreeFamiTF101116.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B6. 2681.
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_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
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.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
SignaLinkiO00762.

Miscellaneous databases

ChiTaRSiUBE2C. human.
EvolutionaryTraceiO00762.
GeneWikiiUBE2C.
GenomeRNAii11065.
NextBioi42051.
PROiO00762.
SOURCEiSearch...

Gene expression databases

BgeeiO00762.
CleanExiHS_UBE2C.
ExpressionAtlasiO00762. baseline and differential.
GenevisibleiO00762. HS.

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. "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], CLEAVAGE OF INITIATOR METHIONINE [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: July 22, 2015
This is version 160 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

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.