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Q95044 (UBE2C_SPISO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 C

EC=6.3.2.19
Alternative name(s):
Ubiquitin carrier protein C
Ubiquitin-protein ligase C
Gene names
Name:UBE2C
Synonyms:UBCH10
OrganismSpisula solidissima (Atlantic surf-clam)
Taxonomic identifier6584 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaBivalviaHeteroconchiaVeneroidaMactroideaMactridaeSpisula

Protein attributes

Sequence length177 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the covalent attachment of ubiquitin to other proteins. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that is essential for the transition from metaphase to anaphase in mitosis. Involved in both degradation of proteins responsible for maintaining sister chromatid cohesion at the onset of anaphase and of mitotic cyclins A and B at the exit of mitosis. Acts by initiating polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit By similarity.

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Component of the APC/C complex By similarity.

Post-translational modification

Autoubiquitinated by the APC/C complex, leading to its degradation by the proteasome By similarity.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
Ubl conjugation pathway
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMUbl conjugation
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processmitosis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-protein ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 177177Ubiquitin-conjugating enzyme E2 C
PRO_0000082563

Sites

Active site1141Glycyl thioester intermediate

Experimental info

Mutagenesis1141C → S: Inhibition of cyclin B degradation. Ref.2

Secondary structure

........................ 177
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q95044 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 06A454E798EE4F3A

FASTA17720,134
        10         20         30         40         50         60 
MSGQNIDPAA NQVRQKERPR DMTTSKERHS VSKRLQQELR TLLMSGDPGI TAFPDGDNLF 

        70         80         90        100        110        120 
KWVATLDGPK DTVYESLKYK LTLEFPSDYP YKPPVVKFTT PCWHPNVDQS GNICLDILKE 

       130        140        150        160        170 
NWTASYDVRT ILLSLQSLLG EPNNASPLNA QAADMWSNQT EYKKVLHEKY KTAQSDK 

« Hide

References

[1]"E2-C, a cyclin-selective ubiquitin carrier protein required for the destruction of mitotic cyclins."
Aristarkhov A., Eytan E., Moghe A., Admon A., Hershko A., Ruderman J.V.
Proc. Natl. Acad. Sci. U.S.A. 93:4294-4299(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"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: MUTAGENESIS OF CYS-114.
[3]"Crystal structure of the cyclin-specific ubiquitin-conjugating enzyme from clam, E2-C, at 2.0 A resolution."
Jiang F., Basavappa R.
Biochemistry 38:6471-6478(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U52949 mRNA. Translation: AAB06237.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E2CX-ray2.00A22-177[»]
ProteinModelPortalQ95044.
SMRQ95044. Positions 22-177.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00143.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ95044.

Entry information

Entry nameUBE2C_SPISO
AccessionPrimary (citable) accession number: Q95044
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 1, 1997
Last modified: February 19, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways