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Protein

Ubiquitin-conjugating enzyme E2 C

Gene

UBE2C

Organism
Spisula solidissima (Atlantic surf-clam)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).PROSITE-ProRule annotation

Catalytic activityi

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

Pathway:iprotein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.PROSITE-ProRule annotation
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

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 C (EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein C
Ubiquitin-protein ligase C
Gene namesi
Name:UBE2C
Synonyms:UBCH10
OrganismiSpisula solidissima (Atlantic surf-clam)
Taxonomic identifieri6584 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaBivalviaHeteroconchiaEuheterodontaVeneroidaMactroideaMactridaeSpisula

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi114 – 1141C → S: Inhibition of cyclin B degradation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 177177Ubiquitin-conjugating enzyme E2 CPRO_0000082563Add
BLAST

Post-translational modificationi

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

Keywords - PTMi

Ubl conjugation

Interactioni

Subunit structurei

Component of the APC/C complex.By similarity

Structurei

Secondary structure

1
177
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 4515Combined sources
Beta strandi50 – 578Combined sources
Beta strandi59 – 679Combined sources
Turni73 – 764Combined sources
Beta strandi78 – 847Combined sources
Turni87 – 904Combined sources
Beta strandi95 – 1006Combined sources
Helixi116 – 1183Combined sources
Turni119 – 1213Combined sources
Helixi128 – 13811Combined sources
Helixi150 – 1556Combined sources
Helixi159 – 17517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E2CX-ray2.00A22-177[»]
ProteinModelPortaliQ95044.
SMRiQ95044. Positions 22-177.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ95044.

Family & Domainsi

Sequence similaritiesi

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

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.

Q95044-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGQNIDPAA NQVRQKERPR DMTTSKERHS VSKRLQQELR TLLMSGDPGI
60 70 80 90 100
TAFPDGDNLF KWVATLDGPK DTVYESLKYK LTLEFPSDYP YKPPVVKFTT
110 120 130 140 150
PCWHPNVDQS GNICLDILKE NWTASYDVRT ILLSLQSLLG EPNNASPLNA
160 170
QAADMWSNQT EYKKVLHEKY KTAQSDK
Length:177
Mass (Da):20,134
Last modified:February 1, 1997 - v1
Checksum:i06A454E798EE4F3A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52949 mRNA. Translation: AAB06237.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52949 mRNA. Translation: AAB06237.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E2CX-ray2.00A22-177[»]
ProteinModelPortaliQ95044.
SMRiQ95044. Positions 22-177.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

EvolutionaryTraceiQ95044.

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

  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).

Entry informationi

Entry nameiUBE2C_SPISO
AccessioniPrimary (citable) accession number: Q95044
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 1, 1997
Last modified: March 4, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.