Q95044 (UBE2C_SPISO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Spisula solidissima (Atlantic surf-clam)

Taxonomic identifier

6584 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Lophotrochozoa › Mollusca › Bivalvia › Heteroconchia › Veneroida › Mactroidea › Mactridae › Spisula

Protein attributes

Sequence length	177 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Cell cycle Cell division Mitosis Ubl conjugation pathway
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Ubl conjugation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 177

177

Ubiquitin-conjugating enzyme E2 C

PRO_0000082563

Sites

Active site

114

1

Glycyl thioester intermediate

Experimental info

Mutagenesis

114

1

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

Secondary structure

1

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177

Helix Strand Turn

Details...

Helix

31 – 45

15

Beta strand

50 – 57

8

Beta strand

59 – 67

9

Turn

73 – 76

4

Beta strand

78 – 84

7

Turn

87 – 90

4

Beta strand

95 – 100

6

Helix

116 – 118

3

Turn

119 – 121

3

Helix

128 – 138

11

Helix

150 – 155

6

Helix

159 – 175

17

Sequences

	Sequence		Length	Mass (Da)
	Q95044 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 06A454E798EE4F3A	FASTA	177	20,134
	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

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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2E2C	X-ray	2.00	A	22-177	[»]

ProteinModelPortal

Q95044.

SMR

Q95044. Positions 22-177.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

UniPathway

UPA00143.

Family and domain databases

Gene3D

3.10.110.10. 1 hit.

InterPro

IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]

Pfam

PF00179. UQ_con. 1 hit.
[Graphical view]

SUPFAM

SSF54495. UBQ-conjugat/RWD-like. 1 hit.

PROSITE

PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q95044.

Entry information

Entry name

UBE2C_SPISO

Accession

Primary (citable) accession number: Q95044

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	February 1, 1997
Last modified:	April 3, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)