Reviewed, UniProtKB/Swiss-Prot Q95044 (UBE2C_SPISO)

Names and origin

Protein names	Recommended name:     Ubiquitin-conjugating enzyme E2 C     EC=6.3.2.19 Alternative name(s):     Ubiquitin-protein ligase C     Ubiquitin carrier protein C
Organism	Spisula solidissima (Atlantic surf-clam)
Taxonomic identifier	6584 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Mollusca › Bivalvia › Heteroconchia › Veneroida › Mactroidea › Mactridae › Spisula

Protein attributes

Sequence length	177 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the covalent attachment of ubiquitin to other proteins. Works in conjunction with the 20S cyclosome/anaphase-promoting complex (APC) and 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.
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
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
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 modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW protein ubiquitination Inferred from electronic annotation. Source: InterPro regulation of protein metabolic process Inferred from electronic annotation. Source: InterPro
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)
	Q95044-1 [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: 8633058] [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: 9122200] [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: 10350465] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

U52949 mRNA. Translation: AAB06237.1.

3D structure databases

PDBPDBe

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

ModBase

Search...

Enzyme and pathway databases

BRENDA

6.3.2.19. 8445.

Family and domain databases

InterPro

IPR015582. Ubiquitin-conj_enz_E2_H10.
IPR016135. UBQ-conjugat/RWD-like.
IPR000608. UBQ-conjugat_E2.
[Graphical view]

Gene3D

G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.

PANTHER

PTHR11621:SF26. UbcH10. 1 hit.

Pfam

PF00179. UQ_con. 1 hit.
[Graphical view]

ProDom

PD000461. UBQ_conjugat. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00212. UBCc. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

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:	June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)