Q9VTY6 (UBE2C_DROME) 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 carrier protein vihar
Ubiquitin-protein ligase C

Gene names

Name:	vih
Synonyms:	Ubch10
ORF Names:	CG10682

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	178 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 controls progression through 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. Ref.1 Ref.5
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Component of the APC/C complex.
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton › centrosome. Note: Localizes in the cytoplasm of mitotic cells but also associates with centrosomes, and its own degradation is initiated at the metaphase-anaphase transition. Ref.1
Post-translational modification	Ubiquitinated by the APC/C complex, leading to its degradation at the metaphase-anaphase transition. Ref.1
Disruption phenotype	Embryonic lethality. Both homozygous and hemizygous females show maternal effect lethality and produce syncytial embryos that fail to develop as a result of mitotic defects. Ref.1
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Cytoskeleton
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from mutant phenotype Ref.5. Source: UniProtKB exit from mitosis Inferred from mutant phenotype Ref.5. Source: UniProtKB regulation of cell cycle Inferred from mutant phenotype Ref.1. Source: FlyBase
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell ubiquitin ligase complex Inferred from physical interaction PubMed 22417125. Source: FlyBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from direct assay Ref.1. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 178	178	Ubiquitin-conjugating enzyme E2 C		PRO_0000390471
Sites
	Active site	116	1	Glycyl thioester intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9VTY6 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 7EF04EE68FEDC7AB	FASTA	178	19,832
	10 20 30 40 50 60 MAQNISPEQS GGAGGGGSKH SDDSMPVKDN HAVSKRLHKE LMNLMMANER GISAFPDGEN 70 80 90 100 110 120 IFKWVGTIAG PRNTVYSGQT YRLSLDFPNS YPYAAPVVKF LTSCFHPNVD LQGAICLDIL 130 140 150 160 170 KDKWSALYDV RTILLSIQSL LGEPNNESPL NAQAAMMWND QKEYKKYLDA FYEKHKDT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The E2-C vihar is required for the correct spatiotemporal proteolysis of cyclin B and itself undergoes cyclical degradation." Mathe E., Kraft C., Giet R., Deak P., Peters J.-M., Glover D.M. Curr. Biol. 14:1723-1733(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION, DISRUPTION PHENOTYPE.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley.
[5]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF410850 mRNA. Translation: AAL02117.1. AE014296 Genomic DNA. Translation: AAF49909.1. BT028772 mRNA. Translation: ABI34153.1.
RefSeq	NP_648582.1. NM_140325.3.
UniGene	Dm.3505.
3D structure databases
HSSP	HSSP built from PDB template 1I7K based on UniProtKB O00762.
ProteinModelPortal	Q9VTY6.
SMR	Q9VTY6. Positions 33-175.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-845845.
STRING	7227.FBpp0075690.
Proteomic databases
PaxDb	Q9VTY6.
PRIDE	Q9VTY6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0075958; FBpp0075690; FBgn0027936.
GeneID	44118.
KEGG	dme:Dmel_CG10682.
UCSC	CG10682-RA. d. melanogaster.
Organism-specific databases
CTD	44118.
FlyBase	FBgn0027936. vih.
Phylogenomic databases
eggNOG	COG5078.
GeneTree	ENSGT00640000091484.
InParanoid	Q9VTY6.
KO	K06688.
OMA	DNLFRWI.
OrthoDB	EOG4STQMV.
PhylomeDB	Q9VTY6.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
Bgee	Q9VTY6.
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
GenomeRNAi	44118.
NextBio	836806.

Entry information

Entry name

UBE2C_DROME

Accession

Primary (citable) accession number: Q9VTY6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2009
Last sequence update:	May 1, 2000
Last modified:	April 3, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project