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Q9VTY6 (UBE2C_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 104. 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 carrier protein vihar
Ubiquitin-protein ligase C
Gene names
Name:vih
Synonyms:Ubch10
ORF Names:CG10682
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length178 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 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. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 178178Ubiquitin-conjugating enzyme E2 C
PRO_0000390471

Sites

Active site1161Glycyl thioester intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9VTY6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 7EF04EE68FEDC7AB

FASTA17819,832
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
RefSeqNP_648582.1. NM_140325.3.
UniGeneDm.3505.

3D structure databases

ProteinModelPortalQ9VTY6.
SMRQ9VTY6. Positions 33-175.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid68841. 7 interactions.
MINTMINT-845845.
STRING7227.FBpp0075690.

Proteomic databases

PaxDbQ9VTY6.
PRIDEQ9VTY6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0075958; FBpp0075690; FBgn0027936.
GeneID44118.
KEGGdme:Dmel_CG10682.
UCSCCG10682-RA. d. melanogaster.

Organism-specific databases

CTD44118.
FlyBaseFBgn0264848. vih.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00730000110854.
InParanoidQ9VTY6.
KOK06688.
OMAAELWDKD.
PhylomeDBQ9VTY6.

Enzyme and pathway databases

SignaLinkQ9VTY6.
UniPathwayUPA00143.

Gene expression databases

BgeeQ9VTY6.

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

GenomeRNAi44118.
NextBio836806.
PROQ9VTY6.

Entry information

Entry nameUBE2C_DROME
AccessionPrimary (citable) accession number: Q9VTY6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase