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Q9VTY6

- UBE2C_DROME

UniProt

Q9VTY6 - UBE2C_DROME

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Protein

Ubiquitin-conjugating enzyme E2 C

Gene
vih, Ubch10, CG10682
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 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 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.2 Publications

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei116 – 1161Glycyl thioester intermediate By similarity

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. ubiquitin-protein transferase activity Source: FlyBase

GO - Biological processi

  1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  2. exit from mitosis Source: UniProtKB
  3. regulation of cell cycle Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_181662. Separation of Sister Chromatids.
REACT_182058. Senescence-Associated Secretory Phenotype (SASP).
REACT_210493. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_224351. Regulation of APC/C activators between G1/S and early anaphase.
REACT_33104. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_92044. APC/C:Cdc20 mediated degradation of Securin.
SignaLinkiQ9VTY6.
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 carrier protein vihar
Ubiquitin-protein ligase C
Gene namesi
Name:vih
Synonyms:Ubch10
ORF Names:CG10682
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0264848. vih.

Subcellular locationi

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.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. microtubule organizing center Source: UniProtKB-SubCell
  3. ubiquitin ligase complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 178178Ubiquitin-conjugating enzyme E2 CPRO_0000390471Add
BLAST

Post-translational modificationi

Ubiquitinated by the APC/C complex, leading to its degradation at the metaphase-anaphase transition.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ9VTY6.
PRIDEiQ9VTY6.

Expressioni

Gene expression databases

BgeeiQ9VTY6.

Interactioni

Subunit structurei

Component of the APC/C complex.

Protein-protein interaction databases

BioGridi68841. 7 interactions.
MINTiMINT-845845.
STRINGi7227.FBpp0075690.

Structurei

3D structure databases

ProteinModelPortaliQ9VTY6.
SMRiQ9VTY6. Positions 33-175.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110854.
InParanoidiQ9VTY6.
KOiK06688.
OMAiAELWDKD.
PhylomeDBiQ9VTY6.

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.

Q9VTY6-1 [UniParc]FASTAAdd to Basket

« Hide

MAQNISPEQS GGAGGGGSKH SDDSMPVKDN HAVSKRLHKE LMNLMMANER    50
GISAFPDGEN IFKWVGTIAG PRNTVYSGQT YRLSLDFPNS YPYAAPVVKF 100
LTSCFHPNVD LQGAICLDIL KDKWSALYDV RTILLSIQSL LGEPNNESPL 150
NAQAAMMWND QKEYKKYLDA FYEKHKDT 178
Length:178
Mass (Da):19,832
Last modified:May 1, 2000 - v1
Checksum:i7EF04EE68FEDC7AB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF410850 mRNA. Translation: AAL02117.1.
AE014296 Genomic DNA. Translation: AAF49909.1.
BT028772 mRNA. Translation: ABI34153.1.
RefSeqiNP_648582.1. NM_140325.3.
UniGeneiDm.3505.

Genome annotation databases

EnsemblMetazoaiFBtr0075958; FBpp0075690; FBgn0027936.
GeneIDi44118.
KEGGidme:Dmel_CG10682.
UCSCiCG10682-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF410850 mRNA. Translation: AAL02117.1 .
AE014296 Genomic DNA. Translation: AAF49909.1 .
BT028772 mRNA. Translation: ABI34153.1 .
RefSeqi NP_648582.1. NM_140325.3.
UniGenei Dm.3505.

3D structure databases

ProteinModelPortali Q9VTY6.
SMRi Q9VTY6. Positions 33-175.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 68841. 7 interactions.
MINTi MINT-845845.
STRINGi 7227.FBpp0075690.

Proteomic databases

PaxDbi Q9VTY6.
PRIDEi Q9VTY6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0075958 ; FBpp0075690 ; FBgn0027936 .
GeneIDi 44118.
KEGGi dme:Dmel_CG10682.
UCSCi CG10682-RA. d. melanogaster.

Organism-specific databases

CTDi 44118.
FlyBasei FBgn0264848. vih.

Phylogenomic databases

eggNOGi COG5078.
GeneTreei ENSGT00730000110854.
InParanoidi Q9VTY6.
KOi K06688.
OMAi AELWDKD.
PhylomeDBi Q9VTY6.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_181662. Separation of Sister Chromatids.
REACT_182058. Senescence-Associated Secretory Phenotype (SASP).
REACT_210493. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_224351. Regulation of APC/C activators between G1/S and early anaphase.
REACT_33104. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_92044. APC/C:Cdc20 mediated degradation of Securin.
SignaLinki Q9VTY6.

Miscellaneous databases

GenomeRNAii 44118.
NextBioi 836806.
PROi Q9VTY6.

Gene expression databases

Bgeei Q9VTY6.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiUBE2C_DROME
AccessioniPrimary (citable) accession number: Q9VTY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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