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Protein

Ubiquitin-conjugating enzyme E2 S

Gene

CG8188

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 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 specifically elongating polyubiquitin chains initiated by the E2 enzyme vih/UbcH10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit.PROSITE-ProRule annotation1 Publication

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation1 Publication

Pathway: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.PROSITE-ProRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei98 – 981Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  • cell division Source: UniProtKB-KW
  • exit from mitosis Source: UniProtKB
  • imaginal disc-derived wing morphogenesis Source: FlyBase
  • protein polyubiquitination Source: GO_Central
  • protein ubiquitination Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Cell division, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ9VX25.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 S (EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein S
Ubiquitin-protein ligase S
Gene namesi
ORF Names:CG8188
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0030863. CG8188.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 209209Ubiquitin-conjugating enzyme E2 SPRO_0000390440Add
BLAST

Proteomic databases

PaxDbiQ9VX25.

Expressioni

Gene expression databases

BgeeiQ9VX25.
GenevisibleiQ9VX25. DM.

Interactioni

Protein-protein interaction databases

BioGridi59074. 9 interactions.
IntActiQ9VX25. 5 interactions.
MINTiMINT-895042.
STRINGi7227.FBpp0099891.

Structurei

3D structure databases

ProteinModelPortaliQ9VX25.
SMRiQ9VX25. Positions 9-159.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
InParanoidiQ9VX25.
KOiK10583.
OMAiGHKGEIC.
OrthoDBiEOG73JKXD.
PhylomeDBiQ9VX25.

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.

Q9VX25-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSQYSNVEN LSPQTIRQVM RELQEMETTP PEGIKVLINE SDVTDIQALI
60 70 80 90 100
DGPAGTPYAA GIFRVKLTLN KDFPLTPPKA YFLTKIFHPN VAANGEICVN
110 120 130 140 150
TLKKDWKPDL GIKHILLTIK CLLIVPNPES ALNEEAGKML LERYDDYSQR
160 170 180 190 200
ARMMTEIHAQ PAKCGVGAVG DAKDDGGPST KKHAGLDKKL QDKKKEKLLK

EKKRMLKRL
Length:209
Mass (Da):23,337
Last modified:July 5, 2004 - v2
Checksum:i65A528912E50A477
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ151896 mRNA. Translation: AAZ57341.1.
DQ151897 mRNA. Translation: AAZ57342.1.
AE014298 Genomic DNA. Translation: ABC67190.1.
AE014298 Genomic DNA. Translation: AAF48756.2.
BT031269 mRNA. Translation: ABY20510.1.
RefSeqiNP_001033852.1. NM_001038763.2.
NP_001285383.1. NM_001298454.1.
NP_001285384.1. NM_001298455.1.
NP_573237.2. NM_133009.3.
UniGeneiDm.11521.

Genome annotation databases

EnsemblMetazoaiFBtr0074476; FBpp0074250; FBgn0030863.
FBtr0100463; FBpp0099891; FBgn0030863.
FBtr0340633; FBpp0309497; FBgn0030863.
FBtr0346186; FBpp0312005; FBgn0030863.
GeneIDi32751.
KEGGidme:Dmel_CG8188.
UCSCiCG8188-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ151896 mRNA. Translation: AAZ57341.1.
DQ151897 mRNA. Translation: AAZ57342.1.
AE014298 Genomic DNA. Translation: ABC67190.1.
AE014298 Genomic DNA. Translation: AAF48756.2.
BT031269 mRNA. Translation: ABY20510.1.
RefSeqiNP_001033852.1. NM_001038763.2.
NP_001285383.1. NM_001298454.1.
NP_001285384.1. NM_001298455.1.
NP_573237.2. NM_133009.3.
UniGeneiDm.11521.

3D structure databases

ProteinModelPortaliQ9VX25.
SMRiQ9VX25. Positions 9-159.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59074. 9 interactions.
IntActiQ9VX25. 5 interactions.
MINTiMINT-895042.
STRINGi7227.FBpp0099891.

Proteomic databases

PaxDbiQ9VX25.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0074476; FBpp0074250; FBgn0030863.
FBtr0100463; FBpp0099891; FBgn0030863.
FBtr0340633; FBpp0309497; FBgn0030863.
FBtr0346186; FBpp0312005; FBgn0030863.
GeneIDi32751.
KEGGidme:Dmel_CG8188.
UCSCiCG8188-RA. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0030863. CG8188.

Phylogenomic databases

eggNOGiCOG5078.
InParanoidiQ9VX25.
KOiK10583.
OMAiGHKGEIC.
OrthoDBiEOG73JKXD.
PhylomeDBiQ9VX25.

Enzyme and pathway databases

UniPathwayiUPA00143.
SignaLinkiQ9VX25.

Miscellaneous databases

ChiTaRSiCG8188. fly.
GenomeRNAii32751.
NextBioi780178.
PROiQ9VX25.

Gene expression databases

BgeeiQ9VX25.
GenevisibleiQ9VX25. DM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Full length sequences of assorted Drosophila melanogaster cDNAs."
    Murphy T.D.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  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, CATALYTIC ACTIVITY, PATHWAY.

Entry informationi

Entry nameiUBE2S_DROME
AccessioniPrimary (citable) accession number: Q9VX25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: July 5, 2004
Last modified: June 24, 2015
This is version 115 of the entry and version 2 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.