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Protein

Ubiquitin-conjugating enzyme E2Q-like protein CG4502

Gene

CG4502

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the covalent attachment of ubiquitin to other proteins.PROSITE-ProRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei234 – 2341Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ligase activity Source: UniProtKB-KW

GO - Biological processi

  1. protein ubiquitination Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ9VM35.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2Q-like protein CG4502 (EC:6.3.2.19)
Gene namesi
ORF Names:CG4502
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0031896. CG4502.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 306306Ubiquitin-conjugating enzyme E2Q-like protein CG4502PRO_0000335813Add
BLAST

Proteomic databases

PRIDEiQ9VM35.

Expressioni

Gene expression databases

BgeeiQ9VM35.

Interactioni

Protein-protein interaction databases

BioGridi60148. 2 interactions.
MINTiMINT-1763215.
STRINGi7227.FBpp0079044.

Structurei

3D structure databases

ProteinModelPortaliQ9VM35.
SMRiQ9VM35. Positions 142-267.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi22 – 4120Poly-AsnAdd
BLAST
Compositional biasi53 – 6614Poly-AsnAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG272407.
GeneTreeiENSGT00390000018573.
InParanoidiQ9VM35.
KOiK10582.
OMAiDSLFEWH.
OrthoDBiEOG7F512D.
PhylomeDBiQ9VM35.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VM35-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSRSKERVV TAFRKIFHKS SNNNNNNNNN HNNNINNNNN NDKVDGATGS
60 70 80 90 100
SPNINNNNNN NNNNNNHDGA AAPSSAGGVA VAGGAVGSSG SSGAAKNAVV
110 120 130 140 150
RMAAEQAVWD SPGKRRRQDH KVAPTTERQL VAAPDHTIRT RRLMKEYREM
160 170 180 190 200
ERLQAKNDAV FTVELVNDSL FEWHVRLHVI DPDSPLARDM AEMGVPAILL
210 220 230 240 250
HLSFPDNFPF APPFMRVVEP HIEKGYVMEG GAICMELLTP RGWASAYTVE
260 270 280 290 300
AVIMQFAASV VKGQGRIARK PKSTKEFTRR QAEESFRSLV KTHEKYGWVT

PALSDG
Length:306
Mass (Da):33,670
Last modified:May 1, 2000 - v1
Checksum:i75897876D46A813A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF52492.1.
AE014134 Genomic DNA. Translation: AAF52493.1.
AY060422 mRNA. Translation: AAL25461.1.
RefSeqiNP_609103.1. NM_135259.3.
NP_723260.1. NM_164741.2.
UniGeneiDm.340.

Genome annotation databases

EnsemblMetazoaiFBtr0079416; FBpp0079044; FBgn0031896.
FBtr0079417; FBpp0079045; FBgn0031896.
GeneIDi34002.
KEGGidme:Dmel_CG4502.
UCSCiCG4502-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF52492.1.
AE014134 Genomic DNA. Translation: AAF52493.1.
AY060422 mRNA. Translation: AAL25461.1.
RefSeqiNP_609103.1. NM_135259.3.
NP_723260.1. NM_164741.2.
UniGeneiDm.340.

3D structure databases

ProteinModelPortaliQ9VM35.
SMRiQ9VM35. Positions 142-267.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60148. 2 interactions.
MINTiMINT-1763215.
STRINGi7227.FBpp0079044.

Proteomic databases

PRIDEiQ9VM35.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0079416; FBpp0079044; FBgn0031896.
FBtr0079417; FBpp0079045; FBgn0031896.
GeneIDi34002.
KEGGidme:Dmel_CG4502.
UCSCiCG4502-RA. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0031896. CG4502.

Phylogenomic databases

eggNOGiNOG272407.
GeneTreeiENSGT00390000018573.
InParanoidiQ9VM35.
KOiK10582.
OMAiDSLFEWH.
OrthoDBiEOG7F512D.
PhylomeDBiQ9VM35.

Enzyme and pathway databases

UniPathwayiUPA00143.
SignaLinkiQ9VM35.

Miscellaneous databases

ChiTaRSiCG4502. fly.
GenomeRNAii34002.
NextBioi786370.
PROiQ9VM35.

Gene expression databases

BgeeiQ9VM35.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiU2QL1_DROME
AccessioniPrimary (citable) accession number: Q9VM35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 1, 2000
Last modified: April 29, 2015
This is version 101 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

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.