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Q9VM35

- U2QL1_DROME

UniProt

Q9VM35 - U2QL1_DROME

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Protein

Ubiquitin-conjugating enzyme E2Q-like protein CG4502

Gene

CG4502

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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. acid-amino acid ligase activity Source: InterPro
  2. ATP binding 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: 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 142-293.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE014134 Genomic DNA. Translation: AAF52492.1 .
AE014134 Genomic DNA. Translation: AAF52493.1 .
AY060422 mRNA. Translation: AAL25461.1 .
RefSeqi NP_609103.1. NM_135259.3.
NP_723260.1. NM_164741.2.
UniGenei Dm.340.

3D structure databases

ProteinModelPortali Q9VM35.
SMRi Q9VM35. Positions 142-293.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 60148. 2 interactions.
MINTi MINT-1763215.
STRINGi 7227.FBpp0079044.

Proteomic databases

PRIDEi Q9VM35.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0079416 ; FBpp0079044 ; FBgn0031896 .
FBtr0079417 ; FBpp0079045 ; FBgn0031896 .
GeneIDi 34002.
KEGGi dme:Dmel_CG4502.
UCSCi CG4502-RA. d. melanogaster.

Organism-specific databases

FlyBasei FBgn0031896. CG4502.

Phylogenomic databases

eggNOGi NOG272407.
GeneTreei ENSGT00390000018573.
InParanoidi Q9VM35.
KOi K10582.
OMAi DSLFEWH.
OrthoDBi EOG7F512D.
PhylomeDBi Q9VM35.

Enzyme and pathway databases

UniPathwayi UPA00143 .
SignaLinki Q9VM35.

Miscellaneous databases

ChiTaRSi CG4502. drosophila.
GenomeRNAii 34002.
NextBioi 786370.

Gene expression databases

Bgeei Q9VM35.

Family and domain databases

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

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: October 29, 2014
This is version 97 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