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P52486 (UBCD4_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2-22 kDa

EC=6.3.2.19
Alternative name(s):
Ubiquitin carrier protein
Ubiquitin-protein ligase
Gene names
Name:UbcD4
ORF Names:CG8284
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length199 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the covalent attachment of ubiquitin to other proteins. Ref.1

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with Rpn10. Ref.1

Tissue specificity

During gastrulation, expression is highest in the invaginating posterior midgut primordium (PMG), high expression is also observed in the cephalic furrow and ventral ectodermal neurogenic region. In stage 10-11 embryos, expression is high in the pole cells present in the pocket formed by the PMG. During germ band retraction, expression appears to reinitiate in many tissues, especially the gut and nervous system. After dorsal closure, expression is detectable at low levels throughout the embryo. Ref.1

Developmental stage

Expressed both maternally and zygotically. Embryonic expression is highest at 0-8 hours. Ref.1

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Contains 1 UBA domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processregulation of cell cycle

Inferred from direct assay PubMed 21548953. Source: FlyBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-protein ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Rpn10P550352EBI-224571,EBI-146479

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 199199Ubiquitin-conjugating enzyme E2-22 kDa
PRO_0000082522

Regions

Domain161 – 19939UBA

Sites

Active site921Glycyl thioester intermediate By similarity

Experimental info

Sequence conflict34 – 363DSW → GQL in CAA63424. Ref.1
Sequence conflict731V → A in CAA63424. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P52486 [UniParc].

Last modified November 9, 2004. Version 2.
Checksum: 2875F9478632C630

FASTA19922,510
        10         20         30         40         50         60 
MANMAVSRIK REFKEVMRSE EIVQCSIKIE LVNDSWTELR GEIAGPPDTP YEGGKFVLEI 

        70         80         90        100        110        120 
KVPETYPFNP PKVRFITRIW HPNISSVTGA ICLDILKDNW AAAMTLRTVL LSLQALLAAA 

       130        140        150        160        170        180 
EPDDPQDAVV AYQFKDKYDL FLLTAKHWTN AYAGGPHTFP DCDSKIQRLR DMGIDEHEAR 

       190 
AVLSKENWNL EKATEGLFS 

« Hide

References

« Hide 'large scale' references
[1]"UbcD4, a ubiquitin-conjugating enzyme in Drosophila melanogaster expressed in pole cells."
Canning M., Kirby R., Finnegan D.
Mol. Genet. Genomics 266:907-913(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RPN10, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: Canton-S and Oregon-R.
[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]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X92838 mRNA. Translation: CAA63424.1.
Y11349 Genomic DNA. Translation: CAA72184.1.
AE014296 Genomic DNA. Translation: AAF50222.1.
AY060381 mRNA. Translation: AAL25420.1.
PIRT08465.
RefSeqNP_524010.2. NM_079286.3.
UniGeneDm.7820.

3D structure databases

ProteinModelPortalP52486.
SMRP52486. Positions 1-199.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid64522. 9 interactions.
DIPDIP-20847N.
IntActP52486. 3 interactions.
MINTMINT-337672.

Proteomic databases

PaxDbP52486.
PRIDEP52486.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0076395; FBpp0076124; FBgn0015321.
GeneID39133.
KEGGdme:Dmel_CG8284.

Organism-specific databases

CTD39133.
FlyBaseFBgn0015321. UbcD4.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00670000098059.
InParanoidP52486.
KOK04649.
OMAKHWTNAY.
OrthoDBEOG7F513F.
PhylomeDBP52486.

Enzyme and pathway databases

SignaLinkP52486.
UniPathwayUPA00143.

Gene expression databases

BgeeP52486.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00627. UBA. 1 hit.
PF00179. UQ_con. 1 hit.
[Graphical view]
SMARTSM00165. UBA. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
SSF54495. SSF54495. 1 hit.
PROSITEPS50030. UBA. 1 hit.
PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi39133.
NextBio812082.
PROP52486.

Entry information

Entry nameUBCD4_DROME
AccessionPrimary (citable) accession number: P52486
Secondary accession number(s): P91633
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 9, 2004
Last modified: April 16, 2014
This is version 111 of the entry and version 2 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