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P25153 (UBCD6_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2-17 kDa

EC=6.3.2.19
Alternative name(s):
Ubiquitin carrier protein
Ubiquitin-protein ligase
Gene names
Name:UbcD6
Synonyms:Dhr6
ORF Names:CG2013
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length151 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the covalent attachment of ubiquitin to other proteins. Required for postreplication repair of UV-damaged DNA.

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Subcellular location

Nucleus.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Ubl conjugation pathway
   Cellular componentNucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from genetic interaction Ref.1. Source: FlyBase

centrosome organization

Inferred from mutant phenotype PubMed 17412918. Source: FlyBase

centrosome separation

Inferred from mutant phenotype PubMed 18798690. Source: FlyBase

endocytic recycling

Inferred from mutant phenotype PubMed 23685073. Source: FlyBase

mitochondrion degradation

Inferred from mutant phenotype PubMed 23685073. Source: FlyBase

mitotic spindle organization

Inferred from mutant phenotype PubMed 17412918. Source: FlyBase

negative regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from mutant phenotype PubMed 21205821. Source: BHF-UCL

negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from mutant phenotype PubMed 21205821. Source: BHF-UCL

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 21205821. Source: BHF-UCL

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 21205821. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 21205821. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 21205821. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

p53 binding

Inferred from physical interaction PubMed 21205821. Source: BHF-UCL

protein domain specific binding

Inferred from physical interaction PubMed 21205821. Source: BHF-UCL

ubiquitin-protein ligase activity

Inferred by curator PubMed 21205821. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 151151Ubiquitin-conjugating enzyme E2-17 kDa
PRO_0000082523

Sites

Active site881Glycyl thioester intermediate By similarity

Experimental info

Sequence conflict991T → R in AAA28308. Ref.1
Sequence conflict991T → R in AAA28309. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P25153 [UniParc].

Last modified June 1, 2001. Version 2.
Checksum: CC4B35992E4A9220

FASTA15117,152
        10         20         30         40         50         60 
MSTPARRRLM RDFKRLQEDP PTGVSGAPTD NNIMIWNAVI FGPHDTPFED GTFKLTIEFT 

        70         80         90        100        110        120 
EEYPNKPPTV RFVSKVFHPN VYADGGICLD ILQNRWSPTY DVSAILTSIQ SLLSDPNPNS 

       130        140        150 
PANSTAAQLY KENRREYEKR VKACVEQSFI D 

« Hide

References

« Hide 'large scale' references
[1]"Dhr6, a Drosophila homolog of the yeast DNA-repair gene RAD6."
Koken M.H.M., Reynolds P., Bootsma D., Hoeijmakers J.H.J., Prakash S., Prakash L.
Proc. Natl. Acad. Sci. U.S.A. 88:3832-3836(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / 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. 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]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63792 mRNA. Translation: AAA28308.1.
M64435, M63791 Genomic DNA. Translation: AAA28309.1.
AE014297 Genomic DNA. Translation: AAF52079.1.
BT003481 mRNA. Translation: AAO39484.1.
PIRA39392.
RefSeqNP_001246916.1. NM_001259987.2.
NP_524230.2. NM_079506.4.
UniGeneDm.2229.

3D structure databases

ProteinModelPortalP25153.
SMRP25153. Positions 2-149.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid65824. 1 interaction.
STRING7227.FBpp0078490.

Proteomic databases

PaxDbP25153.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0078849; FBpp0078490; FBgn0004436.
FBtr0306106; FBpp0297243; FBgn0004436.
GeneID40610.
KEGGdme:Dmel_CG2013.

Organism-specific databases

CTD40610.
FlyBaseFBgn0004436. UbcD6.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00730000110565.
InParanoidP25153.
KOK10573.
OMAPVPDNVM.
OrthoDBEOG7M0NTH.
PhylomeDBP25153.

Enzyme and pathway databases

SignaLinkP25153.
UniPathwayUPA00143.

Gene expression databases

BgeeP25153.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi40610.
NextBio819645.
PROP25153.

Entry information

Entry nameUBCD6_DROME
AccessionPrimary (citable) accession number: P25153
Secondary accession number(s): Q9VN70
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 121 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