Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ubiquitin-conjugating enzyme E2-17 kDa

Gene

UbcD6

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

Functioni

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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei88 – 881Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ligase activity Source: UniProtKB-KW
  3. p53 binding Source: BHF-UCL
  4. protein domain specific binding Source: BHF-UCL
  5. small conjugating protein transferase activity Source: GO_Central
  6. ubiquitin conjugating enzyme activity Source: BHF-UCL
  7. ubiquitin protein ligase activity Source: GO_Central
  8. ubiquitin protein ligase binding Source: GO_Central
  9. ubiquitin-protein transferase activity Source: FlyBase

GO - Biological processi

  1. centrosome organization Source: FlyBase
  2. centrosome separation Source: FlyBase
  3. DNA repair Source: FlyBase
  4. endocytic recycling Source: FlyBase
  5. histone ubiquitination Source: GO_Central
  6. mitochondrion degradation Source: FlyBase
  7. mitotic spindle organization Source: FlyBase
  8. negative regulation of apoptotic process Source: FlyBase
  9. negative regulation of DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
  10. negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: BHF-UCL
  11. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
  12. proteasome-mediated ubiquitin-dependent protein catabolic process Source: FlyBase
  13. protein polyubiquitination Source: GO_Central
  14. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_180708. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiP25153.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2-17 kDa (EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein
Ubiquitin-protein ligase
Gene namesi
Name:UbcD6
Synonyms:Dhr6
ORF Names:CG2013
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0004436. UbcD6.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. HULC complex Source: GO_Central
  3. nuclear chromatin Source: GO_Central
  4. nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 151151Ubiquitin-conjugating enzyme E2-17 kDaPRO_0000082523Add
BLAST

Proteomic databases

PaxDbiP25153.

Expressioni

Gene expression databases

BgeeiP25153.

Interactioni

Protein-protein interaction databases

BioGridi65824. 1 interaction.
STRINGi7227.FBpp0078490.

Structurei

3D structure databases

ProteinModelPortaliP25153.
SMRiP25153. Positions 2-149.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110565.
InParanoidiP25153.
KOiK10573.
OMAiPVPDNVM.
OrthoDBiEOG7M0NTH.
PhylomeDBiP25153.

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.

P25153-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTPARRRLM RDFKRLQEDP PTGVSGAPTD NNIMIWNAVI FGPHDTPFED
60 70 80 90 100
GTFKLTIEFT EEYPNKPPTV RFVSKVFHPN VYADGGICLD ILQNRWSPTY
110 120 130 140 150
DVSAILTSIQ SLLSDPNPNS PANSTAAQLY KENRREYEKR VKACVEQSFI

D
Length:151
Mass (Da):17,152
Last modified:June 1, 2001 - v2
Checksum:iCC4B35992E4A9220
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti99 – 991T → R in AAA28308 (PubMed:1902572).Curated
Sequence conflicti99 – 991T → R in AAA28309 (PubMed:1902572).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63792 mRNA. Translation: AAA28308.1.
M64435, M63791 Genomic DNA. Translation: AAA28309.1.
AE014297 Genomic DNA. Translation: AAF52079.1.
BT003481 mRNA. Translation: AAO39484.1.
PIRiA39392.
RefSeqiNP_001246916.1. NM_001259987.3.
NP_524230.2. NM_079506.4.
UniGeneiDm.2229.

Genome annotation databases

EnsemblMetazoaiFBtr0078849; FBpp0078490; FBgn0004436.
FBtr0306106; FBpp0297243; FBgn0004436.
GeneIDi40610.
KEGGidme:Dmel_CG2013.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63792 mRNA. Translation: AAA28308.1.
M64435, M63791 Genomic DNA. Translation: AAA28309.1.
AE014297 Genomic DNA. Translation: AAF52079.1.
BT003481 mRNA. Translation: AAO39484.1.
PIRiA39392.
RefSeqiNP_001246916.1. NM_001259987.3.
NP_524230.2. NM_079506.4.
UniGeneiDm.2229.

3D structure databases

ProteinModelPortaliP25153.
SMRiP25153. Positions 2-149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65824. 1 interaction.
STRINGi7227.FBpp0078490.

Proteomic databases

PaxDbiP25153.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078849; FBpp0078490; FBgn0004436.
FBtr0306106; FBpp0297243; FBgn0004436.
GeneIDi40610.
KEGGidme:Dmel_CG2013.

Organism-specific databases

CTDi40610.
FlyBaseiFBgn0004436. UbcD6.

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110565.
InParanoidiP25153.
KOiK10573.
OMAiPVPDNVM.
OrthoDBiEOG7M0NTH.
PhylomeDBiP25153.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_180708. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiP25153.

Miscellaneous databases

GenomeRNAii40610.
NextBioi819645.
PROiP25153.

Gene expression databases

BgeeiP25153.

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. 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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry nameiUBCD6_DROME
AccessioniPrimary (citable) accession number: P25153
Secondary accession number(s): Q9VN70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: June 1, 2001
Last modified: March 4, 2015
This is version 128 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.