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Protein

Ubiquitin-conjugating enzyme E2-24 kDa

Gene

UbcD2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the covalent attachment of ubiquitin to other proteins.

Catalytic activityi

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

Pathway: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.PROSITE-ProRule annotation
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei170 – 1701Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ligase activity Source: UniProtKB-KW
  • ubiquitin-protein transferase activity Source: FlyBase

GO - Biological processi

  • lipid storage Source: FlyBase
  • protein polyubiquitination Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_273460. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_274899. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_285954. APC/C:Cdc20 mediated degradation of Securin.
REACT_286636. Regulation of APC/C activators between G1/S and early anaphase.
REACT_295143. APC-Cdc20 mediated degradation of Nek2A.
REACT_320700. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_321324. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_331011. Phosphorylation of the APC/C.
REACT_335593. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_340086. Senescence-Associated Secretory Phenotype (SASP).
REACT_346613. Separation of Sister Chromatids.
REACT_352760. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
SignaLinkiP52485.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2-24 kDa (EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein
Ubiquitin-protein ligase
Gene namesi
Name:UbcD2
ORF Names:CG6720
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0015320. UbcD2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 232232Ubiquitin-conjugating enzyme E2-24 kDaPRO_0000082520Add
BLAST

Proteomic databases

PaxDbiP52485.
PRIDEiP52485.

Expressioni

Gene expression databases

BgeeiP52485.
ExpressionAtlasiP52485. differential.
GenevisibleiP52485. DM.

Interactioni

Protein-protein interaction databases

BioGridi60561. 16 interactions.
DIPiDIP-17329N.
IntActiP52485. 5 interactions.
MINTiMINT-334725.
STRINGi7227.FBpp0305676.

Structurei

3D structure databases

ProteinModelPortaliP52485.
SMRiP52485. Positions 86-232.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5078.
InParanoidiP52485.
KOiK06689.
OMAiEPRKDTK.
OrthoDBiEOG7PCJGX.
PhylomeDBiP52485.

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.

P52485-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSTPAAGSA AEVATSSATS NAPSAPSTTA SNVSNTSQPT TAGTPQARGG
60 70 80 90 100
RGSNANGGAS GSNAGGGDEP RKEAKTTPRI SRALGTSAKR IQKELAEITL
110 120 130 140 150
DPPPNCSAGP KGDNLYEWVS TILGPPGSVY EGGVFFLDIH FSPEYPFKPP
160 170 180 190 200
KVTFRTRIYH CNINSQGVIC LDILKDNWSP ALTISKVLLS ICSLLTDCNP
210 220 230
ADPLVGSIAT QYLQNREEHD RIARLWTKRY AT
Length:232
Mass (Da):24,435
Last modified:October 1, 1996 - v1
Checksum:iDE71AFD8EB618C86
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92663 mRNA. Translation: CAA63351.1.
AE014134 Genomic DNA. Translation: AAF53008.1.
RefSeqiNP_001260362.1. NM_001273433.1.
NP_001285814.1. NM_001298885.1.
NP_477137.1. NM_057789.4.
NP_723616.1. NM_164943.2.
UniGeneiDm.6395.

Genome annotation databases

EnsemblMetazoaiFBtr0080115; FBpp0079704; FBgn0015320.
FBtr0080116; FBpp0079705; FBgn0015320.
FBtr0333492; FBpp0305676; FBgn0015320.
FBtr0345437; FBpp0311562; FBgn0015320.
GeneIDi34487.
KEGGidme:Dmel_CG6720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92663 mRNA. Translation: CAA63351.1.
AE014134 Genomic DNA. Translation: AAF53008.1.
RefSeqiNP_001260362.1. NM_001273433.1.
NP_001285814.1. NM_001298885.1.
NP_477137.1. NM_057789.4.
NP_723616.1. NM_164943.2.
UniGeneiDm.6395.

3D structure databases

ProteinModelPortaliP52485.
SMRiP52485. Positions 86-232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60561. 16 interactions.
DIPiDIP-17329N.
IntActiP52485. 5 interactions.
MINTiMINT-334725.
STRINGi7227.FBpp0305676.

Proteomic databases

PaxDbiP52485.
PRIDEiP52485.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0080115; FBpp0079704; FBgn0015320.
FBtr0080116; FBpp0079705; FBgn0015320.
FBtr0333492; FBpp0305676; FBgn0015320.
FBtr0345437; FBpp0311562; FBgn0015320.
GeneIDi34487.
KEGGidme:Dmel_CG6720.

Organism-specific databases

CTDi34487.
FlyBaseiFBgn0015320. UbcD2.

Phylogenomic databases

eggNOGiCOG5078.
InParanoidiP52485.
KOiK06689.
OMAiEPRKDTK.
OrthoDBiEOG7PCJGX.
PhylomeDBiP52485.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_273460. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_274899. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_285954. APC/C:Cdc20 mediated degradation of Securin.
REACT_286636. Regulation of APC/C activators between G1/S and early anaphase.
REACT_295143. APC-Cdc20 mediated degradation of Nek2A.
REACT_320700. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_321324. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_331011. Phosphorylation of the APC/C.
REACT_335593. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_340086. Senescence-Associated Secretory Phenotype (SASP).
REACT_346613. Separation of Sister Chromatids.
REACT_352760. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
SignaLinkiP52485.

Miscellaneous databases

ChiTaRSiUbcD2. fly.
GenomeRNAii34487.
NextBioi788724.
PROiP52485.

Gene expression databases

BgeeiP52485.
ExpressionAtlasiP52485. differential.
GenevisibleiP52485. DM.

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. "Identification of a novel family of ubiquitin-conjugating enzymes with distinct amino-terminal extensions."
    Matuschewski K., Hauser H.P., Treier M., Jentsch S.
    J. Biol. Chem. 271:2789-2794(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: DP CN BW.
  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.

Entry informationi

Entry nameiUBCD2_DROME
AccessioniPrimary (citable) accession number: P52485
Secondary accession number(s): Q9VKQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 120 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.