P25867 (UBCD1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2-17 kDa
EC=6.3.2.19

Alternative name(s):
Protein effete
Ubiquitin carrier protein
Ubiquitin-protein ligase

Gene names

Name:	eff
Synonyms:	UbcD1
ORF Names:	CG7425

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the covalent attachment of ubiquitin to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. Required for proper telomere behavior during cell divisions and possibly for ubiquitination of proteins involved in postmeiotic stages of spermatogenesis. Deletion mutations are lethal in homozygotes. Ref.5
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Meiosis Ubl conjugation pathway
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	chromosome organization Inferred from mutant phenotype Ref.5. Source: FlyBase compound eye photoreceptor cell differentiation Inferred from mutant phenotype. Source: FlyBase cyclin catabolic process Inferred from mutant phenotype. Source: FlyBase female germ-line stem cell division Inferred from mutant phenotype. Source: FlyBase germ-line stem cell maintenance Inferred from mutant phenotype. Source: FlyBase male meiosis Inferred from mutant phenotype Ref.5. Source: FlyBase mitosis Inferred from mutant phenotype Ref.5. Source: FlyBase neuron remodeling Inferred from direct assay. Source: FlyBase regulation of R7 cell differentiation Inferred from genetic interaction. Source: FlyBase regulation of protein stability Inferred from mutant phenotype. Source: FlyBase spermatid development Inferred from mutant phenotype. Source: FlyBase
Cellular component	microtubule associated complex Inferred from direct assay. Source: FlyBase
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: UniProtKB ubiquitin-protein ligase activity Inferred from genetic interaction Ref.1. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 147	147	Ubiquitin-conjugating enzyme E2-17 kDa		PRO_0000082519
Sites
	Active site	85	1	Glycyl thioester intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P25867 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 82E0CE24F925E2EE	FASTA	147	16,678
	10 20 30 40 50 60 MALKRINKEL QDLGRDPPAQ CSAGPVGDDL FHWQATIMGP PDSPYQGGVF FLTIHFPTDY 70 80 90 100 110 120 PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV 130 140 PEIARIYKTD REKYNELARE WTRKYAM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Drosophila UbcD1 encodes a highly conserved ubiquitin-conjugating enzyme involved in selective protein degradation." Treier M., Seufert W., Jentsch S. EMBO J. 11:367-372(1992) [PubMed: 1310935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Oregon-P2.
[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: 10731132] [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. , 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: 12537572] [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: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
[5]	"UbcD1, a Drosophila ubiquitin-conjugating enzyme required for proper telomere behavior." Cenci G., Rawson R.B., Belloni G., Castrillon D.H., Tudor M., Petrucci R., Goldberg M.L., Wasserman S.A., Gatti M. Genes Dev. 11:863-875(1997) [PubMed: 9106658] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-11, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X62575 mRNA. Translation: CAA44453.1. AE014297 Genomic DNA. Translation: AAF55093.1. AY060304 mRNA. Translation: AAL25343.1. U68298 mRNA. Translation: AAB39622.1.
PIR	S19157.
RefSeq	NP_731941.1. NM_169601.1.
UniGene	Dm.4048.
3D structure databases
ProteinModelPortal	P25867.
SMR	P25867. Positions 1-147.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-18953N.
IntAct	P25867. 6 interactions.
MINT	MINT-1014718.
STRING	P25867.
Proteomic databases
PRIDE	P25867.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0083018; FBpp0082477; FBgn0011217.
GeneID	41785.
KEGG	dme:Dmel_CG7425.
Organism-specific databases
CTD	41785.
FlyBase	FBgn0011217. eff.
Phylogenomic databases
eggNOG	inNOG05738.
GeneTree	EMGT00050000007017.
InParanoid	P25867.
OMA	KVNFTTR.
OrthoDB	EOG4TX985.
PhylomeDB	P25867.
Gene expression databases
Bgee	P25867.
GermOnline	CG7425. Drosophila melanogaster.
Family and domain databases
InterPro	IPR000608. UBQ-conjugat_E2. IPR023313. UBQ-conjugating_AS. IPR016135. UBQ-conjugating_enzyme/RWD. [Graphical view]
Gene3D	G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.
KO	K06689.
Pfam	PF00179. UQ_con. 1 hit. [Graphical view]
SUPFAM	SSF54495. UBQ-conjugat/RWD-like. 1 hit.
PROSITE	PS00183. UBIQUITIN_CONJUGAT_1. 1 hit. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	825564.

Entry information

Entry name

UBCD1_DROME

Accession

Primary (citable) accession number: P25867
Secondary accession number(s): Q9VFG6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	January 25, 2012
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project