P52486 (UBCD4_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	199 AA.
Sequence status	Complete.
Protein existence	Evidence 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 Pros54. Ref.1
Tissue specificity	During gastrulation, expression is highest in the invaginating posterior midgut primordium (PMG), high expression is also 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 process	Ubl conjugation pathway
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Pros54	P55035	2	EBI-224571,EBI-146479

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 199	199	Ubiquitin-conjugating enzyme E2-22 kDa		PRO_0000082522
Regions
	Domain	161 – 199	39	UBA
Sites
	Active site	92	1	Glycyl thioester intermediate By similarity
Experimental info
	Sequence conflict	34 – 36	3	DSW → GQL in CAA63424. Ref.1
	Sequence conflict	73	1	V → A in CAA63424. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P52486 [UniParc]. Last modified November 9, 2004. Version 2. Checksum: 2875F9478632C630	FASTA	199	22,510
	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

References

	« Hide 'large scale' referencesShow '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, FUNCTION, INTERACTION WITH PROS54, 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. , 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. , 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.
PIR	T08465.
RefSeq	NP_524010.2. NM_079286.3.
UniGene	Dm.7820.
3D structure databases
ProteinModelPortal	P52486.
SMR	P52486. Positions 1-199.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-20847N.
IntAct	P52486. 3 interactions.
MINT	MINT-337672.
Proteomic databases
PaxDb	P52486.
PRIDE	P52486.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0076395; FBpp0076124; FBgn0015321.
GeneID	39133.
KEGG	dme:Dmel_CG8284.
Organism-specific databases
CTD	39133.
FlyBase	FBgn0015321. UbcD4.
Phylogenomic databases
eggNOG	COG5078.
GeneTree	ENSGT00670000098059.
InParanoid	P52486.
KO	K04649.
OMA	MAVSRIK.
OrthoDB	EOG4F1VK8.
PhylomeDB	P52486.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
Bgee	P52486.
GermOnline	CG8284. Drosophila melanogaster.
Family and domain databases
Gene3D	3.10.110.10. 1 hit.
InterPro	IPR009060. UBA-like. IPR000449. UBA/transl_elong_EF1B_N. IPR015940. UBA/transl_elong_EF1B_N_euk. IPR000608. UBQ-conjugat_E2. IPR023313. UBQ-conjugating_AS. IPR016135. UBQ-conjugating_enzyme/RWD. [Graphical view]
Pfam	PF00627. UBA. 1 hit. PF00179. UQ_con. 1 hit. [Graphical view]
SMART	SM00165. UBA. 1 hit. [Graphical view]
SUPFAM	SSF46934. UBA_like. 1 hit. SSF54495. UBQ-conjugat/RWD-like. 1 hit.
PROSITE	PS50030. UBA. 1 hit. PS00183. UBIQUITIN_CONJUGAT_1. 1 hit. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	39133.
NextBio	812082.

Entry information

Entry name

UBCD4_DROME

Accession

Primary (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 3, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project