Q9VX25 (UBE2S_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 S
EC=6.3.2.19

Alternative name(s):
Ubiquitin carrier protein S
Ubiquitin-protein ligase S

Gene names

ORF Names:

CG8188

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	209 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the covalent attachment of ubiquitin to other proteins. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by specifically elongating polyubiquitin chains initiated by the E2 enzyme vih/UbcH10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit. Ref.5
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine. Ref.5
Pathway	Protein modification; protein ubiquitination. Ref.5
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Ubl conjugation pathway
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from mutant phenotype Ref.5. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW exit from mitosis Inferred from mutant phenotype Ref.5. Source: UniProtKB imaginal disc-derived wing morphogenesis Inferred from mutant phenotype PubMed 21635778. Source: FlyBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 209	209	Ubiquitin-conjugating enzyme E2 S		PRO_0000390440
Sites
	Active site	98	1	Glycyl thioester intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9VX25 [UniParc]. Last modified July 5, 2004. Version 2. Checksum: 65A528912E50A477	FASTA	209	23,337
	10 20 30 40 50 60 MSSQYSNVEN LSPQTIRQVM RELQEMETTP PEGIKVLINE SDVTDIQALI DGPAGTPYAA 70 80 90 100 110 120 GIFRVKLTLN KDFPLTPPKA YFLTKIFHPN VAANGEICVN TLKKDWKPDL GIKHILLTIK 130 140 150 160 170 180 CLLIVPNPES ALNEEAGKML LERYDDYSQR ARMMTEIHAQ PAKCGVGAVG DAKDDGGPST 190 200 KKHAGLDKKL QDKKKEKLLK EKKRMLKRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Full length sequences of assorted Drosophila melanogaster cDNAs." Murphy T.D. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [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]	"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]	Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	"Identification of a physiological E2 module for the human anaphase-promoting complex." Williamson A., Wickliffe K.E., Mellone B.G., Song L., Karpen G.H., Rape M. Proc. Natl. Acad. Sci. U.S.A. 106:18213-18218(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ151896 mRNA. Translation: AAZ57341.1. DQ151897 mRNA. Translation: AAZ57342.1. AE014298 Genomic DNA. Translation: ABC67190.1. AE014298 Genomic DNA. Translation: AAF48756.2. BT031269 mRNA. Translation: ABY20510.1.
RefSeq	NP_001033852.1. NM_001038763.1. NP_573237.2. NM_133009.2.
UniGene	Dm.11521.
3D structure databases
HSSP	HSSP built from PDB template 1QCQ based on UniProtKB P15731.
ProteinModelPortal	Q9VX25.
SMR	Q9VX25. Positions 9-159.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VX25. 1 interaction.
MINT	MINT-895042.
STRING	7227.FBpp0099891.
Proteomic databases
PaxDb	Q9VX25.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0074476; FBpp0074250; FBgn0030863. FBtr0100463; FBpp0099891; FBgn0030863.
GeneID	32751.
KEGG	dme:Dmel_CG8188.
UCSC	CG8188-RA. d. melanogaster.
Organism-specific databases
FlyBase	FBgn0030863. CG8188.
Phylogenomic databases
eggNOG	COG5078.
GeneTree	ENSGT00680000099547.
InParanoid	Q9VX25.
KO	K10583.
OMA	PDLGIKH.
OrthoDB	EOG4BNZV4.
PhylomeDB	Q9VX25.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
Bgee	Q9VX25.
Family and domain databases
Gene3D	3.10.110.10. 1 hit.
InterPro	IPR000608. UBQ-conjugat_E2. IPR023313. UBQ-conjugating_AS. IPR016135. UBQ-conjugating_enzyme/RWD. [Graphical view]
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
ChiTaRS	CG8188. drosophila.
GenomeRNAi	32751.
NextBio	780178.

Entry information

Entry name

UBE2S_DROME

Accession

Primary (citable) accession number: Q9VX25

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2009
Last sequence update:	July 5, 2004
Last modified:	April 3, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project