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P35122 (UCHL_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase

EC=3.4.19.12
Alternative name(s):
Ubiquitin thioesterase
Gene names
Name:Uch
Synonyms:ubc-D
ORF Names:CG4265
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Ubiquitin-protein hydrolase is involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Ref.2

Catalytic activity

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

Developmental stage

Expressed both maternally and zygotically. Ref.2

Sequence similarities

Belongs to the peptidase C12 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 227227Ubiquitin carboxyl-terminal hydrolase
PRO_0000211072

Sites

Active site931Nucleophile By similarity
Active site1641Proton donor By similarity
Site1791Important for enzyme activity By similarity

Experimental info

Sequence conflict221G → A in AAA15411. Ref.2
Sequence conflict221G → A in CAA49358. Ref.2
Sequence conflict221G → A in CAA49359. Ref.2
Sequence conflict651A → T Ref.1
Sequence conflict651A → T Ref.2
Sequence conflict1071E → G Ref.1

Sequences

Sequence LengthMass (Da)Tools
P35122 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: 298A025569C3D409

FASTA22725,850
        10         20         30         40         50         60 
MLTWTPLESN PEVLTKYIHK LGVSPAWSVT DVIGLEDDTL EWIPRPVKAF ILLFPCSETY 

        70         80         90        100        110        120 
EKHRAEEHDR IKEVEEQHPE DLFYMRQFTH NACGTVALIH SVANNKEVDI DRGVLKDFLE 

       130        140        150        160        170        180 
KTASLSPEER GRALEKDEKF TADHEALAQE GQTNAANHEK VIHHFIALVN KEGTLYELDG 

       190        200        210        220 
RKSFPIKHGP TSEETFVKDA AKVCKEFMAR DPNEVRFTVL ALTAAQQ 

« Hide

References

« Hide 'large scale' references
[1]"Comparisons of neuronal (PGP 9.5) and non-neuronal ubiquitin C-terminal hydrolases."
Wilkinson K.D., Deshpande S., Larsen C.N.
Biochem. Soc. Trans. 20:631-637(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning and analysis of expression of a ubiquitin carboxyl terminal hydrolase expressed during oogenesis in Drosophila melanogaster."
Zhang N., Wilkinson K., Bownes M.
Dev. Biol. 157:214-223(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DEVELOPMENTAL STAGE.
Strain: Oregon-R.
[3]"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. expand/collapse author list , 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.
[4]"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. expand/collapse author list , 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.
[5]"A Drosophila complementary DNA resource."
Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M., Harvey D.A.
Science 287:2222-2224(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S60346 Genomic DNA. Translation: AAA15411.1.
X69678 mRNA. Translation: CAA49358.1.
X69679 Genomic DNA. Translation: CAA49359.1.
AE014134 Genomic DNA. Translation: AAF51291.1.
AF145600 mRNA. Translation: AAD38575.1.
PIRS33956.
RefSeqNP_001188681.1. NM_001201752.2.
NP_476940.1. NM_057592.4.
UniGeneDm.4794.

3D structure databases

ProteinModelPortalP35122.
SMRP35122. Positions 4-225.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid59626. 62 interactions.
MINTMINT-1599795.

Protein family/group databases

MEROPSC12.008.

Proteomic databases

PaxDbP35122.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0077844; FBpp0077516; FBgn0010288.
FBtr0303459; FBpp0292511; FBgn0010288.
GeneID33397.
KEGGdme:Dmel_CG4265.

Organism-specific databases

CTD33397.
FlyBaseFBgn0010288. Uch.

Phylogenomic databases

eggNOGNOG327708.
GeneTreeENSGT00510000046640.
InParanoidP35122.
KOK05609.
OMAYVCFVKG.
OrthoDBEOG7S7SFK.
PhylomeDBP35122.

Gene expression databases

BgeeP35122.

Family and domain databases

Gene3D3.40.532.10. 1 hit.
InterProIPR001578. Peptidase_C12_UCH.
[Graphical view]
PANTHERPTHR10589. PTHR10589. 1 hit.
PfamPF01088. Peptidase_C12. 1 hit.
[Graphical view]
PRINTSPR00707. UBCTHYDRLASE.
PROSITEPS00140. UCH_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi33397.
NextBio783351.

Entry information

Entry nameUCHL_DROME
AccessionPrimary (citable) accession number: P35122
Secondary accession number(s): Q4PIX7, Q9TWA0, Q9V417
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: August 30, 2005
Last modified: July 9, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase