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Q9UUK3 (OTU2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 thioesterase otu2

EC=3.4.19.12
Alternative name(s):
OTU domain-containing protein 2
Gene names
Name:otu2
ORF Names:SPAC1952.03
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Protein existencePredicted

General annotation (Comments)

Function

Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Ref.3

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).

Subcellular location

Cytoplasm Ref.2 Ref.3.

Sequence similarities

Contains 1 OTU domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
   Molecular functionHydrolase
Protease
Thiol protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein deubiquitination

Inferred from direct assay Ref.3. Source: PomBase

   Cellular_componentcytoplasm

Inferred from direct assay Ref.3. Source: PomBase

cytosol

Inferred from direct assay Ref.2. Source: PomBase

   Molecular_functionubiquitin-specific protease activity

Inferred from direct assay Ref.3. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 324324Ubiquitin thioesterase otu2
PRO_0000318138

Regions

Domain185 – 322138OTU

Sequences

Sequence LengthMass (Da)Tools
Q9UUK3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 48BBB435960D4B9C

FASTA32437,516
        10         20         30         40         50         60 
MRCPLAYYYT QTTIPTQQKR KSKKMEELLS KQREECKELQ SKITNLRKQL KEGNKKQKRA 

        70         80         90        100        110        120 
LQQKISQMEA DLSQKHATER QKLDKGDEET NETQQEDLLN TLLQQMEDTK ITTAEKSSVQ 

       130        140        150        160        170        180 
SSLNTKENTP QQPKKSRNRQ KERLERRKAE MKKMSEQAEL ESEKMADLKN EEKKKFSKIL 

       190        200        210        220        230        240 
EEAGLVAVDI PADGNCLFAS ISHQLNYHHN VKLNSQALRN KSADYVLKHC EQFEGFLLDE 

       250        260        270        280        290        300 
ESGEVLPVSD YCNEIRNNSK WGSDIEIQAL ANSLEVPVHV YNTEGPVLKF NPSTVKFEKP 

       310        320 
LCIAYYQHLF GLGAHYNSLL YRDN 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[3]"A global census of fission yeast deubiquitinating enzyme localization and interaction networks reveals distinct compartmentalization profiles and overlapping functions in endocytosis and polarity."
Kouranti I., McLean J.R., Feoktistova A., Liang P., Johnson A.E., Roberts-Galbraith R.H., Gould K.L.
PLoS Biol. 8:708-716(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB52567.1.
PIRT37931.
RefSeqNP_594806.1. NM_001020234.2.

3D structure databases

ProteinModelPortalQ9UUK3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid279011. 29 interactions.
MINTMINT-4714941.
STRING4896.SPAC1952.03-1.

Proteomic databases

MaxQBQ9UUK3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC1952.03.1; SPAC1952.03.1:pep; SPAC1952.03.
GeneID2542554.
KEGGspo:SPAC1952.03.

Organism-specific databases

PomBaseSPAC1952.03.

Phylogenomic databases

eggNOGCOG5539.
HOGENOMHOG000192906.
OMAKHVDDFL.
OrthoDBEOG73JM5N.
PhylomeDBQ9UUK3.

Family and domain databases

InterProIPR003323. OTU.
[Graphical view]
PfamPF02338. OTU. 1 hit.
[Graphical view]
PROSITEPS50802. OTU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20803606.
PROQ9UUK3.

Entry information

Entry nameOTU2_SCHPO
AccessionPrimary (citable) accession number: Q9UUK3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names