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Protein

Ubiquitin thioesterase otu2

Gene

otu2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.1 Publication

Catalytic activityi

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).

GO - Molecular functioni

  1. ubiquitin-specific protease activity Source: PomBase

GO - Biological processi

  1. protein deubiquitination Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin thioesterase otu2 (EC:3.4.19.12)
Alternative name(s):
OTU domain-containing protein 2
Gene namesi
Name:otu2
ORF Names:SPAC1952.03
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1952.03.
PomBaseiSPAC1952.03.

Subcellular locationi

  1. Cytoplasm 2 Publications

GO - Cellular componenti

  1. cytoplasm Source: PomBase
  2. cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 324324Ubiquitin thioesterase otu2PRO_0000318138Add
BLAST

Proteomic databases

MaxQBiQ9UUK3.

Interactioni

Protein-protein interaction databases

BioGridi279011. 31 interactions.
MINTiMINT-4714941.
STRINGi4896.SPAC1952.03-1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini185 – 322138OTUPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 OTU domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5539.
HOGENOMiHOG000192906.
InParanoidiQ9UUK3.
KOiK18342.
OMAiMRKHVDD.
OrthoDBiEOG73JM5N.
PhylomeDBiQ9UUK3.

Family and domain databases

InterProiIPR003323. OTU.
[Graphical view]
PfamiPF02338. OTU. 1 hit.
[Graphical view]
PROSITEiPS50802. OTU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UUK3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRCPLAYYYT QTTIPTQQKR KSKKMEELLS KQREECKELQ SKITNLRKQL
60 70 80 90 100
KEGNKKQKRA LQQKISQMEA DLSQKHATER QKLDKGDEET NETQQEDLLN
110 120 130 140 150
TLLQQMEDTK ITTAEKSSVQ SSLNTKENTP QQPKKSRNRQ KERLERRKAE
160 170 180 190 200
MKKMSEQAEL ESEKMADLKN EEKKKFSKIL EEAGLVAVDI PADGNCLFAS
210 220 230 240 250
ISHQLNYHHN VKLNSQALRN KSADYVLKHC EQFEGFLLDE ESGEVLPVSD
260 270 280 290 300
YCNEIRNNSK WGSDIEIQAL ANSLEVPVHV YNTEGPVLKF NPSTVKFEKP
310 320
LCIAYYQHLF GLGAHYNSLL YRDN
Length:324
Mass (Da):37,516
Last modified:May 1, 2000 - v1
Checksum:i48BBB435960D4B9C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB52567.1.
PIRiT37931.
RefSeqiNP_594806.1. NM_001020234.2.

Genome annotation databases

EnsemblFungiiSPAC1952.03.1; SPAC1952.03.1:pep; SPAC1952.03.
GeneIDi2542554.
KEGGispo:SPAC1952.03.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB52567.1.
PIRiT37931.
RefSeqiNP_594806.1. NM_001020234.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279011. 31 interactions.
MINTiMINT-4714941.
STRINGi4896.SPAC1952.03-1.

Proteomic databases

MaxQBiQ9UUK3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1952.03.1; SPAC1952.03.1:pep; SPAC1952.03.
GeneIDi2542554.
KEGGispo:SPAC1952.03.

Organism-specific databases

EuPathDBiFungiDB:SPAC1952.03.
PomBaseiSPAC1952.03.

Phylogenomic databases

eggNOGiCOG5539.
HOGENOMiHOG000192906.
InParanoidiQ9UUK3.
KOiK18342.
OMAiMRKHVDD.
OrthoDBiEOG73JM5N.
PhylomeDBiQ9UUK3.

Miscellaneous databases

NextBioi20803606.
PROiQ9UUK3.

Family and domain databases

InterProiIPR003323. OTU.
[Graphical view]
PfamiPF02338. OTU. 1 hit.
[Graphical view]
PROSITEiPS50802. OTU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiOTU2_SCHPO
AccessioniPrimary (citable) accession number: Q9UUK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 1, 2000
Last modified: April 29, 2015
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.