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Q9UUB6 (UBLH2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 2
EC=3.4.19.12
Gene names
Name:uch2
ORF Names:SPBC409.06
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›

Protein attributes

Sequence length300 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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).

Subunit structure

Component of the 26S proteasome. Interacts with rpn10. Ref.2

Subcellular location

Nucleus Ref.2 Ref.3.

Sequence similarities

Belongs to the peptidase C12 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 300300Ubiquitin carboxyl-terminal hydrolase 2
PRO_0000234561

Sites

Active site831Nucleophile By similarity
Active site1591Proton donor By similarity
Site1741Important for enzyme activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9UUB6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 93B13076EF2EDB80

FASTA30034,196
        10         20         30         40         50         60 
MSWTTIESDA GVFTDLIENL GVKDVEVDEL YSLDVDSLRQ FPDIYGIIFL FKWNSKVDKP 

        70         80         90        100        110        120 
DGTMDYDSMD NIFFAKQVIN NACATQALLS VLLNHSDEID LGTTLSEFKD FSKTLPPELK 

       130        140        150        160        170        180 
GEALGNSEHI RCCHNSFARS DPFISEEVRA ATDEDEVYHF IAYTNINNVF YELDGLQAAP 

       190        200        210        220        230        240 
INHGSCTKEE FAEKAVSVIQ ARIANYDPAE IRFNLMVICK DKKASLLTRE DLTDEEKAAS 

       250        260        270        280        290        300 
IAVEDEKRLR WKRENQLRRH NFVGLFVELS KLLVKDRIDK NTWNSTLETA KAKYASQKRP

« 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]"Uch2/Uch37 is the major deubiquitinating enzyme associated with the 26S proteasome in fission yeast."
Stone M., Hartmann-Petersen R., Seeger M., Bech-Otschir D., Wallace M., Gordon C.
J. Mol. Biol. 344:697-706(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RPN10, SUBCELLULAR LOCATION.
[3]"Identification of a 26S proteasome-associated UCH in fission yeast."
Li T., Naqvi N.I., Yang H., Teo T.S.
Biochem. Biophys. Res. Commun. 272:270-275(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329671 Genomic DNA. Translation: CAB52608.1.
PIRT40434.
RefSeqNP_595456.1. NM_001021366.2.

3D structure databases

ProteinModelPortalQ9UUB6.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9UUB6. 1 interaction.
STRING4896.SPBC409.06-1.

Protein family/group databases

MEROPSC12.009.

Proteomic databases

PaxDbQ9UUB6.
PRIDEQ9UUB6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC409.06.1; SPBC409.06.1:pep; SPBC409.06.
GeneID2540956.
KEGGspo:SPBC409.06.

Organism-specific databases

PomBaseSPBC409.06.

Phylogenomic databases

eggNOGNOG321645.
HOGENOMHOG000203918.
KOK05610.
OMADESEMET.
OrthoDBEOG4VT96P.

Family and domain databases

Gene3D3.40.532.10. 1 hit.
InterProIPR001578. Peptidase_C12.
IPR017390. Ubiquitinyl_hydrolase_UCH37.
[Graphical view]
PANTHERPTHR10589. PTHR10589. 1 hit.
PfamPF01088. Peptidase_C12. 1 hit.
[Graphical view]
PIRSFPIRSF038120. Ubiquitinyl_hydrolase_UCH37. 1 hit.
PRINTSPR00707. UBCTHYDRLASE.
PROSITEPS00140. UCH_1. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio20802071.

Entry information

Entry nameUBLH2_SCHPO
AccessionPrimary (citable) accession number: Q9UUB6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 1, 2000
Last modified: May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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