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Q9UUD6 (UBP11_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 76. 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 11

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 11
Ubiquitin thioesterase 11
Ubiquitin-specific-processing protease 11
Gene names
Name:ubp11
ORF Names:SPBC19C2.04c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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).

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 USP domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 350350Ubiquitin carboxyl-terminal hydrolase 11
PRO_0000080611

Regions

Domain49 – 344296USP

Sites

Active site591Nucleophile By similarity
Active site3021Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9UUD6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 53986D30F9552DA4

FASTA35039,169
        10         20         30         40         50         60 
MSTTPLSISR AKKYKTVFKG AAILTTFAAL YIVTSPSTGK RLVKNASIKG LYNVSGNDCF 

        70         80         90        100        110        120 
LNCVLQSLAS QESLLEILKL RCSSSTLYAT LYELLQKLNS GPGNPITPGS FLNSLEIATN 

       130        140        150        160        170        180 
KKLVRSIQQD AQEFLQHLVE TLELQKPHTY KWSKVLSFPV DSPFIGTMEQ KVQCCQCLAI 

       190        200        210        220        230        240 
SISYSTATSI QLCLPPEYSG NSNVSLLSLM EADREQHISD YKCDSCFKSS PKHSKTSCIR 

       250        260        270        280        290        300 
TVDWKNPPTI LQIQLERTSY TCQGLTRNNV SISFPSKLIL KNKHHYILRS LITHSGSVTY 

       310        320        330        340        350 
GHYLCYRLQD DIWWKANDSL ITKSSLNEAL SQTRSACLLF YEMESPLALD 

« Hide

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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAB52031.1.
PIRT39795.
RefSeqNP_595689.1. NM_001021586.2.

3D structure databases

ProteinModelPortalQ9UUD6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid277237. 23 interactions.
MINTMINT-4712261.
STRING4896.SPBC19C2.04c-1.

Protein family/group databases

MEROPSC19.A63.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC19C2.04c.1; SPBC19C2.04c.1:pep; SPBC19C2.04c.
GeneID2540714.
KEGGspo:SPBC19C2.04c.

Organism-specific databases

PomBaseSPBC19C2.04c.

Phylogenomic databases

eggNOGCOG5077.
OrthoDBEOG7HB5JX.
PhylomeDBQ9UUD6.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20801836.

Entry information

Entry nameUBP11_SCHPO
AccessionPrimary (citable) accession number: Q9UUD6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 76 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

Peptidase families

Classification of peptidase families and list of entries