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Q9USM5 (UBP1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. 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:
Probable ubiquitin carboxyl-terminal hydrolase 1

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 1
Ubiquitin thioesterase 1
Ubiquitin-specific-processing protease 1
Gene names
Name:ubp1
ORF Names:SPCC16A11.12c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length849 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 DUSP domain.

Contains 1 USP domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 849849Probable ubiquitin carboxyl-terminal hydrolase 1
PRO_0000080602

Regions

Domain20 – 120101DUSP
Domain279 – 848570USP

Sites

Active site2881Nucleophile By similarity
Active site8061Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9USM5 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: C8118042229BA9CB

FASTA84998,656
        10         20         30         40         50         60 
MASTATQNAS TRYSQIWIDQ PASLPFQDSI NLIKEDKEKW KKEKTAFLID YDWFEGYVDF 

        70         80         90        100        110        120 
IYGEGDNPGP ITQWRLLDEK NELKHSLEES IDYSIVSASL WHMLVEWFGL EGLAIERKVL 

       130        140        150        160        170        180 
LVGLAAEQKP FVDIYPINFT LHVLFDPING ENTSYSPLYQ IDEPYHSDEP YAFSFSRSDT 

       190        200        210        220        230        240 
LRSLYKQVME AFQISDGTSF RLWYLNKSNL SSRFVSLSEF NDQPAIALLS EYAVCMTIFE 

       250        260        270        280        290        300 
IDIADGSLLL EFQHPNGEWL SDSITKEQNL TINKEIGLCG LYNLGNSCYM NSALQCMIHT 

       310        320        330        340        350        360 
HELTKYFLSD SYEKDINYNN PLGMMGKVAL SYASLLKMIH HTADMHSVSP SSFKFIIGEF 

       370        380        390        400        410        420 
NTYFSGYRQQ DSQEFIAFFL DGLHEDLNRI QIKPYFERPD LFDEHPLHVQ RVANQCWDIH 

       430        440        450        460        470        480 
TKRNDSIIVQ LFQGMYKSTL ECSICYQKST AFDPFMYLTL PLPTSAKWRH KVVYVPPFGT 

       490        500        510        520        530        540 
QSPVELYLEL LMESTVIQMK FQATEKLQKM GLECGELTAC DIYRGKVYKV LKNKDKISKK 

       550        560        570        580        590        600 
IHKWDHVVLY GSTANGLTIP IVHGCKRPAM PGSYQSNDVF GFPLQLNVRS RNVLTNDLVK 

       610        620        630        640        650        660 
EIVELYRVYA GIDVAIGTLQ LGLKRMESKA GKWECIKEIE VKRFEIVEEE EIVIDDKTVI 

       670        680        690        700        710        720 
MCLWNDQQYE KLFYNCEWIF EKIQFHMESI TLEDCLLEFS KPEQLDLQDS WYCPGCKAFR 

       730        740        750        760        770        780 
PATKRLEIWR LPKILVIHLN RFSGHGGDLR RRRKRRDLVV YPVFDLNLKQ FLSPFIKDHE 

       790        800        810        820        830        840 
WLSSQKSMLY DLYAVDNHHG FMSNGHYTAY ARDASSQTFF KFDDTAICEI DPEDIVTSSA 


YVLFYRAKN 

« 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
CU329672 Genomic DNA. Translation: CAB53084.1.
PIRT41085.
RefSeqNP_587999.1. NM_001022990.2.

3D structure databases

ProteinModelPortalQ9USM5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4896.SPCC16A11.12c-1.

Protein family/group databases

MEROPSC19.A55.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC16A11.12c.1; SPCC16A11.12c.1:pep; SPCC16A11.12c.
GeneID2539228.
KEGGspo:SPCC16A11.12c.

Organism-specific databases

PomBaseSPCC16A11.12c.

Phylogenomic databases

eggNOGCOG5560.
KOK11870.
OMAMESITLE.
OrthoDBEOG7R2BSX.
PhylomeDBQ9USM5.

Family and domain databases

Gene3D3.30.2230.10. 1 hit.
InterProIPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF06337. DUSP. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTSM00695. DUSP. 1 hit.
[Graphical view]
SUPFAMSSF143791. SSF143791. 1 hit.
PROSITEPS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20800398.

Entry information

Entry nameUBP1_SCHPO
AccessionPrimary (citable) accession number: Q9USM5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 87 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