Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q92353 (UBP6_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. 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 6

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 6
Ubiquitin thiollesterase 6
Ubiquitin-specific-processing protease 6
Gene names
Name:ubp6
ORF Names:SPAC6G9.08
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length468 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.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).

Subunit structure

Component of the 26S proteasome. Interacts with rpn1. Ref.3

Subcellular location

Nucleus Ref.3 Ref.4.

Sequence similarities

Belongs to the peptidase C19 family. USP14/UBP6 subfamily.

Contains 1 ubiquitin-like domain.

Contains 1 USP domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 468468Ubiquitin carboxyl-terminal hydrolase 6
PRO_0000080607

Regions

Domain1 – 7171Ubiquitin-like
Domain101 – 465365USP

Sites

Active site1101Nucleophile By similarity
Active site4151Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92353 [UniParc].

Last modified March 21, 2012. Version 2.
Checksum: D54D44B8D76D2F31

FASTA46852,316
        10         20         30         40         50         60 
MMIPIAIRWQ GKKYDLEIEP NETGSTLKHQ LYSLTQVPPE RQKVIVKGGQ LKDDVLLGSV 

        70         80         90        100        110        120 
GIKPNATLLM MGTAGELPTA MPIPAVESVE QEESEDDGYP SGLINLGNTC YMNSTVQMLR 

       130        140        150        160        170        180 
AIPELSDAVS QFNSSGGLVA EYRTLLNSMQ SNAPVTPMRF LQSLRMEYPQ FAEMSRETGG 

       190        200        210        220        230        240 
YAQQDAEECW SFLLSVLQRS LSSEWVQKNM AGKLLSTMKC DENEVQEQPS ISHDTFLSLP 

       250        260        270        280        290        300 
CHISMHTSYM TQGILEGLTQ KISKHSDVLN RDAMYSKISR ISRLPNYLTV NFVRFYWKAS 

       310        320        330        340        350        360 
IGKKAKILRK VKFPFELDAV EFCTPELSQK LIPVRDKLRE IEKNDEEHER AAKRIKIQPS 

       370        380        390        400        410        420 
EDEKEAEAEC RLTQVATCQS LVDPELADDE GANPTGLYDL VGVLSHAGAS ASSGHYQAWI 

       430        440        450        460 
RNSNNRAEWF RFNDAKVSIV PAEKIETLDG GGEADSAYIL LYKAKDIA 

« 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]"Comparative functional genomics of the fission yeasts."
Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K. expand/collapse author list , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVISION OF GENE MODEL.
[3]"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 RPN1, SUBCELLULAR LOCATION.
[4]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB03610.2.
PIRT39070.
RefSeqNP_594117.2. NM_001019541.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278310. 63 interactions.
MINTMINT-4701238.
STRING4896.SPAC6G9.08-1.

Protein family/group databases

MEROPSC19.A60.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC6G9.08.1; SPAC6G9.08.1:pep; SPAC6G9.08.
GeneID2541819.
KEGGspo:SPAC6G9.08.

Organism-specific databases

PomBaseSPAC6G9.08.

Phylogenomic databases

eggNOGNOG286607.
HOGENOMHOG000202292.
KOK11843.
OrthoDBEOG789CMF.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR000626. Ubiquitin-like.
IPR019954. Ubiquitin_CS.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00240. ubiquitin. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTSM00213. UBQ. 1 hit.
[Graphical view]
PROSITEPS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20802907.
PROQ92353.

Entry information

Entry nameUBP6_SCHPO
AccessionPrimary (citable) accession number: Q92353
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 21, 2012
Last modified: April 16, 2014
This is version 111 of the entry and version 2 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