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Protein

Ubiquitin carboxyl-terminal hydrolase 6

Gene

ubp6

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei110 – 1101NucleophilePROSITE-ProRule annotation
Active sitei415 – 4151Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: GO_Central
  2. ubiquitin-specific protease activity Source: PomBase

GO - Biological processi

  1. proteasome-mediated ubiquitin-dependent protein catabolic process Source: GO_Central
  2. protein deubiquitination Source: PomBase
  3. protein deubiquitination involved in ubiquitin-dependent protein catabolic process Source: PomBase
  4. regulation of proteasomal protein catabolic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Protein family/group databases

MEROPSiC19.A60.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ubp6
ORF Names:SPAC6G9.08
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

PomBaseiSPAC6G9.08.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. nucleoplasm Source: PomBase
  2. nucleus Source: PomBase
  3. proteasome complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 468468Ubiquitin carboxyl-terminal hydrolase 6PRO_0000080607Add
BLAST

Proteomic databases

MaxQBiQ92353.

Interactioni

Subunit structurei

Component of the 26S proteasome. Interacts with rpn1.1 Publication

Protein-protein interaction databases

BioGridi278310. 64 interactions.
MINTiMINT-4701238.
STRINGi4896.SPAC6G9.08-1.

Structurei

3D structure databases

ProteinModelPortaliQ92353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7171Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST
Domaini101 – 465365USPAdd
BLAST

Sequence similaritiesi

Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Phylogenomic databases

eggNOGiNOG286607.
HOGENOMiHOG000202292.
InParanoidiQ92353.
KOiK11843.
OMAiDWGNLKI.
OrthoDBiEOG789CMF.

Family and domain databases

InterProiIPR001394. Peptidase_C19_UCH.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS00299. 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]

Sequencei

Sequence statusi: Complete.

Q92353-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMIPIAIRWQ GKKYDLEIEP NETGSTLKHQ LYSLTQVPPE RQKVIVKGGQ
60 70 80 90 100
LKDDVLLGSV GIKPNATLLM MGTAGELPTA MPIPAVESVE QEESEDDGYP
110 120 130 140 150
SGLINLGNTC YMNSTVQMLR AIPELSDAVS QFNSSGGLVA EYRTLLNSMQ
160 170 180 190 200
SNAPVTPMRF LQSLRMEYPQ FAEMSRETGG YAQQDAEECW SFLLSVLQRS
210 220 230 240 250
LSSEWVQKNM AGKLLSTMKC DENEVQEQPS ISHDTFLSLP CHISMHTSYM
260 270 280 290 300
TQGILEGLTQ KISKHSDVLN RDAMYSKISR ISRLPNYLTV NFVRFYWKAS
310 320 330 340 350
IGKKAKILRK VKFPFELDAV EFCTPELSQK LIPVRDKLRE IEKNDEEHER
360 370 380 390 400
AAKRIKIQPS EDEKEAEAEC RLTQVATCQS LVDPELADDE GANPTGLYDL
410 420 430 440 450
VGVLSHAGAS ASSGHYQAWI RNSNNRAEWF RFNDAKVSIV PAEKIETLDG
460
GGEADSAYIL LYKAKDIA
Length:468
Mass (Da):52,316
Last modified:March 21, 2012 - v2
Checksum:iD54D44B8D76D2F31
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB03610.2.
PIRiT39070.
RefSeqiNP_594117.2. NM_001019541.2.

Genome annotation databases

EnsemblFungiiSPAC6G9.08.1; SPAC6G9.08.1:pep; SPAC6G9.08.
GeneIDi2541819.
KEGGispo:SPAC6G9.08.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB03610.2.
PIRiT39070.
RefSeqiNP_594117.2. NM_001019541.2.

3D structure databases

ProteinModelPortaliQ92353.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278310. 64 interactions.
MINTiMINT-4701238.
STRINGi4896.SPAC6G9.08-1.

Protein family/group databases

MEROPSiC19.A60.

Proteomic databases

MaxQBiQ92353.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC6G9.08.1; SPAC6G9.08.1:pep; SPAC6G9.08.
GeneIDi2541819.
KEGGispo:SPAC6G9.08.

Organism-specific databases

PomBaseiSPAC6G9.08.

Phylogenomic databases

eggNOGiNOG286607.
HOGENOMiHOG000202292.
InParanoidiQ92353.
KOiK11843.
OMAiDWGNLKI.
OrthoDBiEOG789CMF.

Miscellaneous databases

NextBioi20802907.
PROiQ92353.

Family and domain databases

InterProiIPR001394. Peptidase_C19_UCH.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS00299. 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]
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(2001) [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.
    , 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(2010) [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(2003) [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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUBP6_SCHPO
AccessioniPrimary (citable) accession number: Q92353
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 21, 2012
Last modified: March 4, 2015
This is version 119 of the entry and version 2 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. Peptidase families
    Classification of peptidase families and list of entries
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.