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Q92353

- UBP6_SCHPO

UniProt

Q92353 - UBP6_SCHPO

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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: 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. ubiquitin-specific protease activity Source: PomBase
  2. ubiquitin thiolesterase activity Source: PomBase

GO - Biological processi

  1. proteasome-mediated ubiquitin-dependent protein catabolic process Source: PomBase
  2. protein deubiquitination Source: PomBase
  3. protein deubiquitination involved in ubiquitin-dependent protein catabolic process Source: PomBase
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: 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: PomBase
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.
OrthoDBiEOG789CMF.

Family and domain databases

InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR028889. UCH/PAN2.
[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 [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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CU329670 Genomic DNA. Translation: CAB03610.2 .
PIRi T39070.
RefSeqi NP_594117.2. NM_001019541.2.

3D structure databases

ProteinModelPortali Q92353.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 278310. 64 interactions.
MINTi MINT-4701238.
STRINGi 4896.SPAC6G9.08-1.

Protein family/group databases

MEROPSi C19.A60.

Proteomic databases

MaxQBi Q92353.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPAC6G9.08.1 ; SPAC6G9.08.1:pep ; SPAC6G9.08 .
GeneIDi 2541819.
KEGGi spo:SPAC6G9.08.

Organism-specific databases

PomBasei SPAC6G9.08.

Phylogenomic databases

eggNOGi NOG286607.
HOGENOMi HOG000202292.
InParanoidi Q92353.
KOi K11843.
OrthoDBi EOG789CMF.

Miscellaneous databases

NextBioi 20802907.
PROi Q92353.

Family and domain databases

InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR028889. UCH/PAN2.
[Graphical view ]
Pfami PF00240. ubiquitin. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view ]
SMARTi SM00213. UBQ. 1 hit.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
PROSITEi PS00299. 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 ]
ProtoNeti Search...

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(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.
    , 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].

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: October 29, 2014
This is version 116 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