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Q9P3U0 (UBP2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. 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 2

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 2
Ubiquitin thioesterase 2
Ubiquitin-specific-processing protease 2
Gene names
Name:ubp2
ORF Names:SPAC328.06
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length1141 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 – 11411141Probable ubiquitin carboxyl-terminal hydrolase 2
PRO_0000080603

Regions

Domain614 – 1124511USP

Sites

Active site6231Nucleophile By similarity
Active site10761Proton acceptor By similarity

Amino acid modifications

Modified residue1121Phosphothreonine Ref.2
Modified residue1131Phosphoserine Ref.2
Modified residue1151Phosphothreonine Ref.2
Modified residue7211Phosphothreonine Ref.2
Modified residue7221Phosphoserine Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9P3U0 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 1499E32DB6CB26CB

FASTA1,141130,297
        10         20         30         40         50         60 
MATVKNLRIG KSPNRLIQDL DVFDSPSAGW NDPWSPHSSR YHWQLHSNLG ESAVFDENDF 

        70         80         90        100        110        120 
WCVCQKTRKH LHVKVRRDRG KPLIEEPEEN YGIKDRIPVY YEEEELPEPH VTSPTKSEFA 

       130        140        150        160        170        180 
TTSTCMKWSS KTTKSEIEVE WRDSYLDANC IKEIIDSRRP SFASLLTKKS SSHQGSSHSS 

       190        200        210        220        230        240 
QPSLFTTFTS LELFLRNVLV HNDQRAISAA PEGTFERHVG KGRQIQSLMK SLLFEYHHEN 

       250        260        270        280        290        300 
VNYVPTIADA PLTDEQKLNL YLARNELIVL ANHFRDTKED PAIVANPFPV RLARPALINA 

       310        320        330        340        350        360 
FGVPNYDSVV PMYTTVFRDN SASLPDDPAF IALGITNDYP DSFVRYFYEE QKKNDEANVR 

       370        380        390        400        410        420 
VYADALAHIY NLRKSSFLRD LIAADRKNGI VSSDVIQAAY SSLGLEAEVG PDYRYSQEKI 

       430        440        450        460        470        480 
FEAFHSALLR KPEFARAIRN DLETIGYARK SSEILNYVLS TEQAFYTVNE AYQWLGIKSN 

       490        500        510        520        530        540 
TEDAMVASVA LVKFEDDSDK AIEAVKWIAE ERNSSILYDF LASQGRPSNK KPKEVPMDED 

       550        560        570        580        590        600 
LAYNTLGVQD RALSDDVLIN VYGFAVEDHP EQSDTLRAAL KCIGEVRNSR LITHYLEHGN 

       610        620        630        640        650        660 
LDIPPEVSSL DTPIGLENTG NLCYLNSLIQ YYFIIKPLRN AILDIDENKD LNMIENKEAV 

       670        680        690        700        710        720 
KKVGGRIVTR IEFLRALQFT YELRKLFIEL ITSKSSSVHP SSVLTYLALI PLTLDQVKSG 

       730        740        750        760        770        780 
TSSVMDLSSS RELSNLNERS ITIDPRAEEQ AQGLEQEQGQ DEAKSPAEQS SSVNLIDFPM 

       790        800        810        820        830        840 
ANTNGESQTQ PHYFEVSEEE INSSMDLGRQ QDVLECIDHV LFQLEASLGR ISNSEDRLGS 

       850        860        870        880        890        900 
DNDLIRRLFS GKLKQTLNDA SQGVRSNYEI FSHLIVDLFE EKQTLYDALD GVFETVNIDM 

       910        920        930        940        950        960 
GSETAQRSLC ITELPIILQL QIQRVQFDRT TGQPFKSNAF VEFGKELSMD RYVEDTDGKM 

       970        980        990       1000       1010       1020 
APLLQRYWDL KREIINLQKR QQLLLTTNSN LMSSVDTLSI LSKWAAQQQD SRLPINPKLP 

      1030       1040       1050       1060       1070       1080 
DILQEEINNV VAEVDMLKKQ EASLKEERTH LFDNYISHSY DLLAVFVHRG QASFGHYWTY 

      1090       1100       1110       1120       1130       1140 
IHDFENNVYR KYNDEYVTVV DESEIFADTT GNNANPYMLT YIRKEYRHII ECVHREHNLL 


L 

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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]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-112; SER-113; THR-115; THR-721 AND SER-722, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB96001.1.
RefSeqNP_594208.1. NM_001019631.2.

3D structure databases

ProteinModelPortalQ9P3U0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278537. 142 interactions.
MINTMINT-4703705.
STRING4896.SPAC328.06-1.

Protein family/group databases

MEROPSC19.A56.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC328.06.1; SPAC328.06.1:pep; SPAC328.06.
GeneID2542059.
KEGGspo:SPAC328.06.

Organism-specific databases

PomBaseSPAC328.06.

Phylogenomic databases

eggNOGNOG275561.
KOK11849.
OMAPESHETK.
OrthoDBEOG7327X3.
PhylomeDBQ9P3U0.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR025305. UCH_repeat_domain.
[Graphical view]
PfamPF13446. RPT. 3 hits.
PF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20803133.

Entry information

Entry nameUBP2_SCHPO
AccessionPrimary (citable) accession number: Q9P3U0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 83 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