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O60079 (UBP12_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. 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 12

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 12
Ubiquitin thioesterase 12
Ubiquitin-specific-processing protease 12
Gene names
Name:ubp12
ORF Names:SPCC1494.05c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length979 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 DUSP domain.

Contains 1 USP domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 979979Probable ubiquitin carboxyl-terminal hydrolase 12
PRO_0000080612

Regions

Domain51 – 152102DUSP
Domain311 – 977667USP

Sites

Active site3201Nucleophile By similarity
Active site9351Proton acceptor By similarity

Amino acid modifications

Modified residue191Phosphoserine Ref.2
Modified residue371Phosphoserine Ref.2
Modified residue391Phosphoserine Ref.2

Sequences

Sequence LengthMass (Da)Tools
O60079 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: A705444BCDB437D2

FASTA979111,967
        10         20         30         40         50         60 
MDSLSESSTS SYHGKRPRSL SEESQSSSNM DDISQKSISL GDASEISKNL PSIAEQKQLI 

        70         80         90        100        110        120 
GELVNNQPEL ELGQVDNYIL SYSWYERLCS YLAEDGPFPG PVDQEDIADL ETGTLKPDLQ 

       130        140        150        160        170        180 
EEIDFTIISR DVWDLLVRWY GLKGPEFPRE TVNLGSESHP HLVVEVYPPI FSLTLLSTNA 

       190        200        210        220        230        240 
VDANESHKPK KISLSSKSTL EDLLEGVKYT LSLPSDQFRL WRVDTDQPLH RTIDPSSFIK 

       250        260        270        280        290        300 
INSKEIIDFL EKSKTLVELG MDSSCSLVAE CMINETWPVD RALRLQFLIQ QRNNQSSNEE 

       310        320        330        340        350        360 
QKQEKRVPGT CGLSNLGNTC YMNSALQCLT HTRELRDFFT SDEWKNQVNE SNPLGMGGQV 

       370        380        390        400        410        420 
ASIFASLIKS LYSPEHSSFA PRQFKATIGK FNHSFLGYGQ QDSQEFLAFL LDGLHEDLNR 

       430        440        450        460        470        480 
IYQKPYTSKP DLYEVDEEKI KNTAEECWRL HKLRNDSLIV DLFQGMYRST LVCPVCNTVS 

       490        500        510        520        530        540 
ITFDPFMDLT LPLPVKQVWS HTVTFIPADT NLTPLAIEVV LESKAATIED LVKYVAEKSG 

       550        560        570        580        590        600 
CSDYRKILVT ETYKGRFYRF LTQLSKSLLM EISEEDEIYL YELERPYEDG SDDILVPVYH 

       610        620        630        640        650        660 
ISDDSTNSAN SYMSSRDFGH PFVLQLSDNE VTDASFISEK LKLKYQQFTT LKNLKNIDSL 

       670        680        690        700        710        720 
ESLELGHEDE QVQKGPLDVD MDHSQTPLFE MRVFHDRFEK IPTGWNMSVS NLPLLTERDK 

       730        740        750        760        770        780 
KDLESTVDPL DAHSIEEEDD SEFKDVAPGS YPEPSKSNEN TKLTAKENDR LLIQGDLLVC 

       790        800        810        820        830        840 
EWPEKSYQFV FSVAPSSPQM GRSLWLESKT ILSDKKDDSE DSRTITLNDC LDEFEKTEQL 

       850        860        870        880        890        900 
GEEDPWYCPT CKEFRQASKQ MEIWRCPEIL IFHLKRFSSE RRFRDKIDDL VEFPIDNLDM 

       910        920        930        940        950        960 
SMRTGSYKLS EKENPKLIYE LYAVDNHYGG LGGGHYTAFA KNPDNGQFYC FDDSRVTPVC 

       970 
PEETVTSAAY LLFYRRKTS 

« 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.
[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 SER-19; SER-37 AND SER-39, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329672 Genomic DNA. Translation: CAA19303.1.
PIRT41006.
RefSeqNP_588530.1. NM_001023518.2.

3D structure databases

ProteinModelPortalO60079.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid275564. 5 interactions.
MINTMINT-4677005.
STRING4896.SPCC1494.05c-1.

Protein family/group databases

MEROPSC19.A64.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC1494.05c.1; SPCC1494.05c.1:pep; SPCC1494.05c.
GeneID2538990.
KEGGspo:SPCC1494.05c.

Organism-specific databases

PomBaseSPCC1494.05c.

Phylogenomic databases

eggNOGCOG5560.
KOK11835.
OMADANESHK.
OrthoDBEOG7R2BSX.
PhylomeDBO60079.

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

NextBio20800165.

Entry information

Entry nameUBP12_SCHPO
AccessionPrimary (citable) accession number: O60079
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 100 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