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O60079

- UBP12_SCHPO

UniProt

O60079 - UBP12_SCHPO

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Protein
Probable ubiquitin carboxyl-terminal hydrolase 12
Gene
ubp12, SPCC1494.05c
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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 sitei320 – 3201Nucleophile By similarity
Active sitei935 – 9351Proton acceptor By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. protein deubiquitination Source: PomBase
  2. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Protein family/group databases

MEROPSiC19.A64.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ubp12
ORF Names:SPCC1494.05c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome III

Organism-specific databases

PomBaseiSPCC1494.05c.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: PomBase
  2. cytosol Source: PomBase
  3. nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 979979Probable ubiquitin carboxyl-terminal hydrolase 12
PRO_0000080612Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphoserine1 Publication
Modified residuei37 – 371Phosphoserine1 Publication
Modified residuei39 – 391Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO60079.

Interactioni

Protein-protein interaction databases

BioGridi275564. 5 interactions.
MINTiMINT-4677005.
STRINGi4896.SPCC1494.05c-1.

Structurei

3D structure databases

ProteinModelPortaliO60079.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 152102DUSP
Add
BLAST
Domaini311 – 977667USP
Add
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family.
Contains 1 DUSP domain.
Contains 1 USP domain.

Phylogenomic databases

eggNOGiCOG5560.
KOiK11835.
OMAiDANESHK.
OrthoDBiEOG7R2BSX.
PhylomeDBiO60079.

Family and domain databases

Gene3Di3.30.2230.10. 1 hit.
InterProiIPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamiPF06337. DUSP. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTiSM00695. DUSP. 1 hit.
[Graphical view]
SUPFAMiSSF143791. SSF143791. 1 hit.
PROSITEiPS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O60079-1 [UniParc]FASTAAdd to Basket

« Hide

MDSLSESSTS SYHGKRPRSL SEESQSSSNM DDISQKSISL GDASEISKNL    50
PSIAEQKQLI GELVNNQPEL ELGQVDNYIL SYSWYERLCS YLAEDGPFPG 100
PVDQEDIADL ETGTLKPDLQ EEIDFTIISR DVWDLLVRWY GLKGPEFPRE 150
TVNLGSESHP HLVVEVYPPI FSLTLLSTNA VDANESHKPK KISLSSKSTL 200
EDLLEGVKYT LSLPSDQFRL WRVDTDQPLH RTIDPSSFIK INSKEIIDFL 250
EKSKTLVELG MDSSCSLVAE CMINETWPVD RALRLQFLIQ QRNNQSSNEE 300
QKQEKRVPGT CGLSNLGNTC YMNSALQCLT HTRELRDFFT SDEWKNQVNE 350
SNPLGMGGQV ASIFASLIKS LYSPEHSSFA PRQFKATIGK FNHSFLGYGQ 400
QDSQEFLAFL LDGLHEDLNR IYQKPYTSKP DLYEVDEEKI KNTAEECWRL 450
HKLRNDSLIV DLFQGMYRST LVCPVCNTVS ITFDPFMDLT LPLPVKQVWS 500
HTVTFIPADT NLTPLAIEVV LESKAATIED LVKYVAEKSG CSDYRKILVT 550
ETYKGRFYRF LTQLSKSLLM EISEEDEIYL YELERPYEDG SDDILVPVYH 600
ISDDSTNSAN SYMSSRDFGH PFVLQLSDNE VTDASFISEK LKLKYQQFTT 650
LKNLKNIDSL ESLELGHEDE QVQKGPLDVD MDHSQTPLFE MRVFHDRFEK 700
IPTGWNMSVS NLPLLTERDK KDLESTVDPL DAHSIEEEDD SEFKDVAPGS 750
YPEPSKSNEN TKLTAKENDR LLIQGDLLVC EWPEKSYQFV FSVAPSSPQM 800
GRSLWLESKT ILSDKKDDSE DSRTITLNDC LDEFEKTEQL GEEDPWYCPT 850
CKEFRQASKQ MEIWRCPEIL IFHLKRFSSE RRFRDKIDDL VEFPIDNLDM 900
SMRTGSYKLS EKENPKLIYE LYAVDNHYGG LGGGHYTAFA KNPDNGQFYC 950
FDDSRVTPVC PEETVTSAAY LLFYRRKTS 979
Length:979
Mass (Da):111,967
Last modified:August 1, 1998 - v1
Checksum:iA705444BCDB437D2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU329672 Genomic DNA. Translation: CAA19303.1.
PIRiT41006.
RefSeqiNP_588530.1. NM_001023518.2.

Genome annotation databases

EnsemblFungiiSPCC1494.05c.1; SPCC1494.05c.1:pep; SPCC1494.05c.
GeneIDi2538990.
KEGGispo:SPCC1494.05c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU329672 Genomic DNA. Translation: CAA19303.1 .
PIRi T41006.
RefSeqi NP_588530.1. NM_001023518.2.

3D structure databases

ProteinModelPortali O60079.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 275564. 5 interactions.
MINTi MINT-4677005.
STRINGi 4896.SPCC1494.05c-1.

Protein family/group databases

MEROPSi C19.A64.

Proteomic databases

MaxQBi O60079.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPCC1494.05c.1 ; SPCC1494.05c.1:pep ; SPCC1494.05c .
GeneIDi 2538990.
KEGGi spo:SPCC1494.05c.

Organism-specific databases

PomBasei SPCC1494.05c.

Phylogenomic databases

eggNOGi COG5560.
KOi K11835.
OMAi DANESHK.
OrthoDBi EOG7R2BSX.
PhylomeDBi O60079.

Miscellaneous databases

NextBioi 20800165.

Family and domain databases

Gene3Di 3.30.2230.10. 1 hit.
InterProi IPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view ]
Pfami PF06337. DUSP. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view ]
SMARTi SM00695. DUSP. 1 hit.
[Graphical view ]
SUPFAMi SSF143791. SSF143791. 1 hit.
PROSITEi PS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-37 AND SER-39, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiUBP12_SCHPO
AccessioniPrimary (citable) accession number: O60079
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: August 1, 1998
Last modified: June 11, 2014
This is version 102 of the entry and version 1 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