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Protein

Probable ubiquitin carboxyl-terminal hydrolase 12

Gene

ubp12

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: 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 – 3201NucleophilePROSITE-ProRule annotation
Active sitei935 – 9351Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. histone deubiquitination Source: GO_Central
  2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: GO_Central
  3. protein deubiquitination 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.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 12PRO_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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 152102DUSPPROSITE-ProRule annotationAdd
BLAST
Domaini311 – 977667USPAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family.Curated
Contains 1 DUSP domain.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Phylogenomic databases

eggNOGiCOG5560.
InParanoidiO60079.
KOiK11835.
OMAiDANESHK.
OrthoDBiEOG7R2BSX.
PhylomeDBiO60079.

Family and domain databases

Gene3Di3.30.2230.10. 1 hit.
InterProiIPR006615. Pept_C19_DUSP.
IPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
[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

        10         20         30         40         50
MDSLSESSTS SYHGKRPRSL SEESQSSSNM DDISQKSISL GDASEISKNL
60 70 80 90 100
PSIAEQKQLI GELVNNQPEL ELGQVDNYIL SYSWYERLCS YLAEDGPFPG
110 120 130 140 150
PVDQEDIADL ETGTLKPDLQ EEIDFTIISR DVWDLLVRWY GLKGPEFPRE
160 170 180 190 200
TVNLGSESHP HLVVEVYPPI FSLTLLSTNA VDANESHKPK KISLSSKSTL
210 220 230 240 250
EDLLEGVKYT LSLPSDQFRL WRVDTDQPLH RTIDPSSFIK INSKEIIDFL
260 270 280 290 300
EKSKTLVELG MDSSCSLVAE CMINETWPVD RALRLQFLIQ QRNNQSSNEE
310 320 330 340 350
QKQEKRVPGT CGLSNLGNTC YMNSALQCLT HTRELRDFFT SDEWKNQVNE
360 370 380 390 400
SNPLGMGGQV ASIFASLIKS LYSPEHSSFA PRQFKATIGK FNHSFLGYGQ
410 420 430 440 450
QDSQEFLAFL LDGLHEDLNR IYQKPYTSKP DLYEVDEEKI KNTAEECWRL
460 470 480 490 500
HKLRNDSLIV DLFQGMYRST LVCPVCNTVS ITFDPFMDLT LPLPVKQVWS
510 520 530 540 550
HTVTFIPADT NLTPLAIEVV LESKAATIED LVKYVAEKSG CSDYRKILVT
560 570 580 590 600
ETYKGRFYRF LTQLSKSLLM EISEEDEIYL YELERPYEDG SDDILVPVYH
610 620 630 640 650
ISDDSTNSAN SYMSSRDFGH PFVLQLSDNE VTDASFISEK LKLKYQQFTT
660 670 680 690 700
LKNLKNIDSL ESLELGHEDE QVQKGPLDVD MDHSQTPLFE MRVFHDRFEK
710 720 730 740 750
IPTGWNMSVS NLPLLTERDK KDLESTVDPL DAHSIEEEDD SEFKDVAPGS
760 770 780 790 800
YPEPSKSNEN TKLTAKENDR LLIQGDLLVC EWPEKSYQFV FSVAPSSPQM
810 820 830 840 850
GRSLWLESKT ILSDKKDDSE DSRTITLNDC LDEFEKTEQL GEEDPWYCPT
860 870 880 890 900
CKEFRQASKQ MEIWRCPEIL IFHLKRFSSE RRFRDKIDDL VEFPIDNLDM
910 920 930 940 950
SMRTGSYKLS EKENPKLIYE LYAVDNHYGG LGGGHYTAFA KNPDNGQFYC
960 970
FDDSRVTPVC PEETVTSAAY LLFYRRKTS
Length:979
Mass (Da):111,967
Last modified:August 1, 1998 - v1
Checksum:iA705444BCDB437D2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA19303.1.
PIRiT41006.
RefSeqiNP_588530.1. NM_001023518.2.

3D structure databases

ProteinModelPortaliO60079.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

MEROPSiC19.A64.

Proteomic databases

MaxQBiO60079.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

PomBaseiSPCC1494.05c.

Phylogenomic databases

eggNOGiCOG5560.
InParanoidiO60079.
KOiK11835.
OMAiDANESHK.
OrthoDBiEOG7R2BSX.
PhylomeDBiO60079.

Miscellaneous databases

NextBioi20800165.

Family and domain databases

Gene3Di3.30.2230.10. 1 hit.
InterProiIPR006615. Pept_C19_DUSP.
IPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
[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]
ProtoNetiSearch...

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: February 4, 2015
This is version 106 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

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.