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P39538 (UBP12_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
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
Ordered Locus Names:YJL197W
ORF Names:J0340
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1254 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ubiquitin carboxyl-terminal hydrolase that recognizes ubiquitin chains that stabilize FZO1 and promote mitochondrial fusion. UBP12 deubiquitylates FZO1 only after oligomerization. Ref.7

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).

Subunit structure

Interacts with FZO1. Ref.7

Miscellaneous

Present with 7110 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 DUSP domain.

Contains 1 USP domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12541254Ubiquitin carboxyl-terminal hydrolase 12
PRO_0000080597

Regions

Domain97 – 199103DUSP
Domain364 – 1110747USP

Sites

Active site3731Nucleophile By similarity
Active site10681Proton acceptor By similarity

Amino acid modifications

Modified residue841Phosphoserine Ref.5
Modified residue11601Phosphoserine Ref.6

Sequences

Sequence LengthMass (Da)Tools
P39538 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 349AFA4C4CEE0EA5

FASTA1,254143,192
        10         20         30         40         50         60 
MGSSDVSSRE CSLVYNEDPD FTDGTTPCDR LGVDLMNVLD DKDEIKQESV PVSDREIEDT 

        70         80         90        100        110        120 
ESDASAVSSF ASANELIAEP HAASETNLGT NGQDGRNVLE QQRDVVARLI EENKETQKEG 

       130        140        150        160        170        180 
DKVCIVPKVW YDKFFDPDVT DPEDIGPINT RMICRDFENF VLEDYNRCPY LSIAEPVFNF 

       190        200        210        220        230        240 
LSEIYGMTSG SYPVVTNLVI NQTTGELETE YNKWFFRLHY LTEKQDGRKR RHGQDDSIMY 

       250        260        270        280        290        300 
LSMSALNLVR DLVEKSMNLF FEKADHLDVN AVDFKIWFVS EGSDIATDSN VSTFLNSSYE 

       310        320        330        340        350        360 
ITPLQFLELP IKKLLIPDMF ENRLDKITSN PSDLVIEIKP IEGNHHWPSN YFAYNKLEPA 

       370        380        390        400        410        420 
SGTTGLVNLG NTCYMNSALQ CLVHIPQLRD YFLYDGYEDE INEENPLGYH GYVARAFSDL 

       430        440        450        460        470        480 
VQKLFQNRMS IMQRNAAFPP SMFKSTIGHF NSMFSGYMQQ DSQEFLAFLL DSLHEDLNRI 

       490        500        510        520        530        540 
IKKEYTEKPS LSPGDDVNDW NVVKKLADDT WEMHLKRNCS VITDLFVGMY KSTLYCPECQ 

       550        560        570        580        590        600 
NVSITFDPYN DVTLPLPVDT VWDKTIKIFP MNSPPLLLEV ELSKSSTYMD LKNYVGKMSG 

       610        620        630        640        650        660 
LDPNTLFGCE IFSNQIYVNY ESTESNAQFL TLQELIKPAD DVIFYELPVT NDNEVIVPVL 

       670        680        690        700        710        720 
NTRIEKGYKN AMLFGVPFFI TLKEDELNNP GAIRMKLQNR FVHLSGGYIP FPEPVGNRTD 

       730        740        750        760        770        780 
FADAFPLLVE KYPDVEFEQY KDILQYTSIK VTDKDKSFFS IKILSVEKEQ QFASNNRTGP 

       790        800        810        820        830        840 
NFWTPISQLN LDKATDIDDK LEDVVKDIYN YSSLVDCAEG VLMQVDDEGD TEGSEAKNFS 

       850        860        870        880        890        900 
KPFQSGDDEE NKETVTNNEN VNNTNDRDED MELTDDVEED ASTEPELTDK PEALDKIKDS 

       910        920        930        940        950        960 
LTSTPFAILS MNDIIVCEWS ELGSNEAFSD DKIYNWENPA TLPNKELENA KLERSNAKER 

       970        980        990       1000       1010       1020 
TITLDDCLQL FSKPEILGLT DSWYCPTCKE HRQATKQIQL WNTPDILLIH LKRFESQRSF 

      1030       1040       1050       1060       1070       1080 
SDKIDATVNF PITDLDLSRY VVYKDDPRGL IYDLYAVDNH YGGLGGGHYT AYVKNFADNK 

      1090       1100       1110       1120       1130       1140 
WYYFDDSRVT ETAPENSIAG SAYLLFYIRR HKDGNGLGSS KLQEIIQKSR HGYDERIKKI 

      1150       1160       1170       1180       1190       1200 
YDEQMKLYEF NKTDEEEDVS DDMIECNEDV QAPEYSNRSL EVGHIETQDC NDEDDNDDGE 

      1210       1220       1230       1240       1250 
RTNSGRRKLR LLKKVYKNNS GLGSSSTSEI SEGCPENEVA DLNLKNGVTL ESPE 

« Hide

References

« Hide 'large scale' references
[1]"The sequence of a 36 kb segment on the left arm of yeast chromosome X identifies 24 open reading frames including NUC1, PRP21 (SPP91), CDC6, CRY2, the gene for S24, a homologue to the aconitase gene ACO1 and two homologues to chromosome III genes."
Purnelle B., Coster F., Goffeau A.
Yeast 10:1235-1249(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Two deubiquitylases act on mitofusin and regulate mitochondrial fusion along independent pathways."
Anton F., Dittmar G., Langer T., Escobar-Henriques M.
Mol. Cell 49:487-498(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEUBIQUITINATION OF FZO1, INTERACTION WITH FZO1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X77688 Genomic DNA. Translation: CAA54762.1.
Z49472 Genomic DNA. Translation: CAA89492.1.
BK006943 Genomic DNA. Translation: DAA08611.1.
PIRS46636.
RefSeqNP_012338.1. NM_001181630.1.

3D structure databases

ProteinModelPortalP39538.
SMRP39538. Positions 362-561, 961-1110.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33567. 26 interactions.
DIPDIP-6312N.
IntActP39538. 6 interactions.
MINTMINT-704453.
STRING4932.YJL197W.

Protein family/group databases

MEROPSC19.103.

Proteomic databases

MaxQBP39538.
PaxDbP39538.
PeptideAtlasP39538.
PRIDEP39538.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJL197W; YJL197W; YJL197W.
GeneID853242.
KEGGsce:YJL197W.

Organism-specific databases

CYGDYJL197w.
SGDS000003733. UBP12.

Phylogenomic databases

eggNOGCOG5560.
GeneTreeENSGT00670000097750.
HOGENOMHOG000057142.
KOK11835.
OMAKWYHTFT.
OrthoDBEOG7R2BSX.

Enzyme and pathway databases

BioCycYEAST:G3O-31628-MONOMER.

Gene expression databases

GenevestigatorP39538.

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]
PfamPF00443. 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

NextBio973472.

Entry information

Entry nameUBP12_YEAST
AccessionPrimary (citable) accession number: P39538
Secondary accession number(s): D6VVZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 14, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries