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P39538

- UBP12_YEAST

UniProt

P39538 - UBP12_YEAST

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Protein

Ubiquitin carboxyl-terminal hydrolase 12

Gene

UBP12

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Ubiquitin carboxyl-terminal hydrolase that recognizes ubiquitin chains that stabilize FZO1 and promote mitochondrial fusion. UBP12 deubiquitylates FZO1 only after oligomerization.1 Publication

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 sitei373 – 3731NucleophilePROSITE-ProRule annotation
Active sitei1068 – 10681Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. ubiquitin-specific protease activity Source: SGD

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BioCyciYEAST:G3O-31628-MONOMER.

Protein family/group databases

MEROPSiC19.103.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:UBP12
Ordered Locus Names:YJL197W
ORF Names:J0340
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome X

Organism-specific databases

CYGDiYJL197w.
SGDiS000003733. UBP12.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12541254Ubiquitin carboxyl-terminal hydrolase 12PRO_0000080597Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei84 – 841Phosphoserine1 Publication
Modified residuei1160 – 11601Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP39538.
PaxDbiP39538.
PeptideAtlasiP39538.
PRIDEiP39538.

Expressioni

Gene expression databases

GenevestigatoriP39538.

Interactioni

Subunit structurei

Interacts with FZO1.1 Publication

Protein-protein interaction databases

BioGridi33567. 26 interactions.
DIPiDIP-6312N.
IntActiP39538. 6 interactions.
MINTiMINT-704453.
STRINGi4932.YJL197W.

Structurei

3D structure databases

ProteinModelPortaliP39538.
SMRiP39538. Positions 362-561, 961-1110.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini97 – 199103DUSPPROSITE-ProRule annotationAdd
BLAST
Domaini364 – 1110747USPAdd
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.
GeneTreeiENSGT00670000097750.
HOGENOMiHOG000057142.
InParanoidiP39538.
KOiK11835.
OMAiKWYHTFT.
OrthoDBiEOG7R2BSX.

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]
PfamiPF00443. 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.

P39538-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSSDVSSRE CSLVYNEDPD FTDGTTPCDR LGVDLMNVLD DKDEIKQESV
60 70 80 90 100
PVSDREIEDT ESDASAVSSF ASANELIAEP HAASETNLGT NGQDGRNVLE
110 120 130 140 150
QQRDVVARLI EENKETQKEG DKVCIVPKVW YDKFFDPDVT DPEDIGPINT
160 170 180 190 200
RMICRDFENF VLEDYNRCPY LSIAEPVFNF LSEIYGMTSG SYPVVTNLVI
210 220 230 240 250
NQTTGELETE YNKWFFRLHY LTEKQDGRKR RHGQDDSIMY LSMSALNLVR
260 270 280 290 300
DLVEKSMNLF FEKADHLDVN AVDFKIWFVS EGSDIATDSN VSTFLNSSYE
310 320 330 340 350
ITPLQFLELP IKKLLIPDMF ENRLDKITSN PSDLVIEIKP IEGNHHWPSN
360 370 380 390 400
YFAYNKLEPA SGTTGLVNLG NTCYMNSALQ CLVHIPQLRD YFLYDGYEDE
410 420 430 440 450
INEENPLGYH GYVARAFSDL VQKLFQNRMS IMQRNAAFPP SMFKSTIGHF
460 470 480 490 500
NSMFSGYMQQ DSQEFLAFLL DSLHEDLNRI IKKEYTEKPS LSPGDDVNDW
510 520 530 540 550
NVVKKLADDT WEMHLKRNCS VITDLFVGMY KSTLYCPECQ NVSITFDPYN
560 570 580 590 600
DVTLPLPVDT VWDKTIKIFP MNSPPLLLEV ELSKSSTYMD LKNYVGKMSG
610 620 630 640 650
LDPNTLFGCE IFSNQIYVNY ESTESNAQFL TLQELIKPAD DVIFYELPVT
660 670 680 690 700
NDNEVIVPVL NTRIEKGYKN AMLFGVPFFI TLKEDELNNP GAIRMKLQNR
710 720 730 740 750
FVHLSGGYIP FPEPVGNRTD FADAFPLLVE KYPDVEFEQY KDILQYTSIK
760 770 780 790 800
VTDKDKSFFS IKILSVEKEQ QFASNNRTGP NFWTPISQLN LDKATDIDDK
810 820 830 840 850
LEDVVKDIYN YSSLVDCAEG VLMQVDDEGD TEGSEAKNFS KPFQSGDDEE
860 870 880 890 900
NKETVTNNEN VNNTNDRDED MELTDDVEED ASTEPELTDK PEALDKIKDS
910 920 930 940 950
LTSTPFAILS MNDIIVCEWS ELGSNEAFSD DKIYNWENPA TLPNKELENA
960 970 980 990 1000
KLERSNAKER TITLDDCLQL FSKPEILGLT DSWYCPTCKE HRQATKQIQL
1010 1020 1030 1040 1050
WNTPDILLIH LKRFESQRSF SDKIDATVNF PITDLDLSRY VVYKDDPRGL
1060 1070 1080 1090 1100
IYDLYAVDNH YGGLGGGHYT AYVKNFADNK WYYFDDSRVT ETAPENSIAG
1110 1120 1130 1140 1150
SAYLLFYIRR HKDGNGLGSS KLQEIIQKSR HGYDERIKKI YDEQMKLYEF
1160 1170 1180 1190 1200
NKTDEEEDVS DDMIECNEDV QAPEYSNRSL EVGHIETQDC NDEDDNDDGE
1210 1220 1230 1240 1250
RTNSGRRKLR LLKKVYKNNS GLGSSSTSEI SEGCPENEVA DLNLKNGVTL

ESPE
Length:1,254
Mass (Da):143,192
Last modified:February 1, 1995 - v1
Checksum:i349AFA4C4CEE0EA5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77688 Genomic DNA. Translation: CAA54762.1.
Z49472 Genomic DNA. Translation: CAA89492.1.
BK006943 Genomic DNA. Translation: DAA08611.1.
PIRiS46636.
RefSeqiNP_012338.1. NM_001181630.1.

Genome annotation databases

EnsemblFungiiYJL197W; YJL197W; YJL197W.
GeneIDi853242.
KEGGisce:YJL197W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77688 Genomic DNA. Translation: CAA54762.1 .
Z49472 Genomic DNA. Translation: CAA89492.1 .
BK006943 Genomic DNA. Translation: DAA08611.1 .
PIRi S46636.
RefSeqi NP_012338.1. NM_001181630.1.

3D structure databases

ProteinModelPortali P39538.
SMRi P39538. Positions 362-561, 961-1110.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33567. 26 interactions.
DIPi DIP-6312N.
IntActi P39538. 6 interactions.
MINTi MINT-704453.
STRINGi 4932.YJL197W.

Protein family/group databases

MEROPSi C19.103.

Proteomic databases

MaxQBi P39538.
PaxDbi P39538.
PeptideAtlasi P39538.
PRIDEi P39538.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YJL197W ; YJL197W ; YJL197W .
GeneIDi 853242.
KEGGi sce:YJL197W.

Organism-specific databases

CYGDi YJL197w.
SGDi S000003733. UBP12.

Phylogenomic databases

eggNOGi COG5560.
GeneTreei ENSGT00670000097750.
HOGENOMi HOG000057142.
InParanoidi P39538.
KOi K11835.
OMAi KWYHTFT.
OrthoDBi EOG7R2BSX.

Enzyme and pathway databases

BioCyci YEAST:G3O-31628-MONOMER.

Miscellaneous databases

NextBioi 973472.

Gene expression databases

Genevestigatori P39538.

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 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

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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.

Entry informationi

Entry nameiUBP12_YEAST
AccessioniPrimary (citable) accession number: P39538
Secondary accession number(s): D6VVZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 29, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7110 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

External Data

Dasty 3