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Q01476

- UBP2_YEAST

UniProt

Q01476 - UBP2_YEAST

Protein

Ubiquitin carboxyl-terminal hydrolase 2

Gene

UBP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Has an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety in natural or engineered linear fusion proteins, irrespective of their size or the presence of an N-terminal extension to ubiquitin. Removes ubiquitin chains that initiate proteolysis of FZO1 and inhibit mitochondrial fusion.2 Publications

    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 sitei745 – 7451NucleophilePROSITE-ProRule annotation
    Active sitei1209 – 12091Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. ubiquitin-specific protease activity Source: SGD

    GO - Biological processi

    1. protein deubiquitination Source: SGD
    2. ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33651-MONOMER.

    Protein family/group databases

    MEROPSiC19.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 2 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 2
    Ubiquitin thioesterase 2
    Ubiquitin-specific-processing protease 2
    Gene namesi
    Name:UBP2
    Ordered Locus Names:YOR124C
    ORF Names:O3281, YOR3281C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOR124c.
    SGDiS000005650. UBP2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12721272Ubiquitin carboxyl-terminal hydrolase 2PRO_0000080586Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei907 – 9071Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ01476.
    PaxDbiQ01476.
    PeptideAtlasiQ01476.

    Expressioni

    Gene expression databases

    GenevestigatoriQ01476.

    Interactioni

    Subunit structurei

    Forms a ternary complex with RSP5 and RUP1. Interacts with FZO1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RUP1Q122423EBI-19826,EBI-38794

    Protein-protein interaction databases

    BioGridi34519. 83 interactions.
    DIPiDIP-2647N.
    IntActiQ01476. 10 interactions.
    MINTiMINT-427685.
    STRINGi4932.YOR124C.

    Structurei

    3D structure databases

    ProteinModelPortaliQ01476.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini736 – 1258523USPAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG275561.
    HOGENOMiHOG000094458.
    KOiK11849.
    OMAiHRGEASY.
    OrthoDBiEOG7327X3.

    Family and domain databases

    InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    IPR025305. UCH_repeat_domain.
    [Graphical view]
    PfamiPF13446. RPT. 2 hits.
    PF00443. UCH. 1 hit.
    [Graphical view]
    PROSITEiPS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q01476-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPNEDNELQK AIENHHNQLL NQDKENADRN GSVIEDLPLY GTSINQQSTP     50
    GDVDDGKHLL YPDIATNLPL KTSDRLLDDI LCDTIFLNST DPKVMQKGLQ 100
    SRGILKESML SYSTFRSSIR PNCLGSLTDQ VVFQTKSEYD SISCPKYNKI 150
    HVFQAVIFNP SLAEQQISTF DDIVKIPIYH LKVSVKVRQE LERLKKHVGV 200
    TQFHSLDHLH EYDRVDLSTF DSSDPNLLDY GIYVSDDTNK LILIEIFKPE 250
    FNSPEEHESF TADAIKKRYN AMCVKNESLD KSETPSQVDC FYTLFKIFKG 300
    PLTRKSKAEP TKTIDSGNLA LNTHLNPEWL TSKYGFQASS EIDEETNEIF 350
    TEYVPPDMVD YVNDLETRKI RESFVRKCLQ LIFWGQLSTS LLAPNSPLKN 400
    TKSVKGMSSL QTSFSTLPWF HLLGESRARI LLNSNEQTHS PLDAEPHFIN 450
    LSVSHYYTDR DIIRNYESLS SLDPENIGLY FDALTYIANR KGAYQLIAYC 500
    GKQDIIGQEA LENALLMFKI NPKECNISEL NEATLLSIYK YETSNKSQVT 550
    SNHLTNLKNA LRLLAKYTKS DKLKFYVDHE PYRALSQAYD TLSIDESVDE 600
    DIIKTAYSVK INDSPGLKLD CDRALYTIAI SKRSLDLFNF LTEECPQFSN 650
    YYGPEKLDYQ EALKLLQVNE NASDETILKI FKQKWFDENV YEPDQFLILR 700
    AALTKISIER NSTLITNFLL TGTIDPNSLP PENWPTGINN IGNTCYLNSL 750
    LQYYFSIAPL RRYVLEYQKT VENFNDHLSN SGHIRRIGGR EISRGEVERS 800
    IQFIYQLRNL FYAMVHTRER CVTPSKELAY LAFAPSNVEV EFEVEGNKVV 850
    DQTGVLSDSK KETTDDAFTT KIKDTSLIDL EMEDGLNGDV GTDANRKKNE 900
    SNDAEVSENE DTTGLTSPTR VAKISSDQLE NALEMGRQQD VTECIGNVLF 950
    QIESGSEPIR YDEDNEQYDL VKQLFYGTTK QSIVPLSATN KVRTKVERFL 1000
    SLLINIGDHP KDIYDAFDSY FKDEYLTMEE YGDVIRTVAV TTFPTILQVQ 1050
    IQRVYYDRER LMPFKSIEPL PFKEVIYMDR YADTENPLLL AKKKETEEMK 1100
    QKLKVMKNRQ RELLSRDDSG LTRKDAFLES IKLLESDTIK KTPLKIEAAN 1150
    DVIKTLRNNV QNIDNELMKL YNDINSLEEK ISHQFDDFKE YGYSLFSVFI 1200
    HRGEASYGHY WIYIKDRNRN GIWRKYNDET ISEVQEEEVF NFNEGNTATP 1250
    YFLVYVKQGQ EGDIEPLKRI LK 1272
    Length:1,272
    Mass (Da):146,355
    Last modified:November 1, 1997 - v2
    Checksum:i6D106539AE5C5F3F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti658 – 6658Missing(PubMed:1429680)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M94916 Genomic DNA. Translation: AAA35190.1.
    X94335 Genomic DNA. Translation: CAA64043.1.
    X90518 Genomic DNA. Translation: CAA62120.1.
    Z75032 Genomic DNA. Translation: CAA99323.1.
    BK006948 Genomic DNA. Translation: DAA10898.1.
    PIRiS60999.
    RefSeqiNP_014767.3. NM_001183543.3.

    Genome annotation databases

    EnsemblFungiiYOR124C; YOR124C; YOR124C.
    GeneIDi854291.
    KEGGisce:YOR124C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M94916 Genomic DNA. Translation: AAA35190.1 .
    X94335 Genomic DNA. Translation: CAA64043.1 .
    X90518 Genomic DNA. Translation: CAA62120.1 .
    Z75032 Genomic DNA. Translation: CAA99323.1 .
    BK006948 Genomic DNA. Translation: DAA10898.1 .
    PIRi S60999.
    RefSeqi NP_014767.3. NM_001183543.3.

    3D structure databases

    ProteinModelPortali Q01476.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34519. 83 interactions.
    DIPi DIP-2647N.
    IntActi Q01476. 10 interactions.
    MINTi MINT-427685.
    STRINGi 4932.YOR124C.

    Protein family/group databases

    MEROPSi C19.003.

    Proteomic databases

    MaxQBi Q01476.
    PaxDbi Q01476.
    PeptideAtlasi Q01476.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOR124C ; YOR124C ; YOR124C .
    GeneIDi 854291.
    KEGGi sce:YOR124C.

    Organism-specific databases

    CYGDi YOR124c.
    SGDi S000005650. UBP2.

    Phylogenomic databases

    eggNOGi NOG275561.
    HOGENOMi HOG000094458.
    KOi K11849.
    OMAi HRGEASY.
    OrthoDBi EOG7327X3.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33651-MONOMER.

    Miscellaneous databases

    NextBioi 976278.

    Gene expression databases

    Genevestigatori Q01476.

    Family and domain databases

    InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    IPR025305. UCH_repeat_domain.
    [Graphical view ]
    Pfami PF13446. RPT. 2 hits.
    PF00443. UCH. 1 hit.
    [Graphical view ]
    PROSITEi PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family."
      Baker R.T., Tobias J.W., Varshavsky A.
      J. Biol. Chem. 267:23364-23375(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Sequencing and analysis of 51 kb on the right arm of chromosome XV from Saccharomyces cerevisiae reveals 30 open reading frames."
      Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C., Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.
      Yeast 12:281-288(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme."
      Kee Y., Lyon N., Huibregtse J.M.
      EMBO J. 24:2414-2424(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RSP5 AND RUP1.
    8. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-907, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    9. "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-907, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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-907, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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 nameiUBP2_YEAST
    AccessioniPrimary (citable) accession number: Q01476
    Secondary accession number(s): D6W2I2, Q99357
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2420 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 XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3