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P25037

- UBP1_YEAST

UniProt

P25037 - UBP1_YEAST

Protein

Ubiquitin carboxyl-terminal hydrolase 1

Gene

UBP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (05 Oct 2010)
      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.

    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 sitei110 – 1101NucleophilePROSITE-ProRule annotation
    Active sitei697 – 6971Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ubiquitin-specific protease activity Source: SGD

    GO - Biological processi

    1. protein deubiquitination Source: SGD
    2. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29521-MONOMER.

    Protein family/group databases

    MEROPSiC19.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 1 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 1
    Ubiquitin thioesterase 1
    Ubiquitin-specific-processing protease 1
    Gene namesi
    Name:UBP1
    Ordered Locus Names:YDL122W
    ORF Names:D2250
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    SGDiS000002280. UBP1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. endoplasmic reticulum Source: SGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 809809Ubiquitin carboxyl-terminal hydrolase 1PRO_0000080585Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei530 – 5301Phosphoserine3 Publications
    Modified residuei531 – 5311Phosphoserine3 Publications
    Modified residuei555 – 5551Phosphoserine2 Publications
    Modified residuei618 – 6181Phosphoserine3 Publications
    Modified residuei638 – 6381Phosphoserine3 Publications
    Modified residuei652 – 6521Phosphothreonine1 Publication
    Modified residuei653 – 6531Phosphoserine1 Publication
    Modified residuei654 – 6541Phosphoserine1 Publication
    Modified residuei670 – 6701Phosphoserine1 Publication
    Modified residuei755 – 7551Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP25037.
    PaxDbiP25037.
    PeptideAtlasiP25037.

    Expressioni

    Gene expression databases

    GenevestigatoriP25037.

    Interactioni

    Protein-protein interaction databases

    BioGridi31941. 107 interactions.
    IntActiP25037. 23 interactions.
    MINTiMINT-2788387.
    STRINGi4932.YDL122W.

    Structurei

    3D structure databases

    ProteinModelPortaliP25037.
    SMRiP25037. Positions 657-735.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini101 – 738638USPAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG259866.
    HOGENOMiHOG000093934.
    KOiK11870.
    OMAiFMLFYEY.
    OrthoDBiEOG7HB5JX.

    Family and domain databases

    InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view]
    PfamiPF00443. 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.

    P25037-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDLFIESKIN SLLQFLFGSR QDFLRNFKTW SNNNNNLSIY LLIFGIVVFF    50
    YKKPDHLNYI VESVSEMTTN FRNNNSLSRW LPRSKFTHLD EEILKRGGFI 100
    AGLVNDGNTC FMNSVLQSLA SSRELMEFLD NNVIRTYEEI EQNEHNEEGN 150
    GQESAQDEAT HKKNTRKGGK VYGKHKKKLN RKSSSKEDEE KSQEPDITFS 200
    VALRDLLSAL NAKYYRDKPY FKTNSLLKAM SKSPRKNILL GYDQEDAQEF 250
    FQNILAELES NVKSLNTEKL DTTPVAKSEL PDDALVGQLN LGEVGTVYIP 300
    TEQIDPNSIL HDKSIQNFTP FKLMTPLDGI TAERIGCLQC GENGGIRYSV 350
    FSGLSLNLPN ENIGSTLKLS QLLSDWSKPE IIEGVECNRC ALTAAHSHLF 400
    GQLKEFEKKP EGSIPEKLIN AVKDRVHQIE EVLAKPVIDD EDYKKLHTAN 450
    MVRKCSKSKQ ILISRPPPLL SIHINRSVFD PRTYMIRKNN SKVLFKSRLN 500
    LAPWCCDINE INLDARLPMS KKEKAAQQDS SEDENIGGEY YTKLHERFEQ 550
    EFEDSEEEKE YDDAEGNYAS HYNHTKDISN YDPLNGEVDG VTSDDEDEYI 600
    EETDALGNTI KKRIIEHSDV ENENVKDNEE LQEIDNVSLD EPKINVEDQL 650
    ETSSDEEDVI PAPPINYARS FSTVPATPLT YSLRSVIVHY GTHNYGHYIA 700
    FRKYRGCWWR ISDETVYVVD EAEVLSTPGV FMLFYEYDFD EETGKMKDDL 750
    EAIQSNNEED DEKEQEQKGV QEPKESQEQG EGEEQEEGQE QMKFERTEDH 800
    RDISGKDVN 809
    Length:809
    Mass (Da):92,769
    Last modified:October 5, 2010 - v2
    Checksum:i07BA266FB43C2C04
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti418 – 4181L → P in AAA35189. (PubMed:2050695)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63484 Genomic DNA. Translation: AAA35189.1.
    Z74170 Genomic DNA. Translation: CAA98690.1.
    BK006938 Genomic DNA. Translation: DAA11738.1.
    PIRiS67665.
    RefSeqiNP_010161.1. NM_001180181.1.

    Genome annotation databases

    EnsemblFungiiYDL122W; YDL122W; YDL122W.
    GeneIDi851435.
    KEGGisce:YDL122W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63484 Genomic DNA. Translation: AAA35189.1 .
    Z74170 Genomic DNA. Translation: CAA98690.1 .
    BK006938 Genomic DNA. Translation: DAA11738.1 .
    PIRi S67665.
    RefSeqi NP_010161.1. NM_001180181.1.

    3D structure databases

    ProteinModelPortali P25037.
    SMRi P25037. Positions 657-735.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31941. 107 interactions.
    IntActi P25037. 23 interactions.
    MINTi MINT-2788387.
    STRINGi 4932.YDL122W.

    Protein family/group databases

    MEROPSi C19.002.

    Proteomic databases

    MaxQBi P25037.
    PaxDbi P25037.
    PeptideAtlasi P25037.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDL122W ; YDL122W ; YDL122W .
    GeneIDi 851435.
    KEGGi sce:YDL122W.

    Organism-specific databases

    SGDi S000002280. UBP1.

    Phylogenomic databases

    eggNOGi NOG259866.
    HOGENOMi HOG000093934.
    KOi K11870.
    OMAi FMLFYEY.
    OrthoDBi EOG7HB5JX.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29521-MONOMER.

    Miscellaneous databases

    NextBioi 968666.

    Gene expression databases

    Genevestigatori P25037.

    Family and domain databases

    InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view ]
    Pfami 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. "Cloning and functional analysis of the ubiquitin-specific protease gene UBP1 of Saccharomyces cerevisiae."
      Tobias J.W., Varshavsky A.
      J. Biol. Chem. 266:12021-12028(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [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. "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-530; SER-531; SER-555; SER-618; SER-638; SER-670 AND SER-755, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    6. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "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-530; SER-531; SER-618; SER-638 AND SER-755, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "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-530; SER-531; SER-555; SER-618; SER-638; THR-652; SER-653; SER-654 AND SER-755, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiUBP1_YEAST
    AccessioniPrimary (citable) accession number: P25037
    Secondary accession number(s): D6VRM8, Q07543
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 126 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 8970 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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3