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P38237

- UBP14_YEAST

UniProt

P38237 - UBP14_YEAST

Protein

Ubiquitin carboxyl-terminal hydrolase 14

Gene

UBP14

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 127 (01 Oct 2014)
      Sequence version 2 (31 Oct 2006)
      Previous versions | rss
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    Functioni

    Has a role in the negative regulation of gluconeogenesis. Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBPase). Accelerates proteasomal breakdown of ubiquitinated proteins as it disassembles free ubiquitin chains that would compete with ubiquitinated proteins to bind to the proteasome.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 sitei332 – 3321Nucleophile
    Active sitei737 – 7371Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri190 – 26273UBP-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. omega peptidase activity Source: InterPro
    2. ubiquitin-specific protease activity Source: SGD
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. negative regulation of gluconeogenesis Source: SGD
    2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29029-MONOMER.

    Protein family/group databases

    MEROPSiC19.083.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 14 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 14
    Glucose-induced degradation protein 6
    Ubiquitin thioesterase 14
    Ubiquitin-specific-processing protease 14
    Gene namesi
    Name:UBP14
    Synonyms:GID6
    Ordered Locus Names:YBR058C
    ORF Names:YBR0515
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBR058c.
    SGDiS000000262. UBP14.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi332 – 3321C → A: Loss of enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 781781Ubiquitin carboxyl-terminal hydrolase 14PRO_0000080599Add
    BLAST

    Proteomic databases

    MaxQBiP38237.
    PaxDbiP38237.

    Expressioni

    Gene expression databases

    GenevestigatoriP38237.

    Interactioni

    Protein-protein interaction databases

    BioGridi32761. 132 interactions.
    DIPiDIP-4897N.
    IntActiP38237. 11 interactions.
    MINTiMINT-486523.
    STRINGi4932.YBR058C.

    Structurei

    3D structure databases

    ProteinModelPortaliP38237.
    SMRiP38237. Positions 4-780.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini323 – 781459USPAdd
    BLAST
    Domaini576 – 62651UBA 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini649 – 68941UBA 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi92 – 954Poly-Asn

    Sequence similaritiesi

    Belongs to the peptidase C19 family.Curated
    Contains 2 UBA domains.PROSITE-ProRule annotation
    Contains 1 UBP-type zinc finger.PROSITE-ProRule annotation
    Contains 1 USP domain.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri190 – 26273UBP-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5207.
    GeneTreeiENSGT00390000000874.
    HOGENOMiHOG000162311.
    KOiK11836.
    OMAiAESAMNW.
    OrthoDBiEOG74TX7J.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    IPR016652. Ubiquitinyl_hydrolase.
    IPR028889. UCH/PAN2.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR001607. Znf_UBP.
    [Graphical view]
    PfamiPF00627. UBA. 2 hits.
    PF00443. UCH. 1 hit.
    PF02148. zf-UBP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016308. UBP. 1 hit.
    SMARTiSM00165. UBA. 2 hits.
    SM00290. ZnF_UBP. 1 hit.
    [Graphical view]
    SUPFAMiSSF46934. SSF46934. 1 hit.
    PROSITEiPS50030. UBA. 2 hits.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    PS50271. ZF_UBP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P38237-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEAVLENVN VPAVVSKDEC IYCFESPYNE PLALNASPKH SLNICLNCFQ    50
    ATCNRHVPLH IRVTEYACDT IHSNYLTIAK VEKPKQENVE ENNNNKKIKL 100
    QVIETSEDDT HNTIWSLQRF NGENVPRTVL SKSTDSDISS TALEKIEKIL 150
    KAKSQDFEDK KNSWVLEIST CPHTENFQIP SKPENTVNLN QCSSCDLTQN 200
    LWLCLHCGNI GCGREQIGID GHSHALDHYR SNNNHPLAIK LGSLSSSTYD 250
    LYCYACDDET RFPDNVNLGS ALQIYGINIQ EKIADEKTLV QLQVEQNENW 300
    QFRMVDSSGK EFEKLSASKN YGCGLINLGN SCYLNSVIQS LVNGGVPNWS 350
    LDFLGSKFPL DVVYPDNNLK CQWIKLLNAM KCEPELYPNG IKPTTFKKCI 400
    GQNHQEFSSN RQQDAMEFLT FLLDLLDKKF FSSSSSGIPN PNDLVRFMME 450
    DRLQCNICGK VKYSYEPTEA IQIPLEENDE PQDMLERIKA YFEGQTIEFK 500
    CANCKEKVTA NKKPGFKSLP QTLILNPIRI RLQNWIPVKT SNELSLPGLI 550
    DRDDMLDVSS YLSQGFDPQT ENLLPDEDEN RSSFTPNQCS ISQLIEMGFT 600
    QNASVRALFN TGNQDAESAM NWLFQHMDDP DLNDPFVPPP NVPKKDKREV 650
    DEVSLTSMLS MGLNPNLCRK ALILNNGDVN RSVEWVFNNM DDDGTFPEPE 700
    VPNEEQQQKK DLGYSTAKPY ALTAVICHKG NSVHSGHYVV FIRKLVADKW 750
    KWVLYNDEKL VAADSIEDMK KNGYIYFYTR C 781
    Length:781
    Mass (Da):88,630
    Last modified:October 31, 2006 - v2
    Checksum:i52B421DCD4A0FCBA
    GO

    Sequence cautioni

    The sequence CAA85001.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA86402.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z35927 Genomic DNA. Translation: CAA85001.1. Different initiation.
    Z46260 Genomic DNA. Translation: CAA86402.1. Different initiation.
    BK006936 Genomic DNA. Translation: DAA07177.1.
    PIRiS45916.
    RefSeqiNP_009614.2. NM_001178406.1.

    Genome annotation databases

    EnsemblFungiiYBR058C; YBR058C; YBR058C.
    GeneIDi852349.
    KEGGisce:YBR058C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z35927 Genomic DNA. Translation: CAA85001.1 . Different initiation.
    Z46260 Genomic DNA. Translation: CAA86402.1 . Different initiation.
    BK006936 Genomic DNA. Translation: DAA07177.1 .
    PIRi S45916.
    RefSeqi NP_009614.2. NM_001178406.1.

    3D structure databases

    ProteinModelPortali P38237.
    SMRi P38237. Positions 4-780.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32761. 132 interactions.
    DIPi DIP-4897N.
    IntActi P38237. 11 interactions.
    MINTi MINT-486523.
    STRINGi 4932.YBR058C.

    Protein family/group databases

    MEROPSi C19.083.

    Proteomic databases

    MaxQBi P38237.
    PaxDbi P38237.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR058C ; YBR058C ; YBR058C .
    GeneIDi 852349.
    KEGGi sce:YBR058C.

    Organism-specific databases

    CYGDi YBR058c.
    SGDi S000000262. UBP14.

    Phylogenomic databases

    eggNOGi COG5207.
    GeneTreei ENSGT00390000000874.
    HOGENOMi HOG000162311.
    KOi K11836.
    OMAi AESAMNW.
    OrthoDBi EOG74TX7J.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29029-MONOMER.

    Miscellaneous databases

    NextBioi 971095.

    Gene expression databases

    Genevestigatori P38237.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    IPR016652. Ubiquitinyl_hydrolase.
    IPR028889. UCH/PAN2.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR001607. Znf_UBP.
    [Graphical view ]
    Pfami PF00627. UBA. 2 hits.
    PF00443. UCH. 1 hit.
    PF02148. zf-UBP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016308. UBP. 1 hit.
    SMARTi SM00165. UBA. 2 hits.
    SM00290. ZnF_UBP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46934. SSF46934. 1 hit.
    PROSITEi PS50030. UBA. 2 hits.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    PS50271. ZF_UBP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and analysis of 24 kb on chromosome II of Saccharomyces cerevisiae."
      Aljinovic G., Pohl T.M.
      Yeast 11:475-479(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [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. "Identification of a novel 29-linked polyubiquitin binding protein, Ufd3, using polyubiquitin chain analogues."
      Russell N.S., Wilkinson K.D.
      Biochemistry 43:4844-4854(2004) [PubMed] [Europe PMC] [Abstract]
    5. "In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome."
      Amerik A.Y., Swaminathan S., Krantz B.A., Wilkinson K.D., Hochstrasser M.
      EMBO J. 16:4826-4838(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-332.
    6. "Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways."
      Regelmann J., Schuele T., Josupeit F.S., Horak J., Rose M., Entian K.-D., Thumm M., Wolf D.H.
      Mol. Biol. Cell 14:1652-1663(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Sequencing and comparison of yeast species to identify genes and regulatory elements."
      Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
      Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiUBP14_YEAST
    AccessioniPrimary (citable) accession number: P38237
    Secondary accession number(s): D6VQ57
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 31, 2006
    Last modified: October 1, 2014
    This is version 127 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 3040 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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 II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3