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Q96V54

- CREB_EMENI

UniProt

Q96V54 - CREB_EMENI

Protein

Ubiquitin carboxyl-terminal hydrolase creB

Gene

creB

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Ubiquitin thioesterase component of the regulatory network controlling carbon source utilization through ubiquitination and deubiquitination involving creA, creB, creC, creD and acrB. Deubiquitinates the creA catabolic repressor and the quinate permease qutD. Plays also a role in response to carbon starvation and the control of extracellular proteases activity.6 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 sitei64 – 641NucleophilePROSITE-ProRule annotation
    Active sitei417 – 4171Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. ubiquitin-specific protease activity Source: ASPGD
    3. ubiquitin thiolesterase activity Source: UniProtKB

    GO - Biological processi

    1. carbon catabolite repression of transcription Source: UniProtKB
    2. ubiquitin-dependent protein catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase creB (EC:3.4.19.12)
    Alternative name(s):
    Carbon catabolite repression protein B
    Deubiquitinating enzyme creB
    Ubiquitin thioesterase creB
    Ubiquitin-hydrolyzing enzyme creB
    Ubiquitin-specific-processing protease creB
    Gene namesi
    Name:creB
    Synonyms:molB
    ORF Names:AN3587
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome II

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 766766Ubiquitin carboxyl-terminal hydrolase creBPRO_0000395684Add
    BLAST

    Interactioni

    Subunit structurei

    Interacts with creA, creC and qutD.2 Publications

    Structurei

    3D structure databases

    ProteinModelPortaliQ96V54.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 466412USPAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili573 – 62048Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi547 – 57226Pro-richAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5533.
    HOGENOMiHOG000192482.
    KOiK11872.
    OMAiGDKPGMA.
    OrthoDBiEOG7TF7JV.

    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.

    Q96V54-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSFLKSFRK DVGSAAPSVG APPAKKEPQP LPMTPLEKML TELGPIRGDG    50
    SDKFYGMENF GNTCYCNSIL QCLYYSVPFR EAVLNYPKRT PIEDLEAALA 100
    KALRYQDPNA RLEAEALAEK QKAANSPRPG QPPNPQQKPE DKDSPEYKKK 150
    LALQTLPLLE TTDNSVSYGI PESLFSSLKD MFESIVGSQS RIGIIRPQHF 200
    LEVLRRENEM FRTAMHQDAH EFLNLLLNEV VVDVEKAAAK LLESPQPASD 250
    VSDSVIPSSS SGSRTPNTTR WVHELFEGLL TSETQCLTCE KASQRDEVFL 300
    DLSVDLEQHS SVTSCLRKFS AEEMLCERNK FHCDNCGGLQ EAEKRMKIKR 350
    LPRILALHLK RFKYTEDLQR LQKLFHRVVY PYHLRLFNTT DDAEDPDRLY 400
    ELYAVVVHIG GGPYHGHYVS IIKTQDRGWL LFDDEMVEPV DKNYVRNFFG 450
    DKPGLACAYV LFYQETTMEA VMKEQEQENT EPPVEVNAST LKQNGFSSSA 500
    TLAHAHSASQ VPTYEDHDRF TGLKRAPTAP QLSTHPEHTT TDSESLPSPA 550
    PDPAPLTSLP PIPPIPETPP APLTSRKSDL QSKKERVKEE KERKAAEKEK 600
    EKQRRKEIET RLKDRQRRED DDLKAALEAS KVSKEDEDRR NHAENGTSKK 650
    NAGGLGRFRS LSQRLSTKES RTSLSRIPPL PNGNHTLSKV PDESEQTHPK 700
    SPTPPAPLSR PASQPLNDDL LGSPRADTLA VPTEQEHIKN SKHDRSSHGK 750
    WRSFSLRKKS FNILSS 766
    Length:766
    Mass (Da):86,229
    Last modified:December 1, 2001 - v1
    Checksum:iA29EC2B530092896
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF327414 Genomic DNA. Translation: AAL04454.1.
    AACD01000061 Genomic DNA. Translation: EAA59795.1.
    BN001302 Genomic DNA. Translation: CBF75829.1.
    RefSeqiXP_661191.1. XM_656099.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00005157; CADANIAP00005157; CADANIAG00005157.
    GeneIDi2873003.
    KEGGiani:AN3587.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF327414 Genomic DNA. Translation: AAL04454.1 .
    AACD01000061 Genomic DNA. Translation: EAA59795.1 .
    BN001302 Genomic DNA. Translation: CBF75829.1 .
    RefSeqi XP_661191.1. XM_656099.1.

    3D structure databases

    ProteinModelPortali Q96V54.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00005157 ; CADANIAP00005157 ; CADANIAG00005157 .
    GeneIDi 2873003.
    KEGGi ani:AN3587.2.

    Phylogenomic databases

    eggNOGi COG5533.
    HOGENOMi HOG000192482.
    KOi K11872.
    OMAi GDKPGMA.
    OrthoDBi EOG7TF7JV.

    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. "Carbon catabolite repression in Aspergillus nidulans involves deubiquitination."
      Lockington R.A., Kelly J.M.
      Mol. Microbiol. 40:1311-1321(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
      Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
      , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
      Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    4. "The function of CreA, the carbon catabolite repressor of Aspergillus nidulans, is regulated at the transcriptional and post-transcriptional level."
      Strauss J., Horvath H.K., Abdallah B.M., Kindermann J., Mach R.L., Kubicek C.P.
      Mol. Microbiol. 32:169-178(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "The WD40-repeat protein CreC interacts with and stabilizes the deubiquitinating enzyme CreB in vivo in Aspergillus nidulans."
      Lockington R.A., Kelly J.M.
      Mol. Microbiol. 43:1173-1182(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CREC.
    6. "Molecular characterization and analysis of the acrB gene of Aspergillus nidulans: a gene identified by genetic interaction as a component of the regulatory network that includes the CreB deubiquitination enzyme."
      Boase N.A., Lockington R.A., Adams J.R., Rodbourn L., Kelly J.M.
      Genetics 164:95-104(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The interaction of induction, repression and starvation in the regulation of extracellular proteases in Aspergillus nidulans: evidence for a role for CreA in the response to carbon starvation."
      Katz M.E., Bernardo S.M., Cheetham B.F.
      Curr. Genet. 54:47-55(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Identifying target proteins of the CreB deubiquitination enzyme in the fungus Aspergillus nidulans."
      Kamlangdee N.
      Thesis (2008), University of Adelaide, Australia
      Cited for: INTERACTION WITH CREA AND QUTD, FUNCTION.

    Entry informationi

    Entry nameiCREB_EMENI
    AccessioniPrimary (citable) accession number: Q96V54
    Secondary accession number(s): C8V4E2, Q5B793
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 13, 2010
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 65 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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

    External Data

    Dasty 3