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Q96V54 (CREB_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:creB
Synonyms:molB
ORF Names:AN3587
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length766 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Catalytic activity

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).

Subunit structure

Interacts with creA, creC and qutD. Ref.5 Ref.8

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 USP domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 766766Ubiquitin carboxyl-terminal hydrolase creB
PRO_0000395684

Regions

Domain55 – 466412USP
Coiled coil573 – 62048 Potential
Compositional bias547 – 57226Pro-rich

Sites

Active site641Nucleophile By similarity
Active site4171Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q96V54 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: A29EC2B530092896

FASTA76686,229
        10         20         30         40         50         60 
MGSFLKSFRK DVGSAAPSVG APPAKKEPQP LPMTPLEKML TELGPIRGDG SDKFYGMENF 

        70         80         90        100        110        120 
GNTCYCNSIL QCLYYSVPFR EAVLNYPKRT PIEDLEAALA KALRYQDPNA RLEAEALAEK 

       130        140        150        160        170        180 
QKAANSPRPG QPPNPQQKPE DKDSPEYKKK LALQTLPLLE TTDNSVSYGI PESLFSSLKD 

       190        200        210        220        230        240 
MFESIVGSQS RIGIIRPQHF LEVLRRENEM FRTAMHQDAH EFLNLLLNEV VVDVEKAAAK 

       250        260        270        280        290        300 
LLESPQPASD VSDSVIPSSS SGSRTPNTTR WVHELFEGLL TSETQCLTCE KASQRDEVFL 

       310        320        330        340        350        360 
DLSVDLEQHS SVTSCLRKFS AEEMLCERNK FHCDNCGGLQ EAEKRMKIKR LPRILALHLK 

       370        380        390        400        410        420 
RFKYTEDLQR LQKLFHRVVY PYHLRLFNTT DDAEDPDRLY ELYAVVVHIG GGPYHGHYVS 

       430        440        450        460        470        480 
IIKTQDRGWL LFDDEMVEPV DKNYVRNFFG DKPGLACAYV LFYQETTMEA VMKEQEQENT 

       490        500        510        520        530        540 
EPPVEVNAST LKQNGFSSSA TLAHAHSASQ VPTYEDHDRF TGLKRAPTAP QLSTHPEHTT 

       550        560        570        580        590        600 
TDSESLPSPA PDPAPLTSLP PIPPIPETPP APLTSRKSDL QSKKERVKEE KERKAAEKEK 

       610        620        630        640        650        660 
EKQRRKEIET RLKDRQRRED DDLKAALEAS KVSKEDEDRR NHAENGTSKK NAGGLGRFRS 

       670        680        690        700        710        720 
LSQRLSTKES RTSLSRIPPL PNGNHTLSKV PDESEQTHPK SPTPPAPLSR PASQPLNDDL 

       730        740        750        760 
LGSPRADTLA VPTEQEHIKN SKHDRSSHGK WRSFSLRKKS FNILSS 

« Hide

References

« Hide 'large scale' references
[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]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF327414 Genomic DNA. Translation: AAL04454.1.
AACD01000061 Genomic DNA. Translation: EAA59795.1.
BN001302 Genomic DNA. Translation: CBF75829.1.
RefSeqXP_661191.1. XM_656099.1.

3D structure databases

ProteinModelPortalQ96V54.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00005157; CADANIAP00005157; CADANIAG00005157.
GeneID2873003.
KEGGani:AN3587.2.

Phylogenomic databases

eggNOGCOG5533.
HOGENOMHOG000192482.
KOK11872.
OMAGDKPGMA.
OrthoDBEOG7TF7JV.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCREB_EMENI
AccessionPrimary (citable) accession number: Q96V54
Secondary accession number(s): C8V4E2, Q5B793
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: December 1, 2001
Last modified: February 19, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries