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Q96V54

- CREB_EMENI

UniProt

Q96V54 - CREB_EMENI

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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

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. ubiquitin-specific protease activity Source: ASPGD
  2. ubiquitin thiolesterase activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Protein family/group databases

MEROPSiC19.062.

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.
InParanoidiQ96V54.
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

        10         20         30         40         50
MGSFLKSFRK DVGSAAPSVG APPAKKEPQP LPMTPLEKML TELGPIRGDG
60 70 80 90 100
SDKFYGMENF GNTCYCNSIL QCLYYSVPFR EAVLNYPKRT PIEDLEAALA
110 120 130 140 150
KALRYQDPNA RLEAEALAEK QKAANSPRPG QPPNPQQKPE DKDSPEYKKK
160 170 180 190 200
LALQTLPLLE TTDNSVSYGI PESLFSSLKD MFESIVGSQS RIGIIRPQHF
210 220 230 240 250
LEVLRRENEM FRTAMHQDAH EFLNLLLNEV VVDVEKAAAK LLESPQPASD
260 270 280 290 300
VSDSVIPSSS SGSRTPNTTR WVHELFEGLL TSETQCLTCE KASQRDEVFL
310 320 330 340 350
DLSVDLEQHS SVTSCLRKFS AEEMLCERNK FHCDNCGGLQ EAEKRMKIKR
360 370 380 390 400
LPRILALHLK RFKYTEDLQR LQKLFHRVVY PYHLRLFNTT DDAEDPDRLY
410 420 430 440 450
ELYAVVVHIG GGPYHGHYVS IIKTQDRGWL LFDDEMVEPV DKNYVRNFFG
460 470 480 490 500
DKPGLACAYV LFYQETTMEA VMKEQEQENT EPPVEVNAST LKQNGFSSSA
510 520 530 540 550
TLAHAHSASQ VPTYEDHDRF TGLKRAPTAP QLSTHPEHTT TDSESLPSPA
560 570 580 590 600
PDPAPLTSLP PIPPIPETPP APLTSRKSDL QSKKERVKEE KERKAAEKEK
610 620 630 640 650
EKQRRKEIET RLKDRQRRED DDLKAALEAS KVSKEDEDRR NHAENGTSKK
660 670 680 690 700
NAGGLGRFRS LSQRLSTKES RTSLSRIPPL PNGNHTLSKV PDESEQTHPK
710 720 730 740 750
SPTPPAPLSR PASQPLNDDL LGSPRADTLA VPTEQEHIKN SKHDRSSHGK
760
WRSFSLRKKS FNILSS
Length:766
Mass (Da):86,229
Last modified:December 1, 2001 - v1
Checksum:iA29EC2B530092896
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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...

Protein family/group databases

MEROPSi C19.062.

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.
InParanoidi Q96V54.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 66 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