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P29747

- CREBA_DROME

UniProt

P29747 - CREBA_DROME

Protein

Cyclic AMP response element-binding protein A

Gene

CrebA

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (10 May 2004)
      Previous versions | rss
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    Functioni

    Transcriptional activator. Binds to fat body-specific enhancers of alcohol dehydrogenase (ADH) and yolk protein genes. BBF-2 may play a role in fat body gene expression. It binds the consensus sequence 5'-T[AC]NACGTAN[TG]C-3'.2 Publications

    GO - Molecular functioni

    1. DNA binding Source: FlyBase
    2. enhancer sequence-specific DNA binding Source: FlyBase
    3. protein homodimerization activity Source: FlyBase
    4. sequence-specific DNA binding Source: FlyBase
    5. sequence-specific DNA binding transcription factor activity Source: FlyBase

    GO - Biological processi

    1. chitin-based larval cuticle pattern formation Source: FlyBase
    2. dorsal/ventral pattern formation Source: FlyBase
    3. larval chitin-based cuticle development Source: FlyBase
    4. positive regulation of transcription, DNA-templated Source: FlyBase
    5. positive regulation of transcription from RNA polymerase II promoter Source: FlyBase
    6. salivary gland development Source: FlyBase
    7. salivary gland morphogenesis Source: FlyBase
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    SignaLinkiP29747.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclic AMP response element-binding protein A
    Short name:
    cAMP response element-binding protein A
    Short name:
    dCREB-A
    Alternative name(s):
    Box B-binding factor 2
    Short name:
    BBF-2
    Gene namesi
    Name:CrebA
    Synonyms:Bbbf2
    ORF Names:CG7450
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0004396. CrebA.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: FlyBase
    2. polytene chromosome Source: FlyBase

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 516516Cyclic AMP response element-binding protein APRO_0000076635Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei75 – 751Phosphoserine1 Publication
    Modified residuei79 – 791Phosphoserine1 Publication
    Modified residuei82 – 821Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP29747.
    PRIDEiP29747.

    Expressioni

    Tissue specificityi

    In all cell types examined, including developing salivary gland in embryos and in adults, brain and optic lobe cell bodies, salivary gland, midgut epithelial cells of the cardia, female ovarian columnar follicle cells and male seminal vesicle, ejaculatory duct, and ejaculatory bulb.1 Publication

    Developmental stagei

    Present throughout development.

    Gene expression databases

    BgeeiP29747.

    Interactioni

    Subunit structurei

    May bind DNA as heterodimers with other bZIP proteins.

    Protein-protein interaction databases

    BioGridi65001. 3 interactions.
    MINTiMINT-883694.

    Structurei

    3D structure databases

    ProteinModelPortaliP29747.
    SMRiP29747. Positions 448-492.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini441 – 50464bZIPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni443 – 46321Basic motifPROSITE-ProRule annotationAdd
    BLAST
    Regioni469 – 4768Leucine-zipperPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the bZIP family.Curated
    Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG294764.
    InParanoidiP29747.
    OMAiPDICSDI.
    OrthoDBiEOG7F24TZ.
    PhylomeDBiP29747.

    Family and domain databases

    InterProiIPR004827. bZIP.
    [Graphical view]
    PfamiPF00170. bZIP_1. 1 hit.
    [Graphical view]
    SMARTiSM00338. BRLZ. 1 hit.
    [Graphical view]
    PROSITEiPS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P29747-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEFYDGDLKD IWDSDLDPES LKISPDHDMH DWLFDRDVKD PTVILNDKLI    50
    SDALLNGTQP IKTEHSYSLS SDVDSLPDSP KSLQAKIEDM DDECFPAISP 100
    KTATNGRVTI DPKYLTFHVP PTHATPISRL SSNPALNTSV ADLTRSSGLQ 150
    SLQAHQPHHG SGSSHVVVAN LEHFQLPQHL YDNDCSSSVS SLRDGSMSPD 200
    ICSDIEIDES AIKDEPMSPD SSCPASPTSQ ASSSQHQLSL NLAHLQSEML 250
    FEPKHCGLLL TASSNSNNSL IKSQQRQQQI LGQDNLLMAK MEIKSEKQST 300
    SNSSDKSHAH GYGIPLTPPS SLPSDDSEGN LSPEHLFAPL SPNATVSISV 350
    ANPAGGESSV RVSRTAASIT RSSSGSASAS GSSTSSTVTT TRQPIHTPLI 400
    SSQPKGSTGT LLLTEEEKRT LLAEGYPIPQ KLPLTKAEEK SLKKIRRKIK 450
    NKISAQESRR KKKEYMDQLE RRVEILVTEN HDYKKRLEGL EETNANLLSQ 500
    LHKLQALVSK HNVKKS 516
    Length:516
    Mass (Da):56,342
    Last modified:May 10, 2004 - v2
    Checksum:i25EA48DAE2ACE7E6
    GO

    Sequence cautioni

    The sequence AAU21396.1 differs from that shown. Reason: Intron retention.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti114 – 1141Y → C in CAA45771. (PubMed:1532159)Curated
    Sequence conflicti114 – 1141Y → C in AAA28427. (PubMed:1508208)Curated
    Sequence conflicti277 – 2782QQ → HE in CAA45771. (PubMed:1532159)Curated
    Sequence conflicti305 – 3051D → G in CAA45771. (PubMed:1532159)Curated
    Sequence conflicti305 – 3051D → G in AAR82739. 1 PublicationCurated
    Sequence conflicti316 – 3161L → T in CAA45771. (PubMed:1532159)Curated
    Sequence conflicti338 – 36427APLSP…VRVSR → RHCRPTQPFPSLWPIQPAVS HPYGSA in CAA45771. (PubMed:1532159)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64429 mRNA. Translation: CAA45771.1.
    M87038 mRNA. Translation: AAA28427.1.
    AE014296 Genomic DNA. Translation: AAF49621.2.
    AY122251 mRNA. Translation: AAU21396.1. Sequence problems.
    BT011074 mRNA. Translation: AAR82739.1.
    PIRiA42140.
    A44494.
    RefSeqiNP_524087.3. NM_079363.4.
    NP_996096.1. NM_206374.1.
    UniGeneiDm.6979.

    Genome annotation databases

    EnsemblMetazoaiFBtr0075557; FBpp0075311; FBgn0004396.
    FBtr0075558; FBpp0089339; FBgn0004396.
    GeneIDi39682.
    KEGGidme:Dmel_CG7450.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64429 mRNA. Translation: CAA45771.1 .
    M87038 mRNA. Translation: AAA28427.1 .
    AE014296 Genomic DNA. Translation: AAF49621.2 .
    AY122251 mRNA. Translation: AAU21396.1 . Sequence problems.
    BT011074 mRNA. Translation: AAR82739.1 .
    PIRi A42140.
    A44494.
    RefSeqi NP_524087.3. NM_079363.4.
    NP_996096.1. NM_206374.1.
    UniGenei Dm.6979.

    3D structure databases

    ProteinModelPortali P29747.
    SMRi P29747. Positions 448-492.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 65001. 3 interactions.
    MINTi MINT-883694.

    Proteomic databases

    PaxDbi P29747.
    PRIDEi P29747.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0075557 ; FBpp0075311 ; FBgn0004396 .
    FBtr0075558 ; FBpp0089339 ; FBgn0004396 .
    GeneIDi 39682.
    KEGGi dme:Dmel_CG7450.

    Organism-specific databases

    CTDi 39682.
    FlyBasei FBgn0004396. CrebA.

    Phylogenomic databases

    eggNOGi NOG294764.
    InParanoidi P29747.
    OMAi PDICSDI.
    OrthoDBi EOG7F24TZ.
    PhylomeDBi P29747.

    Enzyme and pathway databases

    SignaLinki P29747.

    Miscellaneous databases

    ChiTaRSi CrebA. drosophila.
    GenomeRNAii 39682.
    NextBioi 814852.
    PROi P29747.

    Gene expression databases

    Bgeei P29747.

    Family and domain databases

    InterProi IPR004827. bZIP.
    [Graphical view ]
    Pfami PF00170. bZIP_1. 1 hit.
    [Graphical view ]
    SMARTi SM00338. BRLZ. 1 hit.
    [Graphical view ]
    PROSITEi PS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A Drosophila CREB/ATF transcriptional activator binds to both fat body- and liver-specific regulatory elements."
      Abel T., Bhatt R., Maniatis T.
      Genes Dev. 6:466-480(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Strain: Oregon-R.
      Tissue: Embryo.
    2. "A cyclic AMP-responsive element-binding transcriptional activator in Drosophila melanogaster, dCREB-A, is a member of the leucine zipper family."
      Smolik S.M., Rose T.M., Goodman R.H.
      Mol. Cell. Biol. 12:4123-4131(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Embryo.
    3. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-18.
      Strain: Berkeley.
      Tissue: Embryo.
    6. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
      Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 221-516.
      Strain: Berkeley.
      Tissue: Embryo.
    8. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-79 AND SER-82, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiCREBA_DROME
    AccessioniPrimary (citable) accession number: P29747
    Secondary accession number(s): Q24282
    , Q64M72, Q8MQX0, Q9VUQ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: May 10, 2004
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3