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P29747 (CREBA_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. 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:
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 names
Name:CrebA
Synonyms:Bbbf2
ORF Names:CG7450
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length516 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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'. Ref.1 Ref.2

Subunit structure

May bind DNA as heterodimers with other bZIP proteins.

Subcellular location

Nucleus.

Tissue specificity

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. Ref.2

Developmental stage

Present throughout development.

Sequence similarities

Belongs to the bZIP family.

Contains 1 bZIP (basic-leucine zipper) domain.

Sequence caution

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchitin-based larval cuticle pattern formation

Inferred from mutant phenotype PubMed 15901661PubMed 9006079. Source: FlyBase

dorsal/ventral pattern formation

Inferred from genetic interaction PubMed 9006079. Source: FlyBase

larval chitin-based cuticle development

Inferred from mutant phenotype PubMed 15901661. Source: FlyBase

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.2. Source: FlyBase

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 21041443. Source: FlyBase

salivary gland development

Inferred from mutant phenotype PubMed 9006079. Source: FlyBase

salivary gland morphogenesis

Non-traceable author statement PubMed 11598957. Source: FlyBase

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from direct assay Ref.1PubMed 19253394. Source: FlyBase

polytene chromosome

Inferred from direct assay PubMed 23578928. Source: FlyBase

   Molecular_functionDNA binding

Inferred from direct assay Ref.1. Source: FlyBase

enhancer sequence-specific DNA binding

Inferred from direct assay PubMed 21041443. Source: FlyBase

protein homodimerization activity

Inferred from sequence or structural similarity PubMed 12176927. Source: FlyBase

sequence-specific DNA binding

Inferred from direct assay Ref.2. Source: FlyBase

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.2. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 516516Cyclic AMP response element-binding protein A
PRO_0000076635

Regions

Domain441 – 50464bZIP
Region443 – 46321Basic motif By similarity
Region469 – 4768Leucine-zipper By similarity

Amino acid modifications

Modified residue751Phosphoserine Ref.8
Modified residue791Phosphoserine Ref.8
Modified residue821Phosphoserine Ref.8

Experimental info

Sequence conflict1141Y → C in CAA45771. Ref.1
Sequence conflict1141Y → C in AAA28427. Ref.2
Sequence conflict277 – 2782QQ → HE in CAA45771. Ref.1
Sequence conflict3051D → G in CAA45771. Ref.1
Sequence conflict3051D → G in AAR82739. Ref.7
Sequence conflict3161L → T in CAA45771. Ref.1
Sequence conflict338 – 36427APLSP…VRVSR → RHCRPTQPFPSLWPIQPAVS HPYGSA in CAA45771. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P29747 [UniParc].

Last modified May 10, 2004. Version 2.
Checksum: 25EA48DAE2ACE7E6

FASTA51656,342
        10         20         30         40         50         60 
MEFYDGDLKD IWDSDLDPES LKISPDHDMH DWLFDRDVKD PTVILNDKLI SDALLNGTQP 

        70         80         90        100        110        120 
IKTEHSYSLS SDVDSLPDSP KSLQAKIEDM DDECFPAISP KTATNGRVTI DPKYLTFHVP 

       130        140        150        160        170        180 
PTHATPISRL SSNPALNTSV ADLTRSSGLQ SLQAHQPHHG SGSSHVVVAN LEHFQLPQHL 

       190        200        210        220        230        240 
YDNDCSSSVS SLRDGSMSPD ICSDIEIDES AIKDEPMSPD SSCPASPTSQ ASSSQHQLSL 

       250        260        270        280        290        300 
NLAHLQSEML FEPKHCGLLL TASSNSNNSL IKSQQRQQQI LGQDNLLMAK MEIKSEKQST 

       310        320        330        340        350        360 
SNSSDKSHAH GYGIPLTPPS SLPSDDSEGN LSPEHLFAPL SPNATVSISV ANPAGGESSV 

       370        380        390        400        410        420 
RVSRTAASIT RSSSGSASAS GSSTSSTVTT TRQPIHTPLI SSQPKGSTGT LLLTEEEKRT 

       430        440        450        460        470        480 
LLAEGYPIPQ KLPLTKAEEK SLKKIRRKIK NKISAQESRR KKKEYMDQLE RRVEILVTEN 

       490        500        510 
HDYKKRLEGL EETNANLLSQ LHKLQALVSK HNVKKS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
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]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA42140.
A44494.
RefSeqNP_524087.3. NM_079363.4.
NP_996096.1. NM_206374.1.
UniGeneDm.6979.

3D structure databases

ProteinModelPortalP29747.
SMRP29747. Positions 443-494.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid65001. 3 interactions.
MINTMINT-883694.

Proteomic databases

PaxDbP29747.
PRIDEP29747.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0075557; FBpp0075311; FBgn0004396.
FBtr0075558; FBpp0089339; FBgn0004396.
GeneID39682.
KEGGdme:Dmel_CG7450.

Organism-specific databases

CTD39682.
FlyBaseFBgn0004396. CrebA.

Phylogenomic databases

eggNOGNOG294764.
InParanoidP29747.
OMAPDICSDI.
OrthoDBEOG7F24TZ.
PhylomeDBP29747.

Enzyme and pathway databases

SignaLinkP29747.

Gene expression databases

BgeeP29747.

Family and domain databases

InterProIPR004827. bZIP.
[Graphical view]
PfamPF00170. bZIP_1. 1 hit.
[Graphical view]
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCrebA. drosophila.
GenomeRNAi39682.
NextBio814852.
PROP29747.

Entry information

Entry nameCREBA_DROME
AccessionPrimary (citable) accession number: P29747
Secondary accession number(s): Q24282 expand/collapse secondary AC list , Q64M72, Q8MQX0, Q9VUQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 10, 2004
Last modified: April 16, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase