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Protein

Cyclic AMP response element-binding protein A

Gene

CrebA

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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.
ExpressionAtlasiP29747. differential.

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

        10         20         30         40         50
MEFYDGDLKD IWDSDLDPES LKISPDHDMH DWLFDRDVKD PTVILNDKLI
60 70 80 90 100
SDALLNGTQP IKTEHSYSLS SDVDSLPDSP KSLQAKIEDM DDECFPAISP
110 120 130 140 150
KTATNGRVTI DPKYLTFHVP PTHATPISRL SSNPALNTSV ADLTRSSGLQ
160 170 180 190 200
SLQAHQPHHG SGSSHVVVAN LEHFQLPQHL YDNDCSSSVS SLRDGSMSPD
210 220 230 240 250
ICSDIEIDES AIKDEPMSPD SSCPASPTSQ ASSSQHQLSL NLAHLQSEML
260 270 280 290 300
FEPKHCGLLL TASSNSNNSL IKSQQRQQQI LGQDNLLMAK MEIKSEKQST
310 320 330 340 350
SNSSDKSHAH GYGIPLTPPS SLPSDDSEGN LSPEHLFAPL SPNATVSISV
360 370 380 390 400
ANPAGGESSV RVSRTAASIT RSSSGSASAS GSSTSSTVTT TRQPIHTPLI
410 420 430 440 450
SSQPKGSTGT LLLTEEEKRT LLAEGYPIPQ KLPLTKAEEK SLKKIRRKIK
460 470 480 490 500
NKISAQESRR KKKEYMDQLE RRVEILVTEN HDYKKRLEGL EETNANLLSQ
510
LHKLQALVSK HNVKKS
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.Intron retention.Curated

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 (Ref. 7) Curated
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:
EMBLi
GenBanki
DDBJi
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_079363.5.
NP_996096.1. NM_206374.2.
UniGeneiDm.6979.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_079363.5.
NP_996096.1. NM_206374.2.
UniGeneiDm.6979.

3D structure databases

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

Protein-protein interaction databases

BioGridi65001. 3 interactions.
MINTiMINT-883694.

Proteomic databases

PaxDbiP29747.
PRIDEiP29747.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi39682.
FlyBaseiFBgn0004396. CrebA.

Phylogenomic databases

eggNOGiNOG294764.
InParanoidiP29747.
OMAiPDICSDI.
OrthoDBiEOG7F24TZ.
PhylomeDBiP29747.

Enzyme and pathway databases

SignaLinkiP29747.

Miscellaneous databases

ChiTaRSiCrebA. fly.
GenomeRNAii39682.
NextBioi814852.
PROiP29747.

Gene expression databases

BgeeiP29747.
ExpressionAtlasiP29747. differential.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 135 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.