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Protein

Transcription factor AP-1

Gene

Jra

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

Functioni

Transcription factor that recognizes and binds to the enhancer heptamer motif 5'-TGA[CG]TCA-3' (PubMed:1696724, PubMed:2116361). Plays a role in dorsal closure (PubMed:9224723).3 Publications

GO - Molecular functioni

GO - Biological processi

  • dorsal appendage formation Source: FlyBase
  • dorsal closure Source: FlyBase
  • establishment of planar polarity Source: FlyBase
  • imaginal disc fusion, thorax closure Source: FlyBase
  • JNK cascade Source: FlyBase
  • MAPK cascade Source: FlyBase
  • micropyle formation Source: FlyBase
  • multicellular organism aging Source: FlyBase
  • negative regulation of antimicrobial humoral response Source: FlyBase
  • phagocytosis Source: FlyBase
  • positive regulation of heart contraction Source: FlyBase
  • positive regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • R3/R4 cell fate commitment Source: FlyBase
  • R7 cell fate commitment Source: FlyBase
  • regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • synaptic growth at neuromuscular junction Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
  • wound healing Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-DME-2559580. Oxidative Stress Induced Senescence.
R-DME-2871796. FCERI mediated MAPK activation.
R-DME-450341. Activation of the AP-1 family of transcription factors.
SignaLinkiP18289.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor AP-1
Alternative name(s):
Jun-related antigen
dJRA
dJun
Gene namesi
Name:Jra
Synonyms:jun
ORF Names:CG2275
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0001291. Jra.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • nucleus Source: FlyBase
  • transcription factor complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Death in mid to late embryogenesis with large anterior and dorsal holes.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 289289Transcription factor AP-1PRO_0000076437Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei82 – 821Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP18289.
PRIDEiP18289.

PTM databases

iPTMnetiP18289.

Expressioni

Tissue specificityi

During embryogenesis, expression is elevated in the amnioserosa, in the cells of the dorsolateral epidermis during and following germ-band retraction, in the cells at the leading dorsal edge of the epidermis and in the cells along the cephalic furrow (at protein level).1 Publication

Developmental stagei

Expressed during embryonic development.3 Publications

Gene expression databases

BgeeiP18289.
GenevisibleiP18289. DM.

Interactioni

Subunit structurei

Heterodimer with kay/Fra (PubMed:1696724, PubMed:2116361). The kay-Jra complex is bound more stably to the AP-1 site than either of the two proteins alone (PubMed:2116361). Interacts with Atf3; the interaction enhances the DNA-binding activity of Atf3 (PubMed:20023169).3 Publications

GO - Molecular functioni

  • protein heterodimerization activity Source: FlyBase
  • transcription factor binding Source: FlyBase

Protein-protein interaction databases

BioGridi61885. 46 interactions.
DIPiDIP-18982N.
IntActiP18289. 8 interactions.
MINTiMINT-278412.
STRINGi7227.FBpp0303456.

Structurei

3D structure databases

ProteinModelPortaliP18289.
SMRiP18289. Positions 216-273.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini212 – 27564bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni212 – 23928Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni240 – 26829Leucine-zipperPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0837. Eukaryota.
ENOG410XRWH. LUCA.
GeneTreeiENSGT00390000009929.
HOGENOMiHOG000047089.
InParanoidiP18289.
KOiK04448.
OrthoDBiEOG75MVXV.
PhylomeDBiP18289.

Family and domain databases

Gene3Di1.10.880.10. 1 hit.
InterProiIPR004827. bZIP.
IPR005643. JNK.
IPR002112. Leuzip_Jun.
IPR008917. TF_DNA-bd.
[Graphical view]
PfamiPF00170. bZIP_1. 1 hit.
PF03957. Jun. 1 hit.
[Graphical view]
PRINTSiPR00043. LEUZIPPRJUN.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMiSSF47454. SSF47454. 1 hit.
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P18289-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTPVSAAAN LSIQNAGSSG ATAIQIIPKT EPVGEEGPMS LDFQSPNLNT
60 70 80 90 100
STPNPNKRPG SLDLNSKSAK NKRIFAPLVI NSPDLSSKTV NTPDLEKILL
110 120 130 140 150
SNNLMQTPQP GKVFPTKAGP VTVEQLDFGR GFEEALHNLH TNSQAFPSAN
160 170 180 190 200
SAANSAANNT TAAAMTAVNN GISGGTFTYT NMTEGFSVIK DEPVNQASSP
210 220 230 240 250
TVNPIDMEAQ EKIKLERKRQ RNRVAASKCR KRKLERISKL EDRVKVLKGE
260 270 280
NVDLASIVKN LKDHVAQLKQ QVMEHIAAGC TVPPNSTDQ
Length:289
Mass (Da):31,021
Last modified:December 1, 2000 - v2
Checksum:iFCCA13A6D2AF32BF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti267 – 2682QL → HV in AAA28650 (PubMed:1696724).Curated
Sequence conflicti267 – 2682QL → HV in CAA73154 (PubMed:9224723).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36181 Genomic DNA. Translation: AAA28650.1.
X54144 mRNA. Translation: CAA38083.1.
Y12573 Genomic DNA. Translation: CAA73154.1.
AE013599 Genomic DNA. Translation: AAF58845.1.
AY058562 mRNA. Translation: AAL13791.1.
PIRiA36011. TVFFJD.
RefSeqiNP_476586.1. NM_057238.5.
NP_724882.1. NM_165739.2.
UniGeneiDm.3574.

Genome annotation databases

EnsemblMetazoaiFBtr0088410; FBpp0087498; FBgn0001291.
FBtr0088411; FBpp0087499; FBgn0001291.
GeneIDi36057.
KEGGidme:Dmel_CG2275.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36181 Genomic DNA. Translation: AAA28650.1.
X54144 mRNA. Translation: CAA38083.1.
Y12573 Genomic DNA. Translation: CAA73154.1.
AE013599 Genomic DNA. Translation: AAF58845.1.
AY058562 mRNA. Translation: AAL13791.1.
PIRiA36011. TVFFJD.
RefSeqiNP_476586.1. NM_057238.5.
NP_724882.1. NM_165739.2.
UniGeneiDm.3574.

3D structure databases

ProteinModelPortaliP18289.
SMRiP18289. Positions 216-273.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61885. 46 interactions.
DIPiDIP-18982N.
IntActiP18289. 8 interactions.
MINTiMINT-278412.
STRINGi7227.FBpp0303456.

PTM databases

iPTMnetiP18289.

Proteomic databases

PaxDbiP18289.
PRIDEiP18289.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088410; FBpp0087498; FBgn0001291.
FBtr0088411; FBpp0087499; FBgn0001291.
GeneIDi36057.
KEGGidme:Dmel_CG2275.

Organism-specific databases

CTDi36057.
FlyBaseiFBgn0001291. Jra.

Phylogenomic databases

eggNOGiKOG0837. Eukaryota.
ENOG410XRWH. LUCA.
GeneTreeiENSGT00390000009929.
HOGENOMiHOG000047089.
InParanoidiP18289.
KOiK04448.
OrthoDBiEOG75MVXV.
PhylomeDBiP18289.

Enzyme and pathway databases

ReactomeiR-DME-2559580. Oxidative Stress Induced Senescence.
R-DME-2871796. FCERI mediated MAPK activation.
R-DME-450341. Activation of the AP-1 family of transcription factors.
SignaLinkiP18289.

Miscellaneous databases

GenomeRNAii36057.
PROiP18289.

Gene expression databases

BgeeiP18289.
GenevisibleiP18289. DM.

Family and domain databases

Gene3Di1.10.880.10. 1 hit.
InterProiIPR004827. bZIP.
IPR005643. JNK.
IPR002112. Leuzip_Jun.
IPR008917. TF_DNA-bd.
[Graphical view]
PfamiPF00170. bZIP_1. 1 hit.
PF03957. Jun. 1 hit.
[Graphical view]
PRINTSiPR00043. LEUZIPPRJUN.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMiSSF47454. SSF47454. 1 hit.
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Drosophila homolog of the mammalian jun oncogene is expressed during embryonic development and activates transcription in mammalian cells."
    Zhang K., Chaillet J.R., Perkins L.A., Halazonetis T.D., Perrimon N.
    Proc. Natl. Acad. Sci. U.S.A. 87:6281-6285(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH KAY, DEVELOPMENTAL STAGE.
    Strain: Oregon-R.
  2. "The Drosophila Fos-related AP-1 protein is a developmentally regulated transcription factor."
    Perkins K.K., Admon A., Patel N., Tjian R.
    Genes Dev. 4:822-834(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH KAY, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  3. "Jun in Drosophila development: redundant and nonredundant functions and regulation by two MAPK signal transduction pathways."
    Kockel L., Zeitlinger J., Staszewski L., Mlodzik M., Bohmann D.
    Genes Dev. 11:1748-1758(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    Strain: Oregon-R.
  4. "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.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. "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].
    Strain: Berkeley.
    Tissue: Embryo.
  7. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
    Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
    Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Interaction between Drosophila bZIP proteins Atf3 and Jun prevents replacement of epithelial cells during metamorphosis."
    Sekyrova P., Bohmann D., Jindra M., Uhlirova M.
    Development 137:141-150(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATF3.

Entry informationi

Entry nameiJRA_DROME
AccessioniPrimary (citable) accession number: P18289
Secondary accession number(s): Q0E9D8, Q9V5G4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: December 1, 2000
Last modified: June 8, 2016
This is version 168 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, Direct protein sequencing, Reference proteome

Documents

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

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 one 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.