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P18289 (JRA_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 141. 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:
Transcription factor AP-1
Alternative name(s):
Jun-related antigen
dJRA
dJun
Gene names
Name:Jra
Synonyms:jun
ORF Names:CG2275
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription factor that recognizes and binds to the enhancer heptamer motif 5'-TGA[CG]TCA-3'.

Subunit structure

AP-1/dJRA interacts with AP-1/dFra to form a dimer. The dFra-dJRA complex is bound more stably to the AP-1 site than either of the two proteins alone.

Subcellular location

Nucleus.

Developmental stage

Expressed during embryonic development.

Sequence similarities

Belongs to the bZIP family. Jun subfamily.

Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processJNK cascade

Inferred from mutant phenotype PubMed 9224721. Source: FlyBase

R3/R4 cell fate commitment

Traceable author statement PubMed 12414186. Source: FlyBase

R7 cell fate commitment

Traceable author statement PubMed 8946916. Source: FlyBase

dorsal appendage formation

Inferred from mutant phenotype PubMed 11543614. Source: FlyBase

dorsal closure

Non-traceable author statement PubMed 12000787. Source: FlyBase

imaginal disc fusion, thorax closure

Inferred from mutant phenotype PubMed 16930585. Source: FlyBase

micropyle formation

Inferred from mutant phenotype PubMed 11543614. Source: FlyBase

negative regulation of antimicrobial humoral response

Inferred from mutant phenotype PubMed 17803358. Source: FlyBase

phagocytosis, engulfment

Inferred from mutant phenotype PubMed 16336044. Source: FlyBase

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.2. Source: FlyBase

synaptic growth at neuromuscular junction

Inferred from genetic interaction PubMed 18832361. Source: FlyBase

wound healing

Inferred from mutant phenotype PubMed 19884309. Source: FlyBase

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 11509232. Source: FlyBase

transcription factor complex

Inferred from physical interaction Ref.2. Source: FlyBase

   Molecular_functionprotein heterodimerization activity

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

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay Ref.2. Source: FlyBase

transcription factor binding

Traceable author statement PubMed 12000787. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 289289Transcription factor AP-1
PRO_0000076437

Regions

Domain212 – 27564bZIP
Region212 – 23928Basic motif By similarity
Region240 – 26829Leucine-zipper By similarity

Amino acid modifications

Modified residue821Phosphoserine Ref.7

Experimental info

Sequence conflict267 – 2682QL → HV in AAA28650. Ref.1
Sequence conflict267 – 2682QL → HV in CAA73154. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P18289 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: FCCA13A6D2AF32BF

FASTA28931,021
        10         20         30         40         50         60 
MKTPVSAAAN LSIQNAGSSG ATAIQIIPKT EPVGEEGPMS LDFQSPNLNT STPNPNKRPG 

        70         80         90        100        110        120 
SLDLNSKSAK NKRIFAPLVI NSPDLSSKTV NTPDLEKILL SNNLMQTPQP GKVFPTKAGP 

       130        140        150        160        170        180 
VTVEQLDFGR GFEEALHNLH TNSQAFPSAN SAANSAANNT TAAAMTAVNN GISGGTFTYT 

       190        200        210        220        230        240 
NMTEGFSVIK DEPVNQASSP TVNPIDMEAQ EKIKLERKRQ RNRVAASKCR KRKLERISKL 

       250        260        270        280 
EDRVKVLKGE NVDLASIVKN LKDHVAQLKQ QVMEHIAAGC TVPPNSTDQ 

« Hide

References

« Hide 'large scale' references
[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].
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.
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].
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. 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.
[5]"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.
[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, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRTVFFJD. A36011.
RefSeqNP_476586.1. NM_057238.4.
NP_724882.1. NM_165739.2.
UniGeneDm.3574.

3D structure databases

ProteinModelPortalP18289.
SMRP18289. Positions 216-273.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-18982N.
IntActP18289. 8 interactions.
MINTMINT-278412.

Proteomic databases

PaxDbP18289.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0088410; FBpp0087498; FBgn0001291.
FBtr0088411; FBpp0087499; FBgn0001291.
GeneID36057.
KEGGdme:Dmel_CG2275.

Organism-specific databases

CTD36057.
FlyBaseFBgn0001291. Jra.

Phylogenomic databases

eggNOGNOG283376.
GeneTreeENSGT00390000009929.
HOGENOMHOG000047089.
InParanoidP18289.
OMAKDHVAQL.
OrthoDBEOG4KWH8S.
PhylomeDBP18289.

Gene expression databases

BgeeP18289.
GermOnlineCG2275. Drosophila melanogaster.

Family and domain databases

Gene3D1.10.880.10. 1 hit.
InterProIPR004827. bZIP.
IPR008917. Euk_TF_DNA-bd.
IPR005643. JNK.
IPR002112. Leuzip_Jun.
[Graphical view]
PfamPF00170. bZIP_1. 1 hit.
PF03957. Jun. 1 hit.
[Graphical view]
PRINTSPR00043. LEUZIPPRJUN.
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi36057.
NextBio796620.

Entry information

Entry nameJRA_DROME
AccessionPrimary (citable) accession number: P18289
Secondary accession number(s): Q0E9D8, Q9V5G4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: December 1, 2000
Last modified: April 3, 2013
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families