ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P05412


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name JUN_HUMAN
Primary accession number P05412
Secondary accession number Q96G93
Integrated into Swiss-Prot on November 1, 1988
Sequence was last modified on October 1, 1989 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 130)
Name and origin of the protein
Protein name Transcription factor AP-1
Synonyms Activator protein 1
AP1
Proto-oncogene c-jun
V-jun avian sarcoma virus 17 oncogene homolog
p39
Gene name
Name: JUN
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1073/pnas.85.23.9148; PubMed=3194415 [NCBI, ExPASy, EBI, Israel, Japan]
Hattori K., Angel P., le Beau M.M., Karin M.;
"Structure and chromosomal localization of the functional intronless human JUN protooncogene.";
Proc. Natl. Acad. Sci. U.S.A. 85:9148-9152(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
DOI=10.1126/science.2825349; PubMed=2825349 [NCBI, ExPASy, EBI, Israel, Japan]
Bohmann D., Bos T.J., Admon A., Nishimura T., Vogt P.K., Tjian R.;
"Human proto-oncogene c-jun encodes a DNA binding protein with structural and functional properties of transcription factor AP-1.";
Science 238:1386-1392(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=B-cell, Ovary, Testis, and Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PHOSPHORYLATION.
DOI=10.1093/nar/21.5.1289; PubMed=8464713 [NCBI, ExPASy, EBI, Israel, Japan]
Bannister A.J., Gottlieb T.M., Kouzarides T., Jackson S.P.;
"c-Jun is phosphorylated by the DNA-dependent protein kinase in vitro; definition of the minimal kinase recognition motif.";
Nucleic Acids Res. 21:1289-1295(1993).
[8]
INTERACTION WITH TCF20.
DOI=10.1074/jbc.271.30.18231; PubMed=8663478 [NCBI, ExPASy, EBI, Israel, Japan]
Kirstein M., Sanz L., Moscat J., Diaz-Meco M.T., Saus J.;
"Cross-talk between different enhancer elements during mitogenic induction of the human stromelysin-1 gene.";
J. Biol. Chem. 271:18231-18236(1996).
[9]
INTERACTION WITH COPS5.
DOI=10.1038/383453a0; PubMed=8837781 [NCBI, ExPASy, EBI, Israel, Japan]
Claret F.-X., Hibi M., Dhut S., Toda T., Karin M.;
"A new group of conserved coactivators that increase the specificity of AP-1 transcription factors.";
Nature 383:453-457(1996).
[10]
INTERACTION WITH SPIB.
DOI=10.1074/jbc.274.16.11115; PubMed=10196196 [NCBI, ExPASy, EBI, Israel, Japan]
Rao S., Matsumura A., Yoon J., Simon M.C.;
"SPI-B activates transcription via a unique proline, serine, and threonine domain and exhibits DNA binding affinity differences from PU.1.";
J. Biol. Chem. 274:11115-11124(1999).
[11]
INTERACTION WITH BATF3.
DOI=10.1074/jbc.M205048200; PubMed=12087103 [NCBI, ExPASy, EBI, Israel, Japan]
Bower K.E., Zeller R.W., Wachsman W., Martinez T., McGuire K.L.;
"Correlation of transcriptional repression by p21(SNFT) with changes in DNA.NF-AT complex interactions.";
J. Biol. Chem. 277:34967-34977(2002).
[12]
INTERACTION WITH BATF3.
DOI=10.1038/sj.onc.1208109; PubMed=15467742 [NCBI, ExPASy, EBI, Israel, Japan]
Bower K.E., Fritz J.M., McGuire K.L.;
"Transcriptional repression of MMP-1 by p21SNFT and reduced in vitro invasiveness of hepatocarcinoma cells.";
Oncogene 23:8805-8814(2004).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-63; SER-73; THR-239 AND SER-243, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 257-313 OF COMPLEX WITH FOS.
DOI=10.1038/373257a0; PubMed=7816143 [NCBI, ExPASy, EBI, Israel, Japan]
Glover J.N., Harrison S.C.;
"Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA.";
Nature 373:257-261(1995).
[16]
STRUCTURE BY NMR OF 276-314.
DOI=10.1074/jbc.271.23.13663; PubMed=8662824 [NCBI, ExPASy, EBI, Israel, Japan]
Junius F.K., O'Donoghue S.I., Nilges M., Weiss A.S., King G.F.;
"High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer.";
J. Biol. Chem. 271:13663-13667(1996).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J04111; AAA59197.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019759; AAV38564.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY217548; AAO22993.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136985; CAC10201.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002646; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
BC006175; AAH06175.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009874; AAH09874.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC068522; AAH68522.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00008965; -.
PIR A31264; TVHUJN.
RefSeq NP_002219.1; -.
UniGene Hs.714791
3D structure databases
PDB
1A02; X-ray; 2.70 A; J=254-308.[ExPASy / RCSB / EBI]
1FOS; X-ray; 3.05 A; F/H=254-315.[ExPASy / RCSB / EBI]
1JNM; X-ray; 2.20 A; A/B=254-315.[ExPASy / RCSB / EBI]
1JUN; NMR; -; A/B=276-314.[ExPASy / RCSB / EBI]
1S9K; X-ray; 3.10 A; E=257-308.[ExPASy / RCSB / EBI]
1T2K; X-ray; 3.00 A; C=254-314.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A02; -.
1FOS; -.
1JNM; -.
1JUN; -.
1S9K; -.
1T2K; -.
ModBase P05412.
Protein-protein interaction databases
DIP DIP:1054N; -.
DIP:5961N; -.
IntAct P05412; 9.
PTM databases
PhosphoSite P05412; -.
Enzyme and pathway databases
Pathway_Interaction_DB bcr_5pathway; BCR signaling pathway.
nfat_tfpathway; Calcineurin-regulated NFAT-dependent transcription in lymphocytes.
tcrcalciumpathway; Calcium signaling in the CD4+ TCR pathway.
cd8tcrdownstreampathway; Downstream signaling in naive CD8+ T cells.
endothelinpathway; Endothelins.
fcer1pathway; Fc-epsilon receptor I signaling in mast cells.
fgf_pathway; FGF signaling pathway.
hnf3apathway; FOXA1 transcription factor network.
hif1_tfpathway; HIF-1-alpha transcription factor network.
il1pathway; IL1-mediated signaling events.
il12_stat4pathway; IL12 signaling mediated by STAT4.
il2_1pathway; IL2-mediated signaling events.
il6_7pathway; IL6-mediated signaling events.
tcrjnkpathway; JNK signaling in the CD4+ TCR pathway.
lysophospholipid_pathway; LPA receptor mediated events.
avb3_opn_pathway; Osteopontin-mediated events.
pdgfrapathway; PDGFR-alpha signaling pathway.
ps1pathway; Presenilin action in Notch and Wnt signaling.
ar_tf_pathway; Regulation of Androgen receptor activity.
smad2_3nuclearpathway; Regulation of nuclear SMAD2/3 signaling.
telomerasepathway; Regulation of Telomerase.
s1p_s1p2_pathway; S1P2 pathway.
met_pathway; Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
ret_pathway; Signaling events regulated by Ret tyrosine kinase.
p38alphabetadownstreampathway; Signaling mediated by p38-alpha and p38-beta.
Reactome REACT_6900; Signaling in Immune system.
Organism-specific databases
GeneCards GC01M058958; -.
H-InvDB HIX0000635; -.
HGNC HGNC:6204; JUN.
GenAtlas JUN.
HPA CAB003801; -.
CAB007780; -.
MIM 165160; gene. [NCBI / EBI]
PharmGKB PA30006; -.
Gene expression databases
ArrayExpress P05412; -.
Bgee P05412; -.
CleanEx HS_JUN; -.
GermOnline ENSG00000177606; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0000228; Cellular component: nuclear chromosome (traceable author statement from ProtInc).
GO:0010843; Molecular function: promoter binding (inferred from direct assay from UniProtKB).
GO:0046983; Molecular function: protein dimerization activity (inferred from electronic annotation from InterPro).
GO:0070412; Molecular function: R-SMAD binding (inferred from physical interaction from UniProtKB).
GO:0005100; Molecular function: Rho GTPase activator activity (inferred from direct assay from UniProtKB).
GO:0003702; Molecular function: RNA polymerase II transcription factor activity (traceable author statement from ProtInc).
GO:0003700; Molecular function: transcription factor activity (inferred from direct assay from UniProtKB).
GO:0008134; Molecular function: transcription factor binding (inferred from physical interaction from UniProtKB).
GO:0007184; Biological process: SMAD protein nuclear translocation (inferred from direct assay from UniProtKB).
GO:0060395; Biological process: SMAD protein signal transduction (inferred from direct assay from UniProtKB).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR011616; bZIP_1.
IPR015558; C_Jun.
IPR005643; JNK.
IPR002112; Leuzip_Jun.
IPR004827; TF_bZIP.
Graphical view of domain structure.
PANTHER PTHR11462:SF8; C_Jun; 1.
Pfam PF00170; bZIP_1; 1.
PF03957; Jun; 1.
Pfam graphical view of domain structure.
PRINTS PR00043; LEUZIPPRJUN.
SMART SM00338; BRLZ; 1.
SMART graphical view of domain structure.
PROSITE PS50217; BZIP; 1.
PS00036; BZIP_BASIC; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P05412; -.
Genome annotation databases
Ensembl ENSG00000177606; Homo sapiens. [Contig view]
GeneID 3725; -.
KEGG hsa:3725; -.
Phylogenomic databases
HOGENOM P05412; -.
HOVERGEN P05412; -.
OMA P05412; KPHLRNK.
Other
DrugBank DB01169; Arsenic trioxide.
DB01029; Irbesartan.
DB00570; Vinblastine.
NextBio 14583; -.
SOURCE JUN; Homo sapiens.
ProtoNet P05412.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   331  331     Transcription factor AP-1. PRO_0000076429
DOMAIN   280   308  29     Leucine-zipper. 
DNA_BIND   257   276  20     Basic motif. 
MOD_RES   58    58        Phosphoserine. 
MOD_RES   63    63        Phosphoserine; by MAPK8. 
MOD_RES   73    73        Phosphoserine; by MAPK8. 
MOD_RES   239   239        Phosphothreonine. 
MOD_RES   243   243        Phosphoserine. 
VARIANT   297   297  1     T -> M (in dbSNP:rs9989 [NCBI]). VAR_012070 [3D]
CONFLICT   11    11        D -> G (in Ref. 2; AA sequence). 
CONFLICT   14    14        L -> F (in Ref. 2; AA sequence). 
CONFLICT   80    80        I -> V (in Ref. 2; AA sequence). 
HELIX   255   306  52      
Sequence information
Length: 331 AA [This is the length of the unprocessed precursor] Molecular weight: 35676 Da [This is the MW of the unprocessed precursor] CRC64: 0695E23AC4D33561 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTAKMETTFY DDALNASFLP SESGPYGYSN PKILKQSMTL NLADPVGSLK PHLRAKNSDL 

        70         80         90        100        110        120 
LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE 

       130        140        150        160        170        180 
LHSQNTLPSV TSAAQPVNGA GMVAPAVASV AGGSGSGGFS ASLHSEPPVY ANLSNFNPGA 

       190        200        210        220        230        240 
LSSGGGAPSY GAAGLAFPAQ PQQQQQPPHH LPQQMPVQHP RLQALKEEPQ TVPEMPGETP 

       250        260        270        280        290        300 
PLSPIDMESQ ERIKAERKRM RNRIAASKCR KRKLERIARL EEKVKTLKAQ NSELASTANM 

       310        320        330 
LREQVAQLKQ KVMNHVNSGC QLMLTQQLQT F 

P05412 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!