P05412 (JUN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor AP-1

Alternative name(s):
Activator protein 1
Short name=AP1
Proto-oncogene c-Jun
V-jun avian sarcoma virus 17 oncogene homolog
p39

Gene names

Name:

JUN

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	331 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcription factor that recognizes and binds to the enhancer heptamer motif 5'-TGA[CG]TCA-3'. Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. Ref.15 Ref.19
Subunit structure	Heterodimer with either FOS or BATF3 or ATF7. The ATF7/JUN heterodimer is essential for ATF7 transactivation activity. Interacts with DSIPI; the interaction inhibits the binding of active AP1 to its target DNA By similarity. Interacts with HIVEP3 and MYBBP1A By similarity. Interacts with SP1, SPIB and TCF20. Interacts with COPS5; the interaction leads indirectly to its phosphorylation. Component of the SMAD3/SMAD4/JUN/FOS/complex which forms at the AP1 promoter site. The SMAD3/SMAD4 heterodimer acts syngernistically with the JUN/FOS heterodimer to activate transcription in response to TGF-beta. Interacts (via its basic DNA binding and leucine zipper domains) with SMAD3 (via an N-terminal domain); the interaction is required for TGF-beta-mediated transactivation of the SMAD3/SMAD4/JUN/FOS/complex. Interacts with RNF187. Binds to HIPK3. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.20 Ref.25
Subcellular location	Nucleus.
Post-translational modification	Phosphorylated by CaMK4 and PRKDC; phosphorylation enhances the transcriptional activity. Phosphorylated by HIPK3. Phosphorylated by DYRK2 at Ser-243; this primes the protein for subsequent phosphorylation by GSK3B at Thr-239. Phosphorylated at Thr-239, Ser-243 and Ser-249 by GSK3B; phosphorylation reduces its ability to bind DNA. Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-89, Thr-93 and Thr-286 thereby promoting JUN-mediated cell proliferation and transformation. Phosphorylated by PLK3 following hypoxia or UV irradiation, leading to increase DNA-binding activity. Ref.7 Ref.8 Ref.9 Ref.19 Ref.21 Ref.22 Ref.27 Ref.29 Acetylated at Lys-271 by EP300.
Sequence similarities	Belongs to the bZIP family. Jun subfamily. Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Disease	Proto-oncogene
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	MyD88-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome SMAD protein import into nucleus Inferred from direct assay Ref.12. Source: BHF-UCL SMAD protein signal transduction Inferred from direct assay Ref.12. Source: BHF-UCL TRIF-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome Toll signaling pathway Traceable author statement. Source: Reactome aging Inferred from electronic annotation. Source: Compara angiogenesis Inferred from electronic annotation. Source: Compara axon regeneration Inferred from electronic annotation. Source: Compara cellular response to calcium ion Inferred from electronic annotation. Source: Compara cellular response to potassium ion starvation Inferred from electronic annotation. Source: Compara circadian rhythm Inferred from electronic annotation. Source: Compara innate immune response Traceable author statement. Source: Reactome leading edge cell differentiation Inferred from electronic annotation. Source: Compara learning Inferred from electronic annotation. Source: Compara liver development Inferred from electronic annotation. Source: Compara membrane depolarization Inferred from electronic annotation. Source: Compara microglial cell activation Inferred from electronic annotation. Source: Compara monocyte differentiation Inferred from electronic annotation. Source: Compara negative regulation by host of viral transcription Inferred from direct assay PubMed 2833704. Source: UniProtKB negative regulation of DNA binding Inferred from direct assay PubMed 14645924. Source: UniProtKB negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of protein autophosphorylation Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent Inferred from direct assay PubMed 2833704. Source: UniProtKB outflow tract morphogenesis Inferred from electronic annotation. Source: Compara positive regulation by host of viral transcription Inferred from direct assay PubMed 2833704. Source: UniProtKB positive regulation of DNA replication Inferred from electronic annotation. Source: Compara positive regulation of endothelial cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of fibroblast proliferation Inferred from electronic annotation. Source: Compara positive regulation of monocyte differentiation Inferred from electronic annotation. Source: Compara positive regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara regulation of cell cycle Inferred from electronic annotation. Source: Compara regulation of sequence-specific DNA binding transcription factor activity Traceable author statement. Source: Reactome release of cytochrome c from mitochondria Inferred from electronic annotation. Source: Compara response to cAMP Inferred from electronic annotation. Source: Compara response to cytokine stimulus Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to hydrogen peroxide Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to mechanical stimulus Inferred from electronic annotation. Source: Compara response to radiation Inferred from electronic annotation. Source: Compara stress-activated MAPK cascade Traceable author statement. Source: Reactome toll-like receptor 1 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 2 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 3 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 4 signaling pathway Traceable author statement. Source: Reactome transforming growth factor beta receptor signaling pathway Inferred from direct assay Ref.12. Source: BHF-UCL
Cellular_component	cytosol Inferred from electronic annotation. Source: Compara nuclear euchromatin Inferred from direct assay PubMed 19861239. Source: BHF-UCL nucleoplasm Traceable author statement. Source: Reactome transcription factor complex Inferred from electronic annotation. Source: Compara transcriptional repressor complex Inferred from electronic annotation. Source: Compara
Molecular_function	RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Inferred from electronic annotation. Source: Compara RNA polymerase II distal enhancer sequence-specific DNA binding Inferred from direct assay PubMed 19861239. Source: BHF-UCL RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 2833704. Source: UniProtKB RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Inferred by curator PubMed 19861239. Source: BHF-UCL Rho GTPase activator activity Inferred from direct assay PubMed 11804590. Source: UniProtKB cAMP response element binding Inferred from direct assay PubMed 19861239. Source: BHF-UCL double-stranded DNA binding Inferred from electronic annotation. Source: Compara transcription coactivator activity Inferred from direct assay PubMed 2833704. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APLP2	Q06481	3	EBI-852823,EBI-79306
APP	P05067	2	EBI-852823,EBI-77613
ATF2	P15336	4	EBI-852823,EBI-1170906
BBS7	Q8IWZ6	3	EBI-852823,EBI-1806001
CREB3	O43889	4	EBI-852823,EBI-625002
ETS1	P14921	3	EBI-852823,EBI-913209
FOS	P01100	6	EBI-852823,EBI-852851
HSP90AA1	P07900	2	EBI-852823,EBI-296047
jnk-1	Q8WQG9	3	EBI-852823,EBI-321822	From a different organism.
KPNA2	P52292	2	EBI-852823,EBI-349938
MAPK8	P45983	3	EBI-852823,EBI-286483
MAPK8	P45983-1	2	EBI-852823,EBI-288687
MAPRE3	Q9UPY8	3	EBI-852823,EBI-726739
MDM2	Q00987	3	EBI-852823,EBI-389668
PRRC2A	P48634	2	EBI-852823,EBI-347545
STRN4	Q9NRL3	3	EBI-852823,EBI-717245
VRK1	Q99986	4	EBI-852823,EBI-1769146

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 331

331

Transcription factor AP-1

PRO_0000076429

Regions

Domain

252 – 315

64

bZIP

Region

252 – 279

28

Basic motif By similarity

Region

280 – 308

29

Leucine-zipper By similarity

Sites

Site

272

1

Necessary for syngernistic transcriptional activity with SMAD3

Amino acid modifications

Modified residue

2

1

Phosphothreonine; by PAK2 Ref.27

Modified residue

8

1

Phosphothreonine; by PAK2 Ref.27

Modified residue

58

1

Phosphoserine Ref.23 Ref.28

Modified residue

63

1

Phosphoserine; by MAPK8 and PLK3 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.28

Modified residue

73

1

Phosphoserine; by MAPK8 and PLK3 Ref.21 Ref.22

Modified residue

89

1

Phosphothreonine; by PAK2 Ref.27

Modified residue

93

1

Phosphothreonine; by PAK2 Ref.27

Modified residue

239

1

Phosphothreonine; by GSK3-beta Ref.7 Ref.23

Modified residue

243

1

Phosphoserine; by DYRK2 and GSK3-beta Ref.7 Ref.23 Ref.24 Ref.29

Modified residue

249

1

Phosphoserine; by GSK3-beta Ref.7 Ref.8

Modified residue

271

1

N6-acetyllysine Ref.16

Modified residue

286

1

Phosphothreonine; by PAK2 Ref.27

Natural variations

Natural variant

297

1

T → M.
Corresponds to variant rs9989 [ dbSNP | Ensembl ].

VAR_012070

Experimental info

Mutagenesis

2

1

T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-8; A-89; A-93; and A-286. Ref.27

Mutagenesis

8

1

T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-89; A-93; and A-286. Ref.27

Mutagenesis

63

1

S → A: Greatly reduced ATF7-mediated transcriptional activity; when associated with A-73. Ref.14

Mutagenesis

73

1

S → A: Greatly reduced ATF7-mediated transcriptional activity; when associated with A-63. Ref.14

Mutagenesis

89

1

T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-93; and A-286. Ref.27

Mutagenesis

93

1

T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-89; and A-286. Ref.27

Mutagenesis

243

1

S → A: Abolishes phosphorylation by DYRK2. Abolishes phosphorylation by GSK3B at Thr-239. Ref.29

Mutagenesis

272

1

R → V: Abolishes the syngernistic activity with SMAD3 to activate TGF-beta-mediated transcription. Ref.15

Mutagenesis

286

1

T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-89; and A-93. Ref.27

Sequence conflict

11

1

D → G AA sequence Ref.2

Sequence conflict

14

1

L → F AA sequence Ref.2

Sequence conflict

80

1

I → V AA sequence Ref.2

Secondary structure

1

.

.

.

331

Helix Strand Turn

Details...

Helix

255 – 306

52

Sequences

	Sequence		Length	Mass (Da)
	P05412 [UniParc]. Last modified October 1, 1989. Version 2. Checksum: 0695E23AC4D33561	FASTA	331	35,676
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and chromosomal localization of the functional intronless human JUN protooncogene." Hattori K., Angel P., le Beau M.M., Karin M. Proc. Natl. Acad. Sci. U.S.A. 85:9148-9152(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Human proto-oncogene c-jun encodes a DNA binding protein with structural and functional properties of transcription factor AP-1." Bohmann D., Bos T.J., Admon A., Nishimura T., Vogt P.K., Tjian R. Science 238:1386-1392(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	NIEHS SNPs program Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The DNA sequence and biological annotation of human chromosome 1." 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. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: B-cell, Ovary, Testis and Uterus.
[7]	"Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity." Boyle W.J., Smeal T., Defize L.H., Angel P., Woodgett J.R., Karin M., Hunter T. Cell 64:573-584(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-239; SER-243 AND SER-249 BY GSK3B.
[8]	"c-Jun is phosphorylated by the DNA-dependent protein kinase in vitro; definition of the minimal kinase recognition motif." Bannister A.J., Gottlieb T.M., Kouzarides T., Jackson S.P. Nucleic Acids Res. 21:1289-1295(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-249.
[9]	"Regulation of mitogen-activated protein kinases by a calcium/calmodulin-dependent protein kinase cascade." Enslen H., Tokumitsu H., Stork P.J., Davis R.J., Soderling T.R. Proc. Natl. Acad. Sci. U.S.A. 93:10803-10808(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY CAMK4.
[10]	"Cross-talk between different enhancer elements during mitogenic induction of the human stromelysin-1 gene." Kirstein M., Sanz L., Moscat J., Diaz-Meco M.T., Saus J. J. Biol. Chem. 271:18231-18236(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TCF20.
[11]	"A new group of conserved coactivators that increase the specificity of AP-1 transcription factors." Claret F.-X., Hibi M., Dhut S., Toda T., Karin M. Nature 383:453-457(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH COPS5.
[12]	"Smad3 and Smad4 cooperate with c-Jun/c-Fos to mediate TGF-beta-induced transcription." Zhang Y., Feng X.H., Derynck R. Nature 394:909-913(1998) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION AS A COMPONENT OF THE SMAD3/SMAD4/JUN/FOS COMPLEX, INTERACTION WITH SMAD3.
[13]	"SPI-B activates transcription via a unique proline, serine, and threonine domain and exhibits DNA binding affinity differences from PU.1." Rao S., Matsumura A., Yoon J., Simon M.C. J. Biol. Chem. 274:11115-11124(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SPIB.
[14]	"Role of the ATFa/JNK2 complex in Jun activation." De Graeve F., Bahr A., Sabapathy K.T., Hauss C., Wagner E.F., Kedinger C., Chatton B. Oncogene 18:3491-3500(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ATF7, MUTAGENESIS OF SER-63 AND SER-73.
[15]	"Structural and functional characterization of the transforming growth factor-beta -induced Smad3/c-Jun transcriptional cooperativity." Qing J., Zhang Y., Derynck R. J. Biol. Chem. 275:38802-38812(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SMAD3 IN THE SMAD3/SMAD4/JUN/FOS COMPLEX, DNA-BINDING, FUNCTION, MUTAGENESIS OF ARG-272.
[16]	"A specific lysine in c-Jun is required for transcriptional repression by E1A and is acetylated by p300." Vries R.G., Prudenziati M., Zwartjes C., Verlaan M., Kalkhoven E., Zantema A. EMBO J. 20:6095-6103(2001) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-271 BY EP300.
[17]	"Correlation of transcriptional repression by p21(SNFT) with changes in DNA.NF-AT complex interactions." Bower K.E., Zeller R.W., Wachsman W., Martinez T., McGuire K.L. J. Biol. Chem. 277:34967-34977(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BATF3.
[18]	"Transcriptional repression of MMP-1 by p21SNFT and reduced in vitro invasiveness of hepatocarcinoma cells." Bower K.E., Fritz J.M., McGuire K.L. Oncogene 23:8805-8814(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BATF3.
[19]	"Cyclic AMP stimulates SF-1-dependent CYP11A1 expression through homeodomain-interacting protein kinase 3-mediated Jun N-terminal kinase and c-Jun phosphorylation." Lan H.-C., Li H.-J., Lin G., Lai P.-Y., Chung B.-C. Mol. Cell. Biol. 27:2027-2036(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION BY HIPK3.
[20]	"Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription." Hung J.J., Wang Y.T., Chang W.C. Mol. Cell. Biol. 26:1770-1785(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SP1.
[21]	"Stress-induced c-Jun activation mediated by Polo-like kinase 3 in corneal epithelial cells." Wang L., Dai W., Lu L. J. Biol. Chem. 282:32121-32127(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-63 AND SER-73.
[22]	"Activation of Polo-like kinase 3 by hypoxic stresses." Wang L., Gao J., Dai W., Lu L. J. Biol. Chem. 283:25928-25935(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-63 AND SER-73.
[23]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-63; THR-239 AND SER-243, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-243, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[25]	"Identification of a co-activator that links growth factor signalling to c-Jun/AP-1 activation." Davies C.C., Chakraborty A., Cipriani F., Haigh K., Haigh J.J., Behrens A. Nat. Cell Biol. 12:963-972(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RNF187.
[26]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"P21-activated protein kinase (PAK2)-mediated c-Jun phosphorylation at 5 threonine sites promotes cell transformation." Li T., Zhang J., Zhu F., Wen W., Zykova T., Li X., Liu K., Peng C., Ma W., Shi G., Dong Z., Bode A.M., Dong Z. Carcinogenesis 32:659-666(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-2; THR-8; THR-89; THR-93 AND THR-286, MUTAGENESIS OF THR-2; THR-8; THR-89; THR-93 AND THR-286.
[28]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-63, MASS SPECTROMETRY.
[29]	"DYRK2 priming phosphorylation of c-Jun and c-Myc modulates cell cycle progression in human cancer cells." Taira N., Mimoto R., Kurata M., Yamaguchi T., Kitagawa M., Miki Y., Yoshida K. J. Clin. Invest. 122:859-872(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-243, MUTAGENESIS OF SER-243.
[30]	"Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA." Glover J.N., Harrison S.C. Nature 373:257-261(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 257-313 OF COMPLEX WITH FOS.
[31]	"High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer." Junius F.K., O'Donoghue S.I., Nilges M., Weiss A.S., King G.F. J. Biol. Chem. 271:13663-13667(1996) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 276-314.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J04111 Genomic DNA. Translation: AAA59197.1.
BT019759 mRNA. Translation: AAV38564.1.
AY217548 Genomic DNA. Translation: AAO22993.1.
AL136985 Genomic DNA. Translation: CAC10201.1.
BC002646 mRNA. No translation available.
BC006175 mRNA. Translation: AAH06175.1.
BC009874 mRNA. Translation: AAH09874.2.
BC068522 mRNA. Translation: AAH68522.1.

IPI

IPI00008965.

PIR

TVHUJN. A31264.

RefSeq

NP_002219.1. NM_002228.3.

UniGene

Hs.696684.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A02	X-ray	2.70	J	254-308	[»]
1FOS	X-ray	3.05	F/H	254-315	[»]
1JNM	X-ray	2.20	A/B	254-315	[»]
1JUN	NMR	-	A/B	276-314	[»]
1S9K	X-ray	3.10	E	257-308	[»]
1T2K	X-ray	3.00	C	254-314	[»]

ProteinModelPortal

P05412.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5961N.

IntAct

P05412. 53 interactions.

MINT

MINT-105756.

STRING

9606.ENSP00000360266.

PTM databases

PhosphoSite

P05412.

Polymorphism databases

DMDM

135298.

Proteomic databases

PaxDb

P05412.

PRIDE

P05412.

Protocols and materials databases

DNASU

3725.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000371222; ENSP00000360266; ENSG00000177606.

GeneID

3725.

KEGG

hsa:3725.

UCSC

uc001cze.3. human.

Organism-specific databases

CTD

3725.

GeneCards

GC01M059163.

H-InvDB

HIX0000635.

HGNC

HGNC:6204. JUN.

HPA

CAB003801.
CAB007780.

MIM

165160. gene.

neXtProt

NX_P05412.

PharmGKB

PA30006.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG283376.

HOGENOM

HOG000006648.

HOVERGEN

HBG001722.

InParanoid

P05412.

KO

K04448.

OMA

MPVQHPR.

OrthoDB

EOG4RV2RS.

PhylomeDB

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_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.

Gene expression databases

Bgee

P05412.

CleanEx

HS_JUN.

Genevestigator

P05412.

GermOnline

ENSG00000177606. Homo sapiens.

Family and domain databases

Gene3D

1.10.880.10. 1 hit.

InterPro

IPR004827. bZIP.
IPR015558. C_Jun.
IPR008917. Euk_TF_DNA-bd.
IPR005643. JNK.
IPR002112. Leuzip_Jun.
[Graphical view]

PANTHER

PTHR11462:SF8. PTHR11462:SF8. 1 hit.

Pfam

PF00170. bZIP_1. 1 hit.
PF03957. Jun. 1 hit.
[Graphical view]

PRINTS

PR00043. LEUZIPPRJUN.

SMART

SM00338. BRLZ. 1 hit.
[Graphical view]

SUPFAM

SSF47454. Euk_transcr_DNA. 1 hit.

PROSITE

PS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P05412.

ChEMBL

CHEMBL4977.

ChiTaRS

Jun. human.

DrugBank

DB01169. Arsenic trioxide.
DB01029. Irbesartan.
DB00570. Vinblastine.

EvolutionaryTrace

P05412.

GenomeRNAi

3725.

NextBio

14583.

SOURCE

Search...

Entry information

Entry name

JUN_HUMAN

Accession

Primary (citable) accession number: P05412
Secondary accession number(s): Q96G93

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	October 1, 1989
Last modified:	May 1, 2013
This is version 176 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.