Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Transcription factor AP-1

Gene

JUN

Organism
Homo sapiens (Human)
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'. Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei272 – 2721Necessary for synergistic transcriptional activity with SMAD3

GO - Molecular functioni

  • cAMP response element binding Source: BHF-UCL
  • DNA binding Source: ProtInc
  • double-stranded DNA binding Source: Ensembl
  • enzyme binding Source: UniProtKB
  • GTPase activator activity Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: GO_Central
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  • RNA polymerase II distal enhancer sequence-specific DNA binding Source: BHF-UCL
  • RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
  • R-SMAD binding Source: BHF-UCL
  • sequence-specific DNA binding RNA polymerase II transcription factor activity Source: ParkinsonsUK-UCL
  • sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • transcription coactivator activity Source: UniProtKB
  • transcription factor binding Source: BHF-UCL
  • transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_118568. Pre-NOTCH Transcription and Translation.
REACT_163701. FCERI mediated MAPK activation.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169436. Oxidative Stress Induced Senescence.
REACT_21326. Activation of the AP-1 family of transcription factors.
SignaLinkiP05412.

Names & Taxonomyi

Protein namesi
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 namesi
Name:JUN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6204. JUN.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Ensembl
  • nuclear chromosome Source: ProtInc
  • nuclear euchromatin Source: BHF-UCL
  • nucleoplasm Source: HPA
  • nucleus Source: ParkinsonsUK-UCL
  • transcriptional repressor complex Source: Ensembl
  • transcription factor complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-8; A-89; A-93; and A-286. 1 Publication
Mutagenesisi8 – 81T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-89; A-93; and A-286. 1 Publication
Mutagenesisi63 – 631S → A: Greatly reduced ATF7-mediated transcriptional activity; when associated with A-73. Abolishes interaction with FBXW7; when associated with A-73; A-91 and A-93. 2 Publications
Mutagenesisi73 – 731S → A: Greatly reduced ATF7-mediated transcriptional activity; when associated with A-63. Abolishes interaction with FBXW7; when associated with A-63; A-91 and A-93. 2 Publications
Mutagenesisi89 – 891T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-93; and A-286. 1 Publication
Mutagenesisi91 – 911T → A: Abolishes interaction with FBXW7; when associated with A-63; A-73 and A-93. 1 Publication
Mutagenesisi93 – 931T → A: Abolishes interaction with FBXW7; when associated with A-63; A-73 and A-91. 1 Publication
Mutagenesisi93 – 931T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-89; and A-286. 1 Publication
Mutagenesisi243 – 2431S → A: Abolishes phosphorylation by DYRK2. Abolishes phosphorylation by GSK3B at Thr-239. 1 Publication
Mutagenesisi272 – 2721R → V: Abolishes the synergistic activity with SMAD3 to activate TGF-beta-mediated transcription. 1 Publication
Mutagenesisi286 – 2861T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-89; and A-93. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA30006.

Chemistry

DrugBankiDB01169. Arsenic trioxide.
DB01029. Irbesartan.
DB00852. Pseudoephedrine.
DB00570. Vinblastine.

Polymorphism and mutation databases

BioMutaiJUN.
DMDMi135298.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 331331Transcription factor AP-1PRO_0000076429Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21Phosphothreonine; by PAK21 Publication
Modified residuei8 – 81Phosphothreonine; by PAK21 Publication
Modified residuei56 – 561N6-acetyllysineBy similarity
Modified residuei58 – 581Phosphoserine2 Publications
Modified residuei63 – 631Phosphoserine; by MAPK8 and PLK37 Publications
Modified residuei73 – 731Phosphoserine; by MAPK8 and PLK33 Publications
Modified residuei89 – 891Phosphothreonine; by PAK21 Publication
Modified residuei91 – 911Phosphothreonine1 Publication
Modified residuei93 – 931Phosphothreonine; by PAK22 Publications
Modified residuei239 – 2391Phosphothreonine; by GSK3-beta2 Publications
Modified residuei243 – 2431Phosphoserine; by DYRK2 and GSK3-beta4 Publications
Modified residuei249 – 2491Phosphoserine; by GSK3-beta2 Publications
Modified residuei271 – 2711N6-acetyllysine1 Publication
Modified residuei286 – 2861Phosphothreonine; by PAK21 Publication

Post-translational modificationi

Ubiquitinated by the SCF(FBXW7), leading to its degradation. Ubiquitination takes place following phosphorylation, that promotes interaction with FBXW7.1 Publication
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.9 Publications
Acetylated at Lys-271 by EP300.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP05412.
PaxDbiP05412.
PRIDEiP05412.

PTM databases

PhosphoSiteiP05412.

Expressioni

Gene expression databases

BgeeiP05412.
CleanExiHS_JUN.
GenevisibleiP05412. HS.

Organism-specific databases

HPAiCAB003801.
CAB007780.
HPA059474.

Interactioni

Subunit structurei

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 synergistically 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 methylated RNF187. Binds to HIPK3. Interacts (when phosphorylated) with FBXW7 (PubMed:14739463).By similarity12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APLP2Q064813EBI-852823,EBI-79306
APPP050672EBI-852823,EBI-77613
ATF2P153368EBI-852823,EBI-1170906
ATF4P188482EBI-852823,EBI-492498
BBS7Q8IWZ63EBI-852823,EBI-1806001
CITED1Q999662EBI-852823,EBI-2624951
CREB3O438894EBI-852823,EBI-625002
ETS1P149213EBI-852823,EBI-913209
FOSP0110025EBI-852823,EBI-852851
FOSL1P154077EBI-852823,EBI-744510
HSP90AA1P079002EBI-852823,EBI-296047
jnk-1Q8WQG93EBI-852823,EBI-321822From a different organism.
KPNA2P522922EBI-852823,EBI-349938
MAPK10P537792EBI-852823,EBI-713543
MAPK8P459834EBI-852823,EBI-286483
MAPK8P45983-12EBI-852823,EBI-288687
MAPRE3Q9UPY83EBI-852823,EBI-726739
MazP566712EBI-852823,EBI-1809712From a different organism.
MDM2Q009873EBI-852823,EBI-389668
NFATC2Q13469-26EBI-852823,EBI-10087113
PRRC2AP486342EBI-852823,EBI-347545
STRN4Q9NRL33EBI-852823,EBI-717245
VRK1Q999864EBI-852823,EBI-1769146

Protein-protein interaction databases

BioGridi109928. 187 interactions.
DIPiDIP-5961N.
IntActiP05412. 72 interactions.
MINTiMINT-105756.
STRINGi9606.ENSP00000360266.

Structurei

Secondary structure

1
331
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi255 – 30652Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A02X-ray2.70J253-308[»]
1FOSX-ray3.05F/H254-315[»]
1JNMX-ray2.20A/B254-315[»]
1JUNNMR-A/B276-314[»]
1S9KX-ray3.10E257-308[»]
1T2KX-ray3.00C254-314[»]
ProteinModelPortaliP05412.
SMRiP05412. Positions 257-308.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05412.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini252 – 31564bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni252 – 27928Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni280 – 30829Leucine-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

eggNOGiNOG283376.
GeneTreeiENSGT00390000009929.
HOGENOMiHOG000006648.
HOVERGENiHBG001722.
InParanoidiP05412.
KOiK04448.
OMAiAELHNQN.
OrthoDBiEOG75MVXV.
PhylomeDBiP05412.
TreeFamiTF323952.

Family and domain databases

Gene3Di1.10.880.10. 1 hit.
InterProiIPR004827. bZIP.
IPR015558. C_Jun/v-Jun.
IPR005643. JNK.
IPR002112. Leuzip_Jun.
IPR008917. TF_DNA-bd.
[Graphical view]
PANTHERiPTHR11462:SF8. PTHR11462:SF8. 1 hit.
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.

P05412-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAKMETTFY DDALNASFLP SESGPYGYSN PKILKQSMTL NLADPVGSLK
60 70 80 90 100
PHLRAKNSDL LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP
110 120 130 140 150
KNVTDEQEGF AEGFVRALAE LHSQNTLPSV TSAAQPVNGA GMVAPAVASV
160 170 180 190 200
AGGSGSGGFS ASLHSEPPVY ANLSNFNPGA LSSGGGAPSY GAAGLAFPAQ
210 220 230 240 250
PQQQQQPPHH LPQQMPVQHP RLQALKEEPQ TVPEMPGETP PLSPIDMESQ
260 270 280 290 300
ERIKAERKRM RNRIAASKCR KRKLERIARL EEKVKTLKAQ NSELASTANM
310 320 330
LREQVAQLKQ KVMNHVNSGC QLMLTQQLQT F
Length:331
Mass (Da):35,676
Last modified:October 1, 1989 - v2
Checksum:i0695E23AC4D33561
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111D → G AA sequence (PubMed:2825349).Curated
Sequence conflicti14 – 141L → F AA sequence (PubMed:2825349).Curated
Sequence conflicti80 – 801I → V AA sequence (PubMed:2825349).Curated
Sequence conflicti151 – 1511A → S in CAG46525 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti297 – 2971T → M.
Corresponds to variant rs9989 [ dbSNP | Ensembl ].
VAR_012070

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04111 Genomic DNA. Translation: AAA59197.1.
CR541724 mRNA. Translation: CAG46525.1.
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.
CCDSiCCDS610.1.
PIRiA31264. TVHUJN.
RefSeqiNP_002219.1. NM_002228.3.
UniGeneiHs.696684.

Genome annotation databases

EnsembliENST00000371222; ENSP00000360266; ENSG00000177606.
GeneIDi3725.
KEGGihsa:3725.
UCSCiuc001cze.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04111 Genomic DNA. Translation: AAA59197.1.
CR541724 mRNA. Translation: CAG46525.1.
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.
CCDSiCCDS610.1.
PIRiA31264. TVHUJN.
RefSeqiNP_002219.1. NM_002228.3.
UniGeneiHs.696684.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A02X-ray2.70J253-308[»]
1FOSX-ray3.05F/H254-315[»]
1JNMX-ray2.20A/B254-315[»]
1JUNNMR-A/B276-314[»]
1S9KX-ray3.10E257-308[»]
1T2KX-ray3.00C254-314[»]
ProteinModelPortaliP05412.
SMRiP05412. Positions 257-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109928. 187 interactions.
DIPiDIP-5961N.
IntActiP05412. 72 interactions.
MINTiMINT-105756.
STRINGi9606.ENSP00000360266.

Chemistry

BindingDBiP05412.
ChEMBLiCHEMBL2111421.
DrugBankiDB01169. Arsenic trioxide.
DB01029. Irbesartan.
DB00852. Pseudoephedrine.
DB00570. Vinblastine.

PTM databases

PhosphoSiteiP05412.

Polymorphism and mutation databases

BioMutaiJUN.
DMDMi135298.

Proteomic databases

MaxQBiP05412.
PaxDbiP05412.
PRIDEiP05412.

Protocols and materials databases

DNASUi3725.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371222; ENSP00000360266; ENSG00000177606.
GeneIDi3725.
KEGGihsa:3725.
UCSCiuc001cze.3. human.

Organism-specific databases

CTDi3725.
GeneCardsiGC01M059246.
H-InvDBHIX0000635.
HGNCiHGNC:6204. JUN.
HPAiCAB003801.
CAB007780.
HPA059474.
MIMi165160. gene.
neXtProtiNX_P05412.
PharmGKBiPA30006.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG283376.
GeneTreeiENSGT00390000009929.
HOGENOMiHOG000006648.
HOVERGENiHBG001722.
InParanoidiP05412.
KOiK04448.
OMAiAELHNQN.
OrthoDBiEOG75MVXV.
PhylomeDBiP05412.
TreeFamiTF323952.

Enzyme and pathway databases

ReactomeiREACT_118568. Pre-NOTCH Transcription and Translation.
REACT_163701. FCERI mediated MAPK activation.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169436. Oxidative Stress Induced Senescence.
REACT_21326. Activation of the AP-1 family of transcription factors.
SignaLinkiP05412.

Miscellaneous databases

ChiTaRSiJUN. human.
EvolutionaryTraceiP05412.
GeneWikiiC-jun.
GenomeRNAii3725.
NextBioi14583.
PROiP05412.
SOURCEiSearch...

Gene expression databases

BgeeiP05412.
CleanExiHS_JUN.
GenevisibleiP05412. HS.

Family and domain databases

Gene3Di1.10.880.10. 1 hit.
InterProiIPR004827. bZIP.
IPR015558. C_Jun/v-Jun.
IPR005643. JNK.
IPR002112. Leuzip_Jun.
IPR008917. TF_DNA-bd.
[Graphical view]
PANTHERiPTHR11462:SF8. PTHR11462:SF8. 1 hit.
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. "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 open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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].
  5. NIEHS SNPs program
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "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].
  7. "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.
  8. "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.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. Cited for: INTERACTION WITH ATF7, MUTAGENESIS OF SER-63 AND SER-73.
  16. "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.
  17. "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.
  18. "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.
  19. "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.
  20. "The ubiquitin ligase SCFFbw7 antagonizes apoptotic JNK signaling."
    Nateri A.S., Riera-Sans L., Da Costa C., Behrens A.
    Science 303:1374-1378(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-63; SER-73; THR-91 AND THR-93, UBIQUITINATION, INTERACTION WITH FBXW7, MUTAGENESIS OF SER-63; SER-73; THR-91 AND THR-93.
  21. "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.
  22. "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.
  23. "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.
  24. "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.
  25. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-63; THR-239 AND SER-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  28. "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.
  29. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. "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.
  31. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "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.
  33. "Arginine methylation of the c-Jun coactivator RACO-1 is required for c-Jun/AP-1 activation."
    Davies C.C., Chakraborty A., Diefenbacher M.E., Skehel M., Behrens A.
    EMBO J. 32:1556-1567(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF187.
  34. "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.
  35. "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.

Entry informationi

Entry nameiJUN_HUMAN
AccessioniPrimary (citable) accession number: P05412
Secondary accession number(s): Q6FHM7, Q96G93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 1, 1989
Last modified: June 24, 2015
This is version 201 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.