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P05412

- JUN_HUMAN

UniProt

P05412 - JUN_HUMAN

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Protein

Transcription factor AP-1

Gene

JUN

Organism
Homo sapiens (Human)
Status
Reviewed - 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 syngernistic transcriptional activity with SMAD3

GO - Molecular functioni

  1. cAMP response element binding Source: BHF-UCL
  2. DNA binding Source: ProtInc
  3. double-stranded DNA binding Source: Ensembl
  4. enzyme binding Source: UniProt
  5. poly(A) RNA binding Source: UniProtKB
  6. Rho GTPase activator activity Source: UniProtKB
  7. RNA polymerase II activating transcription factor binding Source: BHF-UCL
  8. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  9. RNA polymerase II distal enhancer sequence-specific DNA binding Source: BHF-UCL
  10. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: UniProtKB
  11. RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
  12. R-SMAD binding Source: BHF-UCL
  13. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: ParkinsonsUK-UCL
  14. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  15. transcription coactivator activity Source: UniProtKB
  16. transcription factor binding Source: BHF-UCL
  17. transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  1. aging Source: Ensembl
  2. angiogenesis Source: Ensembl
  3. axon regeneration Source: Ensembl
  4. cellular response to calcium ion Source: Ensembl
  5. cellular response to potassium ion starvation Source: Ensembl
  6. circadian rhythm Source: Ensembl
  7. Fc-epsilon receptor signaling pathway Source: Reactome
  8. innate immune response Source: Reactome
  9. leading edge cell differentiation Source: Ensembl
  10. learning Source: Ensembl
  11. liver development Source: Ensembl
  12. membrane depolarization Source: Ensembl
  13. microglial cell activation Source: Ensembl
  14. monocyte differentiation Source: Ensembl
  15. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  16. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  17. negative regulation by host of viral transcription Source: UniProtKB
  18. negative regulation of cell proliferation Source: Ensembl
  19. negative regulation of DNA binding Source: UniProtKB
  20. negative regulation of neuron apoptotic process Source: Ensembl
  21. negative regulation of protein autophosphorylation Source: Ensembl
  22. negative regulation of transcription, DNA-templated Source: UniProtKB
  23. negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
  24. outflow tract morphogenesis Source: Ensembl
  25. positive regulation by host of viral transcription Source: UniProtKB
  26. positive regulation of DNA replication Source: Ensembl
  27. positive regulation of endothelial cell proliferation Source: Ensembl
  28. positive regulation of fibroblast proliferation Source: Ensembl
  29. positive regulation of monocyte differentiation Source: Ensembl
  30. positive regulation of neuron apoptotic process Source: Ensembl
  31. positive regulation of Rho GTPase activity Source: GOC
  32. positive regulation of smooth muscle cell proliferation Source: Ensembl
  33. positive regulation of transcription, DNA-templated Source: UniProtKB
  34. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  35. regulation of cell cycle Source: Ensembl
  36. regulation of sequence-specific DNA binding transcription factor activity Source: Reactome
  37. release of cytochrome c from mitochondria Source: Ensembl
  38. response to cAMP Source: Ensembl
  39. response to cytokine Source: Ensembl
  40. response to drug Source: Ensembl
  41. response to hydrogen peroxide Source: Ensembl
  42. response to lipopolysaccharide Source: Ensembl
  43. response to mechanical stimulus Source: Ensembl
  44. response to radiation Source: Ensembl
  45. SMAD protein import into nucleus Source: BHF-UCL
  46. SMAD protein signal transduction Source: BHF-UCL
  47. stress-activated MAPK cascade Source: Reactome
  48. toll-like receptor 10 signaling pathway Source: Reactome
  49. toll-like receptor 2 signaling pathway Source: Reactome
  50. toll-like receptor 3 signaling pathway Source: Reactome
  51. toll-like receptor 4 signaling pathway Source: Reactome
  52. toll-like receptor 5 signaling pathway Source: Reactome
  53. toll-like receptor 9 signaling pathway Source: Reactome
  54. toll-like receptor signaling pathway Source: Reactome
  55. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  56. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  57. transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  58. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
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: Chromosome 1

Organism-specific databases

HGNCiHGNC:6204. JUN.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. nuclear chromosome Source: ProtInc
  3. nuclear euchromatin Source: BHF-UCL
  4. nucleoplasm Source: Reactome
  5. nucleus Source: ParkinsonsUK-UCL
  6. transcriptional repressor complex Source: Ensembl
  7. transcription factor complex Source: Ensembl
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. 1 Publication
Mutagenesisi73 – 731S → A: Greatly reduced ATF7-mediated transcriptional activity; when associated with A-63. 1 Publication
Mutagenesisi89 – 891T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-93; and A-286. 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 syngernistic 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.

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 PLK36 Publications
Modified residuei73 – 731Phosphoserine; by MAPK8 and PLK32 Publications
Modified residuei89 – 891Phosphothreonine; by PAK21 Publication
Modified residuei93 – 931Phosphothreonine; by PAK21 Publication
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

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.12 Publications
Acetylated at Lys-271 by EP300.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP05412.
PaxDbiP05412.
PRIDEiP05412.

PTM databases

PhosphoSiteiP05412.

Expressioni

Gene expression databases

BgeeiP05412.
CleanExiHS_JUN.
GenevestigatoriP05412.

Organism-specific databases

HPAiCAB003801.
CAB007780.

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 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 methylated RNF187. Binds to HIPK3.By similarity11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APLP2Q064813EBI-852823,EBI-79306
APPP050672EBI-852823,EBI-77613
ATF2P153365EBI-852823,EBI-1170906
ATF4P188482EBI-852823,EBI-492498
BBS7Q8IWZ63EBI-852823,EBI-1806001
CITED1Q999662EBI-852823,EBI-2624951
CREB3O438894EBI-852823,EBI-625002
ETS1P149213EBI-852823,EBI-913209
FOSP0110021EBI-852823,EBI-852851
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
MDM2Q009873EBI-852823,EBI-389668
PRRC2AP486342EBI-852823,EBI-347545
STRN4Q9NRL33EBI-852823,EBI-717245
VRK1Q999864EBI-852823,EBI-1769146

Protein-protein interaction databases

BioGridi109928. 183 interactions.
DIPiDIP-5961N.
IntActiP05412. 65 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. 1 PublicationCurated

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.

Polymorphism databases

DMDMi135298.

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 .
CCDSi CCDS610.1.
PIRi A31264. TVHUJN.
RefSeqi NP_002219.1. NM_002228.3.
UniGenei Hs.696684.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A02 X-ray 2.70 J 253-308 [» ]
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 [» ]
ProteinModelPortali P05412.
SMRi P05412. Positions 257-308.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109928. 183 interactions.
DIPi DIP-5961N.
IntActi P05412. 65 interactions.
MINTi MINT-105756.
STRINGi 9606.ENSP00000360266.

Chemistry

BindingDBi P05412.
ChEMBLi CHEMBL2111421.
DrugBanki DB01169. Arsenic trioxide.
DB01029. Irbesartan.
DB00852. Pseudoephedrine.
DB00570. Vinblastine.

PTM databases

PhosphoSitei P05412.

Polymorphism databases

DMDMi 135298.

Proteomic databases

MaxQBi P05412.
PaxDbi P05412.
PRIDEi P05412.

Protocols and materials databases

DNASUi 3725.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371222 ; ENSP00000360266 ; ENSG00000177606 .
GeneIDi 3725.
KEGGi hsa:3725.
UCSCi uc001cze.3. human.

Organism-specific databases

CTDi 3725.
GeneCardsi GC01M059246.
H-InvDB HIX0000635.
HGNCi HGNC:6204. JUN.
HPAi CAB003801.
CAB007780.
MIMi 165160. gene.
neXtProti NX_P05412.
PharmGKBi PA30006.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG283376.
GeneTreei ENSGT00390000009929.
HOGENOMi HOG000006648.
HOVERGENi HBG001722.
InParanoidi P05412.
KOi K04448.
OMAi AELHNQN.
OrthoDBi EOG75MVXV.
PhylomeDBi P05412.
TreeFami TF323952.

Enzyme and pathway databases

Reactomei REACT_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.
SignaLinki P05412.

Miscellaneous databases

ChiTaRSi JUN. human.
EvolutionaryTracei P05412.
GeneWikii C-jun.
GenomeRNAii 3725.
NextBioi 14583.
PROi P05412.
SOURCEi Search...

Gene expression databases

Bgeei P05412.
CleanExi HS_JUN.
Genevestigatori P05412.

Family and domain databases

Gene3Di 1.10.880.10. 1 hit.
InterProi IPR004827. bZIP.
IPR015558. C_Jun/v-Jun.
IPR005643. JNK.
IPR002112. Leuzip_Jun.
IPR008917. TF_DNA-bd.
[Graphical view ]
PANTHERi PTHR11462:SF8. PTHR11462:SF8. 1 hit.
Pfami PF00170. bZIP_1. 1 hit.
PF03957. Jun. 1 hit.
[Graphical view ]
PRINTSi PR00043. LEUZIPPRJUN.
SMARTi SM00338. BRLZ. 1 hit.
[Graphical view ]
SUPFAMi SSF47454. SSF47454. 1 hit.
PROSITEi PS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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.
  21. "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.
  22. "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.
  23. "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.
  24. 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.
  25. "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].
  26. "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.
  27. "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.
  28. "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.
  29. "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.
  30. "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].
  31. "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.
  32. "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.
  33. "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.
  34. "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: November 26, 2014
This is version 194 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