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
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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. Involved in activated KRAS-mediated transcriptional activation of USP28 in colorectal cancer (CRC) cells. Binds to the USP28 promoter in colorectal cancer (CRC) cells.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei272Necessary for synergistic transcriptional activity with SMAD3By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

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
Gene namesi
Name:JUN
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

  • nuclear chromatin Source: GO_Central
  • nucleus Source: AgBase
  • transcription factor complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000764311 – 331Transcription factor AP-1Add BLAST331

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2Phosphothreonine; by PAK2By similarity1
Modified residuei8Phosphothreonine; by PAK2By similarity1
Modified residuei58PhosphoserineBy similarity1
Modified residuei63Phosphoserine; by MAPK8 and PLK3By similarity1
Modified residuei73Phosphoserine; by MAPK8 and PLK3By similarity1
Modified residuei89Phosphothreonine; by PAK2By similarity1
Modified residuei91PhosphothreonineBy similarity1
Modified residuei93Phosphothreonine; by PAK2By similarity1
Modified residuei239Phosphothreonine; by GSK3-betaBy similarity1
Modified residuei243Phosphoserine; by DYRK2 and GSK3-betaBy similarity1
Modified residuei249Phosphoserine; by GSK3-betaBy similarity1
Modified residuei271N6-acetyllysineBy similarity1
Modified residuei286Phosphothreonine; by PAK2By similarity1

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

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP56432.

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 (By similarity).By similarity

GO - Molecular functioni

Structurei

3D structure databases

ProteinModelPortaliP56432.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini252 – 315bZIPPROSITE-ProRule annotationAdd BLAST64

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni252 – 279Basic motifPROSITE-ProRule annotationAdd BLAST28
Regioni280 – 308Leucine-zipperPROSITE-ProRule annotationAdd BLAST29

Sequence similaritiesi

Belongs to the bZIP family. Jun subfamily.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000006648.
HOVERGENiHBG001722.
InParanoidiP56432.
KOiK04448.

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.

P56432-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAKMETTFY DDALNASFLQ SESGAYGYSN PKILKQSMTL NLADPVGNLK
60 70 80 90 100
PHLRAQDSDL LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP
110 120 130 140 150
KNVTDEQEGF AEGFVRALAE LHSQNTLPSV TSAAQPVSGA GLVAPAVASV
160 170 180 190 200
AGGSGSGGFS ASLHSEPPVY ANLSNFNPGA LSSGGGAPSY GAAGLAFPAQ
210 220 230 240 250
PQQQQQQPPQ PPHHLPVQHP RLQALKEEPQ TVPEMPGETP PLSPIDMESQ
260 270 280 290 300
ERIKAERKRM RNRIAASKCR KRKLERIARL EEKVKTLKAQ NSELASTANM
310 320 330
LREQVAQLKQ KVMNHVNSGC QLMLTQQLQT F
Length:331
Mass (Da):35,629
Last modified:July 15, 1998 - v1
Checksum:i0B45EAD5911340EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S83515 mRNA. Translation: AAB50808.1.
RefSeqiNP_999045.1. NM_213880.1.
UniGeneiSsc.94492.
Ssc.97579.

Genome annotation databases

GeneIDi396913.
KEGGissc:396913.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S83515 mRNA. Translation: AAB50808.1.
RefSeqiNP_999045.1. NM_213880.1.
UniGeneiSsc.94492.
Ssc.97579.

3D structure databases

ProteinModelPortaliP56432.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP56432.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396913.
KEGGissc:396913.

Organism-specific databases

CTDi3725.

Phylogenomic databases

HOGENOMiHOG000006648.
HOVERGENiHBG001722.
InParanoidiP56432.
KOiK04448.

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...

Entry informationi

Entry nameiJUN_PIG
AccessioniPrimary (citable) accession number: P56432
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: October 5, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.