UniProtKB - O97930 (FOS_PIG)
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Protein
Proto-oncogene c-Fos
Gene
FOS
Organism
Sus scrofa (Pig)
Status
Functioni
Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex, at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation (By similarity). In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum (By similarity).By similarity
GO - Molecular functioni
- DNA binding Source: UniProtKB-KW
- DNA binding transcription factor activity Source: InterPro
GO - Biological processi
- regulation of transcription by RNA polymerase II Source: InterPro
Keywordsi
Molecular function | DNA-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Proto-oncogene c-FosAlternative name(s): Cellular oncogene fos |
Gene namesi | Name:FOS |
Organismi | Sus scrofa (Pig) |
Taxonomic identifieri | 9823 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000076468 | 1 – 380 | Proto-oncogene c-FosAdd BLAST | 380 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 10 | Phosphotyrosine; by SRCBy similarity | 1 | |
Modified residuei | 30 | Phosphotyrosine; by SRCBy similarity | 1 | |
Cross-linki | 113 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Cross-linki | 128 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 232 | PhosphothreonineBy similarity | 1 | |
Cross-linki | 265 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity | ||
Cross-linki | 265 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity | ||
Modified residuei | 325 | Phosphothreonine; by MAPK1 and MAPK3By similarity | 1 | |
Modified residuei | 331 | Phosphothreonine; by MAPK1 and MAPK3By similarity | 1 | |
Modified residuei | 362 | Phosphoserine; by MAPK1, MAPK3 and RPS6KA3By similarity | 1 | |
Modified residuei | 374 | Phosphoserine; by MAPK1 and MAPK3By similarity | 1 |
Post-translational modificationi
Phosphorylated in the C-terminal upon stimulation by nerve growth factor (NGF) and epidermal growth factor (EGF). Phosphorylated, in vitro, by MAPK and RSK1. Phosphorylation on both Ser-362 and Ser-374 by MAPK1/2 and RSK1/2 leads to protein stabilization with phosphorylation on Ser-374 being the major site for protein stabilization on NGF stimulation. Phosphorylation on Ser-362 and Ser-374 primes further phosphorylations on Thr-325 and Thr-331 through promoting docking of MAPK to the DEF domain. Phosphorylation on Thr-232, induced by HA-RAS, activates the transcriptional activity and antagonizes sumoylation. Phosphorylation on Ser-362 by RSK2 in osteoblasts contributes to osteoblast transformation (By similarity).By similarity
Constitutively sumoylated with SUMO1, SUMO2 and SUMO3. Desumoylated by SENP2. Sumoylation requires heterodimerization with JUN and is enhanced by mitogen stimulation. Sumoylation inhibits the AP-1 transcriptional activity and is, itself, inhibited by Ras-activated phosphorylation on Thr-232 (By similarity).By similarity
In quiescent cells, the small amount of FOS present is phosphorylated at Tyr-10 and Tyr-30 by SRC. This Tyr-phosphorylated form is cytosolic. In growing cells, dephosphorylated by PTPN2. Dephosphorylation leads to the association with endoplasmic reticulum membranes and activation of phospholipid synthesis (By similarity).By similarity
Keywords - PTMi
Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | O97930 |
PeptideAtlasi | O97930 |
PRIDEi | O97930 |
Interactioni
Subunit structurei
Heterodimer; with JUN (By similarity). Component of the SMAD3/SMAD4/JUN/FOS complex required for synergistic TGF-beta-mediated transcription at the AP1 promoter site. Interacts with SMAD3; the interaction is weak even on TGF-beta activation. Interacts with MAFB. Interacts with DSIPI; this interaction inhibits the binding of active AP1 to its target DNA. Interacts with MAFB (By similarity). Interacts with CDS1 and PI4K2A (By similarity).By similarity
Protein-protein interaction databases
STRINGi | 9823.ENSSSCP00000002583 |
Structurei
3D structure databases
ProteinModelPortali | O97930 |
SMRi | O97930 |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 137 – 200 | bZIPPROSITE-ProRule annotationAdd BLAST | 64 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 139 – 159 | Basic motif; required for the activation of phospholipid synthesis, but not for CDS1-bindingPROSITE-ProRule annotationAdd BLAST | 21 | |
Regioni | 165 – 193 | Leucine-zipperPROSITE-ProRule annotationAdd BLAST | 29 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG1414 Eukaryota ENOG4111CH5 LUCA |
HOGENOMi | HOG000234334 |
HOVERGENi | HBG005743 |
InParanoidi | O97930 |
KOi | K04379 |
OrthoDBi | EOG091G0GGW |
TreeFami | TF326301 |
Family and domain databases
InterProi | View protein in InterPro IPR000837 AP-1 IPR004827 bZIP IPR029816 c-Fos/v-Fos |
PANTHERi | PTHR23351 PTHR23351, 1 hit PTHR23351:SF4 PTHR23351:SF4, 1 hit |
Pfami | View protein in Pfam PF00170 bZIP_1, 1 hit |
PRINTSi | PR00042 LEUZIPPRFOS |
SMARTi | View protein in SMART SM00338 BRLZ, 1 hit |
PROSITEi | View protein in PROSITE PS50217 BZIP, 1 hit PS00036 BZIP_BASIC, 1 hit |
i Sequence
Sequence statusi: Complete.
O97930-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MMFSGFNADY EASSSRCSSA SPAGDSLSYY HSPADSFSSM GSPVNAQDFC
60 70 80 90 100
TDLAVSSVNF IPTVTAISIS PDLQWLVQPT LVSSVAPSQT RAPHPYGVPT
110 120 130 140 150
PSAGAYSRAG AVKTMPGGRA QSIGRRGKVE QLSPEEEEKR RIRRERNKMA
160 170 180 190 200
AAKCRNRRRE LTDTLQAETD QLEDEKSALQ TEIANLLKEK EKLEFILAAH
210 220 230 240 250
RPACKIPDDL GFPEEMSVAS LDLSGGLPEA ATPESEEAFT LPLLNDPEPK
260 270 280 290 300
PSVEPVKKVS SMELKAEPFD DFLFPASSRP GGSETARSVP DMDLSGSFYA
310 320 330 340 350
ADWEPLHGGS LGMGPMATEL EPLCTPVVTC TPSCTAYTSS FVFTYPEADS
360 370 380
FPSCAAAHRK GSSSNEPSSD SLSSPTLLAL
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 58 | V → A in CAB40144 (Ref. 2) Curated | 1 | |
Sequence conflicti | 69 | I → T in CAB40144 (Ref. 2) Curated | 1 | |
Sequence conflicti | 111 | A → V in CAB40144 (Ref. 2) Curated | 1 | |
Sequence conflicti | 258 | K → N in CAB40144 (Ref. 2) Curated | 1 | |
Sequence conflicti | 336 | A → T in CAB40144 (Ref. 2) Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Y14808 Genomic DNA Translation: CAB39278.1 AJ132510 Genomic DNA Translation: CAB40144.1 |
RefSeqi | NP_001116585.1, NM_001123113.1 |
UniGenei | Ssc.1555 |
Genome annotation databases
GeneIDi | 100144486 |
KEGGi | ssc:100144486 |
Similar proteinsi
Entry informationi
Entry namei | FOS_PIG | |
Accessioni | O97930Primary (citable) accession number: O97930 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 21, 2003 |
Last sequence update: | May 1, 2000 | |
Last modified: | March 28, 2018 | |
This is version 114 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |