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FOS_MESAU
ID   FOS_MESAU               Reviewed;         381 AA.
AC   O88479;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Protein c-Fos {ECO:0000305};
DE   AltName: Full=Cellular oncogene fos;
DE   AltName: Full=Transcription factor AP-1 subunit c-Fos {ECO:0000305};
GN   Name=FOS;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Kidney;
RX   PubMed=10326862;
RX   DOI=10.1002/(sici)1098-2744(199904)24:4<255::aid-mc3>3.0.co;2-c;
RA   Sarabia S.F., Liehr J.G.;
RT   "Differential regulation of c-fos expression in estrogen-induced hamster
RT   renal tumors compared with kidney not due to creation of an estrogen-
RT   response element by point mutation in the gene's flanking sequence.";
RL   Mol. Carcinog. 24:255-262(1999).
CC   -!- FUNCTION: Nuclear phosphoprotein which forms a tight but non-covalently
CC       linked complex with the JUN/AP-1 transcription factor. On TGF-beta
CC       activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex, at the
CC       AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. Has a
CC       critical function in regulating the development of cells destined to
CC       form and maintain the skeleton. It is thought to have an important role
CC       in signal transduction, cell proliferation and differentiation (By
CC       similarity). In growing cells, activates phospholipid synthesis,
CC       possibly by activating CDS1 and PI4K2A. This activity requires Tyr-
CC       dephosphorylation and association with the endoplasmic reticulum (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer; with JUN (By similarity). Component of the
CC       SMAD3/SMAD4/JUN/FOS complex required for synergistic TGF-beta-mediated
CC       transcription at the AP1-binding site (By similarity). Interacts with
CC       SMAD3; the interaction is weak even on TGF-beta activation (By
CC       similarity). Interacts with MAFB (By similarity). Interacts with DSIPI;
CC       this interaction inhibits the binding of active AP1 to its target DNA
CC       (By similarity). Interacts with CDS1 and PI4K2A (By similarity).
CC       Interacts (via bZIP domain and leucine-zipper region) with the
CC       multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF)
CC       subunits SMARCB1, SMARCC2 and SMARCD1 (By similarity). Interacts (via
CC       bZIP domain and leucine-zipper region) with ARID1A (By similarity).
CC       {ECO:0000250|UniProtKB:P01100, ECO:0000250|UniProtKB:P01101,
CC       ECO:0000250|UniProtKB:P12841}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC       Endoplasmic reticulum {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
CC       Note=In quiescent cells, present in very small amounts in the cytosol.
CC       Following induction of cell growth, first localizes to the endoplasmic
CC       reticulum and only later to the nucleus. Localization at the
CC       endoplasmic reticulum requires dephosphorylation at Tyr-10 and Tyr-30
CC       (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated in the C-terminal upon stimulation by nerve growth
CC       factor (NGF) and epidermal growth factor (EGF). Phosphorylated, in
CC       vitro, by MAPK and RSK1. Phosphorylation on both Ser-363 and Ser-375 by
CC       MAPK1/2 and RSK1/2 leads to protein stabilization with phosphorylation
CC       on Ser-375 being the major site for protein stabilization on NGF
CC       stimulation. Phosphorylation on Ser-363 and Ser-375 primes further
CC       phosphorylations on Thr-326 and Thr-332 through promoting docking of
CC       MAPK to the DEF domain. Phosphorylation on Thr-232, induced by HA-RAS,
CC       activates the transcriptional activity and antagonizes sumoylation.
CC       Phosphorylation on Ser-363 by RSK2 in osteoblasts contributes to
CC       osteoblast transformation (By similarity). {ECO:0000250}.
CC   -!- PTM: Constitutively sumoylated with SUMO1, SUMO2 and SUMO3.
CC       Desumoylated by SENP2. Sumoylation requires heterodimerization with JUN
CC       and is enhanced by mitogen stimulation. Sumoylation inhibits the AP-1
CC       transcriptional activity and is, itself, inhibited by Ras-activated
CC       phosphorylation on Thr-232 (By similarity). {ECO:0000250}.
CC   -!- PTM: In quiescent cells, the small amount of FOS present is
CC       phosphorylated at Tyr-10 and Tyr-30 by SRC. This Tyr-phosphorylated
CC       form is cytosolic. In growing cells, dephosphorylated by PTPN2.
CC       Dephosphorylation leads to the association with endoplasmic reticulum
CC       membranes and activation of phospholipid synthesis (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {ECO:0000305}.
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DR   EMBL; AF061881; AAC19354.1; -; Genomic_DNA.
DR   AlphaFoldDB; O88479; -.
DR   SMR; O88479; -.
DR   STRING; 10036.XP_005086426.1; -.
DR   eggNOG; KOG1414; Eukaryota.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005667; C:transcription regulator complex; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   InterPro; IPR000837; AP-1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR029816; c-Fos/v-Fos.
DR   PANTHER; PTHR23351; PTHR23351; 1.
DR   PANTHER; PTHR23351:SF4; PTHR23351:SF4; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   PRINTS; PR00042; LEUZIPPRFOS.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA-binding; Endoplasmic reticulum; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Proto-oncogene; Reference proteome; Ubl conjugation.
FT   CHAIN           1..381
FT                   /note="Protein c-Fos"
FT                   /id="PRO_0000076466"
FT   DOMAIN          137..200
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          118..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..159
FT                   /note="Basic motif; required for the activation of
FT                   phospholipid synthesis, but not for CDS1-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          165..193
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          355..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         10
FT                   /note="Phosphotyrosine; by SRC"
FT                   /evidence="ECO:0000250|UniProtKB:P01100"
FT   MOD_RES         30
FT                   /note="Phosphotyrosine; by SRC"
FT                   /evidence="ECO:0000250|UniProtKB:P01100"
FT   MOD_RES         232
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P01101"
FT   MOD_RES         326
FT                   /note="Phosphothreonine; by MAPK1 and MAPK3"
FT                   /evidence="ECO:0000250|UniProtKB:P01100"
FT   MOD_RES         332
FT                   /note="Phosphothreonine; by MAPK1 and MAPK3"
FT                   /evidence="ECO:0000250|UniProtKB:P01100"
FT   MOD_RES         363
FT                   /note="Phosphoserine; by MAPK1, MAPK3 and RPS6KA3"
FT                   /evidence="ECO:0000250|UniProtKB:P01100"
FT   MOD_RES         375
FT                   /note="Phosphoserine; by MAPK1 and MAPK3"
FT                   /evidence="ECO:0000250|UniProtKB:P01100"
FT   CROSSLNK        113
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P01100"
FT   CROSSLNK        128
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P01100"
FT   CROSSLNK        265
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        265
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P01100"
SQ   SEQUENCE   381 AA;  41020 MW;  ADAACF75614C39CA CRC64;
     MMFSGFNADY EASSSRCSSA SPAGDSLSYY HSPADSFSSM GSPVNAQDFC TDLSVSSANF
     IPTVTAISTS PDLQWLVQPT LVSSVAPSQT RAPHPYGVPT PSTGAYSRAG MVKTVSGGRA
     QSIGRRGKVE QLSPEEEEKR RIRRERNKMA AAKCRNRRRE LTDTLQAETD QLEDEKSALQ
     TEIANLLKEK EKLEFILAAH RPACKIPDDL GFPEEMFVAS LDLTGGLPEA TTPESEEAFS
     LPLLNDPEPK PSLEPVKSIS NVELKAEPFD DFLFPASSRP SGSETTARSV PDMDLSGSFY
     AADWEPLHSS SLGMGPMVTE LEPLCTPVVT CTPSCTTYTS SFVFTYPEAD SFPSCAAAHR
     KGSSSNEPSS DSLSSPTLLA L
 
 
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