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Fibroblast growth factor receptor substrate 3 (FGFR substrate 3) (FGFR-signaling adaptor SNT2) (Suc1-associated neurotrophic factor target 2) (SNT-2)

 FRS3_HUMAN              Reviewed;         492 AA.
O43559; Q5T3D5;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 144.
RecName: Full=Fibroblast growth factor receptor substrate 3;
Short=FGFR substrate 3;
AltName: Full=FGFR-signaling adaptor SNT2;
AltName: Full=Suc1-associated neurotrophic factor target 2;
Short=SNT-2;
Name=FRS3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], MYRISTOYLATION AT GLY-2, PHOSPHORYLATION
AT TYROSINE RESIDUES, AND INTERACTION WITH FGFR1.
TISSUE=Placenta;
PubMed=9660748; DOI=10.1074/jbc.273.29.17987;
Xu H., Lee K.W., Goldfarb M.P.;
"Novel recognition motif on fibroblast growth factor receptor mediates
direct association and activation of SNT adapter proteins.";
J. Biol. Chem. 273:17987-17990(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH ERK2.
PubMed=15485655; DOI=10.1016/j.bbrc.2004.09.152;
Huang L., Gotoh N., Zhang S., Shibuya M., Yamamoto T., Tsuchida N.;
"SNT-2 interacts with ERK2 and negatively regulates ERK2 signaling in
response to EGF stimulation.";
Biochem. Biophys. Res. Commun. 324:1011-1017(2004).
[6]
FUNCTION, INTERACTION WITH FGFR1; NGFR; GRB2 AND PTPN11, AND
PHOSPHORYLATION AT TYROSINE RESIDUES.
PubMed=15094036; DOI=10.1016/S0014-5793(04)00287-X;
Gotoh N., Laks S., Nakashima M., Lax I., Schlessinger J.;
"FRS2 family docking proteins with overlapping roles in activation of
MAP kinase have distinct spatial-temporal patterns of expression of
their transcripts.";
FEBS Lett. 564:14-18(2004).
[7]
STRUCTURE BY NMR OF 6-146.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the complex of the PTB domain of SNT-2 and 19-
residue peptide (aa 1571-1589) of HALK.";
Submitted (FEB-2009) to the PDB data bank.
-!- FUNCTION: Adapter protein that links FGF and NGF receptors to
downstream signaling pathways. Involved in the activation of MAP
kinases. Down-regulates ERK2 signaling by interfering with the
phosphorylation and nuclear translocation of ERK2.
{ECO:0000269|PubMed:15094036}.
-!- SUBUNIT: Binds NTRK1 (By similarity). Binds FGFR1, NGFR, GRB2,
PTPN11 and ERK2. {ECO:0000250}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-725515, EBI-725515;
Q9WMX2:- (xeno); NbExp=3; IntAct=EBI-725515, EBI-6863741;
Q6UY14-3:ADAMTSL4; NbExp=5; IntAct=EBI-725515, EBI-10173507;
Q08117:AES; NbExp=3; IntAct=EBI-725515, EBI-717810;
P15976:GATA1; NbExp=3; IntAct=EBI-725515, EBI-3909284;
P08631-2:HCK; NbExp=2; IntAct=EBI-725515, EBI-9834454;
Q7Z3S9:NOTCH2NL; NbExp=5; IntAct=EBI-725515, EBI-945833;
Q92569:PIK3R3; NbExp=3; IntAct=EBI-725515, EBI-79893;
O15162:PLSCR1; NbExp=3; IntAct=EBI-725515, EBI-740019;
Q8HWS3:RFX6; NbExp=5; IntAct=EBI-725515, EBI-746118;
Q8WXH5:SOCS4; NbExp=2; IntAct=EBI-725515, EBI-3942425;
Q8NA61:SPERT; NbExp=3; IntAct=EBI-725515, EBI-741724;
O43597:SPRY2; NbExp=3; IntAct=EBI-725515, EBI-742487;
P15884:TCF4; NbExp=3; IntAct=EBI-725515, EBI-533224;
Q15654:TRIP6; NbExp=5; IntAct=EBI-725515, EBI-742327;
-!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
-!- PTM: Phosphorylated by ULK2 in vitro (By similarity).
Phosphorylated on tyrosine residues upon stimulation by BFGF or
NGFB. {ECO:0000250, ECO:0000269|PubMed:15094036,
ECO:0000269|PubMed:9660748}.
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EMBL; AF036718; AAB92555.1; -; mRNA.
EMBL; CR457026; CAG33307.1; -; mRNA.
EMBL; AL365205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC010611; AAH10611.1; -; mRNA.
CCDS; CCDS4860.1; -.
RefSeq; NP_006644.1; NM_006653.4.
RefSeq; XP_011512556.1; XM_011514254.2.
RefSeq; XP_011512557.1; XM_011514255.2.
UniGene; Hs.194208; -.
PDB; 2KUP; NMR; -; A=8-146.
PDB; 2KUQ; NMR; -; A=8-120.
PDB; 2YS5; NMR; -; A=8-146.
PDB; 2YT2; NMR; -; A=8-120.
PDBsum; 2KUP; -.
PDBsum; 2KUQ; -.
PDBsum; 2YS5; -.
PDBsum; 2YT2; -.
ProteinModelPortal; O43559; -.
SMR; O43559; -.
BioGrid; 116030; 29.
IntAct; O43559; 108.
MINT; O43559; -.
STRING; 9606.ENSP00000259748; -.
iPTMnet; O43559; -.
PhosphoSitePlus; O43559; -.
BioMuta; FRS3; -.
MaxQB; O43559; -.
PaxDb; O43559; -.
PeptideAtlas; O43559; -.
PRIDE; O43559; -.
ProteomicsDB; 49051; -.
DNASU; 10817; -.
Ensembl; ENST00000259748; ENSP00000259748; ENSG00000137218.
Ensembl; ENST00000373018; ENSP00000362109; ENSG00000137218.
GeneID; 10817; -.
KEGG; hsa:10817; -.
UCSC; uc003orc.3; human.
CTD; 10817; -.
DisGeNET; 10817; -.
EuPathDB; HostDB:ENSG00000137218.10; -.
GeneCards; FRS3; -.
HGNC; HGNC:16970; FRS3.
HPA; HPA030162; -.
HPA; HPA030174; -.
MIM; 607744; gene.
neXtProt; NX_O43559; -.
OpenTargets; ENSG00000137218; -.
PharmGKB; PA134961503; -.
eggNOG; KOG4047; Eukaryota.
eggNOG; ENOG410XS2S; LUCA.
GeneTree; ENSGT00510000046707; -.
HOGENOM; HOG000290694; -.
HOVERGEN; HBG062705; -.
InParanoid; O43559; -.
OMA; RHCLQPL; -.
OrthoDB; EOG091G06AV; -.
PhylomeDB; O43559; -.
TreeFam; TF324994; -.
Reactome; R-HSA-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-HSA-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-HSA-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-HSA-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-9028731; Activated NTRK2 signals through FRS2 and FRS3.
SignaLink; O43559; -.
SIGNOR; O43559; -.
ChiTaRS; FRS3; human.
EvolutionaryTrace; O43559; -.
GeneWiki; FRS3; -.
GenomeRNAi; 10817; -.
PRO; PR:O43559; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000137218; Expressed in 145 organ(s), highest expression level in right hemisphere of cerebellum.
CleanEx; HS_FRS3; -.
ExpressionAtlas; O43559; baseline and differential.
Genevisible; O43559; HS.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005104; F:fibroblast growth factor receptor binding; IPI:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IGI:MGI.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd01202; PTB_FRS2; 1.
InterPro; IPR038742; FRS2_PTB.
InterPro; IPR002404; IRS_PTB.
Pfam; PF02174; IRS; 1.
SMART; SM00310; PTBI; 1.
PROSITE; PS51064; IRS_PTB; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Lipoprotein; Membrane; Myristate;
Phosphoprotein; Polymorphism; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000255}.
CHAIN 2 492 Fibroblast growth factor receptor
substrate 3.
/FTId=PRO_0000087346.
DOMAIN 13 115 IRS-type PTB. {ECO:0000255|PROSITE-
ProRule:PRU00389}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000305|PubMed:9660748}.
VARIANT 221 221 P -> L (in dbSNP:rs3747747).
/FTId=VAR_033855.
STRAND 11 13 {ECO:0000244|PDB:2KUQ}.
STRAND 18 26 {ECO:0000244|PDB:2KUP}.
STRAND 32 40 {ECO:0000244|PDB:2KUP}.
STRAND 45 48 {ECO:0000244|PDB:2KUP}.
STRAND 50 52 {ECO:0000244|PDB:2KUP}.
STRAND 55 57 {ECO:0000244|PDB:2KUP}.
HELIX 59 61 {ECO:0000244|PDB:2KUP}.
STRAND 65 68 {ECO:0000244|PDB:2KUP}.
STRAND 71 76 {ECO:0000244|PDB:2KUP}.
STRAND 80 82 {ECO:0000244|PDB:2KUP}.
STRAND 84 90 {ECO:0000244|PDB:2KUP}.
HELIX 94 105 {ECO:0000244|PDB:2KUP}.
SEQUENCE 492 AA; 54462 MW; F06BFC662B531765 CRC64;
MGSCCSCLNR DSVPDNHPTK FKVTNVDDEG VELGSGVMEL TQSELVLHLH RREAVRWPYL
CLRRYGYDSN LFSFESGRRC QTGQGIFAFK CSRAEEIFNL LQDLMQCNSI NVMEEPVIIT
RNSHPAELDL PRAPQPPNAL GYTVSSFSNG CPGEGPRFSA PRRLSTSSLR HPSLGEESTH
ALIAPDEQSH TYVNTPASED DHRRGRHCLQ PLPEGQAPFL PQARGPDQRD PQVFLQPGQV
KFVLGPTPAR RHMVKCQGLC PSLHDPPHHN NNNEAPSECP AQPKCTYENV TGGLWRGAGW
RLSPEEPGWN GLAHRRAALL HYENLPPLPP VWESQAQQLG GEAGDDGDSR DGLTPSSNGF
PDGEEDETPL QKPTSTRAAI RSHGSFPVPL TRRRGSPRVF NFDFRRPGPE PPRQLNYIQV
ELKGWGGDRP KGPQNPSSPQ APMPTTHPAR SSDSYAVIDL KKTVAMSNLQ RALPRDDGTA
RKTRHNSTDL PL


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