ID   FRS3_HUMAN              Reviewed;         492 AA.
AC   O43559; Q5T3D5;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   28-JUN-2023, entry version 170.
DE   RecName: Full=Fibroblast growth factor receptor substrate 3;
DE            Short=FGFR substrate 3;
DE   AltName: Full=FGFR-signaling adaptor SNT2;
DE   AltName: Full=Suc1-associated neurotrophic factor target 2;
DE            Short=SNT-2;
GN   Name=FRS3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT
RP   TYROSINE RESIDUES, AND INTERACTION WITH FGFR1.
RC   TISSUE=Placenta;
RX   PubMed=9660748; DOI=10.1074/jbc.273.29.17987;
RA   Xu H., Lee K.W., Goldfarb M.P.;
RT   "Novel recognition motif on fibroblast growth factor receptor mediates
RT   direct association and activation of SNT adapter proteins.";
RL   J. Biol. Chem. 273:17987-17990(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH ERK2.
RX   PubMed=15485655; DOI=10.1016/j.bbrc.2004.09.152;
RA   Huang L., Gotoh N., Zhang S., Shibuya M., Yamamoto T., Tsuchida N.;
RT   "SNT-2 interacts with ERK2 and negatively regulates ERK2 signaling in
RT   response to EGF stimulation.";
RL   Biochem. Biophys. Res. Commun. 324:1011-1017(2004).
RN   [6]
RP   FUNCTION, INTERACTION WITH FGFR1; NGFR; GRB2 AND PTPN11, AND
RP   PHOSPHORYLATION AT TYROSINE RESIDUES.
RX   PubMed=15094036; DOI=10.1016/s0014-5793(04)00287-x;
RA   Gotoh N., Laks S., Nakashima M., Lax I., Schlessinger J.;
RT   "FRS2 family docking proteins with overlapping roles in activation of MAP
RT   kinase have distinct spatial-temporal patterns of expression of their
RT   transcripts.";
RL   FEBS Lett. 564:14-18(2004).
RN   [7]
RP   STRUCTURE BY NMR OF 6-146.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the complex of the PTB domain of SNT-2 and 19-
RT   residue peptide (aa 1571-1589) of HALK.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: Adapter protein that links FGF and NGF receptors to
CC       downstream signaling pathways. Involved in the activation of MAP
CC       kinases. Down-regulates ERK2 signaling by interfering with the
CC       phosphorylation and nuclear translocation of ERK2.
CC       {ECO:0000269|PubMed:15094036}.
CC   -!- SUBUNIT: Binds NTRK1 (By similarity). Binds FGFR1, NGFR, GRB2, PTPN11
CC       and ERK2. {ECO:0000250}.
CC   -!- INTERACTION:
CC       O43559; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-725515, EBI-10173507;
CC       O43559; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-725515, EBI-357530;
CC       O43559; Q9NYG5-2: ANAPC11; NbExp=3; IntAct=EBI-725515, EBI-12224467;
CC       O43559; Q3KP44: ANKRD55; NbExp=3; IntAct=EBI-725515, EBI-14493093;
CC       O43559; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-725515, EBI-12811889;
CC       O43559; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-725515, EBI-2548012;
CC       O43559; Q9H5F2: C11orf1; NbExp=3; IntAct=EBI-725515, EBI-718615;
CC       O43559; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-725515, EBI-11976299;
CC       O43559; Q6P5X5: C22orf39; NbExp=3; IntAct=EBI-725515, EBI-7317823;
CC       O43559; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-725515, EBI-744545;
CC       O43559; Q8NA61: CBY2; NbExp=3; IntAct=EBI-725515, EBI-741724;
CC       O43559; P48745: CCN3; NbExp=3; IntAct=EBI-725515, EBI-3904822;
CC       O43559; Q6NVV7: CDPF1; NbExp=3; IntAct=EBI-725515, EBI-2802782;
CC       O43559; P27658: COL8A1; NbExp=3; IntAct=EBI-725515, EBI-747133;
CC       O43559; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-725515, EBI-350590;
CC       O43559; Q02930-3: CREB5; NbExp=3; IntAct=EBI-725515, EBI-10192698;
CC       O43559; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-725515, EBI-3867333;
CC       O43559; A2VCK2: DCDC2B; NbExp=3; IntAct=EBI-725515, EBI-10173222;
CC       O43559; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-725515, EBI-9679045;
CC       O43559; A0A0U1RQF7: DPEP2NB; NbExp=3; IntAct=EBI-725515, EBI-18398199;
CC       O43559; Q16610: ECM1; NbExp=3; IntAct=EBI-725515, EBI-947964;
CC       O43559; Q9NQ30: ESM1; NbExp=3; IntAct=EBI-725515, EBI-12260294;
CC       O43559; O43559: FRS3; NbExp=5; IntAct=EBI-725515, EBI-725515;
CC       O43559; P15976: GATA1; NbExp=3; IntAct=EBI-725515, EBI-3909284;
CC       O43559; P15976-2: GATA1; NbExp=5; IntAct=EBI-725515, EBI-9090198;
CC       O43559; P08631-2: HCK; NbExp=2; IntAct=EBI-725515, EBI-9834454;
CC       O43559; P49639: HOXA1; NbExp=7; IntAct=EBI-725515, EBI-740785;
CC       O43559; P35452-2: HOXD12; NbExp=3; IntAct=EBI-725515, EBI-17244356;
CC       O43559; Q02363: ID2; NbExp=3; IntAct=EBI-725515, EBI-713450;
CC       O43559; Q02535: ID3; NbExp=3; IntAct=EBI-725515, EBI-1387094;
CC       O43559; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-725515, EBI-747204;
CC       O43559; Q0VD86: INCA1; NbExp=3; IntAct=EBI-725515, EBI-6509505;
CC       O43559; Q9ULR0-1: ISY1; NbExp=3; IntAct=EBI-725515, EBI-18398632;
CC       O43559; Q9H079: KATNBL1; NbExp=3; IntAct=EBI-725515, EBI-715394;
CC       O43559; Q8TAV5: KCNJ5-AS1; NbExp=3; IntAct=EBI-725515, EBI-12810853;
CC       O43559; Q6ZU52: KIAA0408; NbExp=3; IntAct=EBI-725515, EBI-739493;
CC       O43559; Q5T749: KPRP; NbExp=5; IntAct=EBI-725515, EBI-10981970;
CC       O43559; Q15323: KRT31; NbExp=3; IntAct=EBI-725515, EBI-948001;
CC       O43559; Q14525: KRT33B; NbExp=3; IntAct=EBI-725515, EBI-1049638;
CC       O43559; O76011: KRT34; NbExp=5; IntAct=EBI-725515, EBI-1047093;
CC       O43559; Q92764: KRT35; NbExp=3; IntAct=EBI-725515, EBI-1058674;
CC       O43559; Q01546: KRT76; NbExp=3; IntAct=EBI-725515, EBI-2952745;
CC       O43559; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-725515, EBI-11959885;
CC       O43559; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-725515, EBI-10171774;
CC       O43559; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-725515, EBI-1052037;
CC       O43559; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-725515, EBI-9996449;
CC       O43559; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-725515, EBI-751260;
CC       O43559; Q3LI66: KRTAP6-2; NbExp=5; IntAct=EBI-725515, EBI-11962084;
CC       O43559; Q96FE5: LINGO1; NbExp=3; IntAct=EBI-725515, EBI-719955;
CC       O43559; Q8N456: LRRC18; NbExp=3; IntAct=EBI-725515, EBI-751373;
CC       O43559; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-725515, EBI-12516603;
CC       O43559; Q5JXC2: MIIP; NbExp=3; IntAct=EBI-725515, EBI-2801965;
CC       O43559; Q6IA69: NADSYN1; NbExp=3; IntAct=EBI-725515, EBI-748610;
CC       O43559; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-725515, EBI-945833;
CC       O43559; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-725515, EBI-22310682;
CC       O43559; Q92824-2: PCSK5; NbExp=3; IntAct=EBI-725515, EBI-11956269;
CC       O43559; Q9NR12: PDLIM7; NbExp=3; IntAct=EBI-725515, EBI-350517;
CC       O43559; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-725515, EBI-10232538;
CC       O43559; Q92569: PIK3R3; NbExp=3; IntAct=EBI-725515, EBI-79893;
CC       O43559; Q6P1J6-2: PLB1; NbExp=3; IntAct=EBI-725515, EBI-10694821;
CC       O43559; Q9Y342: PLLP; NbExp=3; IntAct=EBI-725515, EBI-3919291;
CC       O43559; O15162: PLSCR1; NbExp=3; IntAct=EBI-725515, EBI-740019;
CC       O43559; Q8WVV4-1: POF1B; NbExp=3; IntAct=EBI-725515, EBI-11986735;
CC       O43559; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-725515, EBI-12000762;
CC       O43559; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-725515, EBI-11320284;
CC       O43559; Q8HWS3: RFX6; NbExp=6; IntAct=EBI-725515, EBI-746118;
CC       O43559; Q9UFD9: RIMBP3; NbExp=3; IntAct=EBI-725515, EBI-10182375;
CC       O43559; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-725515, EBI-748391;
CC       O43559; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-725515, EBI-10269374;
CC       O43559; Q8N1D0-2: SLC22A18AS; NbExp=3; IntAct=EBI-725515, EBI-12829638;
CC       O43559; Q8WXH5: SOCS4; NbExp=2; IntAct=EBI-725515, EBI-3942425;
CC       O43559; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-725515, EBI-11959123;
CC       O43559; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-725515, EBI-10696971;
CC       O43559; O43597: SPRY2; NbExp=3; IntAct=EBI-725515, EBI-742487;
CC       O43559; Q8IWL8: STH; NbExp=3; IntAct=EBI-725515, EBI-12843506;
CC       O43559; O75716: STK16; NbExp=3; IntAct=EBI-725515, EBI-749295;
CC       O43559; P15884: TCF4; NbExp=3; IntAct=EBI-725515, EBI-533224;
CC       O43559; Q8TDR4: TCP10L; NbExp=3; IntAct=EBI-725515, EBI-3923210;
CC       O43559; Q96PF1: TGM7; NbExp=3; IntAct=EBI-725515, EBI-12029034;
CC       O43559; Q08117: TLE5; NbExp=3; IntAct=EBI-725515, EBI-717810;
CC       O43559; Q08117-2: TLE5; NbExp=5; IntAct=EBI-725515, EBI-11741437;
CC       O43559; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-725515, EBI-3650647;
CC       O43559; Q15654: TRIP6; NbExp=6; IntAct=EBI-725515, EBI-742327;
CC       O43559; Q86WV8: TSC1; NbExp=3; IntAct=EBI-725515, EBI-12806590;
CC       O43559; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-725515, EBI-10241197;
CC       O43559; O14817: TSPAN4; NbExp=3; IntAct=EBI-725515, EBI-8652667;
CC       O43559; Q9H9P5-5: UNKL; NbExp=3; IntAct=EBI-725515, EBI-12817837;
CC       O43559; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-725515, EBI-11957216;
CC       O43559; Q9BRX9: WDR83; NbExp=3; IntAct=EBI-725515, EBI-7705033;
CC       O43559; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-725515, EBI-12040603;
CC       O43559; Q8TF47: ZFP90; NbExp=3; IntAct=EBI-725515, EBI-11419867;
CC       O43559; Q8NF64-3: ZMIZ2; NbExp=3; IntAct=EBI-725515, EBI-12011330;
CC       O43559; Q15973: ZNF124; NbExp=3; IntAct=EBI-725515, EBI-2555767;
CC       O43559; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-725515, EBI-740727;
CC       O43559; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-725515, EBI-11962468;
CC       O43559; Q9NWS9-2: ZNF446; NbExp=3; IntAct=EBI-725515, EBI-740232;
CC       O43559; Q9H707: ZNF552; NbExp=3; IntAct=EBI-725515, EBI-2555731;
CC       O43559; Q9UC07-2: ZNF69; NbExp=3; IntAct=EBI-725515, EBI-12310821;
CC       O43559; Q86W11: ZSCAN30; NbExp=3; IntAct=EBI-725515, EBI-11793064;
CC       O43559; PRO_0000037548 [Q9WMX2]; Xeno; NbExp=3; IntAct=EBI-725515, EBI-6863741;
CC   -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
CC   -!- PTM: Phosphorylated by ULK2 in vitro (By similarity). Phosphorylated on
CC       tyrosine residues upon stimulation by BFGF or NGFB. {ECO:0000250,
CC       ECO:0000269|PubMed:15094036, ECO:0000269|PubMed:9660748}.
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DR   EMBL; AF036718; AAB92555.1; -; mRNA.
DR   EMBL; CR457026; CAG33307.1; -; mRNA.
DR   EMBL; AL365205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC010611; AAH10611.1; -; mRNA.
DR   CCDS; CCDS4860.1; -.
DR   RefSeq; NP_006644.1; NM_006653.4.
DR   RefSeq; XP_011512556.1; XM_011514254.2.
DR   RefSeq; XP_011512557.1; XM_011514255.2.
DR   PDB; 2KUP; NMR; -; A=8-146.
DR   PDB; 2KUQ; NMR; -; A=8-120.
DR   PDB; 2YS5; NMR; -; A=8-146.
DR   PDB; 2YT2; NMR; -; A=8-120.
DR   PDBsum; 2KUP; -.
DR   PDBsum; 2KUQ; -.
DR   PDBsum; 2YS5; -.
DR   PDBsum; 2YT2; -.
DR   AlphaFoldDB; O43559; -.
DR   BMRB; O43559; -.
DR   SMR; O43559; -.
DR   BioGRID; 116030; 113.
DR   IntAct; O43559; 108.
DR   MINT; O43559; -.
DR   STRING; 9606.ENSP00000362109; -.
DR   GlyGen; O43559; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O43559; -.
DR   PhosphoSitePlus; O43559; -.
DR   SwissPalm; O43559; -.
DR   BioMuta; FRS3; -.
DR   jPOST; O43559; -.
DR   MassIVE; O43559; -.
DR   MaxQB; O43559; -.
DR   PaxDb; O43559; -.
DR   PeptideAtlas; O43559; -.
DR   ProteomicsDB; 49051; -.
DR   Antibodypedia; 30086; 238 antibodies from 28 providers.
DR   DNASU; 10817; -.
DR   Ensembl; ENST00000259748.6; ENSP00000259748.2; ENSG00000137218.10.
DR   Ensembl; ENST00000373018.7; ENSP00000362109.3; ENSG00000137218.10.
DR   GeneID; 10817; -.
DR   KEGG; hsa:10817; -.
DR   MANE-Select; ENST00000373018.7; ENSP00000362109.3; NM_006653.5; NP_006644.1.
DR   UCSC; uc003orc.3; human.
DR   AGR; HGNC:16970; -.
DR   CTD; 10817; -.
DR   DisGeNET; 10817; -.
DR   GeneCards; FRS3; -.
DR   HGNC; HGNC:16970; FRS3.
DR   HPA; ENSG00000137218; Low tissue specificity.
DR   MIM; 607744; gene.
DR   neXtProt; NX_O43559; -.
DR   OpenTargets; ENSG00000137218; -.
DR   PharmGKB; PA134961503; -.
DR   VEuPathDB; HostDB:ENSG00000137218; -.
DR   eggNOG; KOG4047; Eukaryota.
DR   GeneTree; ENSGT00940000159495; -.
DR   HOGENOM; CLU_022374_0_0_1; -.
DR   InParanoid; O43559; -.
DR   OMA; CQPDRGG; -.
DR   OrthoDB; 2996885at2759; -.
DR   PhylomeDB; O43559; -.
DR   TreeFam; TF324994; -.
DR   PathwayCommons; O43559; -.
DR   Reactome; R-HSA-5654693; FRS-mediated FGFR1 signaling.
DR   Reactome; R-HSA-5654700; FRS-mediated FGFR2 signaling.
DR   Reactome; R-HSA-5654706; FRS-mediated FGFR3 signaling.
DR   Reactome; R-HSA-5654712; FRS-mediated FGFR4 signaling.
DR   Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-HSA-9028731; Activated NTRK2 signals through FRS2 and FRS3.
DR   Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR   Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR   Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR   SignaLink; O43559; -.
DR   SIGNOR; O43559; -.
DR   BioGRID-ORCS; 10817; 10 hits in 1154 CRISPR screens.
DR   ChiTaRS; FRS3; human.
DR   EvolutionaryTrace; O43559; -.
DR   GeneWiki; FRS3; -.
DR   GenomeRNAi; 10817; -.
DR   Pharos; O43559; Tbio.
DR   PRO; PR:O43559; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; O43559; protein.
DR   Bgee; ENSG00000137218; Expressed in right hemisphere of cerebellum and 121 other tissues.
DR   ExpressionAtlas; O43559; baseline and differential.
DR   Genevisible; O43559; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005104; F:fibroblast growth factor receptor binding; IPI:MGI.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IBA:GO_Central.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IGI:MGI.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   CDD; cd01202; PTB_FRS2; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR038742; FRS2_PTB.
DR   InterPro; IPR002404; IRS_PTB.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   PANTHER; PTHR21258; DOCKING PROTEIN RELATED; 1.
DR   PANTHER; PTHR21258:SF39; FIBROBLAST GROWTH FACTOR RECEPTOR SUBSTRATE 3; 1.
DR   Pfam; PF02174; IRS; 1.
DR   SMART; SM01244; IRS; 1.
DR   SMART; SM00310; PTBI; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS51064; IRS_PTB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Lipoprotein; Membrane; Myristate; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..492
FT                   /note="Fibroblast growth factor receptor substrate 3"
FT                   /id="PRO_0000087346"
FT   DOMAIN          13..115
FT                   /note="IRS-type PTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT   REGION          153..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          467..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000305|PubMed:9660748"
FT   VARIANT         221
FT                   /note="P -> L (in dbSNP:rs3747747)"
FT                   /id="VAR_033855"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:2KUQ"
FT   STRAND          18..26
FT                   /evidence="ECO:0007829|PDB:2KUP"
FT   STRAND          32..40
FT                   /evidence="ECO:0007829|PDB:2KUP"
FT   STRAND          45..48
FT                   /evidence="ECO:0007829|PDB:2KUP"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:2KUP"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:2KUP"
FT   HELIX           59..61
FT                   /evidence="ECO:0007829|PDB:2KUP"
FT   STRAND          65..68
FT                   /evidence="ECO:0007829|PDB:2KUP"
FT   STRAND          71..76
FT                   /evidence="ECO:0007829|PDB:2KUP"
FT   STRAND          80..82
FT                   /evidence="ECO:0007829|PDB:2KUP"
FT   STRAND          84..90
FT                   /evidence="ECO:0007829|PDB:2KUP"
FT   HELIX           94..105
FT                   /evidence="ECO:0007829|PDB:2KUP"
SQ   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
//