FRS3_HUMAN
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 03-AUG-2022, entry version 165.
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; Q8TAV5: C11orf45; NbExp=3; IntAct=EBI-725515, EBI-12810853;
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; 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 BioMuta; FRS3; -.
DR jPOST; O43559; -.
DR MassIVE; O43559; -.
DR MaxQB; O43559; -.
DR PaxDb; O43559; -.
DR PeptideAtlas; O43559; -.
DR PRIDE; O43559; -.
DR ProteomicsDB; 49051; -.
DR Antibodypedia; 30086; 218 antibodies from 27 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 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; 473504at2759; -.
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 1076 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 GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd01202; PTB_FRS2; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR038742; FRS2_PTB.
DR InterPro; IPR002404; IRS_PTB.
DR InterPro; IPR011993; PH-like_dom_sf.
DR Pfam; PF02174; IRS; 1.
DR SMART; SM00310; PTBI; 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
