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Fibroblast growth factor receptor substrate 2 (FGFR substrate 2) (FGFR-signaling adaptor SNT) (Suc1-associated neurotrophic factor target 1) (SNT-1)

 FRS2_HUMAN              Reviewed;         508 AA.
Q8WU20; B0LPF2; B2R684; O43558; Q7LDQ6;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
14-OCT-2008, sequence version 4.
23-MAY-2018, entry version 149.
RecName: Full=Fibroblast growth factor receptor substrate 2;
Short=FGFR substrate 2;
AltName: Full=FGFR-signaling adaptor SNT;
AltName: Full=Suc1-associated neurotrophic factor target 1;
Short=SNT-1;
Name=FRS2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FGFR1, MYRISTOYLATION AT
GLY-2, AND PHOSPHORYLATION AT TYROSINE RESIDUES.
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].
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
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).
[7]
INTERACTION WITH CKS2; GRB2; PTPN11; SRC; NTRK1; NTRK2 AND NTRK3,
MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT TYROSINE RESIDUES, AND
TISSUE SPECIFICITY.
PubMed=10092678; DOI=10.1074/jbc.274.14.9861;
Meakin S.O., MacDonald J.I.S., Gryz E.A., Kubu C.J., Verdi J.M.;
"The signaling adapter FRS-2 competes with Shc for binding to the
nerve growth factor receptor TrkA. A model for discriminating
proliferation and differentiation.";
J. Biol. Chem. 274:9861-9870(1999).
[8]
PHOSPHORYLATION BY MAPK1/ERK2 AND MAPK3/ERK1, INTERACTION WITH
MAPK1/ERK2 AND MAPK3/ERK1, AND FUNCTION.
PubMed=12974390; DOI=10.1515/BC.2003.134;
Wu Y., Chen Z., Ullrich A.;
"EGFR and FGFR signaling through FRS2 is subject to negative feedback
control by ERK1/2.";
Biol. Chem. 384:1215-1226(2003).
[9]
INTERACTION WITH NTRK1.
PubMed=15488758; DOI=10.1016/j.ccr.2004.09.011;
Tacconelli A., Farina A.R., Cappabianca L., Desantis G., Tessitore A.,
Vetuschi A., Sferra R., Rucci N., Argenti B., Screpanti I., Gulino A.,
Mackay A.R.;
"TrkA alternative splicing: a regulated tumor-promoting switch in
human neuroblastoma.";
Cancer Cell 6:347-360(2004).
[10]
INTERACTION WITH ALK, AND PHOSPHORYLATION.
PubMed=17274988; DOI=10.1016/j.febslet.2007.01.039;
Degoutin J., Vigny M., Gouzi J.Y.;
"ALK activation induces Shc and FRS2 recruitment: Signaling and
phenotypic outcomes in PC12 cells differentiation.";
FEBS Lett. 581:727-734(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
FUNCTION IN ACTIVATION OF AKT1; PLCG1; MAPK1/ERK2, MAPK3/ERK1 AND MAP
KINASE SIGNALING, INTERACTION WITH FGFR1, AND PHOSPHORYLATION.
PubMed=21765395; DOI=10.1038/emboj.2011.234;
Persaud A., Alberts P., Hayes M., Guettler S., Clarke I., Sicheri F.,
Dirks P., Ciruna B., Rotin D.;
"Nedd4-1 binds and ubiquitylates activated FGFR1 to control its
endocytosis and function.";
EMBO J. 30:3259-3273(2011).
[13]
REVIEW ON FUNCTION; SUBUNIT AND PHOSPHORYLATION.
PubMed=18452557; DOI=10.1111/j.1349-7006.2008.00840.x;
Gotoh N.;
"Regulation of growth factor signaling by FRS2 family docking/scaffold
adaptor proteins.";
Cancer Sci. 99:1319-1325(2008).
[14]
REVIEW ON FUNCTION IN FGF SIGNALING.
PubMed=20094046; DOI=10.1038/nrc2780;
Turner N., Grose R.;
"Fibroblast growth factor signalling: from development to cancer.";
Nat. Rev. Cancer 10:116-129(2010).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-365, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
STRUCTURE BY NMR OF 11-136 IN COMPLEX WITH FGFR1.
PubMed=11090629; DOI=10.1016/S1097-2765(05)00087-0;
Dhalluin C., Yan K.S., Plotnikova O., Lee K.W., Zeng L., Kuti M.,
Mujtaba S., Goldfarb M.P., Zhou M.-M.;
"Structural basis of SNT PTB domain interactions with distinct
neurotrophic receptors.";
Mol. Cell 6:921-929(2000).
-!- FUNCTION: Adapter protein that links activated FGR and NGF
receptors to downstream signaling pathways. Plays an important
role in the activation of MAP kinases and in the phosphorylation
of PIK3R1, the regulatory subunit of phosphatidylinositol 3-
kinase, in response to ligand-mediated activation of FGFR1.
Modulates signaling via SHC1 by competing for a common binding
site on NTRK1. {ECO:0000269|PubMed:12974390,
ECO:0000269|PubMed:21765395}.
-!- SUBUNIT: Part of a complex containing FRS2, GRB2, GAB1, PIK3R1 and
SOS1. Part of a complex containing GRB2 and CBL. Identified in a
complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1,
GAP43 and CTTN. Binds RET (By similarity). Binds ALK, FGFR1, CKS2,
MAPK1/ERK2, MAPK3/ERK1 and SRC. The tyrosine-phosphorylated
protein binds the SH2 domains of GRB2 and PTPN11. Interacts with
NTRK1, NTRK2 and NTRK3 (phosphorylated upon ligand-binding).
{ECO:0000250, ECO:0000269|PubMed:10092678,
ECO:0000269|PubMed:11090629, ECO:0000269|PubMed:12974390,
ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:17274988,
ECO:0000269|PubMed:21765395, ECO:0000269|PubMed:9660748}.
-!- SUBCELLULAR LOCATION: Endomembrane system. Note=Cytoplasmic,
membrane-bound.
-!- TISSUE SPECIFICITY: Highly expressed in heart, brain, spleen,
lung, liver, skeletal muscle, kidney and testis.
{ECO:0000269|PubMed:10092678}.
-!- PTM: Phosphorylated by ULK2 in vitro (By similarity).
Phosphorylated on tyrosine residues upon stimulation by NGF or
FGF2. Phosphorylated on tyrosine residues by activated ALK and
FGFR1. Phosphorylated on tyrosine residues upon activation of
FGFR2 and FGFR3. Phosphorylated on threonine residues by MAP
kinases; this inhibits tyrosine phosphorylation, and thereby down-
regulates FRS2-mediated activation of MAP kinases. {ECO:0000250,
ECO:0000269|PubMed:10092678, ECO:0000269|PubMed:12974390,
ECO:0000269|PubMed:17274988, ECO:0000269|PubMed:21765395,
ECO:0000269|PubMed:9660748}.
-!- PTM: Ubiquitinated when tyrosine phosphorylated and in a complex
with GRB2. The unphosphorylated form is not subject to
ubiquitination (By similarity). {ECO:0000250}.
-!- SEQUENCE CAUTION:
Sequence=AAH21562.1; Type=Erroneous termination; Positions=509; Note=Translated as stop.; Evidence={ECO:0000305};
Sequence=BAG35381.1; Type=Erroneous termination; Positions=509; Note=Translated as stop.; Evidence={ECO:0000305};
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EMBL; AF036717; AAB92554.1; -; mRNA.
EMBL; AK312477; BAG35381.1; ALT_SEQ; mRNA.
EMBL; EU332842; ABY87531.1; -; Genomic_DNA.
EMBL; AC018921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW97225.1; -; Genomic_DNA.
EMBL; BC021562; AAH21562.1; ALT_SEQ; mRNA.
CCDS; CCDS41809.1; -.
RefSeq; NP_001036020.1; NM_001042555.2.
RefSeq; NP_001265280.1; NM_001278351.1.
RefSeq; NP_001265282.1; NM_001278353.1.
RefSeq; NP_001265283.1; NM_001278354.1.
RefSeq; NP_001265284.1; NM_001278355.1.
RefSeq; NP_001265285.1; NM_001278356.1.
RefSeq; NP_001265286.1; NM_001278357.1.
RefSeq; NP_006645.3; NM_006654.4.
RefSeq; XP_016874206.1; XM_017018717.1.
RefSeq; XP_016874207.1; XM_017018718.1.
RefSeq; XP_016874208.1; XM_017018719.1.
UniGene; Hs.593446; -.
PDB; 1XR0; NMR; -; B=11-136.
PDB; 2MFQ; NMR; -; A=11-122.
PDBsum; 1XR0; -.
PDBsum; 2MFQ; -.
ProteinModelPortal; Q8WU20; -.
SMR; Q8WU20; -.
BioGrid; 116031; 28.
ELM; Q8WU20; -.
IntAct; Q8WU20; 9.
MINT; Q8WU20; -.
STRING; 9606.ENSP00000299293; -.
iPTMnet; Q8WU20; -.
PhosphoSitePlus; Q8WU20; -.
DMDM; 209572769; -.
MaxQB; Q8WU20; -.
PaxDb; Q8WU20; -.
PeptideAtlas; Q8WU20; -.
PRIDE; Q8WU20; -.
Ensembl; ENST00000397997; ENSP00000381083; ENSG00000166225.
Ensembl; ENST00000549921; ENSP00000450048; ENSG00000166225.
Ensembl; ENST00000550389; ENSP00000447241; ENSG00000166225.
GeneID; 10818; -.
KEGG; hsa:10818; -.
UCSC; uc009zrj.5; human.
CTD; 10818; -.
DisGeNET; 10818; -.
EuPathDB; HostDB:ENSG00000166225.8; -.
GeneCards; FRS2; -.
HGNC; HGNC:16971; FRS2.
HPA; HPA038323; -.
MIM; 607743; gene.
neXtProt; NX_Q8WU20; -.
OpenTargets; ENSG00000166225; -.
PharmGKB; PA134850063; -.
eggNOG; KOG4047; Eukaryota.
eggNOG; ENOG410XS2S; LUCA.
GeneTree; ENSGT00510000046707; -.
HOGENOM; HOG000290694; -.
HOVERGEN; HBG062705; -.
InParanoid; Q8WU20; -.
KO; K12461; -.
OMA; SAHKVEF; -.
OrthoDB; EOG091G06AV; -.
PhylomeDB; Q8WU20; -.
TreeFam; TF324994; -.
Reactome; R-HSA-109704; PI3K Cascade.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-170968; Frs2-mediated activation.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-5654689; PI-3K cascade:FGFR1.
Reactome; R-HSA-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-HSA-5654695; PI-3K cascade:FGFR2.
Reactome; R-HSA-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-HSA-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-HSA-5654710; PI-3K cascade:FGFR3.
Reactome; R-HSA-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-HSA-5654720; PI-3K cascade:FGFR4.
Reactome; R-HSA-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-HSA-5654727; Negative regulation of FGFR2 signaling.
Reactome; R-HSA-5654732; Negative regulation of FGFR3 signaling.
Reactome; R-HSA-5654733; Negative regulation of FGFR4 signaling.
Reactome; R-HSA-5655253; Signaling by FGFR2 in disease.
Reactome; R-HSA-5655291; Signaling by FGFR4 in disease.
Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-8853334; Signaling by FGFR3 fusions in cancer.
Reactome; R-HSA-8853338; Signaling by FGFR3 point mutants in cancer.
Reactome; R-HSA-8853659; RET signaling.
Reactome; R-HSA-9028731; Activated NTRK2 signals through FRS2 and FRS3.
SignaLink; Q8WU20; -.
SIGNOR; Q8WU20; -.
ChiTaRS; FRS2; human.
EvolutionaryTrace; Q8WU20; -.
GeneWiki; FRS2; -.
GenomeRNAi; 10818; -.
PRO; PR:Q8WU20; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000166225; -.
CleanEx; HS_FRS2; -.
ExpressionAtlas; Q8WU20; baseline and differential.
Genevisible; Q8WU20; HS.
GO; GO:0005913; C:cell-cell adherens junction; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005768; C:endosome; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; TAS:UniProtKB.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; TAS:Reactome.
GO; GO:0005104; F:fibroblast growth factor receptor binding; IPI:MGI.
GO; GO:0005168; F:neurotrophin TRKA receptor binding; IPI:UniProtKB.
GO; GO:0019211; F:phosphatase activator activity; TAS:UniProtKB.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; TAS:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; IEA:Ensembl.
GO; GO:0000186; P:activation of MAPKK activity; TAS:Reactome.
GO; GO:0008595; P:anterior/posterior axis specification, embryo; IEA:Ensembl.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IGI:MGI.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:UniProtKB.
GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
GO; GO:0070307; P:lens fiber cell development; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:2000726; P:negative regulation of cardiac muscle cell differentiation; IGI:BHF-UCL.
GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
GO; GO:0046619; P:optic placode formation involved in camera-type eye formation; IEA:Ensembl.
GO; GO:0001759; P:organ induction; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; TAS:Reactome.
GO; GO:0060527; P:prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis; IEA:Ensembl.
GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
GO; GO:0050678; P:regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0007185; P:transmembrane receptor protein tyrosine phosphatase signaling pathway; TAS:UniProtKB.
GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
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; Ubl conjugation.
INIT_MET 1 1 Removed.
CHAIN 2 508 Fibroblast growth factor receptor
substrate 2.
/FTId=PRO_0000087344.
DOMAIN 13 115 IRS-type PTB. {ECO:0000255|PROSITE-
ProRule:PRU00389}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 196 196 Phosphotyrosine; by FGFR1.
{ECO:0000250|UniProtKB:Q8C180}.
MOD_RES 211 211 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 221 221 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 306 306 Phosphotyrosine; by FGFR1.
{ECO:0000250|UniProtKB:Q8C180}.
MOD_RES 349 349 Phosphotyrosine; by FGFR1.
{ECO:0000250|UniProtKB:Q8C180}.
MOD_RES 365 365 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 392 392 Phosphotyrosine; by FGFR1.
{ECO:0000250|UniProtKB:Q8C180}.
MOD_RES 436 436 Phosphotyrosine; by FGFR1.
{ECO:0000250|UniProtKB:Q8C180}.
MOD_RES 471 471 Phosphotyrosine; by FGFR1.
{ECO:0000250|UniProtKB:Q8C180}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:10092678,
ECO:0000269|PubMed:9660748}.
VARIANT 303 303 K -> N (in dbSNP:rs12580717).
/FTId=VAR_046966.
VARIANT 449 449 N -> D (in dbSNP:rs35232109).
/FTId=VAR_046967.
TURN 15 18 {ECO:0000244|PDB:2MFQ}.
STRAND 20 26 {ECO:0000244|PDB:1XR0}.
STRAND 32 34 {ECO:0000244|PDB:2MFQ}.
STRAND 36 40 {ECO:0000244|PDB:1XR0}.
STRAND 45 49 {ECO:0000244|PDB:1XR0}.
TURN 50 52 {ECO:0000244|PDB:1XR0}.
STRAND 53 57 {ECO:0000244|PDB:1XR0}.
TURN 59 61 {ECO:0000244|PDB:2MFQ}.
STRAND 62 67 {ECO:0000244|PDB:1XR0}.
STRAND 69 76 {ECO:0000244|PDB:1XR0}.
STRAND 84 90 {ECO:0000244|PDB:1XR0}.
HELIX 94 107 {ECO:0000244|PDB:1XR0}.
SEQUENCE 508 AA; 57029 MW; 833714EE12097C75 CRC64;
MGSCCSCPDK DTVPDNHRNK FKVINVDDDG NELGSGIMEL TDTELILYTR KRDSVKWHYL
CLRRYGYDSN LFSFESGRRC QTGQGIFAFK CARAEELFNM LQEIMQNNSI NVVEEPVVER
NNHQTELEVP RTPRTPTTPG FAAQNLPNGY PRYPSFGDAS SHPSSRHPSV GSARLPSVGE
ESTHPLLVAE EQVHTYVNTT GVQEERKNRT SVHVPLEARV SNAESSTPKE EPSSIEDRDP
QILLEPEGVK FVLGPTPVQK QLMEKEKLEQ LGRDQVSGSG ANNTEWDTGY DSDERRDAPS
VNKLVYENIN GLSIPSASGV RRGRLTSTST SDTQNINNSA QRRTALLNYE NLPSLPPVWE
ARKLSRDEDD NLGPKTPSLN GYHNNLDPMH NYVNTENVTV PASAHKIEYS RRRDCTPTVF
NFDIRRPSLE HRQLNYIQVD LEGGSDSDNP QTPKTPTTPL PQTPTRRTEL YAVIDIERTA
AMSNLQKALP RDDGTSRKTR HNSTDLPM


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