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GRB2-associated-binding protein 1 (GRB2-associated binder 1) (Growth factor receptor bound protein 2-associated protein 1)

 GAB1_MOUSE              Reviewed;         695 AA.
Q9QYY0; Q91VW7;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 2.
10-OCT-2018, entry version 146.
RecName: Full=GRB2-associated-binding protein 1;
AltName: Full=GRB2-associated binder 1;
AltName: Full=Growth factor receptor bound protein 2-associated protein 1;
Name=Gab1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Sachs M.;
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary tumor;
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).
[3]
PHOSPHORYLATION IN RESPONSE TO FGFR1 SIGNALING, AND INTERACTION WITH
GRB2.
PubMed=11353842; DOI=10.1073/pnas.111114298;
Ong S.H., Hadari Y.R., Gotoh N., Guy G.R., Schlessinger J., Lax I.;
"Stimulation of phosphatidylinositol 3-kinase by fibroblast growth
factor receptors is mediated by coordinated recruitment of multiple
docking proteins.";
Proc. Natl. Acad. Sci. U.S.A. 98:6074-6079(2001).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Lung, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
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).
[6]
TISSUE SPECIFICITY.
PubMed=29408807; DOI=10.1172/JCI97350;
Yousaf R., Ahmed Z.M., Giese A.P., Morell R.J., Lagziel A.,
Dabdoub A., Wilcox E.R., Riazuddin S., Friedman T.B., Riazuddin S.;
"Modifier variant of METTL13 suppresses human GAB1-associated profound
deafness.";
J. Clin. Invest. 128:1509-1522(2018).
-!- FUNCTION: Adapter protein that plays a role in intracellular
signaling cascades triggered by activated receptor-type kinases.
Plays a role in FGFR1 signaling. Probably involved in signaling by
the epidermal growth factor receptor (EGFR) and the insulin
receptor (INSR). Involved in the MET/HGF-signaling pathway.
{ECO:0000250|UniProtKB:Q13480}.
-!- SUBUNIT: Interacts with GRB2 and with other SH2-containing
proteins (PubMed:11353842). Interacts with phosphorylated LAT2.
Interacts with PTPRJ (By similarity). Interacts (phosphorylated)
with PTPN11 (By similarity). Interacts with HCK (By similarity).
Identified in a complex containing FRS2, GRB2, GAB1, PIK3R1 and
SOS1 (By similarity). Part of a tripartite complex containing
GAB1, METTL13 and SPRY2. Interacts with METTL13 (By similarity).
{ECO:0000250|UniProtKB:Q13480, ECO:0000269|PubMed:11353842}.
-!- INTERACTION:
Q60631:Grb2; NbExp=8; IntAct=EBI-644784, EBI-1688;
-!- TISSUE SPECIFICITY: Expressed in the inner ear. Expression is
detected in the cochlear duct, spiral limbus region, efferent and
afferent nerves, and in spiral ganglion neurons.
{ECO:0000269|PubMed:29408807}.
-!- PTM: Phosphorylated on tyrosine residue(s) by the epidermal growth
factor receptor (EGFR) and the insulin receptor (INSR). Tyrosine
phosphorylation of GAB1 mediates interaction with several proteins
that contain SH2 domains. Phosphorylated on tyrosine residues by
HCK upon IL6 signaling (By similarity). Phosphorylated in response
to FGFR1 activation. {ECO:0000250, ECO:0000269|PubMed:11353842}.
-!- SIMILARITY: Belongs to the GAB family. {ECO:0000305}.
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EMBL; AJ250669; CAB59832.1; -; mRNA.
EMBL; BC007483; AAH07483.1; -; mRNA.
CCDS; CCDS22443.1; -.
RefSeq; NP_067331.2; NM_021356.2.
UniGene; Mm.277409; -.
ProteinModelPortal; Q9QYY0; -.
BioGrid; 199793; 8.
DIP; DIP-39377N; -.
IntAct; Q9QYY0; 12.
MINT; Q9QYY0; -.
STRING; 10090.ENSMUSP00000034150; -.
iPTMnet; Q9QYY0; -.
PhosphoSitePlus; Q9QYY0; -.
MaxQB; Q9QYY0; -.
PaxDb; Q9QYY0; -.
PRIDE; Q9QYY0; -.
Ensembl; ENSMUST00000034150; ENSMUSP00000034150; ENSMUSG00000031714.
GeneID; 14388; -.
KEGG; mmu:14388; -.
UCSC; uc009mjb.2; mouse.
CTD; 2549; -.
MGI; MGI:108088; Gab1.
eggNOG; ENOG410IEIX; Eukaryota.
eggNOG; ENOG4111RDE; LUCA.
GeneTree; ENSGT00510000046662; -.
HOGENOM; HOG000236270; -.
HOVERGEN; HBG051685; -.
InParanoid; Q9QYY0; -.
KO; K09593; -.
OrthoDB; EOG091G03BY; -.
PhylomeDB; Q9QYY0; -.
TreeFam; TF329487; -.
Reactome; R-MMU-109704; PI3K Cascade.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-180292; GAB1 signalosome.
Reactome; R-MMU-1963642; PI3K events in ERBB2 signaling.
Reactome; R-MMU-5654689; PI-3K cascade:FGFR1.
Reactome; R-MMU-5654695; PI-3K cascade:FGFR2.
Reactome; R-MMU-5654710; PI-3K cascade:FGFR3.
Reactome; R-MMU-5654720; PI-3K cascade:FGFR4.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-8851907; MET activates PI3K/AKT signaling.
Reactome; R-MMU-8853659; RET signaling.
Reactome; R-MMU-8865999; MET activates PTPN11.
Reactome; R-MMU-8875555; MET activates RAP1 and RAC1.
Reactome; R-MMU-8875656; MET receptor recycling.
Reactome; R-MMU-9032759; NTRK2 activates RAC1.
ChiTaRS; Gab1; mouse.
PRO; PR:Q9QYY0; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031714; Expressed in 284 organ(s), highest expression level in vestibular membrane of cochlear duct.
ExpressionAtlas; Q9QYY0; baseline and differential.
Genevisible; Q9QYY0; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:MGI.
GO; GO:0007257; P:activation of JUN kinase activity; IMP:MGI.
GO; GO:0000187; P:activation of MAPK activity; IDA:MGI.
GO; GO:0001525; P:angiogenesis; ISO:MGI.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IDA:BHF-UCL.
GO; GO:0090668; P:endothelial cell chemotaxis to vascular endothelial growth factor; ISO:MGI.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IMP:MGI.
GO; GO:0008544; P:epidermis development; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IMP:MGI.
GO; GO:0060711; P:labyrinthine layer development; IMP:MGI.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
GO; GO:0038089; P:positive regulation of cell migration by vascular endothelial growth factor signaling pathway; IDA:BHF-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
GO; GO:0030334; P:regulation of cell migration; IGI:MGI.
GO; GO:0035728; P:response to hepatocyte growth factor; ISO:MGI.
GO; GO:0006979; P:response to oxidative stress; IDA:MGI.
GO; GO:0007165; P:signal transduction; IDA:MGI.
GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; ISO:MGI.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
Pfam; PF00169; PH; 1.
SMART; SM00233; PH; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q13480}.
CHAIN 2 695 GRB2-associated-binding protein 1.
/FTId=PRO_0000050284.
DOMAIN 5 116 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
COMPBIAS 450 541 Pro-rich.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q13480}.
MOD_RES 251 251 Phosphoserine.
{ECO:0000250|UniProtKB:Q13480}.
MOD_RES 253 253 Phosphoserine.
{ECO:0000250|UniProtKB:Q13480}.
MOD_RES 266 266 Phosphoserine.
{ECO:0000250|UniProtKB:Q13480}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000250|UniProtKB:Q13480}.
MOD_RES 388 388 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13480}.
MOD_RES 403 403 Phosphoserine.
{ECO:0000250|UniProtKB:Q13480}.
MOD_RES 455 455 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 628 628 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q13480}.
MOD_RES 639 639 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13480}.
MOD_RES 652 652 Phosphoserine.
{ECO:0000250|UniProtKB:Q13480}.
MOD_RES 660 660 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q13480}.
MOD_RES 684 684 Phosphoserine.
{ECO:0000250|UniProtKB:Q13480}.
CONFLICT 236 236 F -> L (in Ref. 1; CAB59832).
{ECO:0000305}.
CONFLICT 351 351 T -> S (in Ref. 1; CAB59832).
{ECO:0000305}.
CONFLICT 379 379 A -> V (in Ref. 1; CAB59832).
{ECO:0000305}.
SEQUENCE 695 AA; 76812 MW; F0A567896E058C58 CRC64;
MSGGEVVCSG WLRKSPPEKK LKRYAWKRRW FVLRSGRLTG DPDVLEYYKN DHAKKPIRII
DLNLCQQVDA GLTFNKKEFE NSYIFDINTI DRIFYLVADS EEDMNKWVRC ICDICGFNPT
EEDPVKPLTG SSQAPVDSPF AISTAPASSQ MEASSVALPP PYQVISLPPH PDTLGLQDDP
QDYLLLINCQ SKKPEPNRTL FDSAKPTFSE TDCNDNVPSH QTPASSQSKH GMNGFFQQQM
MYDCPPSRLT SVSGESSLYN LPRSYSHDVL PKESPSSTEA DGELYTFNTP SGTAGVETQM
RHVSISYDIP PTPGNTYQIP RTFPESTLGQ SSKLDTIPDI PPPRPPKPHP THDRSPVETC
GVPRTASDTD SSYCIPPPAG MTPSRSNTIS TVDLNKLRKD ASSQDCYDIP RTFPSDRSSS
LEGFHSQYKI KSVLTAGGVS GEELDENYVP MNPNSPPRQH SGSFTEPIQE PNYVPMTPGT
FDFSSFGMQV PPPAHMGFRS SPKTPPRRPV PVADCEPPPV DRNLKPDRKV KPAPLDIKPL
SEWEELQAPV RSPITRSFAR DSSRFPMSPR PDSVHSTTSS SDSHDSEENY VPMNPNLSGE
DPNLFASNSL DGGSSPMNKP KGDKQVEYLD LDLDSGKSTP PRKQKSSGSG SSMADERVDY
VVVDQQKTLA LKSTREAWTD GRQSTESETP TKNVK


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