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GRB2-associated-binding protein 2 (GRB2-associated binder 2) (Growth factor receptor bound protein 2-associated protein 2) (PH domain-containing adaptor molecule p97)

 GAB2_MOUSE              Reviewed;         665 AA.
Q9Z1S8; Q9R1X3;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 2.
12-SEP-2018, entry version 124.
RecName: Full=GRB2-associated-binding protein 2;
AltName: Full=GRB2-associated binder 2;
AltName: Full=Growth factor receptor bound protein 2-associated protein 2;
AltName: Full=PH domain-containing adaptor molecule p97;
Name=Gab2;
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], PROTEIN SEQUENCE OF 2-5; 81-91; 251-270;
277-293; 512-529; 630-635 AND 640-648, FUNCTION, PHOSPHORYLATION,
INTERACTION WITH GRB2; PTPN11 AND SHC1, AND TISSUE SPECIFICITY.
PubMed=9885561; DOI=10.1016/S1097-2765(00)80288-9;
Gu H., Pratt J.C., Burakoff S.J., Neel B.G.;
"Cloning of p97/Gab2, the major SHP2-binding protein in hematopoietic
cells, reveals a novel pathway for cytokine-induced gene activation.";
Mol. Cell 2:729-740(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY,
PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN11, AND INTERACTION WITH
GRB2; PTPN11 AND PI-3 KINASE.
PubMed=10068651;
Nishida K., Yoshida Y., Itoh M., Fukada T., Ohtani T., Shirogane T.,
Atsumi T., Takahashi-Tezuka M., Ishihara K., Hibi M., Hirano T.;
"Gab-family adapter proteins act downstream of cytokine and growth
factor receptors and T- and B-cell antigen receptors.";
Blood 93:1809-1816(1999).
[3]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11449275; DOI=10.1038/35084076;
Gu H., Saito K., Klaman L.D., Shen J., Fleming T., Wang Y.,
Pratt J.C., Lin G., Lim B., Kinet J.-P., Neel B.G.;
"Essential role for Gab2 in the allergic response.";
Nature 412:186-190(2001).
[4]
FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH TNFRSF11A, AND
PHOSPHORYLATION AT TYR-441.
PubMed=15750601; DOI=10.1038/nm1203;
Wada T., Nakashima T., Oliveira-dos-Santos A.J., Gasser J., Hara H.,
Schett G., Penninger J.M.;
"The molecular scaffold Gab2 is a crucial component of RANK signaling
and osteoclastogenesis.";
Nat. Med. 11:394-399(2005).
[5]
INTERACTION WITH SYK, LIPID-BINDING, AND MUTAGENESIS OF ARG-32.
PubMed=16456001; DOI=10.4049/jimmunol.176.4.2421;
Yu M., Lowell C.A., Neel B.G., Gu H.;
"Scaffolding adapter Grb2-associated binder 2 requires Syk to transmit
signals from FcepsilonRI.";
J. Immunol. 176:2421-2429(2006).
[6]
FUNCTION.
PubMed=17374739; DOI=10.1182/blood-2006-11-060707;
Zhang Y., Diaz-Flores E., Li G., Wang Z., Kang Z., Haviernikova E.,
Rowe S., Qu C.-K., Tse W., Shannon K.M., Bunting K.D.;
"Abnormal hematopoiesis in Gab2 mutant mice.";
Blood 110:116-124(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261; THR-262; TYR-263
AND TYR-290, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[8]
MUTAGENESIS OF ARG-32, AND PHOSPHORYLATION AT SER-211 AND THR-388.
PubMed=19172738; DOI=10.1038/emboj.2008.159;
Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
Guilhaus M., James D.E., Daly R.J.;
"Phosphorylation-dependent binding of 14-3-3 terminates signalling by
the Gab2 docking protein.";
EMBO J. 27:2305-2316(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-405, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Lung, Spleen, 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).
-!- FUNCTION: Adapter protein which acts downstream of several
membrane receptors including cytokine, antigen, hormone, cell
matrix and growth factor receptors to regulate multiple signaling
pathways. Regulates osteoclast differentiation mediating the
TNFRSF11A/RANK signaling. In allergic response, it plays a role in
mast cells activation and degranulation through PI-3-kinase
regulation. Also involved in the regulation of cell proliferation
and hematopoiesis. {ECO:0000269|PubMed:10068651,
ECO:0000269|PubMed:11449275, ECO:0000269|PubMed:15750601,
ECO:0000269|PubMed:17374739, ECO:0000269|PubMed:9885561}.
-!- SUBUNIT: Interacts with HCK (By similarity). Interacts with SHC1;
may mediate interaction with receptors. Interacts with SYK.
Interacts with PI-3 kinase. Interacts with GRB2 (via SH3 2
domain). Interacts (phosphorylated) with PTPN11. Interacts with
TNFRSF11A (via cytoplasmic domain). Interacts (phosphorylated)
with 14-3-3 family proteins SFN, YWHAB, YWHAE, YWHAG, YWHAH, YWHAQ
and YWHAZ; prevents interaction with GRB2 and attenuates GAB2
signaling. {ECO:0000250, ECO:0000269|PubMed:10068651,
ECO:0000269|PubMed:15750601, ECO:0000269|PubMed:16456001,
ECO:0000269|PubMed:9885561}.
-!- INTERACTION:
P25911:Lyn; NbExp=2; IntAct=EBI-641738, EBI-643537;
P29351:Ptpn6; NbExp=2; IntAct=EBI-641738, EBI-2620699;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:10068651, ECO:0000269|PubMed:9885561}.
-!- DOMAIN: The SH3-binding motifs mediate interaction with SHC1 and
GRB2.
-!- DOMAIN: The PH domain mediates phosphatidylinositol 3,4,5-
trisphosphate and phosphatidylinositol 3,4-bisphosphate binding.
-!- PTM: Phosphorylated upon EGF stimulation. Phosphorylated on
tyrosine residues by HCK upon IL6 signaling (By similarity).
Phosphorylated on tyrosine residue(s) by the thrombopoietin
receptor (TPOR), stem cell factor receptor (SCFR), and T-cell and
B-cell antigen receptors, gp130, IL-2R and IL-3R. Phosphorylated
upon stimulation of TNFRSF11A/RANK by TNFSF11/RANKL. {ECO:0000250,
ECO:0000269|PubMed:10068651, ECO:0000269|PubMed:15750601,
ECO:0000269|PubMed:19172738, ECO:0000269|PubMed:9885561}.
-!- PTM: Dephosphorylated by PTPN11.
-!- DISRUPTION PHENOTYPE: Mice are viable and healthy for up to 15
months. However, they have reduced number of mast cells and
develop osteopetrosis. {ECO:0000269|PubMed:11449275,
ECO:0000269|PubMed:15750601}.
-!- SIMILARITY: Belongs to the GAB family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF104244; AAD05166.1; -; mRNA.
EMBL; AB018414; BAA76738.1; -; mRNA.
CCDS; CCDS85340.1; -.
UniGene; Mm.42033; -.
ProteinModelPortal; Q9Z1S8; -.
CORUM; Q9Z1S8; -.
DIP; DIP-41351N; -.
IntAct; Q9Z1S8; 14.
MINT; Q9Z1S8; -.
STRING; 10090.ENSMUSP00000004622; -.
iPTMnet; Q9Z1S8; -.
PhosphoSitePlus; Q9Z1S8; -.
MaxQB; Q9Z1S8; -.
PaxDb; Q9Z1S8; -.
PRIDE; Q9Z1S8; -.
MGI; MGI:1333854; Gab2.
eggNOG; ENOG410IEDA; Eukaryota.
eggNOG; ENOG4111RDE; LUCA.
HOVERGEN; HBG051685; -.
InParanoid; Q9Z1S8; -.
PhylomeDB; Q9Z1S8; -.
ChiTaRS; Gab2; mouse.
PRO; PR:Q9Z1S8; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; ISS:UniProtKB.
GO; GO:0016477; P:cell migration; IDA:MGI.
GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:MGI.
GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
GO; GO:0030316; P:osteoclast differentiation; IMP:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:CACAO.
GO; GO:0043306; P:positive regulation of mast cell degranulation; IMP:UniProtKB.
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;
Cell membrane; Complete proteome; Cytoplasm;
Direct protein sequencing; Membrane; Phosphoprotein;
Reference proteome.
CHAIN 1 665 GRB2-associated-binding protein 2.
/FTId=PRO_0000050286.
DOMAIN 8 119 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
MOTIF 348 355 SH3-binding. {ECO:0000250}.
MOTIF 499 508 SH3-binding. {ECO:0000250}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 135 135 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 142 142 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 149 149 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 150 150 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 160 160 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 165 165 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 211 211 Phosphoserine.
{ECO:0000269|PubMed:19172738}.
MOD_RES 220 220 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 261 261 Phosphoserine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 262 262 Phosphothreonine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 263 263 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 275 275 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 278 278 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 282 282 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 284 284 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 290 290 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 328 328 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 365 365 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 382 382 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 388 388 Phosphothreonine.
{ECO:0000269|PubMed:19172738}.
MOD_RES 402 402 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 405 405 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 420 420 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 441 441 Phosphotyrosine.
{ECO:0000269|PubMed:15750601}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 532 532 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 612 612 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 632 632 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MUTAGEN 32 32 R->C: Impairs EGF-induced phosphorylation
at S-211 and T-388 and binding to
phosphatidylinositol 3,4,5-trisphosphate
and phosphatidylinositol 3,4-
bisphosphate.
{ECO:0000269|PubMed:16456001,
ECO:0000269|PubMed:19172738}.
CONFLICT 542 542 N -> NS (in Ref. 1; AAD05166).
{ECO:0000305}.
SEQUENCE 665 AA; 73208 MW; E8955EE638174085 CRC64;
MSGGGGDDVV CTGWLRKSPP EKKLRRYAWK KRWFILRSGR MSGDPDVLEY YKNEHSKKPL
RIINLNLCEQ VDAGLTFNKK ELQDSFVFDI KTSERTFYLV AETEADMNKW VQSICQICGF
NQAEESTDSL RNLSSASHGP RSSPAEFSSS QHLLRERKSS APSHSSQPTL FTFEPPVSSH
MQPTLSTSAP QEYLYLHQCI SRRTENARSA SFSQGTRQKS DTAVQKLAQS NGHCINGVGG
QVHGFYSLPK PSRHNTEFKD STYDLPRSLA SHGHTKSSLT GSETDNEDVY TFKMPSNTLC
RELGDLLVDN MDVPTTPLSA YQIPRTFTLD KNHNAMTVAT PGDSAIAPPP RPPKPSQAET
SQWGSIQQRP PISENSRSVA ATIPRRNTLP AMDNSRLHRA SSCETYEYPA RGSGESASWS
AEPPGKTAVG RSNSASSDDN YVPMNPGSST LLAMERPGDN SQSVYIPMSP GPHHFDPLGY
PSTALPIHRG PSRGSEIQPP PVNRNLKPDR KAKPTPLDLR NNTVIDELPF KSPVTKSWSR
INHTFNSSSS QYCRPISTQS ITSTDSGDSE ENYVPMQNPV SASPVPSGTN SPAPKKSTGS
VDYLALDFQP GSPSPHRKPS TSSVTSDEKV DYVQVDKEKT QALQNTMQEW TDVRQSSEPS
KGAKL


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