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

 GAB2_RAT                Reviewed;         665 AA.
Q9EQH1;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2001, sequence version 2.
23-MAY-2018, entry version 100.
RecName: Full=GRB2-associated-binding protein 2;
AltName: Full=GRB2-associated binder 2;
AltName: Full=Growth factor receptor bound protein 2-associated protein 2;
Name=Gab2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Kong M., Mounier C., Wu J., Posner B.I.;
"Identification of Gab2 as the major molecule responsible for EGF-
induced PI3-kinase activation and DNA synthesis in rat hepatocytes.";
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[2]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with HCK. Interacts with SHC1; may mediate
interaction with receptors (By similarity). Interacts with SYK (By
similarity). Interacts with PI-3 kinase (By similarity). Interacts
with GRB2 (via SH3 2 domain) (By similarity). Interacts
(phosphorylated) with PTPN11 (By similarity). Interacts with
TNFRSF11A (via cytoplasmic domain) (By similarity). Interacts
(phosphorylated) with 14-3-3 family proteins SFN, YWHAB, YWHAE,
YWHAG, YWHAH, YWHAQ and YWHAZ; prevents interaction with GRB2 and
attenuates GAB2 signaling (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}.
-!- DOMAIN: The SH3-binding motifs mediate interaction with SHC1 and
GRB2. {ECO:0000250}.
-!- DOMAIN: The PH domain mediates phosphatidylinositol 3,4,5-
trisphosphate and phosphatidylinositol 3,4-bisphosphate binding.
{ECO:0000250}.
-!- 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 (By similarity).
Phosphorylated upon stimulation of TNFRSF11A/RANK by TNFSF11/RANKL
(By similarity). {ECO:0000250}.
-!- PTM: Dephosphorylated by PTPN11. {ECO:0000250}.
-!- SIMILARITY: Belongs to the GAB family. {ECO:0000305}.
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EMBL; AF230367; AAG44268.2; -; mRNA.
RefSeq; NP_445869.1; NM_053417.1.
UniGene; Rn.211990; -.
ProteinModelPortal; Q9EQH1; -.
SMR; Q9EQH1; -.
BioGrid; 249977; 1.
CORUM; Q9EQH1; -.
IntAct; Q9EQH1; 1.
MINT; Q9EQH1; -.
STRING; 10116.ENSRNOP00000016361; -.
iPTMnet; Q9EQH1; -.
PhosphoSitePlus; Q9EQH1; -.
PaxDb; Q9EQH1; -.
PRIDE; Q9EQH1; -.
GeneID; 84477; -.
KEGG; rno:84477; -.
UCSC; RGD:621367; rat.
CTD; 9846; -.
RGD; 621367; Gab2.
HOGENOM; HOG000236270; -.
HOVERGEN; HBG051685; -.
InParanoid; Q9EQH1; -.
KO; K08091; -.
PhylomeDB; Q9EQH1; -.
PRO; PR:Q9EQH1; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISS:UniProtKB.
GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; ISS:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IDA:RGD.
GO; GO:0030316; P:osteoclast differentiation; ISS:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0043306; P:positive regulation of mast cell degranulation; ISS: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; Membrane; Phosphoprotein;
Reference proteome.
CHAIN 1 665 GRB2-associated-binding protein 2.
/FTId=PRO_0000050287.
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:0000250|UniProtKB:Q9UQC2}.
MOD_RES 220 220 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 261 261 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 262 262 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Z1S8}.
MOD_RES 263 263 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9Z1S8}.
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:0000250|UniProtKB:Q9UQC2}.
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:0000250|UniProtKB:Q9UQC2}.
MOD_RES 402 402 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 405 405 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Z1S8}.
MOD_RES 420 420 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 423 423 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQC2}.
MOD_RES 441 441 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9Z1S8}.
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}.
SEQUENCE 665 AA; 73328 MW; BEB170B69406063E CRC64;
MSGGGGDDVV CTGWLRKSPP EKKLRRYAWK KRWFILRSGR MSGDPDVLEY YKNEHSKKPL
RIINLNFCEQ VDAGLTFNKK ELQDSFVFDI KTSERTFYLV AETEADMNKW VQSICQICGF
NQAEESTDSL RNLSSASHGP RSSPAEFSSS QHLLRERKSS APSHSSQPTL FTFEPPMTSH
MQPALSTSAP QEYLYLHQCI SRRTENSRSA SFSQGTRQKS DTAVQKLAQS NGHCINGVSN
QVHGFYSLPK PSRHNTEFKD STYDLPRSLA SHGHTKSSLT GSETDNEDVY TFKMPSNTLC
REFGDLLVDN MDVPTTPLSA YQIPRTFTLD KNHNAMTVAT SGDSAIAPPP RPPKPSQAET
PRWGSPQQKP PIGENSRSVA ATIPRRNTLP AMDNSRLHRA SSCETYEYPT RGSGESASWS
AESPGKTAVG RSDSASSDEN YVPMNPGSST LLAMERAGDN SQSAYIPMGP GPHHFDPLGY
PSTALPIHRG PSRGSEIQPP PVNRNLKPDR KAKPTPLDLR NNTVIDELPF KSPVTKSWSR
INHTFNSSSS QYCRPISTQS ITSTDSGDSE ENYVPMQNPV SASPVPSGTN SPAPRKSTGS
VDYLALDFQP GSPSPHRKPS TSSVTSDEKV DYVQVDKEKT QALQNTMQEW TDVRQSSEPS
KGAKL


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