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GRB2-related adapter protein 2 (Adapter protein GRID) (GRB-2-like protein) (GRB2L) (GRBLG) (GRBX) (Grf40 adapter protein) (Grf-40) (Growth factor receptor-binding protein) (Hematopoietic cell-associated adapter protein GrpL) (P38) (Protein GADS) (SH3-SH2-SH3 adapter Mona)

 GRAP2_HUMAN             Reviewed;         330 AA.
O75791; B7Z8I3; O43726; Q9NRB7;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
30-AUG-2017, entry version 168.
RecName: Full=GRB2-related adapter protein 2;
AltName: Full=Adapter protein GRID;
AltName: Full=GRB-2-like protein;
Short=GRB2L;
AltName: Full=GRBLG;
AltName: Full=GRBX;
AltName: Full=Grf40 adapter protein;
Short=Grf-40;
AltName: Full=Growth factor receptor-binding protein;
AltName: Full=Hematopoietic cell-associated adapter protein GrpL;
AltName: Full=P38;
AltName: Full=Protein GADS;
AltName: Full=SH3-SH2-SH3 adapter Mona;
Name=GRAP2; Synonyms=GADS, GRB2L, GRID;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9878555; DOI=10.1006/bbrc.1998.9795;
Qiu M., Hua S., Agrawal M., Li G., Cai J., Chan E., Zhou H., Luo Y.,
Liu M.;
"Molecular cloning and expression of human grap-2, a novel leukocyte-
specific SH2- and SH3-containing adaptor-like protein that binds to
gab-1.";
Biochem. Biophys. Res. Commun. 253:443-447(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10209041; DOI=10.1084/jem.189.8.1243;
Law C.-L., Ewings M.K., Chaudhary P.M., Solow S.A., Yun T.J.,
Marshall A.J., Hood L., Clark E.A.;
"GrpL, a Grb2-related adaptor protein, interacts with SLP-76 to
regulate nuclear factor of activated T cell activation.";
J. Exp. Med. 189:1243-1253(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10224278; DOI=10.1084/jem.189.9.1383;
Asada H., Ishii N., Sasaki Y., Endo K., Kasai H., Tanaka N.,
Takeshita T., Tsuchiya S., Konno T., Sugamura K.;
"Grf40, A novel Grb2 family member, is involved in T cell signaling
through interaction with SLP-76 and LAT.";
J. Exp. Med. 189:1383-1390(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PHE-319.
PubMed=10820259; DOI=10.4049/jimmunol.164.11.5805;
Ellis J.H., Ashman C., Burden M.N., Kilpatrick K.E., Morse M.A.,
Hamblin P.A.;
"GRID: a novel Grb-2-related adapter protein that interacts with the
activated T cell costimulatory receptor CD28.";
J. Immunol. 164:5805-5814(2000).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=12062812; DOI=10.1016/S0378-1119(02)00555-3;
Guyot B., Arnaud S., Phothirath P., Bourette R.P., Grasset M.F.,
Rigal D., Mouchiroud G.;
"Genomic organization and restricted expression of the human Mona/Gads
gene suggests regulation by two specific promoters.";
Gene 290:173-179(2002).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Blood;
Frearson J.;
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Kedra D., Dumanski J.P.;
"Cloning of the human and mouse growth factor receptor binding protein
like genes.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Teramoto T., Nagashima M., Terai S., Thorgeirsson S.S.;
"GrbX, new recruited signaling gene having homology with Grb2.";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Thymus;
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).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, and Spleen;
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).
[13]
INTERACTION WITH LAT.
PubMed=10811803; DOI=10.1074/jbc.M000404200;
Zhang W., Trible R.P., Zhu M., Liu S.K., McGlade C.J., Samelson L.E.;
"Association of Grb2, Gads, and phospholipase C-gamma 1 with
phosphorylated LAT tyrosine residues. Effect of LAT tyrosine mutations
on T cell antigen receptor-mediated signaling.";
J. Biol. Chem. 275:23355-23361(2000).
[14]
INTERACTION WITH SHB.
PubMed=12084069; DOI=10.1046/j.1432-1033.2002.03008.x;
Lindholm C.K., Henriksson M.L., Hallberg B., Welsh M.;
"Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells.";
Eur. J. Biochem. 269:3279-3288(2002).
[15]
INTERACTION WITH LAX1.
PubMed=12359715; DOI=10.1074/jbc.M208946200;
Zhu M., Janssen E., Leung K., Zhang W.;
"Molecular cloning of a novel gene encoding a membrane-associated
adaptor protein (LAX) in lymphocyte signaling.";
J. Biol. Chem. 277:46151-46158(2002).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-262, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=12522270; DOI=10.1073/pnas.2436191100;
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,
Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
"Profiling of tyrosine phosphorylation pathways in human cells using
mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-45 AND THR-262, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-262, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-45, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-106, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[21]
INTERACTION WITH PTPN23, AND SUBCELLULAR LOCATION.
PubMed=21179510; DOI=10.1371/journal.pone.0014339;
Tanase C.A.;
"Histidine domain-protein tyrosine phosphatase interacts with Grb2 and
GrpL.";
PLoS ONE 5:E14339-E14339(2010).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-262, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-262, 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).
-!- FUNCTION: Interacts with SLP-76 to regulate NF-AT activation.
Binds to tyrosine-phosphorylated shc.
-!- SUBUNIT: Interacts with phosphorylated LIME1 upon TCR activation
(By similarity). Interacts with phosphorylated LAT and LAX1 upon
TCR activation. Interacts with SHB. Interacts with PTPN23.
{ECO:0000250, ECO:0000269|PubMed:10811803,
ECO:0000269|PubMed:12084069, ECO:0000269|PubMed:12359715,
ECO:0000269|PubMed:21179510}.
-!- INTERACTION:
P00533:EGFR; NbExp=2; IntAct=EBI-740418, EBI-297353;
P04626:ERBB2; NbExp=2; IntAct=EBI-740418, EBI-641062;
Q9H706:GAREM1; NbExp=5; IntAct=EBI-740418, EBI-3440103;
Q08460:Kcnma1 (xeno); NbExp=3; IntAct=EBI-740418, EBI-1633915;
P10721:KIT; NbExp=2; IntAct=EBI-740418, EBI-1379503;
Q13094:LCP2; NbExp=19; IntAct=EBI-740418, EBI-346946;
Q8TBB1:LNX1; NbExp=4; IntAct=EBI-740418, EBI-739832;
Q9H3S7:PTPN23; NbExp=8; IntAct=EBI-740418, EBI-724478;
O43597:SPRY2; NbExp=3; IntAct=EBI-740418, EBI-742487;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21179510}.
Cytoplasm {ECO:0000269|PubMed:21179510}. Endosome
{ECO:0000269|PubMed:21179510}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O75791-1; Sequence=Displayed;
Name=2;
IsoId=O75791-2; Sequence=VSP_055234, VSP_055235;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the GRB2/sem-5/DRK family. {ECO:0000305}.
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EMBL; AF102694; AAD04926.1; -; mRNA.
EMBL; AF129476; AAD41782.1; -; mRNA.
EMBL; AF042380; AAC69273.1; -; mRNA.
EMBL; AF236119; AAF60319.1; -; mRNA.
EMBL; AF236120; AAF60320.1; -; mRNA.
EMBL; AF121002; AAF31758.1; -; mRNA.
EMBL; AY069959; AAL58573.1; -; mRNA.
EMBL; Y18051; CAA77021.1; -; mRNA.
EMBL; AJ011736; CAA09757.1; -; mRNA.
EMBL; AF090456; AAD13027.1; -; mRNA.
EMBL; CR456498; CAG30384.1; -; mRNA.
EMBL; AK303470; BAH13969.1; -; mRNA.
EMBL; Z82206; CAI42713.1; -; Genomic_DNA.
EMBL; BC025692; AAH25692.1; -; mRNA.
EMBL; BC026002; AAH26002.1; -; mRNA.
CCDS; CCDS13999.1; -. [O75791-1]
PIR; JE0376; JE0376.
RefSeq; NP_001278753.1; NM_001291824.1. [O75791-1]
RefSeq; NP_001278754.1; NM_001291825.1. [O75791-1]
RefSeq; NP_001278757.1; NM_001291828.1. [O75791-2]
RefSeq; NP_004801.1; NM_004810.3. [O75791-1]
UniGene; Hs.517499; -.
PDB; 5GJH; X-ray; 1.20 A; A/C=58-155.
PDBsum; 5GJH; -.
ProteinModelPortal; O75791; -.
SMR; O75791; -.
BioGrid; 114799; 49.
DIP; DIP-38435N; -.
IntAct; O75791; 66.
MINT; MINT-140970; -.
STRING; 9606.ENSP00000339186; -.
iPTMnet; O75791; -.
PhosphoSitePlus; O75791; -.
BioMuta; GRAP2; -.
PaxDb; O75791; -.
PeptideAtlas; O75791; -.
PRIDE; O75791; -.
DNASU; 9402; -.
Ensembl; ENST00000344138; ENSP00000339186; ENSG00000100351. [O75791-1]
Ensembl; ENST00000407075; ENSP00000385607; ENSG00000100351. [O75791-1]
GeneID; 9402; -.
KEGG; hsa:9402; -.
CTD; 9402; -.
DisGeNET; 9402; -.
GeneCards; GRAP2; -.
HGNC; HGNC:4563; GRAP2.
HPA; CAB022073; -.
HPA; HPA005788; -.
MIM; 604518; gene.
neXtProt; NX_O75791; -.
OpenTargets; ENSG00000100351; -.
PharmGKB; PA28959; -.
eggNOG; KOG3601; Eukaryota.
eggNOG; ENOG410XR1G; LUCA.
GeneTree; ENSGT00820000126999; -.
HOGENOM; HOG000251625; -.
HOVERGEN; HBG005404; -.
InParanoid; O75791; -.
KO; K07366; -.
OMA; LSSQEEW; -.
OrthoDB; EOG091G0HWS; -.
PhylomeDB; O75791; -.
TreeFam; TF354288; -.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-202433; Generation of second messenger molecules.
Reactome; R-HSA-2424491; DAP12 signaling.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-389356; CD28 co-stimulation.
SignaLink; O75791; -.
ChiTaRS; GRAP2; human.
GeneWiki; GRAP2; -.
GenomeRNAi; 9402; -.
PMAP-CutDB; O75791; -.
PRO; PR:O75791; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100351; -.
CleanEx; HS_GRAP2; -.
ExpressionAtlas; O75791; baseline and differential.
Genevisible; O75791; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0005102; F:receptor binding; IBA:GO_Central.
GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0007265; P:Ras protein signal transduction; TAS:ProtInc.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
CDD; cd11950; SH3_GRAP2_C; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR035646; GRAP2_C_SH3.
InterPro; IPR000980; SH2.
InterPro; IPR001452; SH3_domain.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 2.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 2.
SUPFAM; SSF50044; SSF50044; 2.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Endosome; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; SH2 domain; SH3 domain.
CHAIN 1 330 GRB2-related adapter protein 2.
/FTId=PRO_0000088208.
DOMAIN 1 56 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 58 149 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 271 330 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
MOD_RES 45 45 Phosphotyrosine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:19690332}.
MOD_RES 106 106 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 187 187 Phosphoserine.
{ECO:0000250|UniProtKB:O89100}.
MOD_RES 236 236 Phosphoserine.
{ECO:0000250|UniProtKB:O89100}.
MOD_RES 262 262 Phosphothreonine.
{ECO:0000244|PubMed:12522270,
ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 39 MEAVAKFDFTASGEDELSFHTGDVLKILSNQEEWFKAEL
-> MVSRRPLSTPGRELTHGQGGWLLHHPGQPELPRGLLHL
C (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055234.
VAR_SEQ 40 152 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055235.
VARIANT 319 319 L -> F (in dbSNP:rs12759).
{ECO:0000269|PubMed:10820259}.
/FTId=VAR_012079.
HELIX 65 73 {ECO:0000244|PDB:5GJH}.
STRAND 80 84 {ECO:0000244|PDB:5GJH}.
STRAND 86 88 {ECO:0000244|PDB:5GJH}.
STRAND 91 97 {ECO:0000244|PDB:5GJH}.
STRAND 99 109 {ECO:0000244|PDB:5GJH}.
STRAND 115 119 {ECO:0000244|PDB:5GJH}.
STRAND 121 124 {ECO:0000244|PDB:5GJH}.
HELIX 125 134 {ECO:0000244|PDB:5GJH}.
STRAND 139 141 {ECO:0000244|PDB:5GJH}.
SEQUENCE 330 AA; 37909 MW; 74F4C8D0EBB56D55 CRC64;
MEAVAKFDFT ASGEDELSFH TGDVLKILSN QEEWFKAELG SQEGYVPKNF IDIQFPKWFH
EGLSRHQAEN LLMGKEVGFF IIRASQSSPG DFSISVRHED DVQHFKVMRD NKGNYFLWTE
KFPSLNKLVD YYRTNSISRQ KQIFLRDRTR EDQGHRGNSL DRRSQGGPHL SGAVGEEIRP
SMNRKLSDHP PTLPLQQHQH QPQPPQYAPA PQQLQQPPQQ RYLQHHHFHQ ERRGGSLDIN
DGHCGTGLGS EMNAALMHRR HTDPVQLQAA GRVRWARALY DFEALEDDEL GFHSGEVVEV
LDSSNPSWWT GRLHNKLGLF PANYVAPMTR


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