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GRB2-related adaptor protein 2 (Adapter protein GRID) (GADS protein) (GRB-2-like protein) (GRB2L) (GRB-2-related monocytic adapter protein) (MONA) (Monocytic adapter) (GRBLG) (Growth factor receptor-binding protein) (Hematopoietic cell-associated adaptor protein GrpL)

 GRAP2_MOUSE             Reviewed;         322 AA.
O89100;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
22-NOV-2017, entry version 151.
RecName: Full=GRB2-related adaptor protein 2;
AltName: Full=Adapter protein GRID;
AltName: Full=GADS protein;
AltName: Full=GRB-2-like protein;
Short=GRB2L;
AltName: Full=GRB-2-related monocytic adapter protein;
Short=MONA;
Short=Monocytic adapter;
AltName: Full=GRBLG;
AltName: Full=Growth factor receptor-binding protein;
AltName: Full=Hematopoietic cell-associated adaptor protein GrpL;
Name=Grap2; Synonyms=Gads, Grb2l, Grid, Mona;
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].
PubMed=9857184; DOI=10.1093/emboj/17.24.7273;
Bourette R.P., Arnaud S., Myles G.M., Blanchet J.P.,
Rohrschneider L.R., Mouchiroud G.;
"Mona, a novel hematopoietic-specific adaptor interacting with the
macrophage colony-stimulating factor receptor, is implicated in
monocyte/macrophage development.";
EMBO J. 17:7273-7281(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9872323; DOI=10.1038/sj.onc.1202337;
Liu S.K., McGlade C.J.;
"Gads is a novel SH2 and SH3 domain-containing adaptor protein that
binds to tyrosine-phosphorylated Shc.";
Oncogene 17:3073-3082(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
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].
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Thymus;
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 LIME1.
PubMed=14610044; DOI=10.1084/jem.20030232;
Hur E.M., Son M., Lee O.-H., Choi Y.B., Park C., Lee H., Yun Y.;
"LIME, a novel transmembrane adaptor protein, associates with p56lck
and mediates T cell activation.";
J. Exp. Med. 198:1463-1473(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; SER-230 AND
THR-254, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Lung, and Spleen;
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: Interacts with SLP-76 to regulate NF-AT activation.
Binds to tyrosine-phosphorylated shc.
-!- SUBUNIT: Interacts with phosphorylated LAT and LAX1 upon TCR
activation. Interacts with SHB. Interacts with PTPN23 (By
similarity). Interacts with phosphorylated LIME1 upon TCR
activation. {ECO:0000250, ECO:0000269|PubMed:14610044}.
-!- INTERACTION:
Q13094:LCP2 (xeno); NbExp=4; IntAct=EBI-642151, EBI-346946;
Q60787:Lcp2; NbExp=7; IntAct=EBI-642151, EBI-5324248;
Q9H3S7:PTPN23 (xeno); NbExp=3; IntAct=EBI-642151, EBI-724478;
Q6PB44:Ptpn23; NbExp=3; IntAct=EBI-642151, EBI-4284816;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
{ECO:0000250}. Endosome {ECO:0000250}.
-!- SIMILARITY: Belongs to the GRB2/sem-5/DRK family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF055465; AAD08803.1; -; mRNA.
EMBL; AF053405; AAC98669.1; -; mRNA.
EMBL; AF129477; AAD41783.1; -; mRNA.
EMBL; AF236118; AAF60318.1; -; mRNA.
EMBL; AJ011735; CAA09756.1; -; mRNA.
EMBL; BC052496; AAH52496.1; -; mRNA.
CCDS; CCDS27663.1; -.
RefSeq; NP_001276371.1; NM_001289442.1.
RefSeq; NP_034945.1; NM_010815.3.
UniGene; Mm.12947; -.
PDB; 1H3H; NMR; -; A=263-322.
PDB; 1OEB; X-ray; 1.76 A; A/B=265-322.
PDB; 1R1P; X-ray; 1.80 A; A/B/C/D=50-147.
PDB; 1R1Q; X-ray; 1.80 A; A/B=50-147.
PDB; 1R1S; X-ray; 1.90 A; A/C/E/G=50-147.
PDB; 1UTI; X-ray; 1.50 A; A=265-322.
PDB; 2D0N; X-ray; 1.57 A; A/C=267-322.
PDB; 2W10; X-ray; 1.90 A; A/B=265-322.
PDBsum; 1H3H; -.
PDBsum; 1OEB; -.
PDBsum; 1R1P; -.
PDBsum; 1R1Q; -.
PDBsum; 1R1S; -.
PDBsum; 1UTI; -.
PDBsum; 2D0N; -.
PDBsum; 2W10; -.
ProteinModelPortal; O89100; -.
SMR; O89100; -.
BioGrid; 201466; 9.
DIP; DIP-41343N; -.
IntAct; O89100; 15.
MINT; MINT-244269; -.
STRING; 10090.ENSMUSP00000046532; -.
iPTMnet; O89100; -.
PhosphoSitePlus; O89100; -.
EPD; O89100; -.
PaxDb; O89100; -.
PRIDE; O89100; -.
Ensembl; ENSMUST00000043149; ENSMUSP00000046532; ENSMUSG00000042351.
GeneID; 17444; -.
KEGG; mmu:17444; -.
UCSC; uc007wvo.2; mouse.
CTD; 9402; -.
MGI; MGI:1333842; Grap2.
eggNOG; KOG3601; Eukaryota.
eggNOG; ENOG410XR1G; LUCA.
GeneTree; ENSGT00820000126999; -.
HOGENOM; HOG000251625; -.
HOVERGEN; HBG005404; -.
InParanoid; O89100; -.
KO; K07366; -.
OMA; LSSQEEW; -.
OrthoDB; EOG091G0HWS; -.
PhylomeDB; O89100; -.
TreeFam; TF354288; -.
Reactome; R-MMU-1433557; Signaling by SCF-KIT.
Reactome; R-MMU-202433; Generation of second messenger molecules.
Reactome; R-MMU-2424491; DAP12 signaling.
Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-MMU-389356; CD28 co-stimulation.
EvolutionaryTrace; O89100; -.
PRO; PR:O89100; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000042351; -.
CleanEx; MM_GRAP2; -.
ExpressionAtlas; O89100; baseline and differential.
Genevisible; O89100; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005768; C:endosome; ISS:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005634; C:nucleus; ISS: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:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
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; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
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; 3.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm; Endosome;
Nucleus; Phosphoprotein; Reference proteome; Repeat; SH2 domain;
SH3 domain.
CHAIN 1 322 GRB2-related adaptor protein 2.
/FTId=PRO_0000088209.
DOMAIN 1 56 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 58 149 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 263 322 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
MOD_RES 45 45 Phosphotyrosine.
{ECO:0000250|UniProtKB:O75791}.
MOD_RES 106 106 N6-acetyllysine.
{ECO:0000250|UniProtKB:O75791}.
MOD_RES 186 186 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 230 230 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 254 254 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
TURN 54 58 {ECO:0000244|PDB:1R1P}.
HELIX 65 73 {ECO:0000244|PDB:1R1P}.
STRAND 79 84 {ECO:0000244|PDB:1R1P}.
STRAND 86 88 {ECO:0000244|PDB:1R1P}.
STRAND 92 97 {ECO:0000244|PDB:1R1P}.
STRAND 99 106 {ECO:0000244|PDB:1R1P}.
STRAND 115 119 {ECO:0000244|PDB:1R1P}.
STRAND 121 124 {ECO:0000244|PDB:1R1P}.
HELIX 125 132 {ECO:0000244|PDB:1R1P}.
STRAND 137 141 {ECO:0000244|PDB:1R1P}.
STRAND 267 272 {ECO:0000244|PDB:1UTI}.
STRAND 278 281 {ECO:0000244|PDB:1H3H}.
STRAND 286 288 {ECO:0000244|PDB:1H3H}.
STRAND 289 294 {ECO:0000244|PDB:1UTI}.
STRAND 297 305 {ECO:0000244|PDB:1UTI}.
STRAND 308 313 {ECO:0000244|PDB:1UTI}.
HELIX 314 316 {ECO:0000244|PDB:1UTI}.
STRAND 317 319 {ECO:0000244|PDB:1UTI}.
SEQUENCE 322 AA; 36810 MW; 736311D0640CD3D0 CRC64;
MEATAKFDFM ASGEDELSFR TGDILKILSN QEEWLKAELG SQEGYVPKNF IDIEFPEWFH
EGLSRHQAEN LLMGKDIGFF IIRASQSSPG DFSISVRHED DVQHFKVMRD TKGNYFLWTE
KFPSLNKLVD YYRTTSISKQ KQVFLRDGTQ DQGHRGNSLD RRSQGGPHPS GTVGEEIRPS
VNRKLSDHLP LGPQQFHPHQ QPSPQFTPGP QPPQQQRYLQ HFHQDRRGGS LDINDGHCGL
GSEVNATLMH RRHTDPVQLQ AAGRVRWARA LYDFEALEED ELGFRSGEVV EVLDSSNPSW
WTGRLHNKLG LFPANYVAPM MR


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