ID GRAP2_HUMAN Reviewed; 330 AA. AC O75791; B7Z8I3; O43726; Q9NRB7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 24-JAN-2024, entry version 210. DE RecName: Full=GRB2-related adapter protein 2; DE AltName: Full=Adapter protein GRID; DE AltName: Full=GRB-2-like protein; DE Short=GRB2L; DE AltName: Full=GRBLG; DE AltName: Full=GRBX; DE AltName: Full=Grf40 adapter protein; DE Short=Grf-40; DE AltName: Full=Growth factor receptor-binding protein; DE AltName: Full=Hematopoietic cell-associated adapter protein GrpL; DE AltName: Full=P38; DE AltName: Full=Protein GADS; DE AltName: Full=SH3-SH2-SH3 adapter Mona; GN Name=GRAP2; Synonyms=GADS, GRB2L, GRID; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9878555; DOI=10.1006/bbrc.1998.9795; RA Qiu M., Hua S., Agrawal M., Li G., Cai J., Chan E., Zhou H., Luo Y., RA Liu M.; RT "Molecular cloning and expression of human grap-2, a novel leukocyte- RT specific SH2- and SH3-containing adaptor-like protein that binds to RT gab-1."; RL Biochem. Biophys. Res. Commun. 253:443-447(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=10209041; DOI=10.1084/jem.189.8.1243; RA Law C.-L., Ewings M.K., Chaudhary P.M., Solow S.A., Yun T.J., RA Marshall A.J., Hood L., Clark E.A.; RT "GrpL, a Grb2-related adaptor protein, interacts with SLP-76 to regulate RT nuclear factor of activated T cell activation."; RL J. Exp. Med. 189:1243-1253(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=10224278; DOI=10.1084/jem.189.9.1383; RA Asada H., Ishii N., Sasaki Y., Endo K., Kasai H., Tanaka N., Takeshita T., RA Tsuchiya S., Konno T., Sugamura K.; RT "Grf40, A novel Grb2 family member, is involved in T cell signaling through RT interaction with SLP-76 and LAT."; RL J. Exp. Med. 189:1383-1390(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PHE-319. RX PubMed=10820259; DOI=10.4049/jimmunol.164.11.5805; RA Ellis J.H., Ashman C., Burden M.N., Kilpatrick K.E., Morse M.A., RA Hamblin P.A.; RT "GRID: a novel Grb-2-related adapter protein that interacts with the RT activated T cell costimulatory receptor CD28."; RL J. Immunol. 164:5805-5814(2000). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=12062812; DOI=10.1016/s0378-1119(02)00555-3; RA Guyot B., Arnaud S., Phothirath P., Bourette R.P., Grasset M.F., Rigal D., RA Mouchiroud G.; RT "Genomic organization and restricted expression of the human Mona/Gads gene RT suggests regulation by two specific promoters."; RL Gene 290:173-179(2002). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Blood; RA Frearson J.; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Kedra D., Dumanski J.P.; RT "Cloning of the human and mouse growth factor receptor binding protein like RT genes."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Teramoto T., Nagashima M., Terai S., Thorgeirsson S.S.; RT "GrbX, new recruited signaling gene having homology with Grb2."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Thymus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung, and Spleen; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [13] RP INTERACTION WITH LAT. RX PubMed=10811803; DOI=10.1074/jbc.m000404200; RA Zhang W., Trible R.P., Zhu M., Liu S.K., McGlade C.J., Samelson L.E.; RT "Association of Grb2, Gads, and phospholipase C-gamma 1 with phosphorylated RT LAT tyrosine residues. Effect of LAT tyrosine mutations on T cell antigen RT receptor-mediated signaling."; RL J. Biol. Chem. 275:23355-23361(2000). RN [14] RP INTERACTION WITH SHB. RX PubMed=12084069; DOI=10.1046/j.1432-1033.2002.03008.x; RA Lindholm C.K., Henriksson M.L., Hallberg B., Welsh M.; RT "Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells."; RL Eur. J. Biochem. 269:3279-3288(2002). RN [15] RP INTERACTION WITH LAX1. RX PubMed=12359715; DOI=10.1074/jbc.m208946200; RA Zhu M., Janssen E., Leung K., Zhang W.; RT "Molecular cloning of a novel gene encoding a membrane-associated adaptor RT protein (LAX) in lymphocyte signaling."; RL J. Biol. Chem. 277:46151-46158(2002). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-262, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=12522270; DOI=10.1073/pnas.2436191100; RA Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., RA Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.; RT "Profiling of tyrosine phosphorylation pathways in human cells using mass RT spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-45 AND THR-262, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=15144186; DOI=10.1021/ac035352d; RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., RA Peters E.C.; RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from RT human T cells using immobilized metal affinity chromatography and tandem RT mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-262, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-45, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-106, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [21] RP INTERACTION WITH PTPN23, AND SUBCELLULAR LOCATION. RX PubMed=21179510; DOI=10.1371/journal.pone.0014339; RA Tanase C.A.; RT "Histidine domain-protein tyrosine phosphatase interacts with Grb2 and RT GrpL."; RL PLoS ONE 5:E14339-E14339(2010). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-262, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-262, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Interacts with SLP-76 to regulate NF-AT activation. Binds to CC tyrosine-phosphorylated shc. CC -!- SUBUNIT: Interacts with phosphorylated LIME1 upon TCR activation (By CC similarity). Interacts with phosphorylated LAT and LAX1 upon TCR CC activation. Interacts with SHB. Interacts with PTPN23. {ECO:0000250, CC ECO:0000269|PubMed:10811803, ECO:0000269|PubMed:12084069, CC ECO:0000269|PubMed:12359715, ECO:0000269|PubMed:21179510}. CC -!- INTERACTION: CC O75791; O14672: ADAM10; NbExp=3; IntAct=EBI-740418, EBI-1536151; CC O75791; P00533: EGFR; NbExp=3; IntAct=EBI-740418, EBI-297353; CC O75791; P04626: ERBB2; NbExp=2; IntAct=EBI-740418, EBI-641062; CC O75791; Q9UQC2: GAB2; NbExp=3; IntAct=EBI-740418, EBI-975200; CC O75791; Q9H706: GAREM1; NbExp=4; IntAct=EBI-740418, EBI-3440103; CC O75791; P10721: KIT; NbExp=2; IntAct=EBI-740418, EBI-1379503; CC O75791; Q5T749: KPRP; NbExp=3; IntAct=EBI-740418, EBI-10981970; CC O75791; Q13094: LCP2; NbExp=40; IntAct=EBI-740418, EBI-346946; CC O75791; Q8TBB1: LNX1; NbExp=4; IntAct=EBI-740418, EBI-739832; CC O75791; P00540: MOS; NbExp=3; IntAct=EBI-740418, EBI-1757866; CC O75791; P30039: PBLD; NbExp=3; IntAct=EBI-740418, EBI-750589; CC O75791; P54646: PRKAA2; NbExp=3; IntAct=EBI-740418, EBI-1383852; CC O75791; P0CG20: PRR35; NbExp=3; IntAct=EBI-740418, EBI-11986293; CC O75791; Q9H3S7: PTPN23; NbExp=6; IntAct=EBI-740418, EBI-724478; CC O75791; Q8IY67: RAVER1; NbExp=3; IntAct=EBI-740418, EBI-2105155; CC O75791; Q9H788: SH2D4A; NbExp=5; IntAct=EBI-740418, EBI-747035; CC O75791; O43597: SPRY2; NbExp=3; IntAct=EBI-740418, EBI-742487; CC O75791; O95630: STAMBP; NbExp=4; IntAct=EBI-740418, EBI-396676; CC O75791; P15622-3: ZNF250; NbExp=3; IntAct=EBI-740418, EBI-10177272; CC O75791; Q9P2F9: ZNF319; NbExp=3; IntAct=EBI-740418, EBI-11993110; CC O75791; Q9Y5A6: ZSCAN21; NbExp=4; IntAct=EBI-740418, EBI-10281938; CC O75791; Q7Z783; NbExp=3; IntAct=EBI-740418, EBI-9088990; CC O75791; Q08460: Kcnma1; Xeno; NbExp=3; IntAct=EBI-740418, EBI-1633915; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21179510}. Cytoplasm CC {ECO:0000269|PubMed:21179510}. Endosome {ECO:0000269|PubMed:21179510}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O75791-1; Sequence=Displayed; CC Name=2; CC IsoId=O75791-2; Sequence=VSP_055234, VSP_055235; CC -!- SIMILARITY: Belongs to the GRB2/sem-5/DRK family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF102694; AAD04926.1; -; mRNA. DR EMBL; AF129476; AAD41782.1; -; mRNA. DR EMBL; AF042380; AAC69273.1; -; mRNA. DR EMBL; AF236119; AAF60319.1; -; mRNA. DR EMBL; AF236120; AAF60320.1; -; mRNA. DR EMBL; AF121002; AAF31758.1; -; mRNA. DR EMBL; AY069959; AAL58573.1; -; mRNA. DR EMBL; Y18051; CAA77021.1; -; mRNA. DR EMBL; AJ011736; CAA09757.1; -; mRNA. DR EMBL; AF090456; AAD13027.1; -; mRNA. DR EMBL; CR456498; CAG30384.1; -; mRNA. DR EMBL; AK303470; BAH13969.1; -; mRNA. DR EMBL; Z82206; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC025692; AAH25692.1; -; mRNA. DR EMBL; BC026002; AAH26002.1; -; mRNA. DR CCDS; CCDS13999.1; -. [O75791-1] DR PIR; JE0376; JE0376. DR RefSeq; NP_001278753.1; NM_001291824.1. [O75791-1] DR RefSeq; NP_001278754.1; NM_001291825.1. [O75791-1] DR RefSeq; NP_001278757.1; NM_001291828.1. [O75791-2] DR RefSeq; NP_004801.1; NM_004810.3. [O75791-1] DR PDB; 5GJH; X-ray; 1.20 A; A/C=58-155. DR PDBsum; 5GJH; -. DR AlphaFoldDB; O75791; -. DR SMR; O75791; -. DR BioGRID; 114799; 98. DR DIP; DIP-38435N; -. DR IntAct; O75791; 79. DR MINT; O75791; -. DR STRING; 9606.ENSP00000339186; -. DR iPTMnet; O75791; -. DR PhosphoSitePlus; O75791; -. DR BioMuta; GRAP2; -. DR jPOST; O75791; -. DR MassIVE; O75791; -. DR MaxQB; O75791; -. DR PaxDb; 9606-ENSP00000339186; -. DR PeptideAtlas; O75791; -. DR ProteomicsDB; 50196; -. [O75791-1] DR ProteomicsDB; 6952; -. DR Pumba; O75791; -. DR ABCD; O75791; 1 sequenced antibody. DR Antibodypedia; 236; 535 antibodies from 38 providers. DR DNASU; 9402; -. DR Ensembl; ENST00000344138.9; ENSP00000339186.4; ENSG00000100351.17. [O75791-1] DR Ensembl; ENST00000407075.3; ENSP00000385607.3; ENSG00000100351.17. [O75791-1] DR GeneID; 9402; -. DR KEGG; hsa:9402; -. DR MANE-Select; ENST00000344138.9; ENSP00000339186.4; NM_004810.4; NP_004801.1. DR AGR; HGNC:4563; -. DR CTD; 9402; -. DR DisGeNET; 9402; -. DR GeneCards; GRAP2; -. DR HGNC; HGNC:4563; GRAP2. DR HPA; ENSG00000100351; Tissue enriched (lymphoid). DR MIM; 604518; gene. DR neXtProt; NX_O75791; -. DR OpenTargets; ENSG00000100351; -. DR PharmGKB; PA28959; -. DR VEuPathDB; HostDB:ENSG00000100351; -. DR eggNOG; KOG3601; Eukaryota. DR GeneTree; ENSGT00940000157307; -. DR HOGENOM; CLU_073617_0_0_1; -. DR InParanoid; O75791; -. DR OMA; VAKFDFM; -. DR OrthoDB; 25371at2759; -. DR PhylomeDB; O75791; -. DR TreeFam; TF354288; -. DR PathwayCommons; O75791; -. DR Reactome; R-HSA-1433557; Signaling by SCF-KIT. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2424491; DAP12 signaling. DR Reactome; R-HSA-2871796; FCERI mediated MAPK activation. DR Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization. DR Reactome; R-HSA-389356; CD28 co-stimulation. DR Reactome; R-HSA-9607240; FLT3 Signaling. DR Reactome; R-HSA-9680350; Signaling by CSF1 (M-CSF) in myeloid cells. DR SignaLink; O75791; -. DR BioGRID-ORCS; 9402; 12 hits in 1153 CRISPR screens. DR ChiTaRS; GRAP2; human. DR GeneWiki; GRAP2; -. DR GenomeRNAi; 9402; -. DR Pharos; O75791; Tbio. DR PRO; PR:O75791; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; O75791; Protein. DR Bgee; ENSG00000100351; Expressed in monocyte and 98 other cell types or tissues. DR ExpressionAtlas; O75791; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005768; C:endosome; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0001784; F:phosphotyrosine residue binding; IBA:GO_Central. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0007265; P:Ras protein signal transduction; TAS:ProtInc. DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd09941; SH2_Grb2_like; 1. DR CDD; cd11950; SH3_GRAP2_C; 1. DR CDD; cd11947; SH3_GRAP2_N; 1. DR Gene3D; 3.30.505.10; SH2 domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 2. DR InterPro; IPR035646; GRAP2_C_SH3. DR InterPro; IPR043539; Grb2-like. DR InterPro; IPR000980; SH2. DR InterPro; IPR036860; SH2_dom_sf. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR46037:SF3; GRB2-RELATED ADAPTER PROTEIN 2; 1. DR PANTHER; PTHR46037; PROTEIN ENHANCER OF SEVENLESS 2B; 1. DR Pfam; PF00017; SH2; 1. DR Pfam; PF00018; SH3_1; 2. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00252; SH2; 1. DR SMART; SM00326; SH3; 2. DR SUPFAM; SSF55550; SH2 domain; 1. DR SUPFAM; SSF50044; SH3-domain; 2. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 2. DR Genevisible; O75791; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Endosome; KW Nucleus; Phosphoprotein; Reference proteome; Repeat; SH2 domain; KW SH3 domain. FT CHAIN 1..330 FT /note="GRB2-related adapter protein 2" FT /id="PRO_0000088208" FT DOMAIN 1..56 FT /note="SH3 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 58..149 FT /note="SH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT DOMAIN 271..330 FT /note="SH3 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REGION 143..244 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 143..159 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 45 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15144186, FT ECO:0007744|PubMed:19690332" FT MOD_RES 106 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 187 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O89100" FT MOD_RES 236 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O89100" FT MOD_RES 262 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:12522270, FT ECO:0007744|PubMed:15144186, ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..39 FT /note="MEAVAKFDFTASGEDELSFHTGDVLKILSNQEEWFKAEL -> MVSRRPLST FT PGRELTHGQGGWLLHHPGQPELPRGLLHLC (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055234" FT VAR_SEQ 40..152 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055235" FT VARIANT 319 FT /note="L -> F (in dbSNP:rs12759)" FT /evidence="ECO:0000269|PubMed:10820259" FT /id="VAR_012079" FT HELIX 65..73 FT /evidence="ECO:0007829|PDB:5GJH" FT STRAND 80..84 FT /evidence="ECO:0007829|PDB:5GJH" FT STRAND 86..88 FT /evidence="ECO:0007829|PDB:5GJH" FT STRAND 91..97 FT /evidence="ECO:0007829|PDB:5GJH" FT STRAND 99..109 FT /evidence="ECO:0007829|PDB:5GJH" FT STRAND 115..119 FT /evidence="ECO:0007829|PDB:5GJH" FT STRAND 121..124 FT /evidence="ECO:0007829|PDB:5GJH" FT HELIX 125..134 FT /evidence="ECO:0007829|PDB:5GJH" FT STRAND 139..141 FT /evidence="ECO:0007829|PDB:5GJH" SQ 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 //