GRAP2_HUMAN
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 03-AUG-2022, entry version 202.
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 gab-
RT 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}.
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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; 97.
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; O75791; -.
DR PeptideAtlas; O75791; -.
DR PRIDE; O75791; -.
DR ProteomicsDB; 50196; -. [O75791-1]
DR ProteomicsDB; 6952; -.
DR ABCD; O75791; 1 sequenced antibody.
DR Antibodypedia; 236; 503 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 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 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 SignaLink; O75791; -.
DR BioGRID-ORCS; 9402; 8 hits in 1075 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 97 other tissues.
DR ExpressionAtlas; O75791; baseline and differential.
DR Genevisible; O75791; HS.
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; cd11950; SH3_GRAP2_C; 1.
DR Gene3D; 3.30.505.10; -; 1.
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; PTHR46037; 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; SSF50044; SSF50044; 2.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 2.
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
