ID GAB1_HUMAN Reviewed; 694 AA. AC Q13480; A8K152; Q4W5G2; Q6P1W2; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 2. DT 24-JAN-2024, entry version 201. DE RecName: Full=GRB2-associated-binding protein 1; DE AltName: Full=GRB2-associated binder 1; DE AltName: Full=Growth factor receptor bound protein 2-associated protein 1; GN Name=GAB1; 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=8596638; DOI=10.1038/379560a0; RA Holgado-Madruga M., Emlet D.R., Moscatello D.K., Godwin A.K., Wong A.J.; RT "A Grb2-associated docking protein in EGF- and insulin-receptor RT signalling."; RL Nature 379:560-564(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-311. RG NIEHS SNPs program; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Testis; 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 [7] RP INTERACTION WITH LAT2. RX PubMed=12486104; DOI=10.1084/jem.20021405; RA Brdicka T., Imrich M., Angelisova P., Brdickova N., Horvath O., Spicka J., RA Hilgert I., Luskova P., Draber P., Novak P., Engels N., Wienands J., RA Simeoni L., Oesterreicher J., Aguado E., Malissen M., Schraven B., RA Horejsi V.; RT "Non-T cell activation linker (NTAL): a transmembrane adaptor protein RT involved in immunoreceptor signaling."; RL J. Exp. Med. 196:1617-1626(2002). RN [8] RP INTERACTION WITH PTPRJ. RX PubMed=12475979; DOI=10.1074/jbc.m210656200; RA Palka H.L., Park M., Tonks N.K.; RT "Hepatocyte growth factor receptor tyrosine kinase met is a substrate of RT the receptor protein-tyrosine phosphatase DEP-1."; RL J. Biol. Chem. 278:5728-5735(2003). RN [9] RP PHOSPHORYLATION BY HCK, AND INTERACTION WITH HCK; CRKL PTPN11 AND GRB2. RX PubMed=15010462; DOI=10.1074/jbc.m305783200; RA Podar K., Mostoslavsky G., Sattler M., Tai Y.T., Hayashi T., Catley L.P., RA Hideshima T., Mulligan R.C., Chauhan D., Anderson K.C.; RT "Critical role for hematopoietic cell kinase (Hck)-mediated phosphorylation RT of Gab1 and Gab2 docking proteins in interleukin 6-induced proliferation RT and survival of multiple myeloma cells."; RL J. Biol. Chem. 279:21658-21665(2004). RN [10] RP REVIEW ON ROLE IN FGFR1 SIGNALING; SUBUNIT; PHOSPHORYLATION. RX PubMed=15863030; DOI=10.1016/j.cytogfr.2005.01.001; RA Eswarakumar V.P., Lax I., Schlessinger J.; RT "Cellular signaling by fibroblast growth factor receptors."; RL Cytokine Growth Factor Rev. 16:139-149(2005). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-659, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-547 (ISOFORM 2), AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-627, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251; SER-253; SER-266; RP SER-304; THR-387; SER-402; THR-638; SER-651; TYR-659 AND SER-683, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [15] RP VARIANTS [LARGE SCALE ANALYSIS] CYS-83 AND ASN-387. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [16] RP FUNCTION, INTERACTION WITH METTL13 AND SPRY2, INVOLVEMENT IN DFNB26, RP VARIANT DFNB26 GLU-116, AND CHARACTERIZATION OF VARIANT DFNB26 GLU-116. RX PubMed=29408807; DOI=10.1172/jci97350; RA Yousaf R., Ahmed Z.M., Giese A.P., Morell R.J., Lagziel A., Dabdoub A., RA Wilcox E.R., Riazuddin S., Friedman T.B., Riazuddin S.; RT "Modifier variant of METTL13 suppresses human GAB1-associated profound RT deafness."; RL J. Clin. Invest. 128:1509-1522(2018). CC -!- FUNCTION: Adapter protein that plays a role in intracellular signaling CC cascades triggered by activated receptor-type kinases. Plays a role in CC FGFR1 signaling. Probably involved in signaling by the epidermal growth CC factor receptor (EGFR) and the insulin receptor (INSR). Involved in the CC MET/HGF-signaling pathway (PubMed:29408807). CC {ECO:0000269|PubMed:29408807}. CC -!- SUBUNIT: Identified in a complex containing FRS2, GRB2, GAB1, PIK3R1 CC and SOS1 (By similarity). Forms a tripartite complex containing GAB1, CC METTL13 and SPRY2 (PubMed:29408807). Within the complex interacts with CC METTL13 (PubMed:29408807). Interacts with GRB2 and with other SH2- CC containing proteins (PubMed:15010462). Interacts with phosphorylated CC LAT2 (PubMed:12486104). Interacts with PTPRJ (PubMed:12475979). CC Interacts (phosphorylated) with PTPN11 (PubMed:15010462). Interacts CC with HCK (PubMed:15010462). {ECO:0000250|UniProtKB:Q9QYY0, CC ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:12486104, CC ECO:0000269|PubMed:15010462, ECO:0000269|PubMed:29408807}. CC -!- INTERACTION: CC Q13480; P51451: BLK; NbExp=3; IntAct=EBI-517684, EBI-2105445; CC Q13480; P46108: CRK; NbExp=2; IntAct=EBI-517684, EBI-886; CC Q13480; P46109: CRKL; NbExp=5; IntAct=EBI-517684, EBI-910; CC Q13480; P00533: EGFR; NbExp=5; IntAct=EBI-517684, EBI-297353; CC Q13480; P07332: FES; NbExp=2; IntAct=EBI-517684, EBI-1055635; CC Q13480; P62993: GRB2; NbExp=8; IntAct=EBI-517684, EBI-401755; CC Q13480; Q9UNN4: GTF2A1L; NbExp=3; IntAct=EBI-517684, EBI-10229384; CC Q13480; O15357: INPPL1; NbExp=2; IntAct=EBI-517684, EBI-1384248; CC Q13480; P06239: LCK; NbExp=10; IntAct=EBI-517684, EBI-1348; CC Q13480; P07948: LYN; NbExp=7; IntAct=EBI-517684, EBI-79452; CC Q13480; P16333: NCK1; NbExp=3; IntAct=EBI-517684, EBI-389883; CC Q13480; O43639: NCK2; NbExp=5; IntAct=EBI-517684, EBI-713635; CC Q13480; P27986: PIK3R1; NbExp=33; IntAct=EBI-517684, EBI-79464; CC Q13480; O00459: PIK3R2; NbExp=23; IntAct=EBI-517684, EBI-346930; CC Q13480; Q92569: PIK3R3; NbExp=36; IntAct=EBI-517684, EBI-79893; CC Q13480; P19174: PLCG1; NbExp=36; IntAct=EBI-517684, EBI-79387; CC Q13480; P16885: PLCG2; NbExp=15; IntAct=EBI-517684, EBI-617403; CC Q13480; Q13882: PTK6; NbExp=6; IntAct=EBI-517684, EBI-1383632; CC Q13480; Q06124: PTPN11; NbExp=42; IntAct=EBI-517684, EBI-297779; CC Q13480; Q06124-2: PTPN11; NbExp=2; IntAct=EBI-517684, EBI-17635971; CC Q13480; Q12913: PTPRJ; NbExp=2; IntAct=EBI-517684, EBI-2264500; CC Q13480; P49023: PXN; NbExp=2; IntAct=EBI-517684, EBI-702209; CC Q13480; P20936: RASA1; NbExp=25; IntAct=EBI-517684, EBI-1026476; CC Q13480; O14796: SH2D1B; NbExp=8; IntAct=EBI-517684, EBI-3923013; CC Q13480; Q9NP31: SH2D2A; NbExp=6; IntAct=EBI-517684, EBI-490630; CC Q13480; P29353: SHC1; NbExp=9; IntAct=EBI-517684, EBI-78835; CC Q13480; Q9H6Q3: SLA2; NbExp=4; IntAct=EBI-517684, EBI-1222854; CC Q13480; O14543: SOCS3; NbExp=4; IntAct=EBI-517684, EBI-714146; CC Q13480; O14544: SOCS6; NbExp=9; IntAct=EBI-517684, EBI-3929549; CC Q13480; P12931: SRC; NbExp=12; IntAct=EBI-517684, EBI-621482; CC Q13480; Q9ULZ2: STAP1; NbExp=3; IntAct=EBI-517684, EBI-6083058; CC Q13480; P43405: SYK; NbExp=4; IntAct=EBI-517684, EBI-78302; CC Q13480; P42680: TEC; NbExp=2; IntAct=EBI-517684, EBI-1383480; CC Q13480; P15498: VAV1; NbExp=2; IntAct=EBI-517684, EBI-625518; CC Q13480; P52735: VAV2; NbExp=2; IntAct=EBI-517684, EBI-297549; CC Q13480; Q9UKW4: VAV3; NbExp=6; IntAct=EBI-517684, EBI-297568; CC Q13480; P07947: YES1; NbExp=7; IntAct=EBI-517684, EBI-515331; CC Q13480; P50904: Rasa1; Xeno; NbExp=2; IntAct=EBI-517684, EBI-5747849; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q13480-1; Sequence=Displayed; CC Name=2; CC IsoId=Q13480-2; Sequence=VSP_017137; CC -!- PTM: Phosphorylated in response to FGFR1 activation. Phosphorylated on CC tyrosine residue(s) by the epidermal growth factor receptor (EGFR) and CC the insulin receptor (INSR). Tyrosine phosphorylation of GAB1 mediates CC interaction with several proteins that contain SH2 domains. CC Phosphorylated on tyrosine residues by HCK upon IL6 signaling. CC {ECO:0000269|PubMed:15010462}. CC -!- DISEASE: Deafness, autosomal recessive, 26 (DFNB26) [MIM:605428]: A CC form of non-syndromic sensorineural deafness characterized by CC prelingual, severe to profound hearing loss. Sensorineural deafness CC results from damage to the neural receptors of the inner ear, the nerve CC pathways to the brain, or the area of the brain that receives sound CC information. {ECO:0000269|PubMed:29408807}. Note=The disease is caused CC by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the GAB family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/gab1/"; 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; U43885; AAC50380.1; -; mRNA. DR EMBL; DQ021880; AAY26398.1; -; Genomic_DNA. DR EMBL; AK289767; BAF82456.1; -; mRNA. DR EMBL; AC097658; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC104685; AAY40964.1; -; Genomic_DNA. DR EMBL; CH471056; EAX05072.1; -; Genomic_DNA. DR EMBL; BC064848; AAH64848.1; -; mRNA. DR CCDS; CCDS3759.1; -. [Q13480-1] DR CCDS; CCDS3760.1; -. [Q13480-2] DR PIR; S68442; S68442. DR RefSeq; NP_002030.2; NM_002039.3. [Q13480-1] DR RefSeq; NP_997006.1; NM_207123.2. [Q13480-2] DR PDB; 4QSY; X-ray; 2.10 A; B=621-633. DR PDBsum; 4QSY; -. DR AlphaFoldDB; Q13480; -. DR SMR; Q13480; -. DR BioGRID; 108824; 161. DR CORUM; Q13480; -. DR ELM; Q13480; -. DR IntAct; Q13480; 142. DR MINT; Q13480; -. DR STRING; 9606.ENSP00000262995; -. DR ChEMBL; CHEMBL4523286; -. DR MoonDB; Q13480; Predicted. DR GlyCosmos; Q13480; 2 sites, 1 glycan. DR GlyGen; Q13480; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q13480; -. DR PhosphoSitePlus; Q13480; -. DR BioMuta; GAB1; -. DR DMDM; 90180201; -. DR CPTAC; CPTAC-1557; -. DR EPD; Q13480; -. DR jPOST; Q13480; -. DR MassIVE; Q13480; -. DR MaxQB; Q13480; -. DR PaxDb; 9606-ENSP00000262995; -. DR PeptideAtlas; Q13480; -. DR ProteomicsDB; 59477; -. [Q13480-1] DR ProteomicsDB; 59478; -. [Q13480-2] DR Pumba; Q13480; -. DR Antibodypedia; 3614; 486 antibodies from 42 providers. DR DNASU; 2549; -. DR Ensembl; ENST00000262994.9; ENSP00000262994.4; ENSG00000109458.10. [Q13480-1] DR Ensembl; ENST00000262995.9; ENSP00000262995.4; ENSG00000109458.10. [Q13480-2] DR GeneID; 2549; -. DR KEGG; hsa:2549; -. DR MANE-Select; ENST00000262994.9; ENSP00000262994.4; NM_002039.4; NP_002030.2. DR UCSC; uc003ijd.4; human. [Q13480-1] DR AGR; HGNC:4066; -. DR CTD; 2549; -. DR DisGeNET; 2549; -. DR GeneCards; GAB1; -. DR HGNC; HGNC:4066; GAB1. DR HPA; ENSG00000109458; Low tissue specificity. DR MalaCards; GAB1; -. DR MIM; 604439; gene. DR MIM; 605428; phenotype. DR neXtProt; NX_Q13480; -. DR OpenTargets; ENSG00000109458; -. DR PharmGKB; PA28477; -. DR VEuPathDB; HostDB:ENSG00000109458; -. DR eggNOG; KOG3751; Eukaryota. DR GeneTree; ENSGT00940000156801; -. DR HOGENOM; CLU_028652_0_0_1; -. DR InParanoid; Q13480; -. DR OMA; EPMRTHA; -. DR OrthoDB; 2904117at2759; -. DR PhylomeDB; Q13480; -. DR TreeFam; TF329487; -. DR PathwayCommons; Q13480; -. DR Reactome; R-HSA-109704; PI3K Cascade. DR Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants. DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling. DR Reactome; R-HSA-180292; GAB1 signalosome. DR Reactome; R-HSA-1963642; PI3K events in ERBB2 signaling. DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer. DR Reactome; R-HSA-5637810; Constitutive Signaling by EGFRvIII. DR Reactome; R-HSA-5654689; PI-3K cascade:FGFR1. DR Reactome; R-HSA-5654695; PI-3K cascade:FGFR2. DR Reactome; R-HSA-5654710; PI-3K cascade:FGFR3. DR Reactome; R-HSA-5654720; PI-3K cascade:FGFR4. DR Reactome; R-HSA-5655253; Signaling by FGFR2 in disease. DR Reactome; R-HSA-5655291; Signaling by FGFR4 in disease. DR Reactome; R-HSA-5655302; Signaling by FGFR1 in disease. DR Reactome; R-HSA-5655332; Signaling by FGFR3 in disease. DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR Reactome; R-HSA-8851907; MET activates PI3K/AKT signaling. DR Reactome; R-HSA-8853659; RET signaling. DR Reactome; R-HSA-8865999; MET activates PTPN11. DR Reactome; R-HSA-8875555; MET activates RAP1 and RAC1. DR Reactome; R-HSA-8875656; MET receptor recycling. DR Reactome; R-HSA-9027276; Erythropoietin activates Phosphoinositide-3-kinase (PI3K). DR Reactome; R-HSA-9028335; Activated NTRK2 signals through PI3K. DR Reactome; R-HSA-9664565; Signaling by ERBB2 KD Mutants. DR Reactome; R-HSA-9665348; Signaling by ERBB2 ECD mutants. DR SignaLink; Q13480; -. DR SIGNOR; Q13480; -. DR BioGRID-ORCS; 2549; 59 hits in 1155 CRISPR screens. DR ChiTaRS; GAB1; human. DR GeneWiki; GAB1; -. DR GenomeRNAi; 2549; -. DR Pharos; Q13480; Tchem. DR PRO; PR:Q13480; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q13480; Protein. DR Bgee; ENSG00000109458; Expressed in secondary oocyte and 191 other cell types or tissues. DR ExpressionAtlas; Q13480; baseline and differential. DR GO; GO:0005911; C:cell-cell junction; IMP:ARUK-UCL. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0035591; F:signaling adaptor activity; IBA:GO_Central. DR GO; GO:0001525; P:angiogenesis; IMP:BHF-UCL. DR GO; GO:0090668; P:endothelial cell chemotaxis to vascular endothelial growth factor; IMP:BHF-UCL. DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:ProtInc. DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:ProtInc. DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL. DR GO; GO:0038089; P:positive regulation of cell migration by vascular endothelial growth factor signaling pathway; ISS:BHF-UCL. DR GO; GO:0035728; P:response to hepatocyte growth factor; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; IMP:BHF-UCL. DR CDD; cd01266; PH_Gab1_Gab2; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR046355; Gab1-4-like. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR PANTHER; PTHR45960; GRB2-ASSOCIATED-BINDING PROTEIN; 1. DR PANTHER; PTHR45960:SF5; GRB2-ASSOCIATED-BINDING PROTEIN 1; 1. DR Pfam; PF00169; PH; 1. DR SMART; SM00233; PH; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR Genevisible; Q13480; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Deafness; Disease variant; KW Non-syndromic deafness; Phosphoprotein; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 2..694 FT /note="GRB2-associated-binding protein 1" FT /id="PRO_0000050282" FT DOMAIN 5..116 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT REGION 122..164 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 194..231 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 323..386 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 493..656 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 671..694 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 143..161 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 201..231 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 360..386 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 519..534 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 568..613 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 622..638 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22223895" FT MOD_RES 251 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 253 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 266 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 304 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 387 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 402 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 454 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9QYY0" FT MOD_RES 627 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 638 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 651 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 659 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 683 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 528 FT /note="K -> KGQSPKILRLKPHGLERTDSQTIGDFATRRK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_017137" FT VARIANT 83 FT /note="Y -> C (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036132" FT VARIANT 116 FT /note="G -> E (in DFNB26; results in dysregulation of FT MET-signaling pathway genes expression; does not affect FT interaction with METTL13; dbSNP:rs1553950635)" FT /evidence="ECO:0000269|PubMed:29408807" FT /id="VAR_080809" FT VARIANT 311 FT /note="P -> L (in dbSNP:rs28925904)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_025261" FT VARIANT 377 FT /note="T -> I (in dbSNP:rs2229879)" FT /id="VAR_053096" FT VARIANT 387 FT /note="T -> N (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036133" FT CONFLICT 204 FT /note="A -> G (in Ref. 1; AAC50380)" FT /evidence="ECO:0000305" FT CONFLICT 213 FT /note="C -> S (in Ref. 1; AAC50380)" FT /evidence="ECO:0000305" FT MOD_RES Q13480-2:547 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" SQ SEQUENCE 694 AA; 76616 MW; E0FAC78772B6677B CRC64; MSGGEVVCSG WLRKSPPEKK LKRYAWKRRW FVLRSGRLTG DPDVLEYYKN DHAKKPIRII DLNLCQQVDA GLTFNKKEFE NSYIFDINTI DRIFYLVADS EEEMNKWVRC ICDICGFNPT EEDPVKPPGS SLQAPADLPL AINTAPPSTQ ADSSSATLPP PYQLINVPPH LETLGIQEDP QDYLLLINCQ SKKPEPTRTH ADSAKSTSSE TDCNDNVPSH KNPASSQSKH GMNGFFQQQM IYDSPPSRAP SASVDSSLYN LPRSYSHDVL PKVSPSSTEA DGELYVFNTP SGTSSVETQM RHVSISYDIP PTPGNTYQIP RTFPEGTLGQ TSKLDTIPDI PPPRPPKPHP AHDRSPVETC SIPRTASDTD SSYCIPTAGM SPSRSNTIST VDLNKLRKDA SSQDCYDIPR AFPSDRSSSL EGFHNHFKVK NVLTVGSVSS EELDENYVPM NPNSPPRQHS SSFTEPIQEA NYVPMTPGTF DFSSFGMQVP PPAHMGFRSS PKTPPRRPVP VADCEPPPVD RNLKPDRKVK PAPLEIKPLP EWEELQAPVR SPITRSFARD SSRFPMSPRP DSVHSTTSSS DSHDSEENYV PMNPNLSSED PNLFGSNSLD GGSSPMIKPK GDKQVEYLDL DLDSGKSTPP RKQKSSGSGS SVADERVDYV VVDQQKTLAL KSTREAWTDG RQSTESETPA KSVK //