GAB1_HUMAN
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 03-AUG-2022, entry version 194.
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=4; 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/";
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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; 135.
DR CORUM; Q13480; -.
DR ELM; Q13480; -.
DR IntAct; Q13480; 117.
DR MINT; Q13480; -.
DR STRING; 9606.ENSP00000262995; -.
DR ChEMBL; CHEMBL4523286; -.
DR MoonDB; Q13480; Predicted.
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; Q13480; -.
DR PeptideAtlas; Q13480; -.
DR PRIDE; Q13480; -.
DR ProteomicsDB; 59477; -. [Q13480-1]
DR ProteomicsDB; 59478; -. [Q13480-2]
DR Antibodypedia; 3614; 389 antibodies from 42 providers.
DR DNASU; 2549; -.
DR Ensembl; ENST00000262994.9; ENSP00000262994.4; ENSG00000109458.9. [Q13480-1]
DR Ensembl; ENST00000262995.8; ENSP00000262995.4; ENSG00000109458.9. [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 CTD; 2549; -.
DR DisGeNET; 2549; -.
DR GeneCards; GAB1; -.
DR HGNC; HGNC:4066; GAB1.
DR HPA; ENSG00000109458; Tissue enhanced (brain).
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 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; 58 hits in 1077 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 189 other tissues.
DR ExpressionAtlas; Q13480; baseline and differential.
DR Genevisible; Q13480; HS.
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:0031532; P:actin cytoskeleton reorganization; IMP:BHF-UCL.
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 Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR046355; Gab1-4-like.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR45960; PTHR45960; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
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 MET-
FT 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
