GAB1_MESAU
ID GAB1_MESAU Reviewed; 694 AA.
AC Q99PF6;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 78.
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 Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11432805;
RA Kameda H., Risinger J.I., Han B.B., Baek S.J., Barrett J.C., Glasgow W.C.,
RA Eling T.E.;
RT "Identification of epidermal growth factor receptor- Grb2-associated
RT binder-1-SHP-2 complex formation and its functional loss during neoplastic
RT cell progression.";
RL Cell Growth Differ. 12:307-318(2001).
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. {ECO:0000250|UniProtKB:Q13480}.
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 (By similarity). Within the complex interacts with
CC METTL13 (By similarity). Interacts with GRB2 and with other SH2-
CC containing proteins (By similarity). Interacts with phosphorylated LAT2
CC (By similarity). Interacts with PTPRJ (By similarity). Interacts
CC (phosphorylated) with PTPN11 (By similarity). Interacts with HCK (By
CC similarity). {ECO:0000250|UniProtKB:Q13480,
CC ECO:0000250|UniProtKB:Q9QYY0}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GAB family. {ECO:0000305}.
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DR EMBL; AF307847; AAG59808.1; -; mRNA.
DR RefSeq; NP_001268473.1; NM_001281544.1.
DR AlphaFoldDB; Q99PF6; -.
DR SMR; Q99PF6; -.
DR STRING; 10036.XP_005077819.1; -.
DR GeneID; 101837885; -.
DR CTD; 2549; -.
DR eggNOG; KOG3751; Eukaryota.
DR OrthoDB; 1153633at2759; -.
DR Proteomes; UP000189706; Unplaced.
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 2: Evidence at transcript level;
KW Acetylation; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13480"
FT CHAIN 2..694
FT /note="GRB2-associated-binding protein 1"
FT /id="PRO_0000050283"
FT DOMAIN 5..116
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 125..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..658
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 201..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..469
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 555..614
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:0000250|UniProtKB:Q13480"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13480"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13480"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13480"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13480"
FT MOD_RES 387
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13480"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13480"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYY0"
FT MOD_RES 627
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q13480"
FT MOD_RES 638
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13480"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13480"
FT MOD_RES 659
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q13480"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13480"
SQ SEQUENCE 694 AA; 76549 MW; 4DFE7C6FCABC91A4 CRC64;
MSGGEVVCSG WLRKSPPEKK LKRYAWKRRW FVLRSGRLTG DPDVLEYYKN DHAKKPIRII
DLNLCQQVDA GLTFNKKEFE NSYIFDINTI DRIFYLVADS EEDMNKWVRC ICDICGFNPT
EEDPVKPLGN SSQAPVDSPF AGNTAPASTQ LEASPVTLPP SYQLISLPPH PDTLGLQDDP
QDYLLLINCQ SKKPEPTRTH ADSAKPTSSE TDCNDNVPSH KTPASSQSKH GVNGFFQQQM
LYDCPPSRAA SVSVDSSLYN LPRSYSHDVL PKESPSSTEA DGQLYIFNTP SGTSSVEAQM
RHVSISYDIP PTPGNTYQIP RTFPEGTLGQ SSKLDTIPDI PPPRPPKPHL THDRSPVETC
GAPRTASDTD SSYCVPTAGM PPSRSNTIST VDLNKLWKDA SSQDCYDIPR TFPSDRSSSL
EGFHNQSKIK NVLTVASVSG EEPDENYVPM NPNSPPRQHS SSFTEPIQEP NYVPMTPGTF
DFSSFGMQVP PPAHLGFRSS PKTPPRRPVP VADCEPPPVD RNLKPDRKAK PAPLEIKPLP
EWEELQAPVR SPITRSFARD SSRFPLSPRP NSVHSTTSSS DSHDSEENYV PMNPNLSSED
PNLFGSNSLD GGSSSMIKPK GDKQVEYLDL DLDSGKSTPP RKQKNSGSGS SMADERVDYV
VVDQQKTLAL KSTREAWTDG RQSTESETPT KSVK
