GAB1_BOVIN
ID GAB1_BOVIN Reviewed; 694 AA.
AC A6QLU3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; BC148087; AAI48088.1; -; mRNA.
DR RefSeq; NP_001094671.1; NM_001101201.1.
DR AlphaFoldDB; A6QLU3; -.
DR SMR; A6QLU3; -.
DR BioGRID; 196652; 1.
DR STRING; 9913.ENSBTAP00000029800; -.
DR PaxDb; A6QLU3; -.
DR Ensembl; ENSBTAT00000029804; ENSBTAP00000029800; ENSBTAG00000002813.
DR GeneID; 540085; -.
DR KEGG; bta:540085; -.
DR CTD; 2549; -.
DR VEuPathDB; HostDB:ENSBTAG00000002813; -.
DR VGNC; VGNC:29183; GAB1.
DR eggNOG; KOG3751; Eukaryota.
DR GeneTree; ENSGT00940000156801; -.
DR HOGENOM; CLU_028652_0_0_1; -.
DR InParanoid; A6QLU3; -.
DR OMA; EPMRTHA; -.
DR OrthoDB; 1153633at2759; -.
DR TreeFam; TF329487; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000002813; Expressed in midbrain and 104 other tissues.
DR ExpressionAtlas; A6QLU3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0035591; F:signaling adaptor activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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_0000318942"
FT DOMAIN 5..116
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 194..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..378
FT /note="Polar 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: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; 76435 MW; 87BA5764A117DB4E CRC64;
MSGGEVVCSG WLRKSPPEKK LKRYAWKRRW FVLRSGRLTG DPDVLEYYKN DHAKKPIRII
DLNLCQQVDA GLTFNKKEFE NSYIFDINTI DRIFYLVADS EEEMNKWVRC ICDICGFNPT
EEDPVKAPGS SLQAPADIPL AISTAPPSSQ VGASAAAAPP PYQLISLPPH LETLGIQEDP
QDYLLLINCQ SKKPEPTRTH ADSAKSTSSE TDCNDNVPSH KNPASSQSKH GVNGFFQQHM
MYDSPPSRAA SLSVDSSLYN LPRSYSHDVL PKVSPSSTEA DGELYVFNTP SGTSSVEPQM
RHVSISYDIP PTPGNTYQIP RTFPEGTLGQ TSKLDTIPDI PPPRPPKPHP AHDRSPVDTC
SITRTASDTD SSYCIPTAGL PPSRSNTIST VDLNKLRKDA SSQDCYDTPR TFPSDRSSSL
EGFHNHFKIK NILTAGSVSS EELDENYVPM NPNSPPRQHS SSFTEPIQEA NYVPMTPGTF
DFSSFGMQVP PPAHMGFRSS PKTPPRRPVP VADCEPPPVD RNLKPDRKVK PAPLEIKPLP
EWEELQAPVR SPITRSFARD SSRFPLSPRP DSVHSTTSSS DSHDSEENYV PMNPNLSSED
SNLFGSNSLD GGNSPMIKPK GDKQVEYLDL DLDSGKSTPP RKQKSSGSGS SVADERVDYV
VVDQQKTLAL KSTREAWTDG RQSTESETPA KNVK
