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Protein Page:
Grb2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
Grb2 an adaptor protein of the GRB2 / sem-5 / DRK family. Associates with many different tyrosine-phosphorylated proteins via its SH2 domain, including EGFR, PDGFR, IRS-1, SHC and LNK. It also seems to interact with RAS in the signaling pathway leading to DNA synthesis. Binds to and translocates the guanine nucleotide exchange factors SOS. Four alternatively spliced isoforms have been described. Isoform GRB3-3 does not bind to phosphorylated epidermal growth factor receptor (EGFR) but inhibits EGF-induced transactivation of a RAS-responsive element. GRB3-3 acts as a dominant negative protein over GRB2 and by suppressing proliferative signals, may trigger active programmed cell death. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Adaptor/scaffold; Cell development/differentiation
Cellular Component: signalosome; Golgi apparatus; cytoplasm; plasma membrane; vesicle membrane; nucleus; cytosol; endosome
Molecular Function: identical protein binding; protein binding; SH3/SH2 adaptor activity; ephrin receptor binding; phosphotyrosine binding; insulin receptor substrate binding; neurotrophin TRKA receptor binding; protein kinase binding; SH3 domain binding; protein phosphatase binding; epidermal growth factor receptor binding
Biological Process: negative regulation of epidermal growth factor receptor signaling pathway; epidermal growth factor receptor signaling pathway; platelet activation; axon guidance; phosphoinositide-mediated signaling; fibroblast growth factor receptor signaling pathway; viral reproduction; nerve growth factor receptor signaling pathway; positive regulation of signal transduction; protein heterooligomerization; DNA damage response, signal transduction; cell-cell signaling; positive regulation of actin filament polymerization; regulation of MAPKKK cascade; receptor internalization; T cell costimulation; Ras protein signal transduction; insulin receptor signaling pathway; anatomical structure formation; innate immune response; blood coagulation; leukocyte migration; aging
Reference #:  P62993 (UniProtKB)
Alt. Names/Synonyms: abundant SRC homology; Adapter protein GRB2; ASH; EGFRBP-GRB2; epidermal growth factor receptor-binding protein GRB2; GRB2; Grb3-3; Growth factor receptor-bound protein 2; growth factor receptor-bound protein 3; HT027; MST084; MSTP084; NCKAP2; Protein Ash; SH2/SH3 adapter GRB2
Gene Symbols: GRB2
Molecular weight: 25,206 Da
Basal Isoelectric point: 5.89  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics  |  B Cell Receptor Signaling  |  ErbB/HER Signaling  |  GPCR Signaling to MAPKs  |  Growth And Differentiation Control by MAPKs  |  IL6 Signaling  |  Insulin Receptor Signaling  |  SAPK/JNK Signaling Cascades  |  T Cell Receptor Signaling  |  TGF-├č Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Grb2

Protein Structure Not Found.


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Sites Implicated In
cell growth, altered: Y7‑p, Y37‑p, Y52‑p, Y209‑p
molecular association, regulation: Y209‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 K6-ac __MEAIAkyDFKATA
1 2 Y7-p _MEAIAkyDFKATAD
0 1 K10 AIAkyDFKATADDEL
0 2 S18-p ATADDELsFkRGDIL
0 1 K20-ub ADDELsFkRGDILKV
1 0 Y37-p EECDQNWykAELNGk
0 1 K38 ECDQNWyKAELNGkD
0 1 K38-ac ECDQNWykAELNGkD
0 3 K44-ub ykAELNGkDGFIPkN
0 1 K50-ac GkDGFIPkNyIEMkP
1 1 Y52-p DGFIPkNyIEMkPHP
0 1 K56-ub PkNyIEMkPHPWFFG
0 1 K69-ub FGKIPRAkAEEMLSk
0 1 K76-ub kAEEMLSkQRHDGAF
0 1 S88-p GAFLIREsESAPGDF
0 56 K109-ub GNDVQHFkVLRDGAG
0 1 K109-ac GNDVQHFkVLRDGAG
0 1 K117-ac VLRDGAGkYFLWVVK
0 2 T159-p EQVPQQPtyVQALFD
2 35 Y160-p QVPQQPtyVQALFDF
3 206 Y209-p TGMFPRNyVtPVNRN
0 5 T211-p MFPRNyVtPVNRNV_
  Grb2 iso2  
K6 __MEAIAKYDFKATA
Y7 _MEAIAKYDFKATAD
K10 AIAKYDFKATADDEL
S18 ATADDELSFKRGDIL
K20 ADDELSFKRGDILKV
Y37 EECDQNWYKAELNGK
K38 ECDQNWYKAELNGKD
K38 ECDQNWYKAELNGKD
K44 YKAELNGKDGFIPKN
K50 GKDGFIPKNyIEMKP
Y52-p DGFIPKNyIEMKPHP
K56 PKNyIEMKPHPFGND
- gap
- gap
- gap
K68 GNDVQHFKVLRDGAG
K68 GNDVQHFKVLRDGAG
K76 VLRDGAGKYFLWVVK
T118 EQVPQQPTYVQALFD
Y119 QVPQQPTYVQALFDF
Y168 TGMFPRNYVTPVNRN
T170 MFPRNYVTPVNRNV_
  mouse

 
K6 __MEAIAKYDFkATA
Y7 _MEAIAKYDFkATAD
K10-ub AIAKYDFkATADDEL
S18-p ATADDELsFKRGDIL
K20 ADDELsFKRGDILKV
Y37 EECDQNWYkAELNGk
K38-ub ECDQNWYkAELNGkD
K38 ECDQNWYKAELNGkD
K44-ub YkAELNGkDGFIPKN
K50 GkDGFIPKNYIEMKP
Y52 DGFIPKNYIEMKPHP
K56 PKNYIEMKPHPWFFG
K69 FGKIPRAKAEEMLSK
K76 KAEEMLSKQRHDGAF
S88 GAFLIRESESAPGDF
K109-ub GNDVQHFkVLRDGAG
K109 GNDVQHFKVLRDGAG
K117 VLRDGAGKYFLWVVK
T159 EQMPQQPTyVQALFD
Y160-p QMPQQPTyVQALFDF
Y209-p TGMFPRNyVTPVNRN
T211 MFPRNyVTPVNRNV_
  rat

 
K6 __MEAIAKYDFKATA
Y7 _MEAIAKYDFKATAD
K10 AIAKYDFKATADDEL
S18 ATADDELSFKRGDIL
K20 ADDELSFKRGDILKV
Y37 EECDQNWYKAELNGK
K38 ECDQNWYKAELNGKD
K38 ECDQNWYKAELNGKD
K44 YKAELNGKDGFIPKN
K50 GKDGFIPKNYIEMKP
Y52 DGFIPKNYIEMKPHP
K56 PKNYIEMKPHPWFFG
K69 FGKIPRAKAEEMLSK
K76 KAEEMLSKQRHDGAF
S88 GAFLIRESESAPGDF
K109 GNDVQHFKVLRDGAG
K109 GNDVQHFKVLRDGAG
K117 VLRDGAGKYFLWVVK
T159 EQVPQQPTyVQALFD
Y160-p QVPQQPTyVQALFDF
Y209 TGMFPRNYVTPVNRN
T211 MFPRNYVTPVNRNV_
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