GRB2 (Growth factor receptor-bound protein 2)

Identity

Other names	ASH (Abundant Src Homology)
	Grb3-3
	MST084
	MSTP084
	HTO27
	EGFRBP (Epidermal Growth Factor Receptor Binding Protein)-GRB2
HGNC	GRB2
Location	17q25.1
Location_base_pair	Starts at 70825752 and ends at 70913384 bp from pter ( according to hg18-Mar_2006).
Local_order	Chromosome 17, 87,632 bases, 5'- 70913384 - 70825752 -3'; strand: (-). The human GRB2 gene is telomeric to GGA3 (Golgi associated, gamma adaptin ear containing, ARF binding protein 3) and centromeric to ITGB4 (integrin, beta 4).

DNA/RNA

Transcription

The GRB2 gene structure consists of five exons (ranging from 78 to 186 bp) and four introns (from approximately 1 to approximately 7 kb). Two human mRNA transcript variants arise from alternative splicing. GRB2 variant 1 mRNA encodes protein isoform 1, which is longer. Variant 2 mRNA, which encodes protein isoform 2, lacks an in-frame exon present in the 3' coding region of variant 1 encompassing residues 59 - 100 of the mature protein (see Protein, below).

Pseudogene

At least one potential human pseudogene may exist: LOC391157. A pseudogene of the mouse Grb2 homolog, known as Grb2-ps1 (growth factor receptor bound protein 2, pseudogene 1) also has been identified.

Protein

	A schematic representation of the domain structure of GRB2, which consists of a single Src homology 2 (SH2) domain (residues 59 - 152) flanked by two SH3 domains (amino-terminal: residues 3 - 54; carboxy-terminal: residues 160-212).
Description	GRB2 (isoform 1) is a 217 residue protein with an expected molecular mass of 25,206 Da. GRB2 protein has homology to non-catalytic regions of c-Src, consisting of a single Src homology 2 (SH2) domain flanked by two Src homology 3 (SH3) domains. GRB2 isoform 2, encoded by an alternatively spliced mRNA transcript known as variant 2, has a deletion in the amino-terminal portion of the SH2 domain encompassing residues 59 - 100 of isoform 1. This protein isoform, known originally as GRB3-3, does not bind to phosphotyrosyl-containing proteins like isoform 1, but retains two functional SH3 domains.
Expression	Expressed in virtually all embryonic and adult tissues.
Localisation	Primarily cytosolic, but transient plasma membrane and nuclear localizations have been reported.
Function	Cell surface receptor signaling - The two GRB2 SH3 domains bind to the proline-rich regions of the guanine nucleotide releasing factor son of sevenless (SOS-1) protein, and the GRB2-SOS-1 complex preexists in the cytoplasm of resting cells. Phosphotyrosyl residues on in the context of the motif NH2- pYXNX-COOH (where pY represents phosphotyrosine, N represents asparagine, and X represents any other residue) are selectively recognized by the GRB2 SH2 domain. Growth factor receptor tyrosine kinases (RTKs), including those for epidermal growth factor (EGF), fibroblast growth factor, nerve growth factor (TrkA/TrkB), platelet-derived growth factor, colony-stimulating factor-1, and hepatocyte growth factor (HGF), as well as non-receptor tyrosine kinases (TKs) such as BCR-Abl and focal adhesion kinase (FAK), intracellular effectors such as insulin receptor substrate-1 and Shc, and phosphotyrosine phosphatases such as SHP-2 (PTPN11) and receptor-like tyrosine phosphatase alpha, all conditionally possess the pYXNX motif. Note that the environmental cue leading to protein tyrosyl phosphorylation on an appropriate GRB2 recognition motif is independent of GRB2 interaction; thus, ligand independent EGFR activation, such as growth hormone-induced EGFR tyrosine phosphorylation by JAK2, also leads to GRB2-mediated ERK kinase pathway activation and c-fos expression. Similarly, mechanical stress leading to increased angiotensin II production and transactivation of EGFR and other intracellular kinases implicates GRB2 recruitment in cardiac hypertrophy and myocardial remodeling. In many mitogenic signaling pathways, recruitment of GRB2 from the cytosol, where it is already bound to the guanine nucleotide exchange factor SOS-1 via its amino-terminal SH3 domain, brings SOS1 in close proximity to Ras at the plasma membrane. Ras, a small GTPase in the GDP-bound inactive state in quiescent cells, then undergoes nucleotide exchange of GDP for GTP, which facilitates binding of the serine/threonine protein kinase Raf-1 and its subsequent activation. This initiates a cascade of kinase activation: activated Raf-1 phosphorylates and activates MEK1/MEK2, which in turn phosphorylate and stimulate the MAP kinases ERK1/ERK2. Activated ERKs translocate to the nucleus and phosphorylate transcription factors such as Elk-1, STAT1, STAT3 and Myc, activating gene expression. In parallel, the phosphatidyl inositol 3-kinase (PI3K)/Akt pathway is activated via the adaptor Gab1, which is bound to the GRB2 carboxyl-terminal SH3 domain in many epithelial cell types. The gene expression programs activated by these pathways initiate a spectrum of fundamental cellular activities including proliferation, growth (increase in cell size), differentiation and survival. These processes are critical for normal embryonic development and adult homeostasis, and are frequently aberrantly activated in cancer. Stimulation of the T cell antigen receptor (TCR) induces the tyrosine phosphorylation of a variety of cellular proteins, including a protein called p36-38 or Linker for Activation of T cells (LAT), a protein tightly associated with the plasma membrane. Tyrosyl-phosphorylated sequences of LAT bind to the GRB2 SH2 domain. In these cells the SH3 domains of GRB2 bind Vav-family proteins, guanine nucleotide exchange factors for Rho-family GTPases. These interactions are essential for TCR-induced calcium flux and activation of the MAP kinase cascade, ultimately leading to T cell proliferation and effector functions. Receptor endocytosis and ubiquitinylation - Upon ligand-dependant activation of EGFR TK, c-Cbl binds to the EGFR directly through its SH2 domain and indirectly through its SH3 domain. c-Cbl binding and its consequential phosphorylation results in activation of the E3 ubiquitin ligase complex of which c-Cbl is a component, resulting in receptor ubiquitinylation. GRB2 also regulates internalization of EGF receptors through clathrin-coated pits. Actin-based cell motility - GRB2 participates directly in the regulation of actin filament formation and actin-based cell motility. GRB2 is a critical link between Wiskott-Aldrich Syndrome protein (WASp) and the actin cytoskeleton; WAS patients show defects in T cell polarization and migration in response to physiologic stimuli, resulting in thrombocytopenia, eczema and immunodeficiency. Studies of WASp function and the intracellular motility of invasive microbial pathogens such as Listeria monocytogenes and Vaccinia virus helped to elucidate an important role for GRB2 in directly promoting actin based motility. In most mammalian cells, the WASp family member N-WASp interacts with the Arp2/3 complex and G-actin to stimulate actin polymerization. N-WASp activity is enhanced by other effectors such as Nck, Cdc42 and GRB2; disruption of GRB2 SH3 or SH2 domains diminishes actin polymerization and thus actin-based motility.
Homology	GRB2 amino acid sequence is very highly conserved among species. Human GRB2 shows 50% overall amino acid sequence identity with S. cerevisiae YPR154w, 58% identity with Sem-5 of C. elegans, 66% identity with the D. melanogaster homolog Drk and over 99% identity with both rat and mouse homologs.

Mutations

Note	No known naturally-occurring mutations in human GRB2 have been reported.

Implicated in

Entity	Normal embryogenesis
Note	A null mutation introduced into the mouse gene for Grb2 was used to demonstrate that Grb2 is required during embryogenesis for the differentiation of endodermal cells and epiblast formation. Replacing the carboxy-terminus of SOS-1 with the Grb2 SH2 domain yielded a fusion protein that rescued the defects caused by this Grb2 mutation. Grb2 signaling primarily regulates differentiation, rather than proliferation, in the early mouse embryo.
Entity	Cardiac hypertrophy
Note	Engineered Grb2 +/- mice subjected to cardiac stress failed to activate p38 MAP kinase (MAPK14) and Jun N-terminal kinase (JNK), and the cardiac hypertrophy and fibrosis observed in normal mice were blocked. Transgenic mice with dominant-negative forms of MAPK p38-alpha and p38-beta developed cardiac hypertrophy but were resistant to cardiac fibrosis when subjected to cardiac stress. These and other findings suggest that Grb2 activity is essential for cardiac hypertrophy and fibrosis in response to pressure overload, and that different signaling pathways downstream of Grb2 regulate fibrosis, fetal gene induction, and cardiomyocyte growth.
Entity	Cancer
Note	As a pivotal activator of cell-cycle control and motility pathways downstream of several growth factor receptors, GRB2 is involved in oncogenic signaling in a wide variety of human tumors. For example, GRB2 directly interacts with SOS-1 and the Bcr portion of the Bcr-Abl fusion protein, a tyrosine kinase oncoprotein which has been implicated in the pathogenesis of Philadelphia chromosome positive leukemias, such as CML, ALL, and AML. GRB2 is rate limiting for mammary carcinomas induced by polyomavirus middle T antigen. GRB2 over expression has been reported in human breast, bladder and prostate cancer cell lines. Selective small molecule inhibitors of GRB2 SH2 domain binding block solid tumor metastasis in animal models.

External links

	Nomenclature
HGNC	GRB2   4566
Entrez_Gene	GRB2  2885  growth factor receptor-bound protein 2
	Cards
Atlas	GRB2ID386ch17q25
GeneCards	GRB2
Ensembl	GRB2 [Search_View]   ENSG00000177885 [Gene_View]  GRB2 [Vega]
Genatlas	GRB2
GeneLynx	GRB2
eGenome	GRB2
euGene	2885
	Genomic and cartography
GoldenPath	GRB2  -  17q25.1   chr17:70825752-70913384 -  17q24-q25   [Description]    (hg18-Mar_2006)
Ensembl	GRB2 - 17q24-q25 [CytoView]
NCBI	Mapview
OMIM	Disease map [OMIM]
HomoloGene	GRB2
	Gene and transcription
Genbank	AA452034 [ ENTREZ ]
Genbank	AF171699 [ ENTREZ ]
Genbank	AF246238 [ ENTREZ ]
Genbank	AF302079 [ ENTREZ ]
Genbank	AF498925 [ ENTREZ ]
RefSeq	NM_002086 [ SRS ]    NM_002086 [ ENTREZ ]
RefSeq	NM_203506 [ SRS ]    NM_203506 [ ENTREZ ]
RefSeq	AC_000060 [ SRS ]    AC_000060 [ ENTREZ ]
RefSeq	AC_000149 [ SRS ]    AC_000149 [ ENTREZ ]
RefSeq	NC_000017 [ SRS ]    NC_000017 [ ENTREZ ]
RefSeq	NT_010641 [ SRS ]    NT_010641 [ ENTREZ ]
RefSeq	NW_001838454 [ SRS ]    NW_001838454 [ ENTREZ ]
RefSeq	NW_926918 [ SRS ]    NW_926918 [ ENTREZ ]
CCDS	GRB2 CCDS - NCBI
AceView	GRB2 AceView - NCBI
Unigene	Hs.708119 [ SRS ]    Hs.708119 [ NCBI ]     HS708119 [ spliceNest ]
Fast-db	14732 (alternative variants)
	Protein : pattern, domain, 3D structure
SwissProt	P62993 [ SRS]    P62993 [ EXPASY ]     P62993 [ INTERPRO ]     P62993 [ UNIPROT ] P62993 [ VarSplice ]
Prosite	PS50001 SH2 [ SRS ]    PS50001 SH2 [ Expasy ]
Prosite	PS50002 SH3 [ SRS ]    PS50002 SH3 [ Expasy ]
Interpro	IPR000108 Neu_cyt_fact_2 [ SRS ]    IPR000108 Neu_cyt_fact_2 [ EBI ]
Interpro	IPR000980 SH2 [ SRS ]    IPR000980 SH2 [ EBI ]
Interpro	IPR001452 SH3 [ SRS ]    IPR001452 SH3 [ EBI ]
CluSTr	P62993
Pfam	PF00017 SH2 [ SRS ]    PF00017 SH2 [ Sanger ]    pfam00017 [ NCBI-CDD ]
Pfam	PF00018 SH3_1 [ SRS ]    PF00018 SH3_1 [ Sanger ]    pfam00018 [ NCBI-CDD ]
Smart	SM00252 SH2 [EMBL]
Smart	SM00326 SH3 [EMBL]
Prodom	PD000093 SH2[INRA-Toulouse]
Prodom	P62993 GRB2_HUMAN [ Domain structure ]   P62993 GRB2_HUMAN  [ sequences sharing at least 1 domain ]
Prodom	PD000093[INRA-Toulouse]
Prodom	P62993 GRB2_HUMAN [ Domain structure ]   P62993 GRB2_HUMAN  [ sequences sharing at least 1 domain ]
Blocks	P62993
PDB	1AZE [ SRS ]    1AZE [ PdbSum ],   1AZE [ IMB ]   1AZE [ RSDB ]
PDB	1BM2 [ SRS ]    1BM2 [ PdbSum ],   1BM2 [ IMB ]   1BM2 [ RSDB ]
PDB	1BMB [ SRS ]    1BMB [ PdbSum ],   1BMB [ IMB ]   1BMB [ RSDB ]
PDB	1CJ1 [ SRS ]    1CJ1 [ PdbSum ],   1CJ1 [ IMB ]   1CJ1 [ RSDB ]
PDB	1FHS [ SRS ]    1FHS [ PdbSum ],   1FHS [ IMB ]   1FHS [ RSDB ]
PDB	1FYR [ SRS ]    1FYR [ PdbSum ],   1FYR [ IMB ]   1FYR [ RSDB ]
PDB	1GCQ [ SRS ]    1GCQ [ PdbSum ],   1GCQ [ IMB ]   1GCQ [ RSDB ]
PDB	1GFC [ SRS ]    1GFC [ PdbSum ],   1GFC [ IMB ]   1GFC [ RSDB ]
PDB	1GFD [ SRS ]    1GFD [ PdbSum ],   1GFD [ IMB ]   1GFD [ RSDB ]
PDB	1GHU [ SRS ]    1GHU [ PdbSum ],   1GHU [ IMB ]   1GHU [ RSDB ]
PDB	1GRI [ SRS ]    1GRI [ PdbSum ],   1GRI [ IMB ]   1GRI [ RSDB ]
PDB	1IO6 [ SRS ]    1IO6 [ PdbSum ],   1IO6 [ IMB ]   1IO6 [ RSDB ]
PDB	1JYQ [ SRS ]    1JYQ [ PdbSum ],   1JYQ [ IMB ]   1JYQ [ RSDB ]
PDB	1JYR [ SRS ]    1JYR [ PdbSum ],   1JYR [ IMB ]   1JYR [ RSDB ]
PDB	1JYU [ SRS ]    1JYU [ PdbSum ],   1JYU [ IMB ]   1JYU [ RSDB ]
PDB	1QG1 [ SRS ]    1QG1 [ PdbSum ],   1QG1 [ IMB ]   1QG1 [ RSDB ]
PDB	1TZE [ SRS ]    1TZE [ PdbSum ],   1TZE [ IMB ]   1TZE [ RSDB ]
PDB	1X0N [ SRS ]    1X0N [ PdbSum ],   1X0N [ IMB ]   1X0N [ RSDB ]
PDB	1ZFP [ SRS ]    1ZFP [ PdbSum ],   1ZFP [ IMB ]   1ZFP [ RSDB ]
PDB	2AOA [ SRS ]    2AOA [ PdbSum ],   2AOA [ IMB ]   2AOA [ RSDB ]
PDB	2AOB [ SRS ]    2AOB [ PdbSum ],   2AOB [ IMB ]   2AOB [ RSDB ]
PDB	2H46 [ SRS ]    2H46 [ PdbSum ],   2H46 [ IMB ]   2H46 [ RSDB ]
PDB	2H5K [ SRS ]    2H5K [ PdbSum ],   2H5K [ IMB ]   2H5K [ RSDB ]
PDB	2HUW [ SRS ]    2HUW [ PdbSum ],   2HUW [ IMB ]   2HUW [ RSDB ]
PDB	2HUY [ SRS ]    2HUY [ PdbSum ],   2HUY [ IMB ]   2HUY [ RSDB ]
HPRD	00150
	Protein Interaction databases
DIP	P62993
IntAct	P62993
	Polymorphism : SNP, mutations, diseases
OMIM	108355    [ map ]
GENECLINICS	108355
SNP	GRB2 [dbSNP-NCBI]
SNP	NM_002086 [SNP-NCI]
SNP	NM_203506 [SNP-NCI]
SNP	GRB2 [GeneSNPs - Utah]  GRB2] [HGBASE - SRS]
HAPMAP	GRB2 [HAPMAP]
COSMIC	GRB2 [Somatic mutation (COSMIC-CGP-Sanger)]
HGMD	GRB2
Genetic Association	GRB2
CDC HuGE	GRB2
	General knowledge
Family Browser	GRB2 [UCSC Family Browser]
SOURCE	NM_002086
SOURCE	NM_203506
SMD	Hs.708119
SAGE	Hs.708119
GO	SH3/SH2 adaptor activity [Amigo]  SH3/SH2 adaptor activity
GO	epidermal growth factor receptor binding [Amigo]  epidermal growth factor receptor binding
GO	Golgi apparatus [Amigo]  Golgi apparatus
GO	cytosol [Amigo]  cytosol
GO	cytosol [Amigo]  cytosol
GO	epidermal growth factor receptor signaling pathway [Amigo]  epidermal growth factor receptor signaling pathway
GO	Ras protein signal transduction [Amigo]  Ras protein signal transduction
GO	Ras protein signal transduction [Amigo]  Ras protein signal transduction
GO	cell-cell signaling [Amigo]  cell-cell signaling
GO	insulin receptor signaling pathway [Amigo]  insulin receptor signaling pathway
GO	insulin receptor substrate binding [Amigo]  insulin receptor substrate binding
GO	interspecies interaction between organisms [Amigo]  interspecies interaction between organisms
BIOCARTA	Angiotensin II mediated activation of JNK Pathway via Pyk2 dependent signaling    [Genes]
BIOCARTA	Calcium Signaling by HBx of Hepatitis B virus    [Genes]
BIOCARTA	TPO Signaling Pathway    [Genes]
BIOCARTA	BCR Signaling Pathway    [Genes]
BIOCARTA	Bioactive Peptide Induced Signaling Pathway    [Genes]
BIOCARTA	CBL mediated ligand-induced downregulation of EGF receptors    [Genes]
BIOCARTA	Transcription factor CREB and its extracellular signals    [Genes]
BIOCARTA	The Co-Stimulatory Signal During T-cell Activation    [Genes]
BIOCARTA	EGF Signaling Pathway    [Genes]
BIOCARTA	EPO Signaling Pathway    [Genes]
BIOCARTA	Role of Erk5 in Neuronal Survival    [Genes]
BIOCARTA	Erk1/Erk2 Mapk Signaling pathway    [Genes]
BIOCARTA	Fc Epsilon Receptor I Signaling in Mast Cells    [Genes]
BIOCARTA	Growth Hormone Signaling Pathway    [Genes]
BIOCARTA	Inhibition of Cellular Proliferation by Gleevec    [Genes]
BIOCARTA	Role of ERBB2 in Signal Transduction and Oncology    [Genes]
BIOCARTA	IGF-1 Signaling Pathway    [Genes]
BIOCARTA	Multiple antiapoptotic pathways from IGF-1R signaling lead to BAD phosphorylation    [Genes]
BIOCARTA	IL 2 signaling pathway    [Genes]
BIOCARTA	IL-2 Receptor Beta Chain in T cell Activation    [Genes]
BIOCARTA	IL 3 signaling pathway    [Genes]
BIOCARTA	IL 4 signaling pathway    [Genes]
BIOCARTA	IL 6 signaling pathway    [Genes]
BIOCARTA	Insulin Signaling Pathway    [Genes]
BIOCARTA	Integrin Signaling Pathway    [Genes]
BIOCARTA	MAPKinase Signaling Pathway    [Genes]
BIOCARTA	Signaling of Hepatocyte Growth Factor Receptor    [Genes]
BIOCARTA	Nerve growth factor pathway (NGF)    [Genes]
BIOCARTA	p38 MAPK Signaling Pathway    [Genes]
BIOCARTA	PDGF Signaling Pathway    [Genes]
BIOCARTA	PTEN dependent cell cycle arrest and apoptosis    [Genes]
BIOCARTA	Links between Pyk2 and Map Kinases    [Genes]
BIOCARTA	Sprouty regulation of tyrosine kinase signals    [Genes]
BIOCARTA	Activation of Src by Protein-tyrosine phosphatase alpha    [Genes]
BIOCARTA	T Cell Receptor Signaling Pathway    [Genes]
BIOCARTA	Trefoil Factors Initiate Mucosal Healing    [Genes]
BIOCARTA	Trka Receptor Signaling Pathway    [Genes]
KEGG	Neurodegenerative Disorders
KEGG	MAPK signaling pathway
KEGG	Dorso-ventral axis formation
KEGG	Focal adhesion
KEGG	Gap junction
KEGG	Jak-STAT signaling pathway
KEGG	Natural killer cell mediated cytotoxicity
KEGG	T cell receptor signaling pathway
KEGG	Fc epsilon RI signaling pathway
KEGG	Insulin signaling pathway
KEGG	GnRH signaling pathway
KEGG	Huntington's disease
KEGG	Colorectal cancer
PubGene	GRB2
TreeFam	GRB2
CTD	2885 [Comparative ToxicoGenomics Database]
	Other databases
Other database	Jackson Laboratory Mouse Genome Informatics Database; MGI: 99843
	Probes
Probe	GRB2 Related clones (RZPD - Berlin)
	PubMed
PubMed	373 Pubmed reference(s) in Entrez

Bibliography

C. elegans cell-signalling gene sem-5 encodes a protein with SH2 and SH3 domains.

Clark SG, Stern MJ, Horvitz HR

Nature. 1992 ; 356 (6367) : 340-344.

PMID 1372395

The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling.

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PMID 1322798

A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos.

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PMID 8462098

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PMID 8462097

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PMID 8402896

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Molecular biology of the cell. 1993 ; 4 (11) : 1175-1188.

PMID 8305738

Activation of the Ras signalling pathway in human breast cancer cells overexpressing erbB-2.

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PMID 7970720

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PMID 7479904

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PMID 8662733

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PMID 8662889

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PMID 9391119

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PMID 9790226

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PMID 9865697

Concomitant activation of pathways downstream of Grb2 and PI 3-kinase is required for MET-mediated metastasis.

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Oncogene. 1999 ; 18 (5) : 1139-1146.

PMID 10022119

Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7.

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The Journal of biological chemistry. 1999 ; 274 (44) : 31707-31712.

PMID 10531381

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Bochmann H, Gehrisch S, Jaross W

Genomics. 1999 ; 56 (2) : 203-207.

PMID 10051406

GRB2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-WASp) with actin-related protein (ARP2/3) complex.

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The Journal of biological chemistry. 2000 ; 275 (29) : 21946-21952.

PMID 10781580

Significance of the Grb2 and son of sevenless (Sos) proteins in human bladder cancer cell lines.

Watanabe T, Shinohara N, Moriya K, Sazawa A, Kobayashi Y, Ogiso Y, Takiguchi M, Yasuda J, Koyanagi T, Kuzumaki N, Hashimoto A

IUBMB life. 2000 ; 49 (4) : 317-320.

PMID 10995035

The role of membrane-associated adaptors in T cell receptor signalling.

Zhang W, Samelson LE

Seminars in immunology. 2000 ; 12 (1) : 35-41.

PMID 10723796

Up-regulation of the protein tyrosine phosphatase SHP-1 in human breast cancer and correlation with GRB2 expression.

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PMID 11054664

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PMID 11135575

Coordinated traffic of Grb2 and Ras during epidermal growth factor receptor endocytosis visualized in living cells.

Jiang X, Sorkin A

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PMID 12006650

Grb2 and Nck act cooperatively to promote actin-based motility of vaccinia virus.

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Current biology : CB. 2002 ; 12 (9) : 740-745.

PMID 12007418

Use of signal specific receptor tyrosine kinase oncoproteins reveals that pathways downstream from Grb2 or Shc are sufficient for cell transformation and metastasis.

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PMID 11896612

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PMID 12655641

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PMID 14685170

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PMID 12639989

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PMID 15672868

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Contributor(s)

Written	05-2007	Gagani Athauda, Donald P Bottaro
		Miami Project to Cure Paralysis, Miller School of Medicine, University of Miami, Miami, FL 33136 USA and Urologic Oncology Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA (GA) ; Urologic Oncology Branch, CCR, NCI, Bldg 10 CRC Rm 1-3961, 10 Center Drive MSC 1107, Bethesda, MD 20892-1107, USA (DPB)

Citation

This paper should be referenced as such :

Athauda G, Bottaro DP . GRB2 (Growth factor receptor-bound protein 2). Atlas Genet Cytogenet Oncol Haematol. May 2007 . URL : http://AtlasGeneticsOncology.org/Genes/GRB2ID386ch17q25.html

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indexed on : Sun Nov 9 19:41:25 2008