SHC1 (SHC (Src homology 2 domain containing) transforming protein 1)

2009-02-01   Lucilla Luzi , Enrica Migliaccio , Pier Giuseppe Pelicci 

IFOM, FIRC Institute for Molecular Oncology Foundation, Via Adamello 16, 20139 Milano, Italy (LL); EIO, European Institute of Oncology, Via Ripamonti 435, 20141 Milano, Italy (EM, PGP)


Atlas Image
Mapping of SHC1 gene on genomic context of the human chromosome 1.


Atlas Image
SHC1 locus organization and alternative splicing isoforms. Dark blue boxes correspond to CDS; light blue portions represent 5 and 3 UTR respectively; red triangles point to the first ATG codon of p66, p52 and p46 isoforms in that order.


SHC1 gene covers 12,066 bp of DNA on q21.3 arm of chr1 and counts 13 exons and 13 introns.


SHC1 locus produces two distinct transcripts directed from alternative promoters; altogether they encode for three overlapping protein isoforms of 66, 52, and 46 kDa thus called p66Shc, p52Shc and p46Shc. The first transcript (NM_003029) is 3,076 bp long and specifically encodes for the p52 and p46 forms from two different in-frame ATGs and derives from the splicing of the first non-coding exon to an internal site of the second exon; this process produces the skipping of the sequence that encodes for the longest p66Shc isoform. The second transcript (NM_183001 and BX647149) is 3,497bp long, it is transcribed starting from the beginning of the second exon, under the regulation of a different promoter and it encodes for all three p66, p52 and p46Shc isoforms by means of alternative ATGs usage.


Two possible processed pseudogenes of SHC1 are located on chrX and chr17.


Atlas Image
Modular domain organization of the three SHC1 protein isoforms.


Regardless of their high structural similarity, a growing bunch of experimental evidences suggests that the p66Shc and p52/p46Shc isoforms are functionally non-redundant. P66, p52 and p46Shc consist of 583, 474 and 428 aa, respectively. All the three SHC1 protein isoforms share the same basic modular organization: they contain two different phosphotyrosine-binding domains, namely a PTB domain in the amino-terminal and a SH2 in the carboxy-terminal, separated by a poorly characterized glycine/proline-rich region rather similar to the collagen protein and therefore called Collagen Homology domain 1, CH1. In vitro experiments suggest that the "proline rich motif" found in the CH1 domain might be responsible for the interaction between p52Shc and the SH3 domain of SRC, LYN, FYN cytoplasmic tyrosine kinases, but the functional role of this interaction is still unclear and there are no genetic or biochemical evidences that these proteins interact in vivo. The longest p66Shc isoform contains a supplementary amino-terminal glycine/proline-rich region, called CH2. The N-term PTB and C-term SH2 modularity is an exclusive feature of the Shc protein family. Both PTB and SH2 domains bind to phosphorylated tyrosines within specific, short peptide sequences: amino-terminal residues immediately adjacent to the pY confer specificity on PTB domain; conversely carboxy-terminal amino acids draw specificity for the SH2. The CH1 region contains three key tyrosines, Y239, Y240 and Y317 that become phosphorylated upon commitment of a number of cell surface ligand-activated receptors. Recently, in murine systems, was demonstrated that SHC1 may signal through the CH1 pYs motif both in a dependent and independent manner supporting different pathways in tissue morphogenesis. The p66Shc specific CH2 region does not become tyrosine phosphorylated, but gets phosphorylation on serine 36 (S36) upon oxidative stress; Tetradecanoylphorbol-13-acetate (TPA) induces phosphorylation both of Ser 36 and Ser 138 of p66Shc. A new functional region, the "redox centre", responsible for cytochrome c binding, has been recently characterized within the p66Shc CH2-PTB domains. It has been mapped within a portion that presents the highest degree of identity in sequence alignments of p66Shc vertebrate orthologous and it is essential for the p66Shc function in ROS regulation. This region (designated CB, for cytochrome c binding) contains three glutamic acid (E125, E132, E133) and two tryptophan (W134 and W148) conserved residues.


p52/p46Shc are widely expressed in cultured cell and in almost all adult mouse tissues with an invariable relative amount; p66Shc protein instead shows a more peculiar pattern since it is expressed in the most of cells except in the hematopoietic lineage, where it is absent or barely recognizable. During early rat embryonic development SHC1 is most significantly expressed in the endothelium, in mesenchymal cells of the cardiovascular system and in the forebrains area of active proliferation of immature neuroblasts. In postnatal and adult rat brain, SHC1 mRNAs and proteins are not expressed. In the adult olfactory epithelium, in which neuronal cell renewal occurs throughout life, SHC1 remained strongly expressed. In both human and murine adult tissues, p52Shc and p46Shc (mRNA and proteins) are ubiquitously expressed, while p66Shc is expressed at different levels in specific tissues, such as lung, spleen, liver, heart, and kidney and is absent in the hematopoietic lineage.
The level of p66Shc mRNA is highest in human dermal fibroblasts (DFs) from centenarians in respect to DFs from old and young people suggesting that the expression of p66Shc increases with age and associates with human longevity.


P52Shc proteins is localized on endoplasmic reticulum membranes and is redistributed after tyrosine kinase receptor activation; p46Shc localizes to the mitochondrial matrix via a N-terminal mitochondrial targeting signal. The p66Shc isoform localizes in different intracellular compartments including endoplasmic reticulum and mitochondria.


P52/p46Shc and the p66Shc proteins carry out very different cellular roles, therefore p52/p46Shc and p66Shc functions are individually described.


  • Ras regulation. Upon growth factor stimulation p56Shc physically associate with the activated receptor tyrosine kinases via the SH2 domain and become rapidly and efficiently tyrosine-phosphorylated in three major tyrosine residues present in the CH1 domain (Y239/240, Y317). Tyrosine phosphorylation mediates interactions with the SH2 domain of the Grb2 adaptor protein that is constitutively complexed with Sos, an ubiquitously expressed Ras guanine nucleotide exchange factor. Recruitment of the Grb2/Sos complex by phosphorylated p52/p46Shc proteins results in the membrane relocalization of Sos, an event considered sufficient to induce Ras activation.
  • Growth factors signaling and survival. P52/p46Shc has been shown to function in signaling of many receptors that are themselves tyrosine kinases, such those for epidermal growth factor (EGF), Insulin (I), platelet growth factor (PDGF), nerve growth factor (NGF), hepatocyte growth factor/scatter factor (HGF/SF and ErbB2, but it also signals on receptors associated with cytoplasmic tyrosine kinases such as the antigen T and B cell receptors, and those for the Stem cell factor (SCF) otherwise known as KIT ligand or Steel factor (SLF), granulocyte macrophage colony-stimulating factor (GM-CSF), erythropoietin (EPO) and interleukin IL-2, IL-3, IL-5. In particular, in the interleukin receptors signaling, SHC1, binding to the Grb2-Gab2 complex, also has an essential role in the PI-3K/Akt pathway. It was reported that Shc could regulate c-Myc activation in response to IL-3 stimulation but little is known about mechanism and target genes affected.
  • Signaling by cell adhesion molecules. The role of SHC1 in signaling lastly includes the integrin family and G-protein coupled receptors. Indeed, in endothelial cells, beside the roles in mediating Receptor Tyrosine Kinases signaling, Shc was recently demonstrated contributing to sense shear stress, which is the mechanical force generated by the blood fluid moving along the vascular endothelium. SHC1 exerts a role in all mechanisms described to be responsible for the mechano-transduction signaling that are TRK pathways, cell matrix adhesion through integrins binding and cell-cell adhesion by interaction with cadherins in adherent junctions.
  • Cytoskeleton Organization. MEFs lacking p52/p46Shc exhibit defective cytoskeletal organization and reduced ERK activation when plated on fibronectin (an extracellular matrix protein), a defect that is rescued reintroducing p52/p46Shc.
  • Animal model. SHC1 knock-out is embryonic lethal, infact SHC1 mutants die by E11.5 with evidence of a gross cardiovascular defect.
  • Negative regulation of growth factors signaling. In contrast to p52Shc, overexpression of p66Shc is incapable of transforming mouse fibroblasts, does not induce MAPK activation and has a negative effect on the FOS promoter in an a transactivation assay.
  • ROS production. P66Shc is involved in the intracellular pathway(s) that regulates reactive oxygen species (ROS) metabolism and apoptosis. For this function, p66Shc uses reducing equivalents of the mitochondrial electron-transfer chain through the direct oxidation of cytochrome c forming hydrogen peroxide that in turn induces mitochondrial permeability pore opening and apoptosis.
  • Animal model. P66Shc is a genetic determinant of life span in mammals, as its deletion in mice (p66Shc-/-) results in retarded aging, decreased incidence of aging-associated diseases, such as atherosclerosis, and prolonged life span. p66Shc-generated ROS is implicated in regulation of insulin signaling in the fat tissue, suggesting that intracellular oxidative stress might accelerate aging by favoring fat deposition and increasing the incidence and penetrance of fat-related disorders.
Atlas Image
Schematic description of different contribution of SHC1 proteins in survival and apoptosis. Upon growth factor (GF) stimulation p52Shc binds to activated receptor (RTKs) becomes phosphorylated and binds to Grb2-Sos complex. The translocation of Grab2/SOS complex from the cytosol to the cellular membrane induces Ras activation that in turn leads to MAP kinase/Erk pathway triggering that finally regulates cell proliferation and/or differentiation. Pro-apoptotic signals, instead, induce p66Shc release from a putative inhibitory complex (Tim -Tom mitochondrial import complex) on mitochondria. Activated p66Shc then reduces cytochrome c and generates hydrogen peroxide (H2O2) that leads to permeability transition pore (PTP) opening, mitochondrial swelling, cytochrome c release, caspase activation and apoptosis.


P52Shc protein is highly conserved during evolution accounting homologues already in worms and insects; the longest isoform, p66Shc seems to represent a later specialization of the protein being arisen later in the evolution, infact the first organisms where it can be found are fishes.



The SHC1 genes polymorphisms known in the coding region correspond to Met225Val in the p46 isoform, Met300Val in the p52 isoform and to Met410Val in the p66 isoform. This polymorphism has been associated with a significantly decreased risk for breast cancer, strongly in women diagnosed below the age of 50. The same polymorphism in SHC1 was associated with longevity.

Implicated in

Entity name
Cancers (indirect)
P52/p46 proteins are implicated in cell proliferation and carcinogenesis.
The p52Shc and p46Shc isoforms of Shc are overexpressed or hyper-phosphorylated in many tumor types where known Tyrosine kinases Receptors are constitutively activated.
Constitutively activated p52Shc Human tumor cell lines Constitutively activated receptor
  Vulval carcinoma, Bladder carcinoma, Neuroblastoma Hepatocarcinoma EGFR
  Pancreatic carcinoma PDGFR
  Lung carcinoma ErbB2
  Chronic myeloid Leukaemia Bcr-abl
  Thyroid carcinoma Ret
Recently was demonstrated that SHC1 is a crucial determinant of the Neu/ErbB-2 -TGFb cooperation signaling that promotes breast cancer cell motility and invasion.
The involvement of p66Shc in tumorigenesis is still controversial. Altered levels of p66Shc were reported to be found in some tumors but the results seem contradictory. In the breast cancer cells and primary tumors p66Shc was described to be both over-expressed and down-regulated. Indeed the ablation of p66Shc does not increase spontaneous or induced tumor incidence in mice. P66Shc adaptor protein may have a potential implication in the pathophysiology of aging.


Pubmed IDLast YearTitleAuthors
188383802008p66Shc-generated oxidative signal promotes fat accumulation.Berniakovich I et al
87552471996Not all Shc's roads lead to Ras.Bonfini L et al
103734451999Mechanotransduction in response to shear stress. Roles of receptor tyrosine kinases, integrins, and Shc.Chen KD et al
113699382001Shc signaling in differentiating neural progenitor cells.Conti L et al
84795361993Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation.Egan SE et al
174094132007RaLP, a new member of the Src homology and collagen family, regulates cell migration and tumor growth of metastatic melanomas.Fagiani E et al
120528292002Serine/threonine phosphorylation of ShcA. Regulation of protein-tyrosine phosphatase-pest binding and involvement in insulin signaling.Faisal A et al
176268872007Combinatorial ShcA docking interactions support diversity in tissue morphogenesis.Hardy WR et al
174524442007Analysis of a Shc family adaptor protein, ShcD/Shc4, that associates with muscle-specific kinase.Jones N et al
108096712000The ShcA phosphotyrosine docking protein sensitizes cardiovascular signaling in the mouse embryo.Lai KM et al
186068452008Shc coordinates signals from intercellular junctions and integrins to regulate flow-induced inflammation.Liu Y et al
86282611996Sch proteins are localized on endoplasmic reticulum membranes and are redistributed after tyrosine kinase receptor activation.Lotti LV et al
110880192000Evolution of Shc functions from nematode to human.Luzi L et al
75560901995Signal transduction by the alpha 6 beta 4 integrin: distinct beta 4 subunit sites mediate recruitment of Shc/Grb2 and association with the cytoskeleton of hemidesmosomes.Mainiero F et al
166771032006Apoptosis and aging: role of p66Shc redox protein.Migliaccio E et al
150364212004Variation in the SHC1 gene and longevity in humans.Mooijaart SP et al
183321262008Signaling through ShcA is required for transforming growth factor beta- and Neu/ErbB-2-induced breast cancer cell motility and invasion.Northey JJ et al
93469571997The 66-kDa Shc isoform is a negative regulator of the epidermal growth factor-stimulated mitogen-activated protein kinase pathway.Okada S et al
150788732004The life span determinant p66Shc localizes to mitochondria where it associates with mitochondrial heat shock protein 70 and regulates trans-membrane potential.Orsini F et al
170811132006Regulatory effects of the mitochondrial energetic status on mitochondrial p66Shc.Orsini F et al
87603051996A family of Shc related proteins with conserved PTB, CH1 and SH2 regions.Pelicci G et al
76754491995Constitutive phosphorylation of Shc proteins in human tumors.Pelicci G et al
122423092002The neuron-specific Rai (ShcC) adaptor protein inhibits apoptosis by coupling Ret to the phosphatidylinositol 3-kinase/Akt signaling pathway.Pelicci G et al
82356131993Interaction of Shc with the zeta chain of the T cell receptor upon T cell activation.Ravichandran KS et al
14651351992Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases.Rozakis-Adcock M et al
82234331993Signal transduction by the high-affinity GM-CSF receptor: two distinct cytoplasmic regions of the common beta subunit responsible for different signaling.Sato N et al
81016471993Shc products are substrates of erbB-2 kinase.Segatto O et al
83168351993The function of GRB2 in linking the insulin receptor to Ras signaling pathways.Skolnik EY et al
191649212009Spatial signaling networks converge at the adaptor protein Shc.Sweet DT et al
168292312006Mitochondrial DNA copy number is regulated by cellular proliferation: a role for Ras and p66(Shc).Trinei M et al
119481812002The p66Shc longevity gene is silenced through epigenetic modifications of an alternative promoter.Ventura A et al
153085842004The insulin-like growth factor-1 pathway mediator genes: SHC1 Met300Val shows a protective effect in breast cancer.Wagner K et al
89295411996The adaptor protein Shc couples a class of integrins to the control of cell cycle progression.Wary KK et al
97416271998A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth.Wary KK et al
75164691994Identification of Src, Fyn, and Lyn SH3-binding proteins: implications for a function of SH3 domains.Weng Z et al
157539842005Enhanced expression of p46 Shc in the nucleus and p52 Shc in the cytoplasm of human gastric cancer.Yukimasa S et al
85243911995Structure and ligand recognition of the phosphotyrosine binding domain of Shc.Zhou MM et al

Other Information

Locus ID:

NCBI: 6464
MIM: 600560
HGNC: 10840
Ensembl: ENSG00000160691


dbSNP: 6464
ClinVar: 6464
TCGA: ENSG00000160691


Gene IDTranscript IDUniprot

Expression (GTEx)



PathwaySourceExternal ID
ErbB signaling pathwayKEGGko04012
Focal adhesionKEGGko04510
Natural killer cell mediated cytotoxicityKEGGko04650
Insulin signaling pathwayKEGGko04910
Chronic myeloid leukemiaKEGGko05220
ErbB signaling pathwayKEGGhsa04012
Focal adhesionKEGGhsa04510
Natural killer cell mediated cytotoxicityKEGGhsa04650
Insulin signaling pathwayKEGGhsa04910
Chronic myeloid leukemiaKEGGhsa05220
Chemokine signaling pathwayKEGGko04062
Chemokine signaling pathwayKEGGhsa04062
Neurotrophin signaling pathwayKEGGko04722
Neurotrophin signaling pathwayKEGGhsa04722
Bacterial invasion of epithelial cellsKEGGko05100
Bacterial invasion of epithelial cellsKEGGhsa05100
Estrogen signaling pathwayKEGGhsa04915
Estrogen signaling pathwayKEGGko04915
Prolactin signaling pathwayKEGGhsa04917
Prolactin signaling pathwayKEGGko04917
MicroRNAs in cancerKEGGhsa05206
MicroRNAs in cancerKEGGko05206
Ras signaling pathwayKEGGhsa04014
Metabolism of proteinsREACTOMER-HSA-392499
Unfolded Protein Response (UPR)REACTOMER-HSA-381119
IRE1alpha activates chaperonesREACTOMER-HSA-381070
XBP1(S) activates chaperone genesREACTOMER-HSA-381038
Diseases of signal transductionREACTOMER-HSA-5663202
Signaling by EGFR in CancerREACTOMER-HSA-1643713
Signaling by Ligand-Responsive EGFR Variants in CancerREACTOMER-HSA-5637815
Constitutive Signaling by Ligand-Responsive EGFR Cancer VariantsREACTOMER-HSA-1236382
Signaling by EGFRvIII in CancerREACTOMER-HSA-5637812
Constitutive Signaling by EGFRvIIIREACTOMER-HSA-5637810
Immune SystemREACTOMER-HSA-168256
Adaptive Immune SystemREACTOMER-HSA-1280218
Signaling by the B Cell Receptor (BCR)REACTOMER-HSA-983705
Antigen activates B Cell Receptor (BCR) leading to generation of second messengersREACTOMER-HSA-983695
Innate Immune SystemREACTOMER-HSA-168249
DAP12 interactionsREACTOMER-HSA-2172127
DAP12 signalingREACTOMER-HSA-2424491
RAF/MAP kinase cascadeREACTOMER-HSA-5673001
Fc epsilon receptor (FCERI) signalingREACTOMER-HSA-2454202
FCERI mediated MAPK activationREACTOMER-HSA-2871796
FCERI mediated Ca+2 mobilizationREACTOMER-HSA-2871809
Role of LAT2/NTAL/LAB on calcium mobilizationREACTOMER-HSA-2730905
Cytokine Signaling in Immune systemREACTOMER-HSA-1280215
Signaling by InterleukinsREACTOMER-HSA-449147
Interleukin-2 signalingREACTOMER-HSA-451927
Interleukin receptor SHC signalingREACTOMER-HSA-912526
Interleukin-3, 5 and GM-CSF signalingREACTOMER-HSA-512988
Platelet activation, signaling and aggregationREACTOMER-HSA-76002
GPVI-mediated activation cascadeREACTOMER-HSA-114604
Platelet Aggregation (Plug Formation)REACTOMER-HSA-76009
Integrin alphaIIb beta3 signalingREACTOMER-HSA-354192
Cell surface interactions at the vascular wallREACTOMER-HSA-202733
Tie2 SignalingREACTOMER-HSA-210993
Signal TransductionREACTOMER-HSA-162582
Signaling by EGFRREACTOMER-HSA-177929
GRB2 events in EGFR signalingREACTOMER-HSA-179812
SHC1 events in EGFR signalingREACTOMER-HSA-180336
Signaling by FGFRREACTOMER-HSA-190236
Signaling by FGFR1REACTOMER-HSA-5654736
Downstream signaling of activated FGFR1REACTOMER-HSA-5654687
SHC-mediated cascade:FGFR1REACTOMER-HSA-5654688
Signaling by FGFR2REACTOMER-HSA-5654738
Downstream signaling of activated FGFR2REACTOMER-HSA-5654696
SHC-mediated cascade:FGFR2REACTOMER-HSA-5654699
Signaling by FGFR3REACTOMER-HSA-5654741
Downstream signaling of activated FGFR3REACTOMER-HSA-5654708
SHC-mediated cascade:FGFR3REACTOMER-HSA-5654704
Signaling by FGFR4REACTOMER-HSA-5654743
Downstream signaling of activated FGFR4REACTOMER-HSA-5654716
SHC-mediated cascade:FGFR4REACTOMER-HSA-5654719
Signaling by Insulin receptorREACTOMER-HSA-74752
Insulin receptor signalling cascadeREACTOMER-HSA-74751
IRS-mediated signallingREACTOMER-HSA-112399
SOS-mediated signallingREACTOMER-HSA-112412
Signal attenuationREACTOMER-HSA-74749
Signalling by NGFREACTOMER-HSA-166520
NGF signalling via TRKA from the plasma membraneREACTOMER-HSA-187037
Signalling to ERKsREACTOMER-HSA-187687
Signalling to RASREACTOMER-HSA-167044
Signalling to p38 via RIT and RINREACTOMER-HSA-187706
Prolonged ERK activation eventsREACTOMER-HSA-169893
Frs2-mediated activationREACTOMER-HSA-170968
ARMS-mediated activationREACTOMER-HSA-170984
Signaling by PDGFREACTOMER-HSA-186797
Downstream signal transductionREACTOMER-HSA-186763
Signaling by VEGFREACTOMER-HSA-194138
VEGFR2 mediated cell proliferationREACTOMER-HSA-5218921
Signaling by SCF-KITREACTOMER-HSA-1433557
Signaling by ERBB2REACTOMER-HSA-1227986
SHC1 events in ERBB2 signalingREACTOMER-HSA-1250196
Signaling by ERBB4REACTOMER-HSA-1236394
SHC1 events in ERBB4 signalingREACTOMER-HSA-1250347
MAPK family signaling cascadesREACTOMER-HSA-5683057
MAPK1/MAPK3 signalingREACTOMER-HSA-5684996
Signaling by GPCRREACTOMER-HSA-372790
GPCR downstream signalingREACTOMER-HSA-388396
G-protein beta:gamma signallingREACTOMER-HSA-397795
G beta:gamma signalling through PI3KgammaREACTOMER-HSA-392451
Gastrin-CREB signalling pathway via PKC and MAPKREACTOMER-HSA-881907
Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R)REACTOMER-HSA-2404192
IGF1R signaling cascadeREACTOMER-HSA-2428924
SHC-related events triggered by IGF1RREACTOMER-HSA-2428933
IRS-related events triggered by IGF1RREACTOMER-HSA-2428928
Signaling by LeptinREACTOMER-HSA-2586552
Developmental BiologyREACTOMER-HSA-1266738
Axon guidanceREACTOMER-HSA-422475
NCAM signaling for neurite out-growthREACTOMER-HSA-375165
Phospholipase D signaling pathwayKEGGko04072
Phospholipase D signaling pathwayKEGGhsa04072
EGFR tyrosine kinase inhibitor resistanceKEGGko01521
Endocrine resistanceKEGGko01522
EGFR tyrosine kinase inhibitor resistanceKEGGhsa01521
Endocrine resistanceKEGGhsa01522
RET signalingREACTOMER-HSA-8853659
Breast cancerKEGGko05224
Breast cancerKEGGhsa05224
Signaling by METREACTOMER-HSA-6806834
MET activates RAS signalingREACTOMER-HSA-8851805

Protein levels (Protein atlas)

Not detected


Entity IDNameTypeEvidenceAssociationPKPDPMIDs


Pubmed IDYearTitleCitations
147648972004The role of Shc and insulin-like growth factor 1 receptor in mediating the translocation of estrogen receptor alpha to the plasma membrane.99
171582372007p66Shc/Notch-3 interplay controls self-renewal and hypoxia survival in human stem/progenitor cells of the mammary gland expanded in vitro as mammospheres.79
217784252011Repression of P66Shc expression by SIRT1 contributes to the prevention of hyperglycemia-induced endothelial dysfunction.76
203796142010Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.62
164813272006The mammalian longevity-associated gene product p66shc regulates mitochondrial metabolism.57
119481812002The p66Shc longevity gene is silenced through epigenetic modifications of an alternative promoter.52
147493892004p66SHC promotes apoptosis and antagonizes mitogenic signaling in T cells.43
118774202002Tyrosine phosphorylation of the beta-amyloid precursor protein cytoplasmic tail promotes interaction with Shc.40
179382552008The opposite effects of IL-15 and IL-21 on CLL B cells correlate with differential activation of the JAK/STAT and ERK1/2 pathways.38
198896382010Oscillatory flow-induced proliferation of osteoblast-like cells is mediated by alphavbeta3 and beta1 integrins through synergistic interactions of focal adhesion kinase and Shc with phosphatidylinositol 3-kinase and the Akt/mTOR/p70S6K pathway.37


Lucilla Luzi ; Enrica Migliaccio ; Pier Giuseppe Pelicci

SHC1 (SHC (Src homology 2 domain containing) transforming protein 1)

Atlas Genet Cytogenet Oncol Haematol. 2009-02-01

Online version: