The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested target is correctly identified as human SHC1, also called ShcA/SHCA, encoding SHC-transforming protein 1 (UniProt P29353). The literature’s three ShcA isoforms—p46Shc, p52Shc, and p66Shc—and its PTB/CH1/SH2 domain organization match the supplied UniProt annotation. This target is distinct from human SHC2/ShcB, SHC3/ShcC, and SHC4/ShcD and from similarly named nonhuman genes such as C. elegans shc-3. No evidence requiring a stop for gene-symbol ambiguity was found. (ahmed2017insightsintothe pages 4-5, ahmed2017insightsintothe pages 1-4, wills2016…shcdeviance pages 14-17)
SHC1 is principally a nonenzymatic phosphotyrosine adaptor/scaffold. It has no established catalytic reaction or enzymatic substrate. Instead, it recognizes phosphorylated receptors and signaling proteins through its PTB and SH2 domains, is itself phosphorylated on CH1 tyrosines, and creates docking sites for GRB2 and other effectors. Its best-established function is coupling activated receptor tyrosine kinases (RTKs), integrins, and selected immune/cytokine receptors to temporally controlled GRB2–SOS–RAS–RAF–MEK–ERK signaling. p66Shc additionally functions in oxidative-stress and mitochondrial/ER-contact-site biology. (wills2016…shcdeviance pages 17-21, ahmed2017insightsintothe pages 4-5, wills2016…shcdeviance pages 14-17)
| Annotation area | Evidence-based functional annotation | Evidence strength / status |
|---|---|---|
| Identity | Human SHC1 (ShcA/SHCA), UniProt P29353 is the nonenzymatic phosphotyrosine-signaling adaptor specified in the query. It is distinct from human SHC2/ShcB, SHC3/ShcC, and SHC4/ShcD, and from similarly named nonhuman shc genes. The literature’s ShcA architecture and three isoforms align with the supplied UniProt identity. (ahmed2017insightsintothe pages 4-5, ahmed2017insightsintothe pages 1-4, wills2016…shcdeviance pages 14-17) | Verified target match; no conflicting same-symbol human protein was identified. |
| Isoforms | SHC1 produces p46Shc, p52Shc, and p66Shc. p46 and p52 arise through alternative translation initiation, whereas p66 is produced from a distinct transcript and carries an additional 110-aa N-terminal extension containing CH2. (ahmed2017insightsintothe pages 4-5, ahmed2017insightsintothe pages 1-4, wills2016…shcdeviance pages 14-17) | Established molecular biology; isoforms can have opposing biological effects. |
| Architecture | Shared organization is PTB–CH1–SH2; p66 additionally has an N-terminal CH2 region. The PTB domain preferentially recognizes receptor NPXpY contexts, while SH2 recognizes other phosphotyrosine motifs. CH1 contains the principal phosphorylated docking residues Tyr239/Tyr240 and Tyr317 (p52 numbering), which recruit GRB2. (wills2016…shcdeviance pages 17-21, ahmed2017insightsintothe pages 4-5, wills2016…shcdeviance pages 14-17) | Strong structural and biochemical support; the supplied InterPro PTB/PID, PH-like, and SH2 annotations are concordant. |
| Primary biochemical role | SHC1 is an adaptor/scaffold, not an enzyme: it has no demonstrated catalytic reaction or substrate turnover. Its primary role is to bind activated receptors or other phosphotyrosine-containing proteins, become phosphorylated, and assemble signaling complexes. (ahmed2017insightsintothe pages 4-5, ahmed2017insightsintothe pages 1-4, wills2016…shcdeviance pages 14-17) | Core functional annotation; “substrate specificity” is therefore inapplicable except as phosphopeptide-binding specificity. |
| Canonical RTK–RAS mechanism | Following activation of EGFR/ERBB or another RTK, SHC1 is recruited through PTB/SH2 interactions and phosphorylated in CH1. GRB2’s SH2 domain binds phosphorylated SHC1; GRB2-associated SOS activates RAS-GDP→RAS-GTP, initiating RAF–MEK–ERK signaling. Live-cell analysis found a biphasic role for p52Shc: during the first <10 min, it increased membrane docking sites for GRB2–SOS and amplified RAS activity; later, cytoplasmic SHC–GRB2 complexes sequestered GRB2 and helped terminate RAS activation. DOI: https://doi.org/10.2142/biophysico.bppb-v18.001 (yoshizawa2021biphasicspatiotemporalregulation pages 1-2) | Strong mechanistic evidence in cultured cells; timing and output depend on receptor, ligand, cell type, and feedback state. |
| p66Shc redox role | Oxidative stress induces Ser36 phosphorylation by PKCβ/JNK, conformational regulation and mitochondrial redistribution. In the mitochondrial intermembrane-space model, p66Shc interacts with cytochrome c through a redox region containing 132-EEW-134, promotes H₂O₂ production and mitochondrial permeability, and favors apoptosis. Historical p66Shc-knockout mice reportedly lived about 30% longer than wild-type littermates, although this should not be interpreted as a demonstrated human longevity effect. (wills2016…shcdeviance pages 44-47, lebiedzinskaarciszewska2024distributionofthe pages 1-2) | Established stress-response model, but localization and whether p66Shc should be classified as a direct redox enzyme remain context-dependent. |
| Localization | Basally, SHC1 isoforms are predominantly cytosolic and ER-associated; receptor stimulation recruits p46/p52 to the plasma membrane and receptor/endosomal complexes. p46 also has reported mitochondrial-matrix localization. A 2024 fractionation study found substantial p66Shc at mitochondria-associated ER membranes (MAM) rather than exclusively inside mitochondria: in control HepG2 cells, p46 and p66 contributed 25.175% and 24.054% of total ShcA, respectively; p66 signal fell about 50% at 0.5 µg/mL trypsin and became undetectable at 2 µg/mL, before mitochondrial markers were disrupted. Published 29 November 2024; DOI: https://doi.org/10.3390/ijms252312835 (lebiedzinskaarciszewska2024distributionofthe pages 9-11, lebiedzinskaarciszewska2024distributionofthe pages 1-2) | Direct biochemical fractionation in HepG2 cells and mouse liver; results refine—not fully negate—the smaller stress-induced mitochondrial pool. |
| 2024 glioblastoma findings | TCGA/GTEx-based analyses associated elevated SHC1/p66Shc with worse survival, while 72-h p66Shc siRNA in U87 cells reduced proliferation and migration, induced apoptosis, and altered mitochondrial ROS/potential readouts. The prognostic model used nine mitochondria-related genes, and multivariable analysis included 111 patients. Published May 2024; DOI: https://doi.org/10.1038/s41598-024-62083-2 (peng2024themitochondriarelatedgene pages 2-3, peng2024themitochondriarelatedgene pages 9-10) | Preliminary biomarker/target evidence, not a clinically validated diagnostic, prognostic assay, or approved SHC1-directed therapy; substantial reliance on retrospective datasets and cell lines. |
| 2024 clear-cell renal carcinoma findings | A multi-database study reported higher SHC1 expression in ccRCC and associations with poorer survival, immune infiltration/escape, and predicted immunotherapy response; protein findings were checked in paired material from only nine patients and in renal cell lines. Published August 2024; DOI: https://doi.org/10.1038/s41598-024-70897-3 | Preliminary translational association, not clinical implementation; small experimental validation set and mainly retrospective/bioinformatic evidence. |
| 2024 non-obstructive azoospermia findings | SHC1 and FGFR1 were selected as immune/oxidative-stress hub genes; SHC1 was enriched in testicular endothelial cells and was elevated in NOA tissue by RT-PCR and immunoblotting. ROC analyses reported AUCs >0.8; the two-gene analysis predicted 24 transcription factors, 82 miRNAs, and 111 potential drugs. Published 26 September 2024; DOI: https://doi.org/10.3389/fendo.2024.1356959 (pan2024identificationandvalidation pages 1-2, pan2024identificationandvalidation pages 10-13) | Exploratory biomarker discovery only—not a validated NOA diagnostic or treatment. Dataset reuse, feature-selection procedures, and limited tissue validation require prospective replication. |
Table: Concise annotation of human SHC1/P29353 integrating molecular mechanism, localization, quantitative evidence, and 2024 translational studies. Emerging disease associations are explicitly separated from clinically implemented uses.
The supplied identity is internally consistent:
The literature recognizes four vertebrate Shc paralogs: ShcA/SHC1, ShcB/SHC2, ShcC/SHC3, and ShcD/SHC4. SHC1 is the broadly expressed, canonical RTK adaptor discussed here; results concerning SHC2–4 or nonhuman shc genes were not treated as evidence for human P29353. (ahmed2017insightsintothe pages 1-4, wills2016…shcdeviance pages 14-17, wills2016…shcdeviance pages 149-152)
SHC1 produces three major protein forms. p46Shc and p52Shc arise through alternative translation initiation, whereas p66Shc is produced from a distinct transcript and has an additional approximately 110-amino-acid N-terminal region. The shorter proteins principally mediate receptor-proximal mitogenic signaling, while p66Shc has additional oxidative-stress functions and may oppose mitogenic signaling in some contexts. (ahmed2017insightsintothe pages 4-5, ahmed2017insightsintothe pages 1-4, wills2016…shcdeviance pages 14-17)
The shared core is PTB–CH1–SH2; p66Shc additionally contains an N-terminal CH2 region. This agrees with the supplied InterPro annotations for a Shc-like PID/PTB domain, PH-like fold, and SH2 domain. The “CEP152/SHC-transforming” label should not be interpreted as making SHC1 a centrosomal CEP152-family protein; the experimentally informative modules are its Shc-like PTB/PID, CH regions, and SH2 domain.
The PTB domain preferentially recognizes phosphorylated NPXpY-type motifs and can also interact with phosphoinositides, supporting membrane recruitment. The SH2 domain binds a different class of phosphotyrosine-containing sequences. This dual recognition system enables SHC1 to bind many activated RTKs and associated phosphoproteins. The central CH1 region contains conserved Tyr239/Tyr240 and Tyr317 in p52 numbering; phosphorylation converts these sites into docking motifs, especially for GRB2. (wills2016…shcdeviance pages 17-21, ahmed2017insightsintothe pages 4-5, wills2016…shcdeviance pages 14-17)
SHC1 is not known to catalyze a chemical reaction. Consequently, enzyme substrate specificity and transporter cargo are not applicable. Its biochemical specificity is instead interaction specificity:
This is better described as a dynamic molecular scaffold than as a passive bridge. Quantitative EGF-network work showed successive SHC1 interaction waves: an early GRB2-dependent mitogenic/survival network, followed by AKT-dependent Ser29 phosphorylation and PTPN12 recruitment, and then delayed complexes implicated in cytoskeletal remodeling, trafficking, morphogenesis, and termination. Thus SHC1 helps route signaling information over time rather than merely switching a pathway on. (yoshizawa2021biphasicspatiotemporalregulation pages 1-2, wills2016…shcdeviance pages 21-24)
The most firmly established pathway is:
growth factor → RTK dimerization/autophosphorylation → SHC1 PTB/SH2 recruitment → SHC1 Tyr239/Tyr240/Tyr317 phosphorylation → GRB2 binding → SOS recruitment → RAS-GDP to RAS-GTP exchange → RAF → MEK → ERK.
GRB2’s SH2 domain recognizes phosphorylated SHC1, while its SH3 domains associate with the SOS guanine-nucleotide exchange factor. SOS activates membrane-bound RAS, which initiates the RAF–MEK–ERK kinase cascade controlling proliferation, differentiation, survival, and cell-state transitions. SHC1 can therefore amplify receptor output by adding GRB2–SOS docking sites beyond those present on the receptor itself. (wills2016…shcdeviance pages 17-21, ahmed2017insightsintothe pages 4-5, yoshizawa2021biphasicspatiotemporalregulation pages 1-2)
Live-cell single-molecule work in heregulin-stimulated MCF7 cells revealed a biphasic mechanism. During the first <10 minutes, p52Shc increased membrane docking sites for GRB2–SOS and amplified RAS activity. Later, cytoplasmic SHC–GRB2 complexes sequestered GRB2 away from the membrane and helped terminate RAS activation despite persistent receptor/SHC behavior. This supports an expert interpretation of SHC1 as a controller of signaling amplitude and duration, not simply a positive pathway component. The study was published online January 8, 2021: https://doi.org/10.2142/biophysico.bppb-v18.001. (yoshizawa2021biphasicspatiotemporalregulation pages 1-2)
SHC1-dependent receptor complexes can also engage PI3K–AKT, directly or through proteins such as GAB adaptors, but this connection is more receptor- and cell-context-dependent than the canonical GRB2–SOS–RAS pathway. Other reported outputs include cytoskeletal remodeling, migration, receptor trafficking, STAT signaling, and PLCγ/PKC-related responses. Phosphatases including PTPN12/PTP-PEST, PTEN, PP2A, and PTPε can reduce SHC1 phosphorylation or SHC1–GRB2 signaling and contribute to pathway termination. (wills2016…shcdeviance pages 21-24, wills2016…shcdeviance pages 40-44)
SHC1 also integrates extracellular-matrix adhesion with growth-factor signaling. Several integrins recruit SHC1 through associated Src-family kinases; SHC1 Tyr317 phosphorylation then recruits GRB2 and activates RAS–MAPK. In T-cell signaling, p52Shc can associate with phospho-CD3 and ZAP-70, linking antigen-receptor activation to RAS/MAPK and Rac responses. These mechanisms explain how SHC1 coordinates biochemical signals with adhesion and cellular context. (wills2016…shcdeviance pages 44-47, wills2016…shcdeviance pages 40-44)
SHC1 is primarily cytosolic and ER-associated under basal conditions. Only a small membrane-associated pool is expected without stimulation; growth-factor exposure recruits p46/p52Shc to activated receptors at the plasma membrane and subsequently to receptor-containing endosomal complexes. One literature synthesis estimated that approximately 5% of p52Shc is membrane-associated basally, followed by redistribution toward the cell periphery after stimulation. (wills2016…shcdeviance pages 17-21, lebiedzinskaarciszewska2024distributionofthe pages 1-2)
p46Shc has also been reported in the mitochondrial matrix, where it may regulate ACAA2 and lipid oxidation, and in hepatocyte nuclei during proliferation and hepatocellular-carcinoma development. These isoform-specific localizations indicate that “SHC1 localization” cannot be represented by one fixed compartment. (ahmed2017insightsintothe pages 4-5, lebiedzinskaarciszewska2024distributionofthe pages 1-2)
The classical stress model proposes that oxidative stress induces p66Shc Ser36 phosphorylation by PKCβ or JNK, followed by conformational regulation, Pin1-dependent targeting, and redistribution to mitochondria. In the mitochondrial intermembrane-space model, p66Shc interacts with cytochrome c through a redox region containing residues 132-EEW-134, promotes hydrogen-peroxide production, increases mitochondrial permeability, and favors apoptosis. Selective p66Shc deletion was historically reported to extend mouse lifespan by about 30%, although that mouse result does not establish an equivalent effect in humans. (wills2016…shcdeviance pages 44-47, lebiedzinskaarciszewska2024distributionofthe pages 1-2)
A 2024 study refined this localization model using differential fractionation and controlled proteolysis in HepG2 cells and mouse liver. The authors found that a substantial p66Shc pool assigned to “crude mitochondria” was actually associated with mitochondria-associated ER membranes (MAM). In control HepG2 cells, p46 and p66 represented 25.175% and 24.054% of total ShcA, respectively, while p52 was dominant. In crude mitochondrial fractions, p66Shc signal fell by approximately 50% after 0.5 µg/mL trypsin and was undetectable after 2 µg/mL, before protected mitochondrial markers were disrupted. Even after H₂O₂ treatment, most recovered p66Shc behaved more like a MAM-associated pool than an intramitochondrial protein. Published November 29, 2024: https://doi.org/10.3390/ijms252312835. (lebiedzinskaarciszewska2024distributionofthe pages 9-11, lebiedzinskaarciszewska2024distributionofthe pages 1-2)
The most defensible current interpretation is therefore that p66Shc is mainly cytosolic/ER/MAM-associated, with a smaller or condition-dependent mitochondrial pool. Fractionation sensitivity, soluble versus membrane-protein susceptibility to protease, cell type, and stress protocol can explain some discrepancies across studies. (lebiedzinskaarciszewska2024distributionofthe pages 9-11)
The highest-confidence functions are:
Broad associations with cancer, aging, inflammation, metabolism, and neurodegeneration are plausible consequences of these proximal mechanisms, but they should not replace the more precise functional annotation above. Open Targets, for example, lists SHC1 associations with cancer, inflammatory bowel disease/Crohn disease, neurodegenerative disease, and leukocyte-count phenotypes; these are evidence aggregations rather than proof that SHC1 is a clinically actionable driver in every listed condition. (OpenTargets Search: -SHC1)
A May 2024 Scientific Reports study developed a nine-gene mitochondria-related prognostic model and examined SHC1/p66Shc in glioblastoma. TCGA-based analyses associated higher SHC1/p66Shc expression with shorter overall survival, progression-free interval, and disease-specific survival. The multivariable analysis included 111 patients. In U87 cells, 72-hour p66Shc siRNA treatment reduced proliferation and migration, increased apoptosis, and altered mitochondrial ROS and membrane-potential-related readouts. DOI: https://doi.org/10.1038/s41598-024-62083-2. (peng2024themitochondriarelatedgene pages 2-3, peng2024themitochondriarelatedgene pages 9-10)
This is mechanistically suggestive but not clinical validation. The work relies substantially on retrospective datasets and a limited cell-line system; the prognostic model, SHC1 assay, and p66Shc targeting strategy require independent prospective cohorts, isoform-specific human-tissue validation, and in-vivo efficacy and safety studies.
An August 2024 Scientific Reports study reported higher SHC1 RNA and protein in clear-cell renal-cell carcinoma, associations with poorer survival, and correlations with immune infiltration, immune escape, and predicted immunotherapy response. Experimental protein validation used paired tissues from only nine patients, plus renal cell lines. DOI: https://doi.org/10.1038/s41598-024-70897-3.
The study supports SHC1 as a candidate prognostic/immunological biomarker, but not as a validated clinical test. Most evidence was retrospective and bioinformatic, and the tissue-validation cohort was too small to establish generalizable diagnostic thresholds or treatment-selection utility.
A study published September 26, 2024 combined GEO datasets, WGCNA, machine learning, protein-interaction analysis, single-cell RNA sequencing, RT-PCR, and immunoblotting. SHC1 and FGFR1 emerged as immune/oxidative-stress-associated candidate biomarkers; SHC1 was enriched in testicular endothelial cells and elevated in non-obstructive azoospermia tissue. ROC analyses yielded AUCs >0.8. The computational network contained 24 transcription factors, 82 miRNAs, and 111 predicted drugs. DOI: https://doi.org/10.3389/fendo.2024.1356959. (pan2024identificationandvalidation pages 1-2, pan2024identificationandvalidation pages 10-13)
These findings remain exploratory. The predicted drugs are not SHC1 therapies, and the AUCs derive from selected retrospective expression datasets rather than prospective clinical diagnosis. The authors’ finding is best viewed as a hypothesis about endothelial oxidative/immune dysregulation in impaired spermatogenesis.
No evidence retrieved here establishes an approved SHC1-directed drug, a routine clinical SHC1 assay, or a validated SHC1-based treatment-selection algorithm. Present applications are primarily research uses: pathway-state measurement, phosphoproteomics, receptor-signaling models, cancer biomarker discovery, oxidative-stress studies, and experimental perturbation of p66Shc. Quercetin and other compounds have been investigated as indirect modulators of Rac1/p66Shc-associated ROS signaling, but such results do not demonstrate selective SHC1 engagement or clinical efficacy.
Human SHC1/P29353 is best annotated as a multidomain, noncatalytic phosphotyrosine adaptor and temporal signaling scaffold. Its central physiological role is to translate activated receptor and adhesion signals into organized protein complexes, especially the GRB2–SOS–RAS–RAF–MEK–ERK pathway. p46/p52 primarily perform receptor-proximal signal relay, whereas p66 adds an oxidative-stress module involving ER/MAM and condition-dependent mitochondrial localization, ROS generation, and apoptosis. Recent 2024 research has sharpened the p66 localization model and identified candidate disease-biomarker roles, but SHC1 currently remains a research target rather than an established clinical biomarker or directly actionable therapeutic target.
References
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(peng2024themitochondriarelatedgene pages 2-3): Gang Peng, Yabo Feng, Xiangyu Wang, Weicheng Huang, and Yang Li. The mitochondria-related gene risk mode revealed p66shc as a prognostic mitochondria-related gene of glioblastoma. Scientific Reports, May 2024. URL: https://doi.org/10.1038/s41598-024-62083-2, doi:10.1038/s41598-024-62083-2. This article has 5 citations and is from a peer-reviewed journal.
(peng2024themitochondriarelatedgene pages 9-10): Gang Peng, Yabo Feng, Xiangyu Wang, Weicheng Huang, and Yang Li. The mitochondria-related gene risk mode revealed p66shc as a prognostic mitochondria-related gene of glioblastoma. Scientific Reports, May 2024. URL: https://doi.org/10.1038/s41598-024-62083-2, doi:10.1038/s41598-024-62083-2. This article has 5 citations and is from a peer-reviewed journal.
(pan2024identificationandvalidation pages 1-2): Yang Pan, Xiangyu Chen, Hang Zhou, Mingming Xu, Yuezheng Li, Qihua Wang, Zhunan Xu, Congzhe Ren, Li Liu, and Xiaoqiang Liu. Identification and validation of shc1 and fgfr1 as novel immune-related oxidative stress biomarkers of non-obstructive azoospermia. Frontiers in Endocrinology, Sep 2024. URL: https://doi.org/10.3389/fendo.2024.1356959, doi:10.3389/fendo.2024.1356959. This article has 3 citations.
(pan2024identificationandvalidation pages 10-13): Yang Pan, Xiangyu Chen, Hang Zhou, Mingming Xu, Yuezheng Li, Qihua Wang, Zhunan Xu, Congzhe Ren, Li Liu, and Xiaoqiang Liu. Identification and validation of shc1 and fgfr1 as novel immune-related oxidative stress biomarkers of non-obstructive azoospermia. Frontiers in Endocrinology, Sep 2024. URL: https://doi.org/10.3389/fendo.2024.1356959, doi:10.3389/fendo.2024.1356959. This article has 3 citations.
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(OpenTargets Search: -SHC1): Open Targets Query (-SHC1, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.