Type |
Details |
Score |
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1233
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
218
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
801
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
821
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1000
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
194
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
799
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1043
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1014
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
232
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
665
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
230
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1358
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
354
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
887
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
209
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1321
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
822
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
162
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
695
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
245
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Franks SE |
Year: |
2016 |
Journal: |
Oncotarget |
Title: |
Unique roles of Akt1 and Akt2 in IGF-IR mediated lung tumorigenesis. |
Volume: |
7 |
Issue: |
3 |
Pages: |
3297-316 |
|
•
•
•
•
•
|
Publication |
First Author: |
Watson KL |
Year: |
2015 |
Journal: |
BMC Cancer |
Title: |
High levels of dietary soy decrease mammary tumor latency and increase incidence in MTB-IGFIR transgenic mice. |
Volume: |
15 |
|
Pages: |
37 |
|
•
•
•
•
•
|
Publication |
First Author: |
Saleh S |
Year: |
2016 |
Journal: |
BMC Cancer |
Title: |
Osteopontin regulates proliferation, apoptosis, and migration of murine claudin-low mammary tumor cells. |
Volume: |
16 |
|
Pages: |
359 |
|
•
•
•
•
•
|
Publication |
First Author: |
Franks SE |
Year: |
2012 |
Journal: |
Oncogene |
Title: |
Transgenic IGF-IR overexpression induces mammary tumors with basal-like characteristics, whereas IGF-IR-independent mammary tumors express a claudin-low gene signature. |
Volume: |
31 |
Issue: |
27 |
Pages: |
3298-309 |
|
•
•
•
•
•
|
Publication |
First Author: |
Tham YK |
Year: |
2018 |
Journal: |
Biochim Biophys Acta |
Title: |
Distinct lipidomic profiles in models of physiological and pathological cardiac remodeling, and potential therapeutic strategies. |
Volume: |
1863 |
Issue: |
3 |
Pages: |
219-234 |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Tg(MMTV-rtTA)1Lach/? Tg(tetO-IGF1R)1Ramo/? |
Background: |
involves: FVB |
Zygosity: |
cx |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Nishimura T |
Year: |
2021 |
Journal: |
Cell Stem Cell |
Title: |
Generation of Functional Organs Using a Cell-Competitive Niche in Intra- and Inter-species Rodent Chimeras. |
Volume: |
28 |
Issue: |
1 |
Pages: |
141-149.e3 |
|
•
•
•
•
•
|
Publication |
First Author: |
Go GW |
Year: |
2014 |
Journal: |
Cell Metab |
Title: |
The combined hyperlipidemia caused by impaired Wnt-LRP6 signaling is reversed by Wnt3a rescue. |
Volume: |
19 |
Issue: |
2 |
Pages: |
209-20 |
|
•
•
•
•
•
|
Publication |
First Author: |
Damsky W |
Year: |
2015 |
Journal: |
Cancer Cell |
Title: |
mTORC1 activation blocks BrafV600E-induced growth arrest but is insufficient for melanoma formation. |
Volume: |
27 |
Issue: |
1 |
Pages: |
41-56 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ohshima-Hosoyama S |
Year: |
2010 |
Journal: |
Biochem Biophys Res Commun |
Title: |
IGF-1 receptor inhibition by picropodophyllin in medulloblastoma. |
Volume: |
399 |
Issue: |
4 |
Pages: |
727-32 |
|
•
•
•
•
•
|
Publication |
First Author: |
Schwartz S |
Year: |
2015 |
Journal: |
Cancer Cell |
Title: |
Feedback suppression of PI3Kα signaling in PTEN-mutated tumors is relieved by selective inhibition of PI3Kβ. |
Volume: |
27 |
Issue: |
1 |
Pages: |
109-22 |
|
•
•
•
•
•
|
Publication |
First Author: |
Yang F |
Year: |
2019 |
Journal: |
EMBO J |
Title: |
GSTZ1-1 Deficiency Activates NRF2/IGF1R Axis in HCC via Accumulation of Oncometabolite Succinylacetone. |
Volume: |
38 |
Issue: |
15 |
Pages: |
e101964 |
|
•
•
•
•
•
|
Publication |
First Author: |
Cai W |
Year: |
2017 |
Journal: |
Nat Commun |
Title: |
Domain-dependent effects of insulin and IGF-1 receptors on signalling and gene expression. |
Volume: |
8 |
|
Pages: |
14892 |
|
•
•
•
•
•
|
Publication |
First Author: |
Masternak MM |
Year: |
2006 |
Journal: |
Exp Gerontol |
Title: |
Caloric restriction and growth hormone receptor knockout: effects on expression of genes involved in insulin action in the heart. |
Volume: |
41 |
Issue: |
4 |
Pages: |
417-29 |
|
•
•
•
•
•
|
Publication |
First Author: |
Aguayo-Mazzucato C |
Year: |
2017 |
Journal: |
Cell Metab |
Title: |
β Cell Aging Markers Have Heterogeneous Distribution and Are Induced by Insulin Resistance. |
Volume: |
25 |
Issue: |
4 |
Pages: |
898-910.e5 |
|
•
•
•
•
•
|
Publication |
First Author: |
Lu TX |
Year: |
2013 |
Journal: |
J Immunol |
Title: |
MiR-223 deficiency increases eosinophil progenitor proliferation. |
Volume: |
190 |
Issue: |
4 |
Pages: |
1576-82 |
|
•
•
•
•
•
|
Publication |
First Author: |
Nguyen TNQ |
Year: |
2022 |
Journal: |
J Hematol Oncol |
Title: |
The regulation of insulin receptor/insulin-like growth factor 1 receptor ratio, an important factor for breast cancer prognosis, by TRIP-Br1. |
Volume: |
15 |
Issue: |
1 |
Pages: |
82 |
|
•
•
•
•
•
|
Publication |
First Author: |
Turvey SJ |
Year: |
2022 |
Journal: |
RSC Med Chem |
Title: |
Recent developments in the structural characterisation of the IR and IGF1R: implications for the design of IR-IGF1R hybrid receptor modulators. |
Volume: |
13 |
Issue: |
4 |
Pages: |
360-374 |
|
•
•
•
•
•
|
Publication |
First Author: |
Okamoto K |
Year: |
2012 |
Journal: |
EMBO J |
Title: |
miR-493 induction during carcinogenesis blocks metastatic settlement of colon cancer cells in liver. |
Volume: |
31 |
Issue: |
7 |
Pages: |
1752-63 |
|
•
•
•
•
•
|
Publication |
First Author: |
Llobet-Navas D |
Year: |
2014 |
Journal: |
Genes Dev |
Title: |
The miR-424(322)/503 cluster orchestrates remodeling of the epithelium in the involuting mammary gland. |
Volume: |
28 |
Issue: |
7 |
Pages: |
765-82 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hu S |
Year: |
2020 |
Journal: |
Brain Res |
Title: |
Knock down of lncRNA H19 promotes axon sprouting and functional recovery after cerebral ischemic stroke. |
Volume: |
1732 |
|
Pages: |
146681 |
|
•
•
•
•
•
|
Publication |
First Author: |
Simon CM |
Year: |
2015 |
Journal: |
Acta Neuropathol |
Title: |
Dysregulated IGFBP5 expression causes axon degeneration and motoneuron loss in diabetic neuropathy. |
Volume: |
130 |
Issue: |
3 |
Pages: |
373-87 |
|
•
•
•
•
•
|
Publication |
First Author: |
Bulatowicz JJ |
Year: |
2022 |
Journal: |
Front Endocrinol (Lausanne) |
Title: |
Activation Versus Inhibition of IGF1R: A Dual Role in Breast Tumorigenesis. |
Volume: |
13 |
|
Pages: |
911079 |
|
•
•
•
•
•
|
Publication |
First Author: |
Yu Y |
Year: |
2023 |
Journal: |
iScience |
Title: |
PTEN phosphatase inhibits metastasis by negatively regulating the Entpd5/IGF1R pathway through ATF6. |
Volume: |
26 |
Issue: |
2 |
Pages: |
106070 |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
559
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
251
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
207
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
264
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
202
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
154
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
268
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
211
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
208
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
216
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
508
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
207
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
155
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
208
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
424
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1064
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Pandini G |
Year: |
2002 |
Journal: |
J Biol Chem |
Title: |
Insulin/insulin-like growth factor I hybrid receptors have different biological characteristics depending on the insulin receptor isoform involved. |
Volume: |
277 |
Issue: |
42 |
Pages: |
39684-95 |
|
•
•
•
•
•
|
Publication |
First Author: |
Slaaby R |
Year: |
2006 |
Journal: |
J Biol Chem |
Title: |
Hybrid receptors formed by insulin receptor (IR) and insulin-like growth factor I receptor (IGF-IR) have low insulin and high IGF-1 affinity irrespective of the IR splice variant. |
Volume: |
281 |
Issue: |
36 |
Pages: |
25869-74 |
|
•
•
•
•
•
|
Publication |
First Author: |
Van Horn DJ |
Year: |
1994 |
Journal: |
J Biol Chem |
Title: |
Direct activation of the phosphatidylinositol 3'-kinase by the insulin receptor. |
Volume: |
269 |
Issue: |
1 |
Pages: |
29-32 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].Tyrosine-protein kinases can transfer a phosphate group from ATP to a tyrosine residue in a protein. These enzymes can be divided into two main groups []:Receptor tyrosine kinases (RTK), which are transmembrane proteins involved in signal transduction; they play key roles in growth, differentiation, metabolism, adhesion, motility, death and oncogenesis []. RTKs are composed of 3 domains: an extracellular domain (binds ligand), a transmembrane (TM) domain, and an intracellular catalytic domain (phosphorylates substrate). The TM domain plays an important role in the dimerisation process necessary for signal transduction []. Cytoplasmic / non-receptor tyrosine kinases, which act as regulatory proteins, playing key roles in cell differentiation, motility, proliferation, and survival. For example, the Src-family of protein-tyrosine kinases [].This entry represents the insulin receptor, as well as related insulin-like receptors. The insulin receptor binds insulin and has a tyrosine-protein kinase activity, and mediates the metabolic functions of insulin. Binding to insulin stimulates the association of the receptor with downstream mediators, including IRS1 and phosphatidylinositol 3'-kinase (PI3K). The insulin receptor can activate PI3K either directly by binding to the p85 regulatory subunit, or indirectly via IRS1. When the insulin receptor is present in a hybrid receptor with IGF1R (insulin growth factor receptor), it binds IGF1 (insulin growth factor 1) [, , ]. |
|
•
•
•
•
•
|
Publication |
First Author: |
Cao C |
Year: |
2021 |
Journal: |
Front Cell Dev Biol |
Title: |
Lack of miR-379/miR-544 Cluster Resists High-Fat Diet-Induced Obesity and Prevents Hepatic Triglyceride Accumulation in Mice. |
Volume: |
9 |
|
Pages: |
720900 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hishiya A |
Year: |
2005 |
Journal: |
Bone |
Title: |
Ataxia telangiectasia mutated (Atm) knockout mice as a model of osteopenia due to impaired bone formation. |
Volume: |
37 |
Issue: |
4 |
Pages: |
497-503 |
|
•
•
•
•
•
|