RAT:IRS1

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Species (Taxon ID)	Rattus norvegicus (Rat). (taxon:10116)
Gene Name(s)	Irs1 ( synonyms: Irs-1 )
Protein Name(s)	Insulin receptor substrate 1 IRS-1 pp185
External Links
UniProt Identifier	IRS1_RAT
UniProt Accessions	P35570,
EMBL	X58375,
PIR	S16948,
RefSeq	NP_037101.1,
IntAct	P35570,
Pfam	PF02174, PF00169,

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes
	GO:0005829	cytosol		IDA: Inferred from Direct Assay		C	Source: RGD
	GO:0005899	insulin receptor complex		IMP: Inferred from Mutant Phenotype		C	Source: UniProtKB
	GO:0005792	microsome		ISS: Inferred from Sequence or Structural Similarity		C	Source: UniProtKB
	GO:0005634	nucleus		ISS: Inferred from Sequence or Structural Similarity		C	Source: UniProtKB
	GO:0005158	insulin receptor binding		ISS: Inferred from Sequence or Structural Similarity		F	Source: UniProtKB
	GO:0005010	insulin-like growth factor receptor activity		IMP: Inferred from Mutant Phenotype		F	Source: RGD
	GO:0005159	insulin-like growth factor receptor binding		ISS: Inferred from Sequence or Structural Similarity		F	Source: UniProtKB
	GO:0043548	phosphoinositide 3-kinase binding		IDA: Inferred from Direct Assay		F	Source: UniProtKB
	GO:0005080	protein kinase C binding		IPI: Inferred from Physical Interaction		F	Source: UniProtKB
	GO:0042169	SH2 domain binding		IPI: Inferred from Physical Interaction		F	Source: UniProtKB
	GO:0005069	transmembrane receptor protein tyrosine kin...		IMP: Inferred from Mutant Phenotype		F	Source: UniProtKB
	GO:0048009	insulin-like growth factor receptor signali...		ISS: Inferred from Sequence or Structural Similarity		P	Source: UniProtKB
	GO:0046627	negative regulation of insulin receptor sig...		IMP: Inferred from Mutant Phenotype		P	Source: UniProtKB
	GO:0046628	positive regulation of insulin receptor sig...		IMP: Inferred from Mutant Phenotype		P	Source: UniProtKB
	GO:0043552	positive regulation of phosphoinositide 3-k...		IDA: Inferred from Direct Assay		P	Source: UniProtKB
	GO:0051291	protein heterooligomerization		IDA: Inferred from Direct Assay		P	Source: RGD
	GO:0043434	response to peptide hormone stimulus		IDA: Inferred from Direct Assay		P	Source: UniProtKB
	GO:0002053	positive regulation of mesenchymal cell proliferation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063795	P
	GO:0004871	signal transducer activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0807	F
	GO:0005010	insulin-like growth factor receptor activity	PMID:15272025^[1]	IMP: Inferred from Mutant Phenotype		F
	GO:0005068	transmembrane receptor protein tyrosine kinase adaptor activity	PMID:18285345^[2]	IMP: Inferred from Mutant Phenotype		F
	GO:0005080	protein kinase C binding	PMID:18285345^[2]	IPI: Inferred from Physical Interaction	UniProtKB:P28867	F
	GO:0005158	insulin receptor binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR002404	F
	GO:0005158	insulin receptor binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000304895	F
	GO:0005158	insulin receptor binding	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P35568	F
	GO:0005158	insulin receptor binding	PMID:12850498^[3]	IMP: Inferred from Mutant Phenotype		F
	GO:0005159	insulin-like growth factor receptor binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000304895	F
	GO:0005159	insulin-like growth factor receptor binding	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P35568	F
	GO:0005159	insulin-like growth factor receptor binding	PMID:15272025^[1]	IPI: Inferred from Physical Interaction	RGD:2869	F
	GO:0005515	protein binding	PMID:11018022^[4]	IPI: Inferred from Physical Interaction	UniProtKB:Q8VDD9	F
	GO:0005515	protein binding	PMID:11278339^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q63787	F
	GO:0005515	protein binding	PMID:16574739^[6]	IPI: Inferred from Physical Interaction	RGD:3395	F
	GO:0005515	protein binding	PMID:17965023^[7]	IPI: Inferred from Physical Interaction	UniProtKB:Q13625-2	F
	GO:0005515	protein binding	PMID:20144759^[8]	IPI: Inferred from Physical Interaction	UniProtKB:P19525	F
	GO:0005515	protein binding	PMID:20144759^[8]	IPI: Inferred from Physical Interaction	UniProtKB:Q03963	F
	GO:0005515	protein binding	PMID:9295312^[9]	IPI: Inferred from Physical Interaction	UniProtKB:O14983	F
	GO:0005515	protein binding	PMID:9295312^[9]	IPI: Inferred from Physical Interaction	UniProtKB:P11507-1	F
	GO:0005515	protein binding	PMID:9295312^[9]	IPI: Inferred from Physical Interaction	UniProtKB:P11507-2	F
	GO:0005515	protein binding	PMID:9295312^[9]	IPI: Inferred from Physical Interaction	UniProtKB:Q64578	F
	GO:0005634	nucleus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063795	C
	GO:0005634	nucleus	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P35569	C
	GO:0005737	cytoplasm	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063795	C
	GO:0005737	cytoplasm	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P35569	C
	GO:0005792	microsome	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063795	C
	GO:0005792	microsome	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P35569	C
	GO:0005792	microsome	PMID:16445997^[10]	IDA: Inferred from Direct Assay		C
	GO:0005829	cytosol	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000304895	C
	GO:0005829	cytosol	PMID:16445997^[10]	IDA: Inferred from Direct Assay		C
	GO:0005829	cytosol	Reactome:REACT_911	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063795	C
	GO:0005886	plasma membrane	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000304895	C
	GO:0005886	plasma membrane	PMID:16445997^[10]	IDA: Inferred from Direct Assay		C
	GO:0005899	insulin receptor complex	PMID:15069075^[11]	IMP: Inferred from Mutant Phenotype		C
	GO:0005901	caveola	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000304895	C
	GO:0007165	signal transduction	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0807	P
	GO:0007169	transmembrane receptor protein tyrosine kinase signaling pathway	PMID:18285345^[2]	IMP: Inferred from Mutant Phenotype		P
	GO:0008286	insulin receptor signaling pathway	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000304895	P
	GO:0008286	insulin receptor signaling pathway	PMID:17925406^[12]	IDA: Inferred from Direct Assay		P
	GO:0010468	regulation of gene expression	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063795	P
	GO:0010907	positive regulation of glucose metabolic process	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000304895	P
	GO:0014065	phosphatidylinositol 3-kinase cascade	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000304895	P
	GO:0016042	lipid catabolic process	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063795	P
	GO:0019901	protein kinase binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063795	F
	GO:0019901	protein kinase binding	PMID:15701573^[13]	IPI: Inferred from Physical Interaction	RGD:2939	F
	GO:0019904	protein domain specific binding	PMID:12891559^[14]	IPI: Inferred from Physical Interaction	RGD:619758	F
	GO:0030335	positive regulation of cell migration	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063795	P
	GO:0030879	mammary gland development	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063795	P
	GO:0032000	positive regulation of fatty acid beta-oxidation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000304895	P
	GO:0032868	response to insulin stimulus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000304895	P
	GO:0032869	cellular response to insulin stimulus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063795	P
	GO:0032869	cellular response to insulin stimulus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000304895	P
	GO:0042169	SH2 domain binding	PMID:8491186^[15]	IPI: Inferred from Physical Interaction	UniProtKB:P62993	F
	GO:0042327	positive regulation of phosphorylation	PMID:12435589^[16]	IDA: Inferred from Direct Assay		P
	GO:0043434	response to peptide hormone stimulus	PMID:9295312^[9]	IDA: Inferred from Direct Assay		P
	GO:0043548	phosphatidylinositol 3-kinase binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063795	F
	GO:0043548	phosphatidylinositol 3-kinase binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000304895	F
	GO:0043548	phosphatidylinositol 3-kinase binding	PMID:12850498^[3]	IMP: Inferred from Mutant Phenotype		F
	GO:0043548	phosphatidylinositol 3-kinase binding	PMID:12891559^[14]	IPI: Inferred from Physical Interaction	RGD:3329	F
	GO:0043548	phosphatidylinositol 3-kinase binding	PMID:1380456^[17]	IDA: Inferred from Direct Assay		F
	GO:0043552	positive regulation of phosphatidylinositol 3-kinase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063795	P
	GO:0043552	positive regulation of phosphatidylinositol 3-kinase activity	PMID:1380456^[17]	IDA: Inferred from Direct Assay		P
	GO:0045725	positive regulation of glycogen biosynthetic process	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000304895	P
	GO:0046326	positive regulation of glucose import	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000304895	P
	GO:0046627	negative regulation of insulin receptor signaling pathway	PMID:15069075^[11]	IMP: Inferred from Mutant Phenotype		P
	GO:0046628	positive regulation of insulin receptor signaling pathway	PMID:18285345^[2]	IMP: Inferred from Mutant Phenotype		P
	GO:0046676	negative regulation of insulin secretion	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000304895	P
	GO:0046676	negative regulation of insulin secretion	PMID:12435589^[16]	IMP: Inferred from Mutant Phenotype		P
	GO:0048009	insulin-like growth factor receptor signaling pathway	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000304895	P
	GO:0048009	insulin-like growth factor receptor signaling pathway	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P35568	P
	GO:0048009	insulin-like growth factor receptor signaling pathway	PMID:15272025^[1]	IMP: Inferred from Mutant Phenotype		P
	GO:0051291	protein heterooligomerization	PMID:15272025^[1]	IDA: Inferred from Direct Assay		P
	GO:0070094	positive regulation of glucagon secretion	PMID:12435589^[16]	IMP: Inferred from Mutant Phenotype		P
	GO:0090275	negative regulation of somatostatin secretion	PMID:12435589^[16]	IMP: Inferred from Mutant Phenotype		P
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Hayashi K et al. (2004) Insulin receptor substrate-1/SHP-2 interaction, a phenotype-dependent switching machinery of insulin-like growth factor-I signaling in vascular smooth muscle cells. J Biol Chem 279: 40807-18 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Waraich RS et al. (2008) Phosphorylation of Ser357 of rat insulin receptor substrate-1 mediates adverse effects of protein kinase C-delta on insulin action in skeletal muscle cells. J Biol Chem 283: 11226-33 PubMed GONUTS page
↑ ^3.0 ^3.1 Hirata AE et al. (2003) Modulation of IR/PTP1B interaction and downstream signaling in insulin sensitive tissues of MSG-rats. Life Sci 73: 1369-81 PubMed GONUTS page
↑ Farhang-Fallah J et al. (2000) Cloning and characterization of PHIP, a novel insulin receptor substrate-1 pleckstrin homology domain interacting protein. J Biol Chem 275: 40492-7 PubMed GONUTS page
↑ Liu YF et al. (2001) Insulin stimulates PKCzeta -mediated phosphorylation of insulin receptor substrate-1 (IRS-1). A self-attenuated mechanism to negatively regulate the function of IRS proteins. J Biol Chem 276: 14459-65 PubMed GONUTS page
↑ Nawaratne R et al. (2006) Regulation of insulin receptor substrate 1 pleckstrin homology domain by protein kinase C: role of serine 24 phosphorylation. Mol Endocrinol 20: 1838-52 PubMed GONUTS page
↑ Hakuno F et al. (2007) 53BP2S, interacting with insulin receptor substrates, modulates insulin signaling. J Biol Chem 282: 37747-58 PubMed GONUTS page
↑ ^8.0 ^8.1 Nakamura T et al. (2010) Double-stranded RNA-dependent protein kinase links pathogen sensing with stress and metabolic homeostasis. Cell 140: 338-48 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 ^9.4 Algenstaedt P et al. (1997) Insulin receptor substrate proteins create a link between the tyrosine phosphorylation cascade and the Ca2+-ATPases in muscle and heart. J Biol Chem 272: 23696-702 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 Villar M et al. (2006) Altered subcellular distribution of IRS-1 and IRS-3 is associated with defective Akt activation and GLUT4 translocation in insulin-resistant old rat adipocytes. Biochim Biophys Acta 1763: 197-206 PubMed GONUTS page
↑ ^11.0 ^11.1 Moeschel K et al. (2004) Protein kinase C-zeta-induced phosphorylation of Ser318 in insulin receptor substrate-1 (IRS-1) attenuates the interaction with the insulin receptor and the tyrosine phosphorylation of IRS-1. J Biol Chem 279: 25157-63 PubMed GONUTS page
↑ Jensen M et al. (2007) Activation of the insulin receptor by insulin and a synthetic peptide leads to divergent metabolic and mitogenic signaling and responses. J Biol Chem 282: 35179-86 PubMed GONUTS page
↑ Johansen T et al. (2005) Reduction of adiposity with prolonged growth hormone treatment in old obese rats: effects on glucose handling and early insulin signaling. Growth Horm IGF Res 15: 55-63 PubMed GONUTS page
↑ ^14.0 ^14.1 Khamzina L et al. (2003) Insulin signaling through insulin receptor substrate 1 and 2 in normal liver development. Gastroenterology 125: 572-85 PubMed GONUTS page
↑ Skolnik EY et al. (1993) The SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS1 and Shc: implications for insulin control of ras signalling. EMBO J 12: 1929-36 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 Araujo EP et al. (2002) Blockade of IRS1 in isolated rat pancreatic islets improves glucose-induced insulin secretion. FEBS Lett 531: 437-42 PubMed GONUTS page
↑ ^17.0 ^17.1 Backer JM et al. (1992) Phosphatidylinositol 3'-kinase is activated by association with IRS-1 during insulin stimulation. EMBO J 11: 3469-79 PubMed GONUTS page

[PMID:15272025-0] 1.0 ^1.1 ^1.2 ^1.3 Hayashi K et al. (2004) Insulin receptor substrate-1/SHP-2 interaction, a phenotype-dependent switching machinery of insulin-like growth factor-I signaling in vascular smooth muscle cells. J Biol Chem 279: 40807-18 PubMed GONUTS page

[PMID:18285345-1] 2.0 ^2.1 ^2.2 ^2.3 Waraich RS et al. (2008) Phosphorylation of Ser357 of rat insulin receptor substrate-1 mediates adverse effects of protein kinase C-delta on insulin action in skeletal muscle cells. J Biol Chem 283: 11226-33 PubMed GONUTS page

[PMID:12850498-2] 3.0 ^3.1 Hirata AE et al. (2003) Modulation of IR/PTP1B interaction and downstream signaling in insulin sensitive tissues of MSG-rats. Life Sci 73: 1369-81 PubMed GONUTS page

[PMID:11018022-3] Farhang-Fallah J et al. (2000) Cloning and characterization of PHIP, a novel insulin receptor substrate-1 pleckstrin homology domain interacting protein. J Biol Chem 275: 40492-7 PubMed GONUTS page

[PMID:11278339-4] Liu YF et al. (2001) Insulin stimulates PKCzeta -mediated phosphorylation of insulin receptor substrate-1 (IRS-1). A self-attenuated mechanism to negatively regulate the function of IRS proteins. J Biol Chem 276: 14459-65 PubMed GONUTS page

[PMID:16574739-5] Nawaratne R et al. (2006) Regulation of insulin receptor substrate 1 pleckstrin homology domain by protein kinase C: role of serine 24 phosphorylation. Mol Endocrinol 20: 1838-52 PubMed GONUTS page

[PMID:17965023-6] Hakuno F et al. (2007) 53BP2S, interacting with insulin receptor substrates, modulates insulin signaling. J Biol Chem 282: 37747-58 PubMed GONUTS page

[PMID:20144759-7] 8.0 ^8.1 Nakamura T et al. (2010) Double-stranded RNA-dependent protein kinase links pathogen sensing with stress and metabolic homeostasis. Cell 140: 338-48 PubMed GONUTS page

[PMID:9295312-8] 9.0 ^9.1 ^9.2 ^9.3 ^9.4 Algenstaedt P et al. (1997) Insulin receptor substrate proteins create a link between the tyrosine phosphorylation cascade and the Ca2+-ATPases in muscle and heart. J Biol Chem 272: 23696-702 PubMed GONUTS page

[PMID:16445997-9] 10.0 ^10.1 ^10.2 Villar M et al. (2006) Altered subcellular distribution of IRS-1 and IRS-3 is associated with defective Akt activation and GLUT4 translocation in insulin-resistant old rat adipocytes. Biochim Biophys Acta 1763: 197-206 PubMed GONUTS page

[PMID:15069075-10] 11.0 ^11.1 Moeschel K et al. (2004) Protein kinase C-zeta-induced phosphorylation of Ser318 in insulin receptor substrate-1 (IRS-1) attenuates the interaction with the insulin receptor and the tyrosine phosphorylation of IRS-1. J Biol Chem 279: 25157-63 PubMed GONUTS page

[PMID:17925406-11] Jensen M et al. (2007) Activation of the insulin receptor by insulin and a synthetic peptide leads to divergent metabolic and mitogenic signaling and responses. J Biol Chem 282: 35179-86 PubMed GONUTS page

[PMID:15701573-12] Johansen T et al. (2005) Reduction of adiposity with prolonged growth hormone treatment in old obese rats: effects on glucose handling and early insulin signaling. Growth Horm IGF Res 15: 55-63 PubMed GONUTS page

[PMID:12891559-13] 14.0 ^14.1 Khamzina L et al. (2003) Insulin signaling through insulin receptor substrate 1 and 2 in normal liver development. Gastroenterology 125: 572-85 PubMed GONUTS page

[PMID:8491186-14] Skolnik EY et al. (1993) The SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS1 and Shc: implications for insulin control of ras signalling. EMBO J 12: 1929-36 PubMed GONUTS page

[PMID:12435589-15] 16.0 ^16.1 ^16.2 ^16.3 Araujo EP et al. (2002) Blockade of IRS1 in isolated rat pancreatic islets improves glucose-induced insulin secretion. FEBS Lett 531: 437-42 PubMed GONUTS page

[PMID:1380456-16] 17.0 ^17.1 Backer JM et al. (1992) Phosphatidylinositol 3'-kinase is activated by association with IRS-1 during insulin stimulation. EMBO J 11: 3469-79 PubMed GONUTS page

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RAT:IRS1

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