インスリン受容体インスリン受容体の概要

INSR
PDBに登録されている構造
PDB	オルソログ検索: RCSB PDBe PDBj
PDBのIDコード一覧
	1GAG, 1I44, 1IR3, 1IRK, 1P14, 1RQQ, 2AUH, 2B4S, 2HR7, 3BU3, 3BU5, 3BU6, 3EKK, 3EKN, 3ETA, 3W11, 3W12, 3W13, 3W14, 2MFR, 2Z8C, 4IBM, 4OGA, 4XLV, 4XST, 5E1S, 4ZXB, 5J3H, 5HHW
識別子
記号	INSR, CD220, HHF5, insulin receptor
外部ID	OMIM: 147670 MGI: 96575 HomoloGene: 20090 GeneCards: INSR
遺伝子の位置 (ヒト)
染色体	19番染色体 (ヒト)
終点	7,294,414 bp
遺伝子の位置 (マウス)
染色体	8番染色体 (マウス)
終点	3,329,617 bp
RNA発現パターン
	さらなる参照発現データ
遺伝子オントロジー
分子機能	• キナーゼ活性; • insulin-like growth factor II binding; • transmembrane receptor protein tyrosine kinase activity; • ATP binding; • protein kinase activity; • insulin-like growth factor receptor binding; • insulin receptor substrate binding; • transferase activity; • 血漿タンパク結合; • protein tyrosine kinase activity; • ヌクレオチド結合; • insulin-like growth factor I binding; • GTP binding; • PTB domain binding; • phosphatidylinositol 3-kinase binding; • insulin binding; • insulin-activated receptor activity; • protein domain specific binding; • アミロイドβ結合; • cargo receptor activity; • protein-containing complex binding;
細胞の構成要素	• 膜; • カベオラ; • insulin receptor complex; • エキソソーム; • integral component of membrane; • receptor complex; • 細胞膜; • endosome membrane; • integral component of plasma membrane; • 細胞内; • nuclear envelope; • external side of plasma membrane; • 神経繊維; • nuclear lumen; • dendrite membrane; • neuronal cell body membrane;
生物学的プロセス	• positive regulation of glucose import; • insulin receptor signaling pathway; • positive regulation of protein phosphorylation; • regulation of embryonic development; • positive regulation of developmental growth; • タンパク質リン酸化; • regulation of female gonad development; • animal organ morphogenesis; • transformation of host cell by virus; • positive regulation of mitotic nuclear division; • positive regulation of meiotic cell cycle; • positive regulation of protein kinase B signaling; • positive regulation of glycogen biosynthetic process; • regulation of transcription, DNA-templated; • transmembrane receptor protein tyrosine kinase signaling pathway; • male sex determination; • positive regulation of transcription, DNA-templated; • epidermis development; • cellular response to insulin stimulus; • 自己リン酸化; • positive regulation of respiratory burst; • positive regulation of MAPK cascade; • 膵外分泌発生; • Gタンパク質共役受容体シグナル伝達経路; • 男性生殖腺発生; • リン酸化; • 炭水化物代謝; • positive regulation of DNA replication; • peptidyl-tyrosine autophosphorylation; • activation of protein kinase B activity; • positive regulation of cell migration; • positive regulation of nitric oxide biosynthetic process; • cellular response to growth factor stimulus; • heart morphogenesis; • 副腎発生; • positive regulation of cell population proliferation; • positive regulation of glycolytic process; • activation of protein kinase activity; • シグナル伝達; • glucose homeostasis; • peptidyl-tyrosine phosphorylation; • protein heterotetramerization; • intracellular signal transduction; • 受容体介在性エンドサイトーシス; • 学習; • 記憶; • positive regulation of phosphatidylinositol 3-kinase signaling; • positive regulation of protein-containing complex disassembly; • 解剖学的構造の発生; • dendritic spine maintenance; • amyloid-beta clearance; • neuron projection maintenance;
	出典:Amigo / QuickGO
オルソログ
	3643
	16337
	ENSG00000171105
	ENSMUSG00000005534
	P06213
	P15208
	NM_000208; NM_001079817
	NM_010568; NM_001330056
	NP_000199; NP_001073285
	NP_001316985; NP_034698
	ウィキデータ
閲覧/編集ヒト	閲覧/編集マウス

注釈

^ ただし細胞にグルコースを取り込むトランスポータにも何種類か存在しており、GLUT1やGLUT2のようにインスリンのシグナルとは無関係に細胞外からグルコースを取り込むトランスポータも存在する。逆に、GLUT4のように、インスリンのシグナルが入ると動き出して高効率でグルコースを取り込むトランスポータも存在する。

出典

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000171105 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000005534 - Ensembl, May 2017
^ Human PubMed Reference:
^ Mouse PubMed Reference:
^ ^a ^b “Ligand-induced activation of the insulin receptor: a multi-step process involving structural changes in both the ligand and the receptor”. BioEssays 31 (4): 422–34. (April 2009). doi:10.1002/bies.200800210. PMID 19274663.
^ “The human insulin receptor cDNA: the structural basis for hormone-activated transmembrane signalling”. Cell 40 (4): 747–58. (April 1985). doi:10.1016/0092-8674(85)90334-4. PMID 2859121.
^ “Proinsulin binds with high affinity the insulin receptor isoform A and predominantly activates the mitogenic pathway”. Endocrinology 153 (5): 2152–63. (May 2012). doi:10.1210/en.2011-1843. PMID 22355074.
^ ^a ^b “Insulin receptor isoforms and insulin receptor/insulin-like growth factor receptor hybrids in physiology and disease”. Endocrine Reviews 30 (6): 586–623. (October 2009). doi:10.1210/er.2008-0047. PMID 19752219.
^ “Insight into the molecular basis for the kinetic differences between the two insulin receptor isoforms”. The Biochemical Journal 440 (3): 397–403. (December 2011). doi:10.1042/BJ20110550. PMID 21838706.
^ ^a ^b ^c “Structural resolution of a tandem hormone-binding element in the insulin receptor and its implications for design of peptide agonists”. Proceedings of the National Academy of Sciences of the United States of America 107 (15): 6771–6. (April 2010). Bibcode: 2010PNAS..107.6771S. doi:10.1073/pnas.1001813107. PMC 2872410. PMID 20348418.
^ ^a ^b “Structure of the insulin receptor ectodomain reveals a folded-over conformation”. Nature 443 (7108): 218–21. (September 2006). Bibcode: 2006Natur.443..218M. doi:10.1038/nature05106. PMID 16957736.
^ “Visualization of ligand-induced transmembrane signaling in the full-length human insulin receptor”. The Journal of Cell Biology 217 (5): 1643–1649. (May 2018). doi:10.1083/jcb.201711047. PMID 29453311.
^ ^a ^b ^c “Harmonic oscillator model of the insulin and IGF1 receptors' allosteric binding and activation”. Molecular Systems Biology 5 (5): 243. (Feb 2009). doi:10.1038/msb.2008.78. PMC 2657531. PMID 19225456.
^ ^a ^b “Insulin interactions with its receptors: experimental evidence for negative cooperativity”. Biochemical and Biophysical Research Communications 55 (1): 154–61. (November 1973). doi:10.1016/S0006-291X(73)80072-5. PMID 4361269.
^ Berg, Jeremy M.; Tymoczko, John L.; Stryer, Lubert; Berg, Jeremy M.; Tymoczko, John L.; Stryer, Lubert (2002). Biochemistry (5th ed.). W H Freeman. ISBN 0716730510
^ “Insulin degradation: progress and potential”. Endocrine Reviews 19 (5): 608–24. (October 1998). doi:10.1210/er.19.5.608. PMID 9793760.
^ “Insulin Receptor-Mediated Stimulation Boosts T Cell Immunity during Inflammation and Infection”. Cell Metabolism. (August 2018). doi:10.1016/j.cmet.2018.08.003. PMID 30174303.
^ “The Insulin Receptor Plays a Critical Role in T Cell Function and Adaptive Immunity”. Journal of Immunology 198 (5): 1910–1920. (March 2017). doi:10.4049/jimmunol.1601011. PMID 28115529.
^ “Genotype-phenotype correlation in inherited severe insulin resistance”. Human Molecular Genetics 11 (12): 1465–75. (June 2002). doi:10.1093/hmg/11.12.1465. PMID 12023989.
^ “Membrane glycoprotein PC-1 inhibition of insulin receptor function occurs via direct interaction with the receptor alpha-subunit”. Diabetes 49 (1): 13–9. (January 2000). doi:10.2337/diabetes.49.1.13. PMID 10615944.
^ “Identification of Grb10 as a direct substrate for members of the Src tyrosine kinase family”. Oncogene 19 (25): 2895–903. (June 2000). doi:10.1038/sj.onc.1203616. PMID 10871840.
^ “Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus”. The Journal of Biological Chemistry 271 (15): 8882–6. (April 1996). doi:10.1074/jbc.271.15.8882. PMID 8621530.
^ “Grb-IR: a SH2-domain-containing protein that binds to the insulin receptor and inhibits its function”. Proceedings of the National Academy of Sciences of the United States of America 92 (22): 10287–91. (October 1995). Bibcode: 1995PNAS...9210287L. doi:10.1073/pnas.92.22.10287. PMC 40781. PMID 7479769.
^ “Grb10 interacts differentially with the insulin receptor, insulin-like growth factor I receptor, and epidermal growth factor receptor via the Grb10 Src homology 2 (SH2) domain and a second novel domain located between the pleckstrin homology and SH2 domains”. The Journal of Biological Chemistry 273 (12): 6860–7. (March 1998). doi:10.1074/jbc.273.12.6860. PMID 9506989.
^ “Human GRB-IRbeta/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains”. The Journal of Biological Chemistry 272 (5): 2659–67. (January 1997). doi:10.1074/jbc.272.5.2659. PMID 9006901.
^ “Evidence for an interaction between the insulin receptor and Grb7. A role for two of its binding domains, PIR and SH2”. Oncogene 19 (16): 2052–9. (April 2000). doi:10.1038/sj.onc.1203469. PMID 10803466.
^ “Phosphorylation of Ser307 in insulin receptor substrate-1 blocks interactions with the insulin receptor and inhibits insulin action”. The Journal of Biological Chemistry 277 (2): 1531–7. (January 2002). doi:10.1074/jbc.M101521200. PMID 11606564.
^ “Insulin receptor substrate-2 binds to the insulin receptor through its phosphotyrosine-binding domain and through a newly identified domain comprising amino acids 591-786”. The Journal of Biological Chemistry 271 (11): 5980–3. (March 1996). doi:10.1074/jbc.271.11.5980. PMID 8626379.
^ “Interaction of MAD2 with the carboxyl terminus of the insulin receptor but not with the IGFIR. Evidence for release from the insulin receptor after activation”. The Journal of Biological Chemistry 272 (15): 10035–40. (April 1997). doi:10.1074/jbc.272.15.10035. PMID 9092546.
^ “Insulin induces specific interaction between insulin receptor and protein kinase C delta in primary cultured skeletal muscle”. Molecular Endocrinology 15 (4): 565–74. (April 2001). doi:10.1210/mend.15.4.0612. PMID 11266508.
^ “Differential effects of tumor necrosis factor-alpha on protein kinase C isoforms alpha and delta mediate inhibition of insulin receptor signaling”. Diabetes 51 (6): 1921–30. (June 2002). doi:10.2337/diabetes.51.6.1921. PMID 12031982.
^ “Insulin receptor kinase phosphorylates protein tyrosine phosphatase containing Src homology 2 regions and modulates its PTPase activity in vitro”. Biochemical and Biophysical Research Communications 199 (2): 780–5. (March 1994). doi:10.1006/bbrc.1994.1297. PMID 8135823.
^ “Adapter function of protein-tyrosine phosphatase 1D in insulin receptor/insulin receptor substrate-1 interaction”. The Journal of Biological Chemistry 270 (49): 29189–93. (December 1995). doi:10.1074/jbc.270.49.29189. PMID 7493946.
^ “SH2-Balpha is an insulin-receptor adapter protein and substrate that interacts with the activation loop of the insulin-receptor kinase”. The Biochemical Journal 335 ( Pt 1) (1): 103–9. (October 1998). doi:10.1042/bj3350103. PMC 1219757. PMID 9742218.
^ “Alternative splicing, gene localization, and binding of SH2-B to the insulin receptor kinase domain”. Mammalian Genome 10 (12): 1160–7. (December 1999). doi:10.1007/s003359901183. PMID 10594240.

[前の解説]

[続きの解説]

「インスリン受容体」の続きの解説一覧

[8] ただし細胞にグルコースを取り込むトランスポータにも何種類か存在しており、GLUT1やGLUT2のようにインスリンのシグナルとは無関係に細胞外からグルコースを取り込むトランスポータも存在する。逆に、GLUT4のように、インスリンのシグナルが入ると動き出して高効率でグルコースを取り込むトランスポータも存在する。

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000171105 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000005534 - Ensembl, May 2017

[3] Human PubMed Reference:

[4] Mouse PubMed Reference:

[pmid19274663-5] “Ligand-induced activation of the insulin receptor: a multi-step process involving structural changes in both the ligand and the receptor”. BioEssays 31 (4): 422–34. (April 2009). doi:10.1002/bies.200800210. PMID 19274663.

[pmid2859121-6] “The human insulin receptor cDNA: the structural basis for hormone-activated transmembrane signalling”. Cell 40 (4): 747–58. (April 1985). doi:10.1016/0092-8674(85)90334-4. PMID 2859121.

[pmid22355074-7] “Proinsulin binds with high affinity the insulin receptor isoform A and predominantly activates the mitogenic pathway”. Endocrinology 153 (5): 2152–63. (May 2012). doi:10.1210/en.2011-1843. PMID 22355074.

[pmid19752219-9] “Insulin receptor isoforms and insulin receptor/insulin-like growth factor receptor hybrids in physiology and disease”. Endocrine Reviews 30 (6): 586–623. (October 2009). doi:10.1210/er.2008-0047. PMID 19752219.

[pmid21838706-10] “Insight into the molecular basis for the kinetic differences between the two insulin receptor isoforms”. The Biochemical Journal 440 (3): 397–403. (December 2011). doi:10.1042/BJ20110550. PMID 21838706.

[pmid20348418-11] “Structural resolution of a tandem hormone-binding element in the insulin receptor and its implications for design of peptide agonists”. Proceedings of the National Academy of Sciences of the United States of America 107 (15): 6771–6. (April 2010). Bibcode: 2010PNAS..107.6771S. doi:10.1073/pnas.1001813107. PMC 2872410. PMID 20348418.

[pmid16957736-12] “Structure of the insulin receptor ectodomain reveals a folded-over conformation”. Nature 443 (7108): 218–21. (September 2006). Bibcode: 2006Natur.443..218M. doi:10.1038/nature05106. PMID 16957736.

[pmid29453311-13] “Visualization of ligand-induced transmembrane signaling in the full-length human insulin receptor”. The Journal of Cell Biology 217 (5): 1643–1649. (May 2018). doi:10.1083/jcb.201711047. PMID 29453311.

[pmid19225456-14] “Harmonic oscillator model of the insulin and IGF1 receptors' allosteric binding and activation”. Molecular Systems Biology 5 (5): 243. (Feb 2009). doi:10.1038/msb.2008.78. PMC 2657531. PMID 19225456.

[pmid4361269-15] “Insulin interactions with its receptors: experimental evidence for negative cooperativity”. Biochemical and Biophysical Research Communications 55 (1): 154–61. (November 1973). doi:10.1016/S0006-291X(73)80072-5. PMID 4361269.

[:0-16] Berg, Jeremy M.; Tymoczko, John L.; Stryer, Lubert; Berg, Jeremy M.; Tymoczko, John L.; Stryer, Lubert (2002). Biochemistry (5th ed.). W H Freeman. ISBN 0716730510

[pmid9793760-17] “Insulin degradation: progress and potential”. Endocrine Reviews 19 (5): 608–24. (October 1998). doi:10.1210/er.19.5.608. PMID 9793760.

[:1-18] “Insulin Receptor-Mediated Stimulation Boosts T Cell Immunity during Inflammation and Infection”. Cell Metabolism. (August 2018). doi:10.1016/j.cmet.2018.08.003. PMID 30174303.

[:2-19] “The Insulin Receptor Plays a Critical Role in T Cell Function and Adaptive Immunity”. Journal of Immunology 198 (5): 1910–1920. (March 2017). doi:10.4049/jimmunol.1601011. PMID 28115529.

[pmid12023989-20] “Genotype-phenotype correlation in inherited severe insulin resistance”. Human Molecular Genetics 11 (12): 1465–75. (June 2002). doi:10.1093/hmg/11.12.1465. PMID 12023989.

[pmid10615944-21] “Membrane glycoprotein PC-1 inhibition of insulin receptor function occurs via direct interaction with the receptor alpha-subunit”. Diabetes 49 (1): 13–9. (January 2000). doi:10.2337/diabetes.49.1.13. PMID 10615944.

[pmid10871840-22] “Identification of Grb10 as a direct substrate for members of the Src tyrosine kinase family”. Oncogene 19 (25): 2895–903. (June 2000). doi:10.1038/sj.onc.1203616. PMID 10871840.

[pmid8621530-23] “Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus”. The Journal of Biological Chemistry 271 (15): 8882–6. (April 1996). doi:10.1074/jbc.271.15.8882. PMID 8621530.

[pmid7479769-24] “Grb-IR: a SH2-domain-containing protein that binds to the insulin receptor and inhibits its function”. Proceedings of the National Academy of Sciences of the United States of America 92 (22): 10287–91. (October 1995). Bibcode: 1995PNAS...9210287L. doi:10.1073/pnas.92.22.10287. PMC 40781. PMID 7479769.

[pmid9506989-25] “Grb10 interacts differentially with the insulin receptor, insulin-like growth factor I receptor, and epidermal growth factor receptor via the Grb10 Src homology 2 (SH2) domain and a second novel domain located between the pleckstrin homology and SH2 domains”. The Journal of Biological Chemistry 273 (12): 6860–7. (March 1998). doi:10.1074/jbc.273.12.6860. PMID 9506989.

[pmid9006901-26] “Human GRB-IRbeta/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains”. The Journal of Biological Chemistry 272 (5): 2659–67. (January 1997). doi:10.1074/jbc.272.5.2659. PMID 9006901.

[pmid10803466-27] “Evidence for an interaction between the insulin receptor and Grb7. A role for two of its binding domains, PIR and SH2”. Oncogene 19 (16): 2052–9. (April 2000). doi:10.1038/sj.onc.1203469. PMID 10803466.

[pmid11606564-28] “Phosphorylation of Ser307 in insulin receptor substrate-1 blocks interactions with the insulin receptor and inhibits insulin action”. The Journal of Biological Chemistry 277 (2): 1531–7. (January 2002). doi:10.1074/jbc.M101521200. PMID 11606564.

[pmid8626379-29] “Insulin receptor substrate-2 binds to the insulin receptor through its phosphotyrosine-binding domain and through a newly identified domain comprising amino acids 591-786”. The Journal of Biological Chemistry 271 (11): 5980–3. (March 1996). doi:10.1074/jbc.271.11.5980. PMID 8626379.

[pmid9092546-30] “Interaction of MAD2 with the carboxyl terminus of the insulin receptor but not with the IGFIR. Evidence for release from the insulin receptor after activation”. The Journal of Biological Chemistry 272 (15): 10035–40. (April 1997). doi:10.1074/jbc.272.15.10035. PMID 9092546.

[pmid11266508-31] “Insulin induces specific interaction between insulin receptor and protein kinase C delta in primary cultured skeletal muscle”. Molecular Endocrinology 15 (4): 565–74. (April 2001). doi:10.1210/mend.15.4.0612. PMID 11266508.

[pmid12031982-32] “Differential effects of tumor necrosis factor-alpha on protein kinase C isoforms alpha and delta mediate inhibition of insulin receptor signaling”. Diabetes 51 (6): 1921–30. (June 2002). doi:10.2337/diabetes.51.6.1921. PMID 12031982.

[pmid8135823-33] “Insulin receptor kinase phosphorylates protein tyrosine phosphatase containing Src homology 2 regions and modulates its PTPase activity in vitro”. Biochemical and Biophysical Research Communications 199 (2): 780–5. (March 1994). doi:10.1006/bbrc.1994.1297. PMID 8135823.

[pmid7493946-34] “Adapter function of protein-tyrosine phosphatase 1D in insulin receptor/insulin receptor substrate-1 interaction”. The Journal of Biological Chemistry 270 (49): 29189–93. (December 1995). doi:10.1074/jbc.270.49.29189. PMID 7493946.

[pmid9742218-35] “SH2-Balpha is an insulin-receptor adapter protein and substrate that interacts with the activation loop of the insulin-receptor kinase”. The Biochemical Journal 335 ( Pt 1) (1): 103–9. (October 1998). doi:10.1042/bj3350103. PMC 1219757. PMID 9742218.

[pmid10594240-36] “Alternative splicing, gene localization, and binding of SH2-B to the insulin receptor kinase domain”. Mammalian Genome 10 (12): 1160–7. (December 1999). doi:10.1007/s003359901183. PMID 10594240.

[1]

[2]

[3]

[4]

インスリン受容体 インスリン受容体の概要

インスリン受容体

急上昇のことば

「インスリン受容体」の関連用語

インスリン受容体インスリン受容体の概要