INSR
entrez
3643
canonical
uniprot
P06213
canonical
ensembl
ENSG00000171105
resolver
ensp
ENSP00000303830
resolver
ensp
ENSP00000342838
resolver
ensp
ENSP00000574849
resolver
ensp
ENSP00000574850
resolver
genesymbol
INSR
resolver
hgnc
HGNC:6091
resolver
uniprot
Q17RW0
resolver
uniprot
Q59H98
resolver
uniprot
Q9UCB7
resolver
uniprot
Q9UCB8
resolver
uniprot
Q9UCB9
resolver
uniprot_entry
INSR_HUMAN
resolver
uniprot_sec
Q17RW0
resolver
uniprot_sec
Q59H98
resolver
uniprot_sec
Q9UCB7
resolver
uniprot_sec
Q9UCB8
resolver
uniprot_sec
Q9UCB9
resolver
activity_regulation
ACTIVITY REGULATION: Activated in response to insulin. Autophosphorylation activates the kinase activity. PTPN1, PTPRE and PTPRF dephosphorylate important tyrosine residues, thereby reducing INSR activity. Inhibited by ENPP1. GRB10 and GRB14 inhibit the catalytic activity of the INSR, they block access of substrates to the activated receptor. SOCS1 and SOCS3 act as negative regulators of INSR activity, they bind to the activated INRS and interfere with the phosphorylation of INSR substrates. {ECO:0000269|PubMed:10615944, ECO:0000269|PubMed:11598120, ECO:0000269|PubMed:11726652, ECO:0000269|PubMed:12493740, ECO:0000269|PubMed:2211730}.
uniprot
proteins
amino_acid_sequence
MATGGRRGAAAAPLLVAVAALLLGAAGHLYPGEVCPGMDIRNNLTRLHELENCSVIEGHLQILLMFKTRPEDFRDLSFPKLIMITDYLLLFRVYGLESLKDLFPNLTVIRGSRLFFNYALVIFEMVHLKELGLYNLMNITRGSVRIEKNNELCYLATIDWSRILDSVEDNYIVLNKDDNEECGDICPGTAKGKTNCPATVINGQFVERCWTHSHCQKVCPTICKSHGCTAEGLCCHSECLGNCSQPDDPTKCVACRNFYLDGRCVETCPPPYYHFQDWRCVNFSFCQDLHHKCKNSRRQGCHQYVIHNNKCIPECPSGYTMNSSNLLCTPCLGPCPKVCHLLEGEKTIDSVTSAQELRGCTVINGSLIINIRGGNNLAAELEANLGLIEEISGYLKIRRSYALVSLSFFRKLRLIRGETLEIGNYSFYALDNQNLRQLWDWSKHNLTITQGKLFFHYNPKLCLSEIHKMEEVSGTKGRQERNDIALKTNGDQASCENELLKFSYIRTSFDKILLRWEPYWPPDFRDLLGFMLFYKEAPYQNVTEFDGQDACGSNSWTVVDIDPPLRSNDPKSQNHPGWLMRGLKPWTQYAIFVKTLVTFSDERRTYGAKSDIIYVQTDATNPSVPLDPISVSNSSSQIILKWKPPSDPNGNITHYLVFWERQAEDSELFELDYCLKGLKLPSRTWSPPFESEDSQKHNQSEYEDSAGECCSCPKTDSQILKELEESSFRKTFEDYLHNVVFVPRKTSSGTGAEDPRPSRKRRSLGDVGNVTVAVPTVAAFPNTSSTSVPTSPEEHRPFEKVVNKESLVISGLRHFTGYRIELQACNQDTPEERCSVAAYVSARTMPEAKADDIVGPVTHEIFENNVVHLMWQEPKEPNGLIVLYEVSYRRYGDEELHLCVSRKHFALERGCRLRGLSPGNYSVRIRATSLAGNGSWTEPTYFYVTDYLDVPSNIAKIIIGPLIFVFLFSVVIGSIYLFLRKRQPDGPLGPLYASSNPEYLSASDVFPCSVYVPDEWEVSREKITLLRELGQGSFGMVYEGNARDIIKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVMELMAHGDLKSYLRSLRPEAENNPGRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDGGYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLLKDDLHPSFPEVSFFHSEENKAPESEELEMEFEDMENVPLDRSSHCQREEAGGRDGGSSLGFKRSYEEHIPYTHMNGGKKNGRILTLPRSNPS
uniprot
proteins
disease_involvement
DISEASE: Rabson-Mendenhall syndrome (RMS) [MIM:262190]: Severe insulin resistance syndrome characterized by insulin-resistant diabetes mellitus with pineal hyperplasia and somatic abnormalities. Typical features include coarse, senile-appearing facies, dental and skin abnormalities, abdominal distension, and phallic enlargement. Inheritance is autosomal recessive. {ECO:0000269|PubMed:10443650, ECO:0000269|PubMed:12023989, ECO:0000269|PubMed:17201797, ECO:0000269|PubMed:2121734, ECO:0000269|PubMed:2365819, ECO:0000269|PubMed:28765322, ECO:0000269|PubMed:8314008}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Leprechaunism (LEPRCH) [MIM:246200]: Represents the most severe form of insulin resistance syndrome, characterized by intrauterine and postnatal growth retardation and death in early infancy. Inheritance is autosomal recessive. {ECO:0000269|PubMed:12023989, ECO:0000269|PubMed:12538626, ECO:0000269|PubMed:12970295, ECO:0000269|PubMed:1607067, ECO:0000269|PubMed:1730625, ECO:0000269|PubMed:22768670, ECO:0000269|PubMed:2365819, ECO:0000269|PubMed:24498630, ECO:0000269|PubMed:2479553, ECO:0000269|PubMed:2834824, ECO:0000269|PubMed:28765322, ECO:0000269|PubMed:7538143, ECO:0000269|PubMed:7815442, ECO:0000269|PubMed:8188715, ECO:0000269|PubMed:8326490, ECO:0000269|PubMed:8419945, ECO:0000269|PubMed:8636294, ECO:0000269|PubMed:9249867, ECO:0000269|PubMed:9299395, ECO:0000269|PubMed:9703342}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Type 2 diabetes mellitus (T2D) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:1470163, ECO:0000269|PubMed:1607076, ECO:0000269|PubMed:7657032}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Hyperinsulinemic hypoglycemia, familial, 5 (HHF5) [MIM:609968]: A form of hyperinsulinemic hypoglycemia, a clinically and genetically heterogeneous disorder characterized by inappropriate insulin secretion from the pancreatic beta-cells in the presence of low blood glucose levels. HHF5 clinical features include loss of consciousness due to hypoglycemia and hypoglycemic seizures. HHF5 inheritance is autosomal dominant. {ECO:0000269|PubMed:15161766}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Insulin-resistant diabetes mellitus with acanthosis nigricans type A (IRAN type A) [MIM:610549]: Characterized by the association of severe insulin resistance (manifested by marked hyperinsulinemia and a failure to respond to exogenous insulin) with the skin lesion acanthosis nigricans and ovarian hyperandrogenism in adolescent female subjects. Women frequently present with hirsutism, acne, amenorrhea or oligomenorrhea, and virilization. This syndrome is different from the type B that has been demonstrated to be secondary to the presence of circulating autoantibodies against the insulin receptor. {ECO:0000269|PubMed:10733238, ECO:0000269|PubMed:11260230, ECO:0000269|PubMed:12107746, ECO:0000269|PubMed:12970295, ECO:0000269|PubMed:1563582, ECO:0000269|PubMed:1963473, ECO:0000269|PubMed:2002058, ECO:0000269|PubMed:2168397, ECO:0000269|PubMed:2365819, ECO:0000269|PubMed:2544998, ECO:0000269|PubMed:28765322, ECO:0000269|PubMed:3283938, ECO:0000269|PubMed:8243830, ECO:0000269|PubMed:8288049, ECO:0000269|PubMed:8314008, ECO:0000269|PubMed:8388389, ECO:0000269|PubMed:9175790}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
FUNCTION: Receptor tyrosine kinase which mediates the pleiotropic actions of insulin. Binding of insulin leads to phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins serve as docking proteins for other signaling proteins that contain Src-homology-2 domains (SH2 domain) that specifically recognize different phosphotyrosine residues, including the p85 regulatory subunit of PI3K and SHP2. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway, which is responsible for most of the metabolic actions of insulin, and the Ras-MAPK pathway, which regulates expression of some genes and cooperates with the PI3K pathway to control cell growth and differentiation. Binding of the SH2 domains of PI3K to phosphotyrosines on IRS1 leads to the activation of PI3K and the generation of phosphatidylinositol-(3, 4, 5)-triphosphate (PIP3), a lipid second messenger, which activates several PIP3-dependent serine/threonine kinases, such as PDPK1 and subsequently AKT/PKB. The net effect of this pathway is to produce a translocation of the glucose transporter SLC2A4/GLUT4 from cytoplasmic vesicles to the cell membrane to facilitate glucose transport. Moreover, upon insulin stimulation, activated AKT/PKB is responsible for: anti-apoptotic effect of insulin by inducing phosphorylation of BAD; regulates the expression of gluconeogenic and lipogenic enzymes by controlling the activity of the winged helix or forkhead (FOX) class of transcription factors. Another pathway regulated by PI3K-AKT/PKB activation is mTORC1 signaling pathway which regulates cell growth and metabolism and integrates signals from insulin. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 thereby activating mTORC1 pathway. The Ras/RAF/MAP2K/MAPK pathway is mainly involved in mediating cell growth, survival and cellular differentiation of insulin. Phosphorylated IRS1 recruits GRB2/SOS complex, which triggers the activation of the Ras/RAF/MAP2K/MAPK pathway. In addition to binding insulin, the insulin receptor can bind insulin-like growth factors (IGFI and IGFII). Isoform Short has a higher affinity for IGFII binding. When present in a hybrid receptor with IGF1R, binds IGF1. PubMed:12138094 shows that hybrid receptors composed of IGF1R and INSR isoform Long are activated with a high affinity by IGF1, with low affinity by IGF2 and not significantly activated by insulin, and that hybrid receptors composed of IGF1R and INSR isoform Short are activated by IGF1, IGF2 and insulin. In contrast, PubMed:16831875 shows that hybrid receptors composed of IGF1R and INSR isoform Long and hybrid receptors composed of IGF1R and INSR isoform Short have similar binding characteristics, both bind IGF1 and have a low affinity for insulin. In adipocytes, inhibits lipolysis (By similarity). {ECO:0000250|UniProtKB:P15208, ECO:0000269|PubMed:12138094, ECO:0000269|PubMed:16314505, ECO:0000269|PubMed:16831875, ECO:0000269|PubMed:8257688, ECO:0000269|PubMed:8276809, ECO:0000269|PubMed:8452530, ECO:0000269|PubMed:9428692}.
uniprot
proteins
mass_dalton
156333
uniprot
proteins
mutagenesis
MUTAGEN 462; /note="C->A: Does not affect S-nitrosylation."; /evidence="ECO:0000269|PubMed:38056462"; MUTAGEN 825; /note="C->A: Does not affect S-nitrosylation."; /evidence="ECO:0000269|PubMed:38056462"; MUTAGEN 834; /note="C->A: Does not affect S-nitrosylation."; /evidence="ECO:0000269|PubMed:38056462"; MUTAGEN 991; /note="L->A: Reduces interaction with IRS1 but has no effect on interaction with SHC1."; /evidence="ECO:0000269|PubMed:7559478"; MUTAGEN 992; /note="Y->A: Reduces interaction with IRS1 but has no effect on interaction with SHC1."; /evidence="ECO:0000269|PubMed:7559478"; MUTAGEN 996..997; /note="NP->AA: Abolishes interaction with IRS1. Severely disrupts, but does not abolish interaction with SHC1."; /evidence="ECO:0000269|PubMed:7559478"; MUTAGEN 996; /note="N->A: Abolishes interaction with IRS1 and significantly reduces interaction with SHC1. Has no effect on interaction with PIK3R1."; /evidence="ECO:0000269|PubMed:7537849, ECO:0000269|PubMed:7559478"; MUTAGEN 997; /note="P->A: Abolishes interaction with IRS1 and significantly reduces interaction with SHC1. Has no effect on interaction with PIK3R1."; /evidence="ECO:0000269|PubMed:7537849, ECO:0000269|PubMed:7559478"; MUTAGEN 998; /note="E->A: Does not affect interaction with IRS1, SHC1 or PIK3R1."; /evidence="ECO:0000269|PubMed:7537849"; MUTAGEN 999; /note="Y->E: Abolishes interaction with IRS1 and SHC1."; /evidence="ECO:0000269|PubMed:2842060, ECO:0000269|PubMed:7537849, ECO:0000269|PubMed:7559478, ECO:0000269|PubMed:9428692"; MUTAGEN 999; /note="Y->F: Has no effect on insulin-stimulated autophosphorylation, but inhibits the biological activity of the receptor. Abolishes interaction with IRS1 and almost completely prevents interaction with SHC1. Has no effect on interaction with PIK3R1. Abolishes interaction with STAT5B."; /evidence="ECO:0000269|PubMed:2842060, ECO:0000269|PubMed:7537849, ECO:0000269|PubMed:7559478, ECO:0000269|PubMed:9428692"; MUTAGEN 1000; /note="L->A,R: Severely reduces interaction with SHC1. Has no effect on interaction with IRS1."; /evidence="ECO:0000269|PubMed:7559478"; MUTAGEN 1002; /note="A->D: Reduces interaction with IRS1 but has no effect on interaction with SHC1."; /evidence="ECO:0000269|PubMed:7559478"; MUTAGEN 1011; /note="Y->A: Increases kinase activity."; /evidence="ECO:0000269|PubMed:12707268"; MUTAGEN 1057; /note="K->A: Abolishes the kinase activity and abolishes interaction with IRS1, SHC1, GRB7 and PIK3R1."; /evidence="ECO:0000269|PubMed:10803466, ECO:0000269|PubMed:3101064, ECO:0000269|PubMed:7537849"; MUTAGEN 1057; /note="K->M,R: Abolishes the kinase activity."; /evidence="ECO:0000269|PubMed:10803466, ECO:0000269|PubMed:3101064, ECO:0000269|PubMed:7537849"; MUTAGEN 1079; /note="K->R: Increased cell surface stability."; /evidence="ECO:0000269|PubMed:27577745"; MUTAGEN 1083; /note="C->A: Reduced S-nitrosylation by BLVRB, leading to increased receptor tyrosine kinase activity."; /evidence="ECO:0000269|PubMed:38056462"; MUTAGEN 1159; /note="D->N: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:11598120"; MUTAGEN 1163; /note="R->Q: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:11598120"; MUTAGEN 1189; /note="Y->F: Reduced interaction with GRB7."; /evidence="ECO:0000269|PubMed:10803466"; MUTAGEN 1190; /note="Y->F: Strongly reduced interaction with GRB7."; /evidence="ECO:0000269|PubMed:10803466
uniprot
proteins
post_translational_modification
PTM: After being transported from the endoplasmic reticulum to the Golgi apparatus, the single glycosylated precursor is further glycosylated and then cleaved, followed by its transport to the plasma membrane. {ECO:0000269|PubMed:1472036, ECO:0000269|PubMed:16894147, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:23302862, ECO:0000269|PubMed:2983222}.; PTM: Autophosphorylated on tyrosine residues in response to insulin (PubMed:14690593, PubMed:16246733, PubMed:16271887, PubMed:18278056, PubMed:18767165, PubMed:3166375, PubMed:9312016). Phosphorylation of Tyr-999 is required for binding to IRS1, SHC1 and STAT5B (PubMed:14690593, PubMed:16246733, PubMed:16271887, PubMed:18278056, PubMed:18767165, PubMed:3166375, PubMed:9312016). Dephosphorylated by PTPRE at Tyr-999, Tyr-1185, Tyr-1189 and Tyr-1190 (PubMed:14690593, PubMed:16246733, PubMed:16271887, PubMed:18278056, PubMed:18767165, PubMed:3166375, PubMed:9312016). May also be phosphorylated at Tyr-1185 and Tyr-1190 by mTORC2 (PubMed:26584640). Dephosphorylated by PTPRF and PTPN1 (PubMed:8995282). Dephosphorylated by PTPN2; down-regulates insulin-induced signaling (PubMed:10734133, PubMed:12612081). Dephosphorylation at Tyr-1189 and Tyr-1190 requires the SH2/SH3 adapter protein NCK1, probably to recruit its interaction partner PTPN1 (PubMed:21707536). {ECO:0000269|PubMed:10734133, ECO:0000269|PubMed:12612081, ECO:0000269|PubMed:14690593, ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887, ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165, ECO:0000269|PubMed:21707536, ECO:0000269|PubMed:26584640, ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:8995282, ECO:0000269|PubMed:9312016}.; PTM: S-nitrosylation at Cys-1083 by BLVRB inhibits the receptor tyrosine kinase, thereby inhibiting insulin signaling. {ECO:0000269|PubMed:38056462}.; PTM: Ubiquitinated by MARCHF1; leading to degradation thereby reducing surface INSR expression. {ECO:0000269|PubMed:27577745}.
uniprot
proteins
protein_family
Insulin receptor subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10207053
uniprot
proteins
pubmed
10443650
uniprot
proteins
pubmed
10615944
uniprot
proteins
pubmed
10733238
uniprot
proteins
pubmed
10734133
uniprot
proteins
pubmed
10803466
uniprot
proteins
pubmed
11124964
uniprot
proteins
pubmed
11260230
uniprot
proteins
pubmed
11374898
uniprot
proteins
pubmed
11598120
uniprot
proteins
pubmed
11726652
uniprot
proteins
pubmed
12023989
uniprot
proteins
pubmed
12107746
uniprot
proteins
pubmed
12138094
uniprot
proteins
pubmed
12493740
uniprot
proteins
pubmed
12538626
uniprot
proteins
pubmed
12612081
uniprot
proteins
pubmed
12707268
uniprot
proteins
pubmed
12970295
uniprot
proteins
pubmed
1321605
uniprot
proteins
pubmed
14690593
uniprot
proteins
pubmed
1470163
uniprot
proteins
pubmed
1472036
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15161766
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1563582
uniprot
proteins
pubmed
15738637
uniprot
proteins
pubmed
1607067
uniprot
proteins
pubmed
1607076
uniprot
proteins
pubmed
16127460
uniprot
proteins
pubmed
16246733
uniprot
proteins
pubmed
16271887
uniprot
proteins
pubmed
16314505
uniprot
proteins
pubmed
16493415
uniprot
proteins
pubmed
16831875
uniprot
proteins
pubmed
16894147
uniprot
proteins
pubmed
16957736
uniprot
proteins
pubmed
17201797
uniprot
proteins
pubmed
1730625
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17347799
uniprot
proteins
pubmed
18278056
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18767165
uniprot
proteins
pubmed
1890161
uniprot
proteins
pubmed
19056263
uniprot
proteins
pubmed
19071018
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19394223
uniprot
proteins
pubmed
19459609
uniprot
proteins
pubmed
1963473
uniprot
proteins
pubmed
2002058
uniprot
proteins
pubmed
20348418
uniprot
proteins
pubmed
2040394
uniprot
proteins
pubmed
2121734
uniprot
proteins
pubmed
2168397
uniprot
proteins
pubmed
21707536
uniprot
proteins
pubmed
2210055
uniprot
proteins
pubmed
2211730
uniprot
proteins
pubmed
22768670
uniprot
proteins
pubmed
2280779
uniprot
proteins
pubmed
23302862
uniprot
proteins
pubmed
2365819
uniprot
proteins
pubmed
2369896
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24498630
uniprot
proteins
pubmed
2479553
uniprot
proteins
pubmed
25187647
uniprot
proteins
pubmed
2538124
uniprot
proteins
pubmed
2544997
uniprot
proteins
pubmed
2544998
uniprot
proteins
pubmed
2566545
uniprot
proteins
pubmed
26584640
uniprot
proteins
pubmed
27322061
uniprot
proteins
pubmed
27577745
uniprot
proteins
pubmed
27617429
uniprot
proteins
pubmed
2777789
uniprot
proteins
pubmed
2806055
uniprot
proteins
pubmed
2834824
uniprot
proteins
pubmed
2842060
uniprot
proteins
pubmed
2859121
uniprot
proteins
pubmed
28765322
uniprot
proteins
pubmed
2983222
uniprot
proteins
pubmed
3101064
uniprot
proteins
pubmed
3166375
uniprot
proteins
pubmed
3283938
uniprot
proteins
pubmed
3447155
uniprot
proteins
pubmed
3680248
uniprot
proteins
pubmed
38056462
uniprot
proteins
pubmed
7537849
uniprot
proteins
pubmed
7538143
uniprot
proteins
pubmed
7559478
uniprot
proteins
pubmed
7657032
uniprot
proteins
pubmed
7815442
uniprot
proteins
pubmed
7983039
uniprot
proteins
pubmed
7997262
uniprot
proteins
pubmed
8082780
uniprot
proteins
pubmed
8096518
uniprot
proteins
pubmed
8188715
uniprot
proteins
pubmed
8242067
uniprot
proteins
pubmed
8243830
uniprot
proteins
pubmed
8257688
uniprot
proteins
pubmed
8276809
uniprot
proteins
pubmed
8288049
uniprot
proteins
pubmed
8314008
uniprot
proteins
pubmed
8326490
uniprot
proteins
pubmed
8388389
uniprot
proteins
pubmed
8390949
uniprot
proteins
pubmed
8419945
uniprot
proteins
pubmed
8432414
uniprot
proteins
pubmed
8452530
uniprot
proteins
pubmed
8458533
uniprot
proteins
pubmed
8636294
uniprot
proteins
pubmed
8890729
uniprot
proteins
pubmed
8995282
uniprot
proteins
pubmed
8999839
uniprot
proteins
pubmed
9175790
uniprot
proteins
pubmed
9199575
uniprot
proteins
pubmed
9202395
uniprot
proteins
pubmed
9249867
uniprot
proteins
pubmed
9299395
uniprot
proteins
pubmed
9312016
uniprot
proteins
pubmed
9355755
uniprot
proteins
pubmed
9428692
uniprot
proteins
pubmed
9703342
uniprot
proteins
sequence_length
1382
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15208}; Single-pass type I membrane protein {ECO:0000305}. Late endosome {ECO:0000250|UniProtKB:P15208}. Lysosome {ECO:0000250|UniProtKB:P15208}. Note=Binding of insulin to INSR induces internalization and lysosomal degradation of the receptor, a means for down-regulating this signaling pathway after stimulation. In the presence of SORL1, internalized INSR molecules are redirected back to the cell surface, thereby preventing their lysosomal catabolism and strengthening insulin signal reception. {ECO:0000250|UniProtKB:P15208}.
uniprot
proteins
transmembrane_region
TRANSMEM 957..979; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins