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P15127

- INSR_RAT

UniProt

P15127 - INSR_RAT

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Protein

Insulin receptor

Gene

Insr

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 phosphotyrosines 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). When present in a hybrid receptor with IGF1R, binds IGF1 (By similarity).By similarity

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Enzyme regulationi

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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei65 – 651Insulin-bindingBy similarity
Binding sitei1034 – 10341ATPPROSITE-ProRule annotation
Binding sitei1058 – 10581ATPPROSITE-ProRule annotation
Active sitei1160 – 11601Proton donor/acceptorBy similarity
Binding sitei1178 – 11781ATPPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1105 – 11117ATPPROSITE-ProRule annotation
Nucleotide bindingi1164 – 11652ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. 3-phosphoinositide-dependent protein kinase binding Source: RGD
  2. ATP binding Source: UniProtKB-KW
  3. insulin-activated receptor activity Source: RGD
  4. insulin binding Source: RGD
  5. insulin receptor substrate binding Source: RGD
  6. lipoic acid binding Source: RGD
  7. protein complex binding Source: RGD
  8. protein domain specific binding Source: RGD
  9. protein kinase activity Source: RGD
  10. protein kinase binding Source: RGD
  11. protein phosphatase binding Source: RGD
  12. protein tyrosine kinase activity Source: RGD

GO - Biological processi

  1. fat cell differentiation Source: RGD
  2. glucose homeostasis Source: RGD
  3. insulin receptor signaling pathway Source: RGD
  4. negative regulation of gene expression Source: RGD
  5. negative regulation of protein phosphorylation Source: RGD
  6. negative regulation of transporter activity Source: RGD
  7. peptidyl-tyrosine phosphorylation Source: RGD
  8. positive regulation of glycoprotein biosynthetic process Source: RGD
  9. positive regulation of phosphorylation Source: BHF-UCL
  10. protein autophosphorylation Source: RGD
  11. protein heterotetramerization Source: RGD
  12. protein phosphorylation Source: RGD
  13. regulation of hydrogen peroxide metabolic process Source: RGD
  14. response to activity Source: RGD
  15. response to estradiol Source: RGD
  16. response to ethanol Source: RGD
  17. response to glucocorticoid Source: RGD
  18. response to glucose Source: BHF-UCL
  19. response to hormone Source: RGD
  20. response to insulin Source: BHF-UCL
  21. response to manganese ion Source: RGD
  22. response to nutrient levels Source: RGD
  23. response to testosterone Source: RGD
  24. response to tumor necrosis factor Source: RGD
  25. response to vitamin D Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin receptor (EC:2.7.10.1)
Short name:
IR
Alternative name(s):
CD_antigen: CD220
Cleaved into the following 2 chains:
Gene namesi
Name:Insr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2917. Insr.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: RGD
  2. endosome Source: RGD
  3. integral component of membrane Source: UniProtKB-KW
  4. intracellular membrane-bounded organelle Source: RGD
  5. nucleus Source: RGD
  6. plasma membrane Source: RGD
  7. synapse Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Add
BLAST
Chaini27 – 759733Insulin receptor subunit alphaPRO_0000016696Add
BLAST
Chaini764 – 1383620Insulin receptor subunit betaPRO_0000016698Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 ↔ 52By similarity
Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi51 – 511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi137 – 1371N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi152 ↔ 181By similarity
Disulfide bondi185 ↔ 208By similarity
Disulfide bondi195 ↔ 214By similarity
Disulfide bondi218 ↔ 227By similarity
Disulfide bondi222 ↔ 233By similarity
Disulfide bondi234 ↔ 242By similarity
Disulfide bondi238 ↔ 251By similarity
Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi254 ↔ 263By similarity
Disulfide bondi267 ↔ 279By similarity
Glycosylationi281 – 2811N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi285 ↔ 310By similarity
Disulfide bondi292 ↔ 300By similarity
Disulfide bondi314 ↔ 327By similarity
Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi330 ↔ 334By similarity
Disulfide bondi338 ↔ 359By similarity
Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence Analysis
Modified residuei399 – 3991PhosphoserineBy similarity
Modified residuei400 – 4001PhosphotyrosineBy similarity
Modified residuei406 – 4061PhosphoserineBy similarity
Glycosylationi423 – 4231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi444 – 4441N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi461 ↔ 494By similarity
Glycosylationi540 – 5401N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi550 – 550InterchainBy similarity
Glycosylationi634 – 6341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi652 – 6521N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi675 ↔ 900By similarity
Glycosylationi699 – 6991N-linked (GlcNAc...)Sequence Analysis
Glycosylationi770 – 7701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi783 – 7831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi921 – 9211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi934 – 9341N-linked (GlcNAc...)Sequence Analysis
Modified residuei1000 – 10001Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1186 – 11861Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1190 – 11901Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1191 – 11911Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1356 – 13561Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1362 – 13621Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

Autophosphorylated on tyrosine residues in response to insulin. Phosphorylation of Tyr-1000 is required for binding to IRS1, SHC1, and STAT5B. Dephosphorylated by PTPRE on Tyr-1000, Tyr-1186, Tyr-1190 and Tyr-1191 residues. Dephosphorylated by PTPRF and PTPN1. Dephosphorylated by PTPN2; down-regulates insulin-induced signaling.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP15127.
PRIDEiP15127.

PTM databases

PhosphoSiteiP15127.

Expressioni

Gene expression databases

GenevestigatoriP15127.

Interactioni

Subunit structurei

Tetramer of 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains carry the insulin-binding regions, while the beta chains carry the kinase domain. Forms a hybrid receptor with IGF1R, the hybrid is a tetramer consisting of 1 alpha chain and 1 beta chain of INSR and 1 alpha chain and 1 beta chain of IGF1R. Interacts with SORBS1 but dissociates from it following insulin stimulation. Binds SH2B2. Activated form of INSR interacts (via Tyr-1000) with the PTB/PID domains of IRS1 and SHC1. The sequences surrounding the phosphorylated NPXY motif contribute differentially to either IRS1 or SHC1 recognition. Interacts (via tyrosines in the C-terminus) with IRS2 (via PTB domain and 591-786 AA); the 591-786 would be the primary anchor of IRS2 to INSR while the PTB domain would have a stabilizing action on the interaction with INSR. Interacts with the SH2 domains of the 85 kDa regulatory subunit of PI3K (PIK3R1) in vitro, when autophosphorylated on tyrosine residues. Interacts with SOCS7. Interacts (via the phosphorylated Tyr-1000), with SOCS3. Interacts (via the phosphorylated Tyr-1186, Tyr-1190, Tyr-1191) with SOCS1. Interacts with ARRB2 (By similarity). Interacts with GRB10; this interaction blocks the association between IRS1/IRS2 and INSR, significantly reduces insulin-stimulated tyrosine phosphorylation of IRS1 and IRS2 and thus decreases insulin signaling. Interacts with PDPK1. Interacts (via Tyr-1191) with GRB14 (via BPS domain); this interaction protects the tyrosines in the activation loop from dephosphorylation, but promotes dephosphorylation of Tyr-1000, this results in decreased interaction with, and phosphorylation of, IRS1. Interacts (via subunit alpha) with ENPP1 (via 485-599 AA); this interaction blocks autophosphorylation. Interacts with PTPRE; this interaction is dependent of Tyr-1186, Tyr-1190 and Tyr-1191 of the INSR. Interacts with STAT5B (via SH2 domain). Interacts with PTPRF (By similarity). Interacts with GRB7. Interacts with CAV2 (tyrosine-phosphorylated form); the interaction is increased with 'Tyr-27'phosphorylation of CAV2.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Jak2Q626892EBI-7472166,EBI-8656708

Protein-protein interaction databases

IntActiP15127. 5 interactions.
MINTiMINT-1348005.

Structurei

3D structure databases

ProteinModelPortaliP15127.
SMRiP15127. Positions 30-949, 1009-1311.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 759733ExtracellularCuratedAdd
BLAST
Topological domaini764 – 957194ExtracellularCuratedAdd
BLAST
Topological domaini979 – 1383405CytoplasmicCuratedAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei958 – 97821HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini625 – 727103Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini754 – 84895Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini854 – 94895Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini1024 – 1299276Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni734 – 7429Insulin-bindingBy similarity
Regioni997 – 10004Important for interaction with IRS1, SHC1 and STAT5B
Regioni1362 – 13654PIK3R1 bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi27 – 173147Leu-richAdd
BLAST

Domaini

The tetrameric insulin receptor binds insulin via non-identical regions from two alpha chains, primarily via the C-terminal region of the first INSR alpha chain. Residues from the leucine-rich N-terminus of the other INSR alpha chain also contribute to this insulin binding site. A secondary insulin-binding site is formed by residues at the junction of fibronectin type-III domain 1 and 2 (By similarity).By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation
Contains 3 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000038045.
HOVERGENiHBG006134.
InParanoidiP15127.
PhylomeDBiP15127.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProiIPR000494. EGF_rcpt_L.
IPR003961. Fibronectin_type3.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016246. Tyr_kinase_insulin-like_rcpt.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]
PfamiPF00041. fn3. 2 hits.
PF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFiPIRSF000620. Insulin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00060. FN3. 3 hits.
SM00261. FU. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 4 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS50853. FN3. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: P15127-1) [UniParc]FASTAAdd to Basket

Also known as: RIR-B

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGSGRGCETT AVPLLMAVAV AGGTAGHLYP GEVCPGMDIR NNLTRLHELE
60 70 80 90 100
NCSVIEGHLQ ILLMFKTRPE DFRDLSFPKL IMITDYLLLF RVYGLESLKD
110 120 130 140 150
LFPNLTVIRG SRLFFNYALV IFEMVHLKEL GLYNLMNITR GSVRIEKNNE
160 170 180 190 200
LCYLATIDWS RILDYVEDNY IVLNKDDNEE CGDVCPGTAK GKTNCPATVI
210 220 230 240 250
NGQFVERCWT HSHCQKVCPT ICKSHGCTAE GLCCHKECLG NCSEPDDPTK
260 270 280 290 300
CVACRNFYLD GQCVETCPPP YYHFQDWRCV NFSFCQDLHY KCRNSRKPGC
310 320 330 340 350
HQYVIHNNKC IPECPSGYTM NSSNLMCTPC LGPCPKVCQI LEGEKTIDSV
360 370 380 390 400
TSAQELRGCT VINGSLIINI RGGNNLAAEL EANLGLIEEI SGFLKIRRSY
410 420 430 440 450
ALVSLSFFRK LHLIRGETLE IGNYSFYALD NQNLRQLWDW NKHNLTITQG
460 470 480 490 500
KLFFHYNPKL CLSEIHKMEE VSGTKGRQER NDIALKTNGD QASCENELLK
510 520 530 540 550
FSFIRTSFDK ILLRWEPYWP PDFRDLLGFM LFYKEAPYQN VTEFDGQDAC
560 570 580 590 600
GSNSWTVVDI DPPQRSNDPK SQTPSHPGWL MRGLKPWTQY AIFVKTLVTF
610 620 630 640 650
SDERRTYGAK SDIIYVQTDA TNPSVPLDPI SVSNSSSQII LKWKPPSDPN
660 670 680 690 700
GNITHYLVYW ERQAEDSELF ELDYCLKGLK LPSRTWSPPF ESDDSQKHNQ
710 720 730 740 750
SEYDDSASEC CSCPKTDSQI LKELEESSFR KTFEDYLHNV VFVPRKTSSG
760 770 780 790 800
NGAEDTRPSR KRRSLEEVGN VTATTPTLPD FPNISSTIAP TSHEEHRPFE
810 820 830 840 850
KVVNKESLVI SGLRHFTGYR IELQACNQDS PEERSGVAAY VSARTMPEAK
860 870 880 890 900
ADDIVGPVTH EIFENNVVHL MWQEPKEPNG LIVLYEVSYR RYGDEELHLC
910 920 930 940 950
VSRKHFALER GCRLRGLSPG NYSVRVRATS LAGNGSWTEP TYFYVTDYLD
960 970 980 990 1000
VPSNIAKIII GPLIFVFLFS VVIGSIYLFL RKRQPDGPMG PLYASSNPEY
1010 1020 1030 1040 1050
LSASDVFPSS VYVPDEWEVP REKITLLREL GQGSFGMVYE GNAKDIIKGE
1060 1070 1080 1090 1100
VETRVAVKTV NESASLRERI EFLNEASVMK GFTCHHVVRL LGVVSKGQPT
1110 1120 1130 1140 1150
LVVMELMAHG DLKSHLRSLR PDAENNPGRP PPTLQEMIQM TAEIADGMAY
1160 1170 1180 1190 1200
LNAKKFVHRD LAARNCMVAH DFTVKIGDFG MTRDIYETDY YRKGGKGLLP
1210 1220 1230 1240 1250
VRWMSPESLK DGVFTASSDM WSFGVVLWEI TSLAEQPYQG LSNEQVLKFV
1260 1270 1280 1290 1300
MDGGYLDPPD NCPERLTDLM RMCWQFNPKM RPTFLEIVNL LKDDLHPSFP
1310 1320 1330 1340 1350
EVSFFYSEEN KAPESEELEM EFEDMENVPL DRSSHCQREE AGCREGGSSL
1360 1370 1380
SIKRTYDEHI PYTHMNGGKK NGRVLTLPRS NPS
Length:1,383
Mass (Da):156,757
Last modified:April 1, 1990 - v1
Checksum:i4B919566902A944A
GO
Isoform Short (identifier: P15127-2) [UniParc]FASTAAdd to Basket

Also known as: RIR-A

The sequence of this isoform differs from the canonical sequence as follows:
     746-757: Missing.

Show »
Length:1,371
Mass (Da):155,553
Checksum:i146D5FFDA1EF415D
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei746 – 75712Missing in isoform Short. CuratedVSP_036680Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M29014 mRNA. Translation: AAA41441.1.
AF005776 Genomic DNA. Translation: AAB61414.1.
AF005777 Genomic DNA. Translation: AAB61415.1.
AH004882 Genomic DNA. Translation: AAB38967.1.
AH004883 Genomic DNA. Translation: AAB38968.1.
U80633 Genomic DNA. Translation: AAB38746.1.
PIRiA36080.
UniGeneiRn.9876.

Genome annotation databases

UCSCiRGD:2917. rat. [P15127-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M29014 mRNA. Translation: AAA41441.1 .
AF005776 Genomic DNA. Translation: AAB61414.1 .
AF005777 Genomic DNA. Translation: AAB61415.1 .
AH004882 Genomic DNA. Translation: AAB38967.1 .
AH004883 Genomic DNA. Translation: AAB38968.1 .
U80633 Genomic DNA. Translation: AAB38746.1 .
PIRi A36080.
UniGenei Rn.9876.

3D structure databases

ProteinModelPortali P15127.
SMRi P15127. Positions 30-949, 1009-1311.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P15127. 5 interactions.
MINTi MINT-1348005.

Chemistry

BindingDBi P15127.
ChEMBLi CHEMBL5486.

PTM databases

PhosphoSitei P15127.

Proteomic databases

PaxDbi P15127.
PRIDEi P15127.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:2917. rat. [P15127-1 ]

Organism-specific databases

RGDi 2917. Insr.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000038045.
HOVERGENi HBG006134.
InParanoidi P15127.
PhylomeDBi P15127.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 5301.

Miscellaneous databases

NextBioi 13948910.
PROi P15127.

Gene expression databases

Genevestigatori P15127.

Family and domain databases

Gene3Di 2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProi IPR000494. EGF_rcpt_L.
IPR003961. Fibronectin_type3.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016246. Tyr_kinase_insulin-like_rcpt.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view ]
Pfami PF00041. fn3. 2 hits.
PF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view ]
PIRSFi PIRSF000620. Insulin_receptor. 1 hit.
PRINTSi PR00109. TYRKINASE.
SMARTi SM00060. FN3. 3 hits.
SM00261. FU. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 4 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEi PS50853. FN3. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The rat insulin receptor: primary structure and conservation of tissue-specific alternative messenger RNA splicing."
    Goldstein B.J., Dudley A.L.
    Mol. Endocrinol. 4:235-244(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), ALTERNATIVE SPLICING (ISOFORM SHORT).
  2. Liu Y., Tam J.W.O.
    Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 731-756; 758-819; 969-994 AND 1119-1177.
    Strain: Sprague-Dawley.
  3. "Evidence for an interaction between the insulin receptor and Grb7. A role for two of its binding domains, PIR and SH2."
    Kasus-Jacobi A., Bereziat V., Perdereau D., Girard J., Burnol A.F.
    Oncogene 19:2052-2059(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GRB7.
  4. "Insulin and IGF-I action on insulin receptors, IGF-I receptors, and hybrid insulin/IGF-I receptors in vascular smooth muscle cells."
    Johansson G.S., Arnqvist H.J.
    Am. J. Physiol. 291:E1124-E1130(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, FORMATION OF A HYBRID RECEPTOR WITH IGF1R.
  5. "Identification of pY19-caveolin-2 as a positive regulator of insulin-stimulated actin cytoskeleton-dependent mitogenesis."
    Kwon H., Jeong K., Pak Y.
    J. Cell. Mol. Med. 13:1549-1564(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CAV2.

Entry informationi

Entry nameiINSR_RAT
AccessioniPrimary (citable) accession number: P15127
Secondary accession number(s): P97681
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 29, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3