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Protein

Insulin receptor

Gene

Insr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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 similarity1 Publication

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)DescriptionActionsGraphical viewLength
Sitei65Insulin-bindingBy similarity1
Binding sitei1034ATPPROSITE-ProRule annotation1
Binding sitei1058ATPPROSITE-ProRule annotation1
Active sitei1160Proton donor/acceptorBy similarity1
Binding sitei1178ATPPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1105 – 1111ATPPROSITE-ProRule annotation7
Nucleotide bindingi1164 – 1165ATPPROSITE-ProRule annotation2

GO - Molecular functioni

  • 3-phosphoinositide-dependent protein kinase binding Source: RGD
  • ATP binding Source: UniProtKB-KW
  • insulin-activated receptor activity Source: RGD
  • insulin binding Source: RGD
  • insulin receptor substrate binding Source: RGD
  • lipoic acid binding Source: RGD
  • protein complex binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein kinase activity Source: RGD
  • protein kinase binding Source: RGD
  • protein phosphatase binding Source: RGD
  • protein tyrosine kinase activity Source: RGD

GO - Biological processi

  • cerebellum development Source: RGD
  • fat cell differentiation Source: RGD
  • glucose homeostasis Source: RGD
  • hippocampus development Source: RGD
  • insulin receptor signaling pathway Source: RGD
  • negative regulation of gene expression Source: RGD
  • negative regulation of protein phosphorylation Source: RGD
  • negative regulation of transporter activity Source: RGD
  • peptidyl-tyrosine phosphorylation Source: RGD
  • positive regulation of glycoprotein biosynthetic process Source: RGD
  • positive regulation of phosphorylation Source: BHF-UCL
  • protein autophosphorylation Source: RGD
  • protein heterotetramerization Source: RGD
  • protein phosphorylation Source: RGD
  • regulation of hydrogen peroxide metabolic process Source: RGD
  • response to activity Source: RGD
  • response to estradiol Source: RGD
  • response to ethanol Source: RGD
  • response to glucocorticoid Source: RGD
  • response to glucose Source: BHF-UCL
  • response to hormone Source: RGD
  • response to insulin Source: BHF-UCL
  • response to manganese ion Source: RGD
  • response to nutrient levels Source: RGD
  • response to testosterone Source: RGD
  • response to tumor necrosis factor Source: RGD
  • 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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2917. Insr.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini27 – 759ExtracellularCuratedAdd BLAST733
Topological domaini764 – 957ExtracellularCuratedAdd BLAST194
Transmembranei958 – 978HelicalSequence analysisAdd BLAST21
Topological domaini979 – 1383CytoplasmicCuratedAdd BLAST405

GO - Cellular componenti

  • cytosol Source: RGD
  • endosome Source: RGD
  • integral component of membrane Source: UniProtKB-KW
  • intracellular membrane-bounded organelle Source: RGD
  • neuronal cell body Source: RGD
  • nucleus Source: RGD
  • plasma membrane Source: RGD
  • synapse Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5486.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Add BLAST26
ChainiPRO_000001669627 – 759Insulin receptor subunit alphaAdd BLAST733
ChainiPRO_0000016698764 – 1383Insulin receptor subunit betaAdd BLAST620

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi34 ↔ 52By similarity
Glycosylationi42N-linked (GlcNAc...)Sequence analysis1
Glycosylationi51N-linked (GlcNAc...)Sequence analysis1
Glycosylationi104N-linked (GlcNAc...)Sequence analysis1
Glycosylationi137N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi241N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi254 ↔ 263By similarity
Disulfide bondi267 ↔ 279By similarity
Glycosylationi281N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi285 ↔ 310By similarity
Disulfide bondi292 ↔ 300By similarity
Disulfide bondi314 ↔ 327By similarity
Glycosylationi321N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi330 ↔ 334By similarity
Disulfide bondi338 ↔ 359By similarity
Glycosylationi363N-linked (GlcNAc...)Sequence analysis1
Modified residuei399PhosphoserineBy similarity1
Modified residuei400PhosphotyrosineBy similarity1
Modified residuei406PhosphoserineBy similarity1
Glycosylationi423N-linked (GlcNAc...)Sequence analysis1
Glycosylationi444N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi461 ↔ 494By similarity
Glycosylationi540N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi550InterchainBy similarity
Glycosylationi634N-linked (GlcNAc...)Sequence analysis1
Glycosylationi652N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi675 ↔ 900By similarity
Glycosylationi699N-linked (GlcNAc...)Sequence analysis1
Glycosylationi770N-linked (GlcNAc...)Sequence analysis1
Glycosylationi783N-linked (GlcNAc...)Sequence analysis1
Glycosylationi921N-linked (GlcNAc...)Sequence analysis1
Glycosylationi934N-linked (GlcNAc...)Sequence analysis1
Modified residuei1000Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1186Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1190Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1191Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1356Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1362Phosphotyrosine; by autocatalysisBy similarity1

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.
PeptideAtlasiP15127.
PRIDEiP15127.

PTM databases

iPTMnetiP15127.
PhosphoSitePlusiP15127.
UniCarbKBiP15127.

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. Interacts with ATIC; ATIC together with PRKAA2/AMPK2 and HACD3/PTPLAD1 is proposed to be part of a signaling netwok regulating INSR autophosphorylation and endocytosis (PubMed:25687571).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AticO355673EBI-10768746,EBI-10768817
Jak2Q626892EBI-7472166,EBI-8656708

GO - Molecular functioni

  • 3-phosphoinositide-dependent protein kinase binding Source: RGD
  • insulin binding Source: RGD
  • insulin receptor substrate binding Source: RGD
  • protein complex binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein kinase binding Source: RGD
  • protein phosphatase binding Source: RGD

Protein-protein interaction databases

DIPiDIP-42209N.
IntActiP15127. 11 interactors.
MINTiMINT-1348005.
STRINGi10116.ENSRNOP00000060141.

Chemistry databases

BindingDBiP15127.

Structurei

Secondary structure

11383
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi727 – 736Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4XSTX-ray3.00F726-748[»]
ProteinModelPortaliP15127.
SMRiP15127.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini625 – 727Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST103
Domaini754 – 848Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST95
Domaini854 – 948Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST95
Domaini1024 – 1299Protein kinasePROSITE-ProRule annotationAdd BLAST276

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni734 – 742Insulin-bindingBy similarity9
Regioni997 – 1000Important for interaction with IRS1, SHC1 and STAT5B4
Regioni1362 – 1365PIK3R1 bindingBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi27 – 173Leu-richAdd BLAST147

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

eggNOGiKOG4258. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000038045.
HOVERGENiHBG006134.
InParanoidiP15127.
PhylomeDBiP15127.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProiIPR003961. FN3_dom.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000494. Rcpt_L-dom.
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. 1 hit.
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.
SSF52058. SSF52058. 2 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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_036680746 – 757Missing in isoform Short. CuratedAdd BLAST12

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4XSTX-ray3.00F726-748[»]
ProteinModelPortaliP15127.
SMRiP15127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-42209N.
IntActiP15127. 11 interactors.
MINTiMINT-1348005.
STRINGi10116.ENSRNOP00000060141.

Chemistry databases

BindingDBiP15127.
ChEMBLiCHEMBL5486.

PTM databases

iPTMnetiP15127.
PhosphoSitePlusiP15127.
UniCarbKBiP15127.

Proteomic databases

PaxDbiP15127.
PeptideAtlasiP15127.
PRIDEiP15127.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:2917. rat. [P15127-1]

Organism-specific databases

RGDi2917. Insr.

Phylogenomic databases

eggNOGiKOG4258. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000038045.
HOVERGENiHBG006134.
InParanoidiP15127.
PhylomeDBiP15127.

Enzyme and pathway databases

BRENDAi2.7.10.1. 5301.

Miscellaneous databases

PROiP15127.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProiIPR003961. FN3_dom.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000494. Rcpt_L-dom.
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. 1 hit.
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.
SSF52058. SSF52058. 2 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 171 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.