Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P15127 (INSR_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Insulin receptor

Short name=IR
EC=2.7.10.1
Alternative name(s):
CD_antigen=CD220
Gene names
Name:Insr
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1383 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 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. Ref.4

Catalytic activity

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

Enzyme 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 By similarity.

Subunit structure

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. Ref.3 Ref.5

Subcellular location

Cell membrane; Single-pass type I membrane protein.

Domain

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.

Post-translational modification

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

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.

Contains 3 fibronectin type-III domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfat cell differentiation

Inferred from expression pattern PubMed 17286602. Source: RGD

glucose homeostasis

Inferred from direct assay PubMed 18256749. Source: RGD

insulin receptor signaling pathway

Inferred from direct assay PubMed 12891559. Source: RGD

negative regulation of gene expression

Inferred from mutant phenotype PubMed 17585961. Source: RGD

negative regulation of protein phosphorylation

Inferred from mutant phenotype PubMed 17585961. Source: RGD

negative regulation of transporter activity

Inferred from mutant phenotype PubMed 19049803. Source: RGD

peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype PubMed 12850498. Source: RGD

positive regulation of glycoprotein biosynthetic process

Inferred from mutant phenotype PubMed 19049803. Source: RGD

positive regulation of phosphorylation

Inferred from direct assay PubMed 12435589. Source: BHF-UCL

protein autophosphorylation

Inferred from direct assay PubMed 12891559PubMed 17919343PubMed 3275643. Source: RGD

protein heterotetramerization

Inferred from direct assay PubMed 3516142. Source: RGD

protein phosphorylation

Inferred from direct assay PubMed 12891559. Source: RGD

regulation of hydrogen peroxide metabolic process

Inferred from direct assay PubMed 17919343. Source: RGD

response to activity

Inferred from expression pattern PubMed 17603294. Source: RGD

response to estradiol

Inferred from expression pattern PubMed 17931855. Source: RGD

response to ethanol

Inferred from expression pattern PubMed 19185210. Source: RGD

response to glucocorticoid

Inferred from expression pattern PubMed 18401942. Source: RGD

response to glucose

Inferred from expression pattern PubMed 12435589. Source: BHF-UCL

response to hormone

Inferred from expression pattern PubMed 18672341. Source: RGD

response to insulin

Inferred from expression pattern PubMed 12435589. Source: BHF-UCL

response to manganese ion

Inferred from expression pattern PubMed 6368536. Source: RGD

response to nutrient levels

Inferred from expression pattern PubMed 19088253. Source: RGD

response to testosterone

Inferred from expression pattern PubMed 17673259. Source: RGD

response to tumor necrosis factor

Inferred from mutant phenotype PubMed 17761893. Source: RGD

response to vitamin D

Inferred from expression pattern PubMed 18638371. Source: RGD

   Cellular_componentcytosol

Inferred from direct assay PubMed 15665515. Source: RGD

endosome

Inferred from direct assay PubMed 15665515. Source: RGD

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 18657188. Source: RGD

nucleus

Inferred from direct assay PubMed 18798337. Source: RGD

plasma membrane

Inferred from direct assay PubMed 15665515. Source: RGD

synapse

Inferred from direct assay PubMed 16978790. Source: RGD

   Molecular_function3-phosphoinositide-dependent protein kinase binding

Inferred from direct assay PubMed 16314505. Source: RGD

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

insulin binding

Inferred from direct assay PubMed 17023527PubMed 3275643. Source: RGD

insulin receptor substrate binding

Inferred from mutant phenotype PubMed 12850498. Source: RGD

insulin-activated receptor activity

Inferred from direct assay PubMed 12891559PubMed 17023527PubMed 3275643. Source: RGD

lipoic acid binding

Inferred from physical interaction PubMed 17274632. Source: RGD

protein complex binding

Inferred from direct assay PubMed 3516142. Source: RGD

protein domain specific binding

Inferred from physical interaction PubMed 9748281. Source: RGD

protein kinase activity

Inferred from direct assay PubMed 17429032. Source: RGD

protein kinase binding

Inferred from physical interaction PubMed 17318260PubMed 19952103. Source: RGD

protein phosphatase binding

Inferred from mutant phenotype PubMed 12850498. Source: RGD

protein tyrosine kinase activity

Inferred from direct assay PubMed 18657188. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Jak2Q626892EBI-7472166,EBI-8656708

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P15127-1)

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.
Isoform Short (identifier: P15127-2)

Also known as: RIR-A;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626
Chain27 – 759733Insulin receptor subunit alpha
PRO_0000016696
Chain764 – 1383620Insulin receptor subunit beta
PRO_0000016698

Regions

Topological domain27 – 759733Extracellular Probable
Topological domain764 – 957194Extracellular Probable
Transmembrane958 – 97821Helical; Potential
Topological domain979 – 1383405Cytoplasmic Probable
Domain625 – 727103Fibronectin type-III 1
Domain754 – 84895Fibronectin type-III 2
Domain854 – 94895Fibronectin type-III 3
Domain1024 – 1299276Protein kinase
Nucleotide binding1105 – 11117ATP By similarity
Nucleotide binding1164 – 11652ATP By similarity
Region734 – 7429Insulin-binding By similarity
Region997 – 10004Important for interaction with IRS1, SHC1 and STAT5B
Region1362 – 13654PIK3R1 binding By similarity
Compositional bias27 – 173147Leu-rich

Sites

Active site11601Proton donor/acceptor By similarity
Binding site10341ATP By similarity
Binding site10581ATP By similarity
Binding site11781ATP By similarity
Site651Insulin-binding By similarity

Amino acid modifications

Modified residue3991Phosphoserine By similarity
Modified residue4001Phosphotyrosine By similarity
Modified residue4061Phosphoserine By similarity
Modified residue10001Phosphotyrosine; by autocatalysis By similarity
Modified residue11861Phosphotyrosine; by autocatalysis By similarity
Modified residue11901Phosphotyrosine; by autocatalysis By similarity
Modified residue11911Phosphotyrosine; by autocatalysis By similarity
Modified residue13561Phosphotyrosine; by autocatalysis By similarity
Modified residue13621Phosphotyrosine; by autocatalysis By similarity
Glycosylation421N-linked (GlcNAc...) Potential
Glycosylation511N-linked (GlcNAc...) Potential
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1371N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Glycosylation2811N-linked (GlcNAc...) Potential
Glycosylation3211N-linked (GlcNAc...) Potential
Glycosylation3631N-linked (GlcNAc...) Potential
Glycosylation4231N-linked (GlcNAc...) Potential
Glycosylation4441N-linked (GlcNAc...) Potential
Glycosylation5401N-linked (GlcNAc...) Potential
Glycosylation6341N-linked (GlcNAc...) Potential
Glycosylation6521N-linked (GlcNAc...) Potential
Glycosylation6991N-linked (GlcNAc...) Potential
Glycosylation7701N-linked (GlcNAc...) Potential
Glycosylation7831N-linked (GlcNAc...) Potential
Glycosylation9211N-linked (GlcNAc...) Potential
Glycosylation9341N-linked (GlcNAc...) Potential
Disulfide bond34 ↔ 52 By similarity
Disulfide bond152 ↔ 181 By similarity
Disulfide bond185 ↔ 208 By similarity
Disulfide bond195 ↔ 214 By similarity
Disulfide bond218 ↔ 227 By similarity
Disulfide bond222 ↔ 233 By similarity
Disulfide bond234 ↔ 242 By similarity
Disulfide bond238 ↔ 251 By similarity
Disulfide bond254 ↔ 263 By similarity
Disulfide bond267 ↔ 279 By similarity
Disulfide bond285 ↔ 310 By similarity
Disulfide bond292 ↔ 300 By similarity
Disulfide bond314 ↔ 327 By similarity
Disulfide bond330 ↔ 334 By similarity
Disulfide bond338 ↔ 359 By similarity
Disulfide bond461 ↔ 494 By similarity
Disulfide bond550Interchain By similarity
Disulfide bond675 ↔ 900 By similarity

Natural variations

Alternative sequence746 – 75712Missing in isoform Short.
VSP_036680

Sequences

Sequence LengthMass (Da)Tools
Isoform Long (RIR-B) [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 4B919566902A944A

FASTA1,383156,757
        10         20         30         40         50         60 
MGSGRGCETT AVPLLMAVAV AGGTAGHLYP GEVCPGMDIR NNLTRLHELE NCSVIEGHLQ 

        70         80         90        100        110        120 
ILLMFKTRPE DFRDLSFPKL IMITDYLLLF RVYGLESLKD LFPNLTVIRG SRLFFNYALV 

       130        140        150        160        170        180 
IFEMVHLKEL GLYNLMNITR GSVRIEKNNE LCYLATIDWS RILDYVEDNY IVLNKDDNEE 

       190        200        210        220        230        240 
CGDVCPGTAK GKTNCPATVI NGQFVERCWT HSHCQKVCPT ICKSHGCTAE GLCCHKECLG 

       250        260        270        280        290        300 
NCSEPDDPTK CVACRNFYLD GQCVETCPPP YYHFQDWRCV NFSFCQDLHY KCRNSRKPGC 

       310        320        330        340        350        360 
HQYVIHNNKC IPECPSGYTM NSSNLMCTPC LGPCPKVCQI LEGEKTIDSV TSAQELRGCT 

       370        380        390        400        410        420 
VINGSLIINI RGGNNLAAEL EANLGLIEEI SGFLKIRRSY ALVSLSFFRK LHLIRGETLE 

       430        440        450        460        470        480 
IGNYSFYALD NQNLRQLWDW NKHNLTITQG KLFFHYNPKL CLSEIHKMEE VSGTKGRQER 

       490        500        510        520        530        540 
NDIALKTNGD QASCENELLK FSFIRTSFDK ILLRWEPYWP PDFRDLLGFM LFYKEAPYQN 

       550        560        570        580        590        600 
VTEFDGQDAC GSNSWTVVDI DPPQRSNDPK SQTPSHPGWL MRGLKPWTQY AIFVKTLVTF 

       610        620        630        640        650        660 
SDERRTYGAK SDIIYVQTDA TNPSVPLDPI SVSNSSSQII LKWKPPSDPN GNITHYLVYW 

       670        680        690        700        710        720 
ERQAEDSELF ELDYCLKGLK LPSRTWSPPF ESDDSQKHNQ SEYDDSASEC CSCPKTDSQI 

       730        740        750        760        770        780 
LKELEESSFR KTFEDYLHNV VFVPRKTSSG NGAEDTRPSR KRRSLEEVGN VTATTPTLPD 

       790        800        810        820        830        840 
FPNISSTIAP TSHEEHRPFE KVVNKESLVI SGLRHFTGYR IELQACNQDS PEERSGVAAY 

       850        860        870        880        890        900 
VSARTMPEAK ADDIVGPVTH EIFENNVVHL MWQEPKEPNG LIVLYEVSYR RYGDEELHLC 

       910        920        930        940        950        960 
VSRKHFALER GCRLRGLSPG NYSVRVRATS LAGNGSWTEP TYFYVTDYLD VPSNIAKIII 

       970        980        990       1000       1010       1020 
GPLIFVFLFS VVIGSIYLFL RKRQPDGPMG PLYASSNPEY LSASDVFPSS VYVPDEWEVP 

      1030       1040       1050       1060       1070       1080 
REKITLLREL GQGSFGMVYE GNAKDIIKGE VETRVAVKTV NESASLRERI EFLNEASVMK 

      1090       1100       1110       1120       1130       1140 
GFTCHHVVRL LGVVSKGQPT LVVMELMAHG DLKSHLRSLR PDAENNPGRP PPTLQEMIQM 

      1150       1160       1170       1180       1190       1200 
TAEIADGMAY LNAKKFVHRD LAARNCMVAH DFTVKIGDFG MTRDIYETDY YRKGGKGLLP 

      1210       1220       1230       1240       1250       1260 
VRWMSPESLK DGVFTASSDM WSFGVVLWEI TSLAEQPYQG LSNEQVLKFV MDGGYLDPPD 

      1270       1280       1290       1300       1310       1320 
NCPERLTDLM RMCWQFNPKM RPTFLEIVNL LKDDLHPSFP EVSFFYSEEN KAPESEELEM 

      1330       1340       1350       1360       1370       1380 
EFEDMENVPL DRSSHCQREE AGCREGGSSL SIKRTYDEHI PYTHMNGGKK NGRVLTLPRS 


NPS 

« Hide

Isoform Short (RIR-A) [UniParc].

Checksum: 146D5FFDA1EF415D
Show »

FASTA1,371155,553

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA36080.
UniGeneRn.9876.

3D structure databases

ProteinModelPortalP15127.
SMRP15127. Positions 30-949, 1009-1311.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP15127. 5 interactions.
MINTMINT-1348005.

Chemistry

BindingDBP15127.
ChEMBLCHEMBL5486.

PTM databases

PhosphoSiteP15127.

Proteomic databases

PaxDbP15127.
PRIDEP15127.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:2917. rat. [P15127-1]

Organism-specific databases

RGD2917. Insr.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000038045.
HOVERGENHBG006134.
InParanoidP15127.
PhylomeDBP15127.

Enzyme and pathway databases

BRENDA2.7.10.1. 5301.

Gene expression databases

GenevestigatorP15127.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProIPR000494. 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]
PfamPF00041. fn3. 2 hits.
PF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFPIRSF000620. Insulin_receptor. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00060. FN3. 3 hits.
SM00261. FU. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 4 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEPS50853. 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]
ProtoNetSearch...

Other

NextBio13948910.
PROP15127.

Entry information

Entry nameINSR_RAT
AccessionPrimary (citable) accession number: P15127
Secondary accession number(s): P97681
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families