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0INSR_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameINSR
DescriptionInsulin receptor precursor (ec 2.7.1.112) (ir) (cd220 antigen) .
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005887 integral to plasma membrane (TAS)
0005886 plasma membrane (TAS)
0005515 protein binding (IPI)
0004872 receptor activity (TAS)
0004716 receptor signaling protein tyrosine kinase ... (TAS)
0004714 transmembrane receptor protein tyrosine kin... (TAS)
0005066 transmembrane receptor protein tyrosine kin... (TAS)
0005975 carbohydrate metabolism (TAS)
0007275 development (TAS)
0006091 generation of precursor metabolites and energy (TAS)
0006468 protein amino acid phosphorylation (TAS)
0007165 signal transduction (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Protein kinases comprise a large family of enzymes that mediate the response of eukaryotic cells to external stimuli by phosphorylation of hydroxyamino acids. The enzymes fall into two broad classes.haracterised with respect to substrate specificity: serine/threonine specific and tyrosine specific . Tyrosine phosphorylating activity was originally detected in two viral transforming proteins .ut many retroviral transforming proteins and their cellular counterparts have since been shown to possess such activity. The growth factor receptors.hich are activated by ligand binding.nd theinsulin-related peptide receptor.re also family members.
  IPR001245:Tyrosine protein kinase
The furin-like cysteine rich region has been found in a variety of proteins from eukaryotes that are involved in the mechanism of signal transduction by receptor tyrosine kinases.hich involves receptor aggregation .
  IPR006211:Furin-like cysteine rich region
The type-1 insulin-like growth-factor receptor (IGF-1R) and insulin receptor (IR) are closely related members of the tyrosine-kinase receptor superfamily . IR is essential for glucose homeostasis.hereas IGF-1R is involved in both normal growth and development and malignant transformation. Homologues of these receptors are found in animals as simple as cnidarians. The epidermal growth-factor receptor (EGFR) family is closely related to the IR family and has significant sequence identity to the first three domains of the extracellular portion of IGF-IR (L1-Cys-rich-L2). The L domains each consist of a single-stranded right-handed beta-helix. The Cys-rich region is composed of eight disulphide-bonded modules.even of which form a rod-shaped domain with modules associated in an unusual manner. The three domains surround a central space of sufficient size to accommodate a ligand molecule. Although the fragment (residues 1-462) does not bind ligand.any of the determinants responsible for hormone binding and ligand specificity map to this central site. This structure therefore shows how the IR subfamily might interact with their ligands.A number of receptor systems have been implicated to play an important role in the development and progression of many human cancers. The epidermal growth factor (EGF) receptor tyrosine kinase family has been found to consistently play a leading role in tumor progression .
  IPR000494:EGF receptor, L domain
The furin-like cysteine rich region has been found in a variety of proteins from eukaryotes that are involved in the mechanism of signal transduction by receptor tyrosine kinases.hich involves receptor aggregation .
  IPR006212:Furin-like repeat
Fibronectins are multi-domain glycoproteins found in a soluble form in plasma.nd in an insoluble form in loose connective tissue and basement membranes . They contain multiple copies of 3 repeat regions (types I.I and III).hich bind to a variety of substances including heparin.ollagen.NA.ctin.ibrin and fibronectin receptors on cell surfaces. The wide variety of these substances means that fibronectins are involved in a number of important functions: e.g..ound healing; cell adhesion; blood coagulation; cell differentiation and migration; maintenance of the cellular cytoskeleton; and tumour metastasis . The role of fibronectin in cell differentiation is demonstrated by the marked reduction in the expression of its gene when neoplastic transformation occurs. Cell attachment has been found to be mediated by the binding of the tetrapeptide RGDS to integrins on the cell surface .lthough related sequences can also display cell adhesion activity.Plasma fibronectin occurs as a dimer of 2 different subunits.inked together by 2 disulphide bonds near the C-terminus. The difference in the 2 chains occurs in the type III repeat region and is caused by alternative splicing of the mRNA from one gene . The observation that.n a given protein.n individual repeat of one of the 3 types (e.g..he first FnIII repeat) shows much less similarity to its subsequent tandem repeats within that protein than to its equivalent repeat between fibronectins from other species.as suggested that the repeating structure of fibronectin arose at an early stage of evolution. It also seems to suggest that the structure is subject to high selective pressure .The fibronectin type III repeat region is an approximately 100 amino acid domain.ifferent tandem repeats of which contain binding sites for DNA.eparin and the cell surface . The superfamily of sequences believed to contain FnIII repeats represents 45 different families.he majority of which are involved in cell surface binding in some manner.r are receptor protein tyrosine kinases.r cytokine receptors.
  IPR003961:Fibronectin, type III
Eukaryotic protein kinases are enzymesthat belong to a very extensive family of proteins which share a conserved catalytic core common withboth serine/threonine and tyrosine protein kinases. There are a number of conserved regions in thecatalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is aglycine-rich stretch of residues in the vicinity of a lysine residue.hich has been shown to be involvedin ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residuewhich is important for the catalytic activity of the enzyme . This entry includes protein kinases from eukaryotes and viruses and may include some bacterial hits too.
  IPR000719:Protein kinase
Fibronectin is composed of three repeating structural motifs.f which one is the FnIII module. The three modules form a linear sequence of multiple tandem copies connected by short linker peptides. The secondary structure of the FnIII10 module.hich is the only fibronectin module to possess an integrin binding RGD motif.onsists of two beta-sheets containing the antiparallel beta-strands ABE and DCFG.espectively.hich fold up to form a beta-sandwich. The RGD sequence is located in the loop connecting the beta-strands .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008957:Fibronectin, type III-like fold
The growth factor receptor domain is a cysteine-rich region that is found in a variety of eukaryotic proteins that are involved in the mechanism of signal transduction by receptor tyrosine kinases. Proteins containing the growth factor receptor domain include the insulin-like growth factor-binding proteins (IGFBP) .he type-1 insulin-like growth-factor receptor (IGF-1R) .nd the receptor protein-tyrosine kinase Erbb-3 (ErbB3) . The general structure of the growth factor receptor domain is a disulphide-bound fold containing a beta-hairpin with two adjacent disulphides. IGFBPs control the distribution.unction and activity of insulin-like growth factors (IGFs) IGF-I and IGF-II.hich are key regulators of cell proliferation.ifferentiation and transformation. All IGFBPs share a common domain organization.here the highest conservation is found in the N-terminal Cys-rich IGF-binding domain. The N-terminal domain contains 10-12 conserved cysteine residues. IGF-1R is a member of the tyrosine-kinase receptor superfamily that is involved in both normal growth and development and malignant transformation. The Cys-rich domain is flanked by two L-domains.nd together they contribute to hormone binding and ligand specificity.ven though they do not bind ligand directly. The Cys-rich region is composed of eight disulphide-bonded modules.even of which form a rod-shaped domain. ErbB3 is a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. The extracellular region of ErbB3 is made up of two Cys-rich domains and two L-domains.rranged alternately. The two L-domains and the first Cys-rich domain are structurally homologous to those found in IGF-1R. The two Cys-rich domains are extended repeats of seven small disulphide-containing modules. A beta-hairpin loop extends from the first Cys-rich domain to contact the C-terminal portion of the second Cys-rich domain.reating a large pore structure. The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009030:Growth factor, receptor
Protein kinases () catalyze the phosphotransfer reaction fundamental to most signalling and regulatory processes in the eukaryotic cell . The catalytic subunit contains a core that is common to both serine/threonine and tyrosine protein kinases. The catalytic domain contains the nucleotide-binding site and the catalytic apparatus in an inter-lobe cleft. Structurally it shares functional and structural similarities with the ATP-grasp fold.hich is found in enzymes that catalyse the formation of an amide bond.nd with PIPK (phosphoinositol phosphate kinase). The three-dimensional fold of the protein kinase catalytic domain is similar to domains found in several other proteins. These include the catalytic domain of actin-fragmin kinase.n atypical protein kinase that regulates the F-actin capping activity in plasmodia ; the catalytic domain of phosphoinositide-3-kinase (PI3K).hich phosphorylates phosphoinositides and as such is involved in a number of fundamental cellular processes such as apoptosis.roliferation.otility and adhesion ; the catalytic domain of the MHCK/EF2 kinase.n atypical protein kinase that includes the TRP (transient channel potential) calcium-channel kinase involved in the modulation of calcium channels in eukaryotic cells in response to external signals ; choline kinase.hich catalyses the ATP-dependent phosphorylation of choline during the biosynthesis of phosphatidylcholine ; and 3.-aminoglycoside phosphotransferase type IIIa. bacterial enzyme that confers resistance to a range of aminoglycoside antibiotics .
  IPR011009:Protein kinase-like
IPR001245:Pkinase_Tyr 
Evalue:-153.236572265625 
Location:1023-1290IPR006211:Furin-like 
Evalue:-95.0087738037109 
Location:179-340IPR000494:Recep_L_domain 
Evalue:-47.9208183288574 
Location:359-474IPR000494:Recep_L_domain 
Evalue:-44.0043640136719 
Location:52-164IPR008957:FN_III-like 
Evalue:-7.34678745269775 
Location:848-947IPR003961:FN3 
Evalue:-6.10237290870956 
Location:622-831IPR009030:Grow_fac_recept 
Evalue:0 
Location:2-8IPR003961:FN3 
Evalue:1.99122607569249 
Location:496-600
SequencesProtein: INSR_HUMAN (1382 aa)
mRNA: NM_000208
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
the plasma membrane of the postsynaptic neuron. It apposes with presynaptic actiove zone.
sdb:0108 postsynaptic plasma membrane  (Evidence:keywords)
KO assignmentK04527
  Level 3 annotation:
    insulin receptor
  Level 2 annotation:
    Insulin signaling pathway
    Cytokine receptors
    CD molecules
    Adherens junction
    Dentatorubropallidoluysian atrophy (DRPLA)
    Type II diabetes mellitus
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 261 residues, 7067641-7068421Exon2: 47 residues, 7070459-7070594Exon3: 45 residues, 7071630-7071760Exon4: 55 residues, 7073624-7073784Exon5: 39 residues, 7073889-7074000Exon6: 83 residues, 7076293-7076538Exon7: 24 residues, 7077594-7077662Exon8: 36 residues, 7079862-7079965Exon9: 55 residues, 7083168-7083328Exon10: 48 residues, 7092687-7092827Exon11: 93 residues, 7093826-7094101Exon12: 14 residues, 7101507-7101543Exon13: 69 residues, 7103736-7103938Exon14: 58 residues, 7114042-7114210Exon15: 85 residues, 7117164-7117415Exon16: 44 residues, 7118978-7119105Exon17: 73 residues, 7121547-7121762Exon18: 50 residues, 7123300-7123445Exon19: 51 residues, 7125593-7125742Exon20: 109 residues, 7135326-7135648Exon21: 186 residues, 7218355-7218907Exon22: 71 residues, 7244802-7245011Exon23: 2 residues, -Jump to INSR_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3084 7493511-7504871 ~-11K 17845(MCOLN1)(+)Loci: 3085 7608012-7618758 ~-11K 17854(STXBP2)(+)Loci: 4362 7897603-7914538 ~-17K 17882(TIMM44)(-)Loci: 3086 8361295-8374479 ~-13K 17895(RAB11B)(+)Loci: 4361 7067641-7245011 ~-177K 17833(INSR)(-)Link out to UCSC