Gene Report
Approved Symbol | ITGB5 |
---|---|
Approved Name | integrin, beta 5 |
Location | 3q21.2 |
Position | chr3:124481795-124606144 (-) |
External Links |
Entrez Gene: 3693 Ensembl: ENSG00000082781 UCSC: uc003eho.3 HGNC ID: 6160 |
No. of Studies (Positive/Negative) | 1(1/0) |
Type | Literature-origin |
Name in Literature | Reference | Research Type | Statistical Result | Relation Description | |
---|---|---|---|---|---|
Integrin, beta 5 | Tochigi, 2008 | patients and normal controls | Genes differentially expressed in major depression Genes differentially expressed in major depression |
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Note:
1. The different color of the nodes denotes the level of the nodes.
Genetic/Epigenetic Locus | Protein and Other Molecule | Cell and Molecular Pathway | Neural System | Cognition and Behavior | Symptoms and Signs | Environment | MDD |
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Approved Name | UniportKB | No. of Studies (Positive/Negative) | Source | |
---|---|---|---|---|
Integrin beta-5 | P18084 | 0(0/0) | Gene mapped |
Gene mapped GO terms | ||||
ID | Name | Type | Evidence | |
---|---|---|---|---|
GO:0002474 | antigen processing and presentation of peptide antigen via MHC class I | biological process | TAS | |
GO:0007160 | cell-matrix adhesion | biological process | IEA | |
GO:0007275 | multicellular organismal development | biological process | IEA | |
GO:0005886 | plasma membrane | cellular component | TAS | |
GO:0008305 | integrin complex | cellular component | IEA | |
GO:0042590 | antigen processing and presentation of exogenous peptide antigen via MHC class I | biological process | TAS | |
GO:0005925 | focal adhesion | cellular component | IEA | |
GO:0005515 | protein binding | molecular function | IPI | |
GO:0005178 | integrin binding | molecular function | IEA | |
GO:0045335 | phagocytic vesicle | cellular component | TAS | |
GO:0002479 | antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent | biological process | TAS | |
GO:0007229 | integrin-mediated signaling pathway | biological process | IEA | |
GO:0031252 | cell leading edge | cellular component | IEA | |
GO:0006936 | muscle contraction | biological process | TAS | |
GO:0004872 | receptor activity | molecular function | IEA |
Literature-origin KEGG pathway | ||||
ID | Name | Brief Description | Full Description | |
---|---|---|---|---|
hsa04510 | focal adhesion | Focal adhesion | Cell-matrix adhesions play essential roles in important biol...... Cell-matrix adhesions play essential roles in important biological processes including cell motility, cell proliferation, cell differentiation, regulation of gene expression and cell survival. At the cell-extracellular matrix contact points, specialized structures are formed and termed focal adhesions, where bundles of actin filaments are anchored to transmembrane receptors of the integrin family through a multi-molecular complex of junctional plaque proteins. Some of the constituents of focal adhesions participate in the structural link between membrane receptors and the actin cytoskeleton, while others are signalling molecules, including different protein kinases and phosphatases, their substrates, and various adapter proteins. Integrin signaling is dependent upon the non-receptor tyrosine kinase activities of the FAK and src proteins as well as the adaptor protein functions of FAK, src and Shc to initiate downstream signaling events. These signalling events culminate in reorganization of the actin cytoskeleton; a prerequisite for changes in cell shape and motility, and gene expression. Similar morphological alterations and modulation of gene expression are initiated by the binding of growth factors to their respective receptors, emphasizing the considerable crosstalk between adhesion- and growth factor-mediated signalling. More... | |
hsa05412 | arrhythmogenic right_ventricular_cardiomyopathy_arvc | Arrhythmogenic right ventricular cardiomyopathy (ARVC) | Arrhythmogenic right ventricular cardiomyopathy (ARVC) is an...... Arrhythmogenic right ventricular cardiomyopathy (ARVC) is an inherited heart muscle disease that may result in arrhythmia, heart failure, and sudden death. The hallmark pathological findings are progressive myocyte loss and fibrofatty replacement, with a predilection for the right ventricle. A number of genetic studies have identified mutations in various components of the cardiac desmosome that have important roles in the pathogenesis of ARVD/C. Disruption of desmosomal function by defective proteins might lead to death of myocytes under mechanical stress. The myocardial injury may be accompanied by inflammation. Since regeneration of cardiac myocytes is limited, repair by fibrofatty replacement occurs. Several studies have implicated that desmosome dysfunction results in the delocalization and nuclear translocation of plakoglobin. As a result, competition between plakoglobin and beta-catenin will lead to the inhibition of Wnt/beta-catenin signaling, resulting in a shift from a myocyte fate towards an adipocyte fate of cells. The ryanodine receptor plays a crucial part in electromechanical coupling by control of release of calcium from the sarcoplasmic reticulum into the cytosol. Therefore, defects in this receptor could result in an imbalance of calcium homeostasis that might trigger cell death. More... | |
hsa04810 | regulation of_actin_cytoskeleton | Regulation of actin cytoskeleton | ||
hsa04512 | ecm receptor_interaction | ECM-receptor interaction | The extracellular matrix (ECM) consists of a complex mixture...... The extracellular matrix (ECM) consists of a complex mixture of structural and functional macromolecules and serves an important role in tissue and organ morphogenesis and in the maintenance of cell and tissue structure and function. Specific interactions between cells and the ECM are mediated by transmembrane molecules, mainly integrins and perhaps also proteoglycans, CD36, or other cell-surface-associated components. These interactions lead to a direct or indirect control of cellular activities such as adhesion, migration, differentiation, proliferation, and apoptosis. In addition, integrins function as mechanoreceptors and provide a force-transmitting physical link between the ECM and the cytoskeleton. Integrins are a family of glycosylated, heterodimeric transmembrane adhesion receptors that consist of noncovalently bound alpha- and beta-subunits. More... |
Gene mapped KEGG pathways | ||||
ID | Name | Brief Description | Full Description | |
---|---|---|---|---|
hsa05410 | hypertrophic cardiomyopathy_hcm | Hypertrophic cardiomyopathy (HCM) | Hypertrophic cardiomyopathy (HCM) is a primary myocardial di...... Hypertrophic cardiomyopathy (HCM) is a primary myocardial disorder with an autosomal dominant pattern of inheritance that is characterized by hypertrophy of the left ventricles with histological features of myocyte hypertrophy, myofibrillar disarray, and interstitial fibrosis. HCM is one of the most common inherited cardiac disorders, with a prevalence in young adults of 1 in 500. Hundreds of mutations in 11 genes that encode protein constituents of the sarcomere have been identified in HCM. These mutations increase the Ca2+ sensitivity of cardiac myofilaments. Increased myofilament Ca2+ sensitivity is expected to increase the ATP utilization by actomyosin at submaximal Ca2+ concentrations, which might cause an imbalance in energy supply and demand in the heart under severe stress. The inefficient use of ATP suggests that an inability to maintain normal ATP levels could be the central abnormality. This theory might be supported by the discovery of the role of a mutant PRKAG2 gene in HCM, which in active form acts as a central sensing mechanism protecting cells from depletion of ATP supplies. The increase in the myofilament Ca2+ sensitivity well account for the diastolic dysfunction of model animals as well as human patients of HCM. It has been widely proposed that left ventricular hypertrophy is not a primary manifestation but develops as compensatory response to sarcomere dysfunction. More... | |
hsa05414 | dilated cardiomyopathy | Dilated cardiomyopathy | Dilated cardiomyopathy (DCM) is a heart muscle disease chara...... Dilated cardiomyopathy (DCM) is a heart muscle disease characterised by dilation and impaired contraction of the left or both ventricles that results in progressive heart failure and sudden cardiac death from ventricular arrhythmia. Genetically inherited forms of DCM (familial DCM) have been identified in 25-35% of patients presenting with this disease, and the inherited gene defects are an important cause of familial DCM. The pathophysiology may be separated into two categories: defects in force generation and defects in force transmission. In cases where an underlying pathology cannot be identified, the patient is diagnosed with an idiopathic DCM. Current hypotheses regarding causes of idiopathic DCM focus on chronic viral myocarditis and/or on autoimmune abnormalities. Viral myocarditis may progress to an autoimmune phase and then to progressive cardiac dilatation. Antibodies to the beta1-adrenergic receptor (beta1AR), which are detected in a substantial number of patients with idiopathic DCM, may increase the concentration of intracellular cAMP and intracellular Ca2+, a condition often leading to a transient hyper-performance of the heart followed by depressed heart function and heart failure. More... |
Gene mapped Reactome pathways | |||
ID | Name | Description | |
---|---|---|---|
REACT_20558 | smooth muscle_contraction | Layers of smooth muscle cells can be found in the walls of n...... Layers of smooth muscle cells can be found in the walls of numerous organs and tissues within the body. Smooth muscle tissue lacks the striated banding pattern characteristic of skeletal and cardiac muscle. Smooth muscle is triggered to contract by the autonomic nervous system, hormones, autocrine/paracrine agents, local chemical signals, and changes in load or length. Actin:myosin cross bridging is used to develop force with the influx of calcium ions (Ca2+) initiating contraction. Two separate protein pathways, both triggered by calcium influx contribute to contraction, a calmodulin driven kinase pathway, and a caldesmon driven pathway. Recent evidence suggests that actin, myosin, and intermediate filaments may be far more volatile then previously suspected, and that changes in these cytoskeletal elements along with alterations of the focal adhesions that anchor these proteins may contribute to the contractile cycle. Contraction in smooth muscle generally uses a variant of the same sliding filament model found in striated muscle, except in smooth muscle the actin and myosin filaments are anchored to focal adhesions, and dense bodies, spread over the surface of the smooth muscle cell. When actin and myosin move across one another focal adhesions are drawn towards dense bodies, effectively squeezing the cell into a smaller conformation. The sliding is triggered by calcium:caldesmon binding, caldesmon acting in an analogous fashion to troponin in striated muscle. Phosphorylation of myosin light chains also is involved in the initiation of an effective contraction. More... | |
REACT_13552 | integrin cell_surface_interactions | The extracellular matrix (ECM) is a network of macro-molecul...... The extracellular matrix (ECM) is a network of macro-molecules that underlies all epithelia and endothelia and that surrounds all connective tissue cells. This matrix provides the mechanical strength and also influences the behavior and differentiation state of cells in contact with it. The ECM are diverse in composition, but they generally comprise a mixture of fibrillar proteins, polysaccharides synthesized, secreted and organized by neighboring cells. Collagens, fibronectin, and laminins are the principal components involved in cell matrix interactions; other components, such as vitronectin, thrombospondin, and osteopontin, although less abundant, are also important adhesive molecules. Integrins are the receptors that mediate cell adhesion to ECM. Integrins consists of one alpha and one beta subunit forming a noncovalently bound heterodimer. 18 alpha and 8 beta subunits have been identified in humans that combine to form 24 different receptors. The integrin dimers can be broadly divided into three families consisting of the beta1, beta2/beta7, and beta3/alphaV integrins. beta1 associates with 12 alpha-subunits and can be further divided into RGD-, collagen-, or laminin binding and the related alpha4/alpha9 integrins that recognise both matrix and vascular ligands. beta2/beta7 integrins are restricted to leukocytes and mediate cell-cell rather than cell-matrix interactions, although some recognize fibrinogen. The beta3/alphaV family members are all RGD receptors and comprise aIIbb3, an important receptor on platelets, and the remaining b-subunits, which all associate with alphaV. It is the collagen receptors and leukocyte-specific integrins that contain alpha A-domains. More... | |
REACT_17044 | muscle contraction |
ITGB5 related interactors from protein-protein interaction data in HPRD (count: 23)
Gene | Interactor | Interactor in MK4MDD? | Experiment Type | PMID | |
---|---|---|---|---|---|
ITGB5 | ZBTB17 | No | yeast 2-hybrid | 12356872 | |
ITGB5 | ITGB5 | Yes | in vitro | 12606711 | |
ITGB5 | DOK1 | No | in vitro | 12606711 | |
ITGB5 | FLNA | No | yeast 2-hybrid | 16355270 | |
ITGB5 | PAK4 | No | in vivo;yeast 2-hybrid | 12356872 | |
ITGB5 | NUMB | No | in vitro | 12606711 | |
ITGB5 | ITGA5 | No | in vitro;in vivo | 7592829 , 11462216 | |
ITGB5 | TENC1 | No | in vitro | 12606711 | |
ITGB5 | DAB2 | No | in vitro | 12606711 | |
ITGB5 | ITGB3BP | No | in vivo | 10579726 | |
ITGB5 | EPS8 | Yes | in vitro | 12606711 | |
ITGB5 | MYO10 | No | in vivo;yeast 2-hybrid | 15156152 | |
ITGB5 | PALLD | No | yeast 2-hybrid | 16355270 | |
ITGB5 | P2RY2 | No | in vitro;in vivo | 11331301 | |
ITGB5 | CYR61 | No | in vitro | 11287419 | |
ITGB5 | DAB1 | No | in vitro | 12606711 | |
ITGB5 | LTBP3 | No | in vitro;in vivo | 12358597 | |
ITGB5 | ANXA5 | No | in vitro | 12769841 | |
ITGB5 | LTBP1 | Yes | in vitro;in vivo | 12358597 | |
ITGB5 | GNB2L1 | No | in vitro;in vivo;yeast 2-hybrid | 9442085 | |
ITGB5 | FHL2 | No | yeast 2-hybrid | 16355270 | |
ITGB5 | TLN1 | No | in vitro | 12606711 | |
ITGB5 | ITGAV | No | in vitro | 7689573 |