
Gene Report
Approved Symbol | COL1A1 |
---|---|
Approved Name | collagen, type I, alpha 1 |
Symbol Alias | OI4 |
Location | 17q21.33 |
Position | chr17:48278875-48279000 (-) |
External Links |
Entrez Gene: 1277 Ensembl: ENSG00000108821 UCSC: uc002iqm.3 HGNC ID: 2197 |
No. of Studies (Positive/Negative) | 1(1/0)
![]() |
Type | Literature-origin |
Genetic/epigenetic locus | Protein and other molecule | Cell and molecular pathway | Neural system | Cognition and behavior | Symptoms and signs | Environment | |||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
Network loading ...
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 |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
2. User can drag the nodes to rearrange the layout of the network. Click the node will enter the report page of the node. Right-click will show also the menus to link to the report page of the node and remove the node and related edges. Hover the node will show the level of the node and hover the edge will show the evidence/description of the edge.
3. The network is generated using Cytoscape Web

Gene mapped GO terms | ||||
ID | Name | Type | Evidence | |
---|---|---|---|---|
GO:0042542 | response to hydrogen peroxide | biological process | IEA | |
GO:0034504 | protein localization to nucleus | biological process | IDA[20018240] | |
GO:0071306 | cellular response to vitamin E | biological process | IEA | |
GO:0001957 | intramembranous ossification | biological process | IEA | |
GO:0044344 | cellular response to fibroblast growth factor stimulus | biological process | IEA | |
GO:0046872 | metal ion binding | molecular function | IEA | |
GO:0032355 | response to estradiol | biological process | IEA | |
GO:0060346 | bone trabecula formation | biological process | IEA | |
GO:0071364 | cellular response to epidermal growth factor stimulus | biological process | IEA | |
GO:0030198 | extracellular matrix organization | biological process | TAS | |
GO:0071560 | cellular response to transforming growth factor beta stimulus | biological process | IEA | |
GO:0048407 | platelet-derived growth factor binding | molecular function | IDA[8900172] | |
GO:0005515 | protein binding | molecular function | IPI[14749390|18375391|20015075] | |
GO:0090263 | positive regulation of canonical Wnt signaling pathway | biological process | IDA[20018240] | |
GO:0010718 | positive regulation of epithelial to mesenchymal transition | biological process | IDA[20018240] | |
GO:0005615 | extracellular space | cellular component | IDA[20551380] | |
GO:0005788 | endoplasmic reticulum lumen | cellular component | TAS | |
GO:0030141 | secretory granule | cellular component | IEA | |
GO:0051591 | response to cAMP | biological process | IEA | |
GO:0001568 | blood vessel development | biological process | IMP[17211858] | |
GO:0006898 | receptor-mediated endocytosis | biological process | TAS | |
GO:0071300 | cellular response to retinoic acid | biological process | IEA | |
GO:0043589 | skin morphogenesis | biological process | IMP[17211858] | |
GO:0001649 | osteoblast differentiation | biological process | IEA | |
GO:0010812 | negative regulation of cell-substrate adhesion | biological process | IEA | |
GO:0001958 | endochondral ossification | biological process | IEA | |
GO:0005794 | Golgi apparatus | cellular component | IEA | |
GO:0030199 | collagen fibril organization | biological process | IMP[14976317|15095409|17211858|18375391] | |
GO:1902618 | cellular response to fluoride | biological process | IEA | |
GO:0070208 | protein heterotrimerization | biological process | IEA | |
GO:0071356 | cellular response to tumor necrosis factor | biological process | IEA | |
GO:0071230 | cellular response to amino acid stimulus | biological process | IEA | |
GO:0042802 | identical protein binding | molecular function | IDA[17211858] | |
GO:0007605 | sensory perception of sound | biological process | IMP[17489845] | |
GO:0007596 | blood coagulation | biological process | TAS | |
GO:0055093 | response to hyperoxia | biological process | IEA | |
GO:0050776 | regulation of immune response | biological process | TAS | |
GO:0050900 | leukocyte migration | biological process | TAS | |
GO:0060351 | cartilage development involved in endochondral bone morphogenesis | biological process | IEA | |
GO:0032964 | collagen biosynthetic process | biological process | IMP[15095409] | |
GO:0001501 | skeletal system development | biological process | IMP[1874719|8097422|14976317] | |
GO:0005201 | extracellular matrix structural constituent | molecular function | IEA | |
GO:0005584 | collagen type I trimer | cellular component | IMP[14976317|17576241] | |
GO:0007601 | visual perception | biological process | IMP[17557158] | |
GO:0048706 | embryonic skeletal system development | biological process | IMP[18553566] | |
GO:0045893 | positive regulation of transcription, DNA-templated | biological process | IDA[20018240] | |
GO:0015031 | protein transport | biological process | IEA | |
GO:0005576 | extracellular region | cellular component | TAS | |
GO:0034505 | tooth mineralization | biological process | IMP[17118335] | |
GO:0031012 | extracellular matrix | cellular component | IDA[23658023]; IDA[20551380]; ISS[22261194] | |
GO:0030168 | platelet activation | biological process | TAS | |
GO:0022617 | extracellular matrix disassembly | biological process | TAS | |
GO:0030335 | positive regulation of cell migration | biological process | IDA[20018240] | |
GO:0042493 | response to drug | biological process | IEA | |
GO:0071260 | cellular response to mechanical stimulus | biological process | IEA | |
GO:0043434 | response to peptide hormone | biological process | IEA | |
GO:0044691 | tooth eruption | biological process | IEA | |
GO:0031960 | response to corticosteroid | biological process | IEA | |
GO:0030574 | collagen catabolic process | biological process | TAS | |
GO:0060325 | face morphogenesis | biological process | IEA |
Literature-origin KEGG pathway | ||||
ID | Name | Brief Description | Full Description | |
---|---|---|---|---|
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... | |
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... |
Gene mapped KEGG pathways | ||||
ID | Name | Brief Description | Full Description |
---|
Gene mapped Reactome pathways | |||
ID | Name | Description | |
---|---|---|---|
REACT_18334 | ncam signaling_for_neurite_out_growth | The neural cell adhesion molecule, NCAM, is a member of the ...... The neural cell adhesion molecule, NCAM, is a member of the immunoglobulin (Ig) superfamily and is involved in a variety of cellular processes of importance for the formation and maintenance of the nervous system. The role of NCAM in neural differentiation and synaptic plasticity is presumed to depend on the modulation of intracellular signal transduction cascades. NCAM based signaling complexes can initiate downstream intracellular signals by at least two mechanisms: (1) activation of FGFR and (2) formation of intracellular signaling complexes by direct interaction with cytoplasmic interaction partners such as Fyn and FAK. Tyrosine kinases Fyn and FAK interact with NCAM and undergo phosphorylation and this transiently activates the MAPK, ERK 1 and 2, cAMP response element binding protein (CREB) and transcription factors ELK and NFkB. CREB activates transcription of genes which are important for axonal growth, survival, and synaptic plasticity in neurons. NCAM1 mediated intracellular signal transduction is represented in the figure below. The Ig domains in NCAM1 are represented in orange ovals and Fn domains in green squares. The tyrosine residues susceptible to phosphorylation are represented in red circles and their positions are numbered. Phosphorylation is represented by red arrows and dephosphorylation by yellow. Ig, Immunoglobulin domain; Fn, Fibronectin domain; Fyn, Proto-oncogene tyrosine-protein kinase Fyn; FAK, focal adhesion kinase; RPTPalpha, Receptor-type tyrosine-protein phosphatase; Grb2, Growth factor receptor-bound protein 2; SOS, Son of sevenless homolog; Raf, RAF proto-oncogene serine/threonine-protein kinase; MEK, MAPK and ERK kinase; ERK, Extracellular signal-regulated kinase; MSK1, Mitogen and stress activated protein kinase 1; CREB, Cyclic AMP-responsive element-binding protein; CRE, cAMP response elements. More... | |
REACT_20 | formation of_platelet_plug | Hemostasis is a physiological response that culminates in th...... Hemostasis is a physiological response that culminates in the arrest of bleeding from an injured vessel. Acute vessel injury results in its constriction to reduce the loss of blood. Under normal conditions vascular endothelium supports vasodilation, inhibits platelet adhesion and activation, suppresses coagulation, enhances fibrin cleavage and is anti-inflammatory in character. Under acute vascular trauma vasoconstrictor mechanisms predominate and the endothelium becomes prothrombotic, procoagulatory and proinflammatory in nature. This is achieved by a reduction of endothelial dilating agents: adenosine, NO and prostacyclin; and the direct action of ADP, serotonin and thromboxane on vascular smooth muscle cells to elicit their contraction. The chief trigger for the change in endothelial function that leads to the formation of haemostatic thrombus is the loss of the endothelial cell barrier between blood and ECM components. Circulating platelets identify and discriminate areas of endothelial lesions; here, they adhere to the exposed sub endothelium. Their interaction with the various thrombogenic substrates and locally generated or released agonists results in platelet activation. This process is described as possessing two stages, firstly, adhesion - the initial tethering to a surface, and secondly aggregation - the platelet-platelet cohesion. More... | |
REACT_18312 | ncam1 interactions | The neural cell adhesion molecule, NCAM1 is generally consid...... The neural cell adhesion molecule, NCAM1 is generally considered as a cell adhesion mediator, but it is also considered to be a signal transducing receptor molecule. NCAM1 is involved in multiple cis- and trans-homophilic interactions. It is also involved in several heterophilic interactions with a broad range of other molecules, thereby modulating diverse biological phenomena including cellular adhesion, migration, proliferation, differentiation, survival and synaptic plasticity. More... | |
REACT_798 | platelet activation | Platelet activation begins with the initial binding of adhes...... Platelet activation begins with the initial binding of adhesive ligands and of the excitatory platelet agonists. Intracellular signaling reactions will then enhance the adhesive and procoagulant properties of tethered platelets or of platelets circulating in the proximity. From the subendothelial adhesive substrates, collagen and possibly vWF are the main inducers of platelet activation. GP VI is the most potent collagen receptor initiating signal generation, an ability derived from its interaction with the FcRI gamma chain. This results in the phosphorylation of the gamma-chain by the non-receptor tyrosine kinases of the Src family. The phosphotyrosine motif is recognized by the SH2 domains of Syk, a tyrosine kinase. This association activates the Syk enzyme, leading to activation. Four PARs are identified, of which PARs 1 ,3 and 4 are substrates for thrombin. PAR 1 is the predominant thrombin receptor, PAR 3 is minimally expressed and PAR 4 is less responsive to thrombin. Platelets do not store PAR1, due to limited protein synthesis, they are capable of responding to thrombin only once. Platelet activation further results in the scramblase-mediated transport of negatively-charged phospholipids to the platelet surface. These phospholipids provide a catalytic surface (with the charge provided by phosphatidylserine and phosphatidylethanolamine) for the tenase complex (formed by the activated forms of the blood coagulation factors factor VIII and factor I). More... | |
REACT_622 | platelet activation_triggers | In the initial response to injury, platelets adhere to damag...... In the initial response to injury, platelets adhere to damaged blood vessels, responding to the exposure of collagen from the vascular epithelium. Once adhered they degranulate, releasing agents such as serotonin and ADP and synthesize Thromboxane A2, all of which amplify the response, recruiting further platelets to the area and promoting platelet aggregation. More... | |
REACT_16888 | signaling by_pdgf | Platelet-derived Growth Factor (PDGF) is a potent stimulator...... Platelet-derived Growth Factor (PDGF) is a potent stimulator of growth and motility of connective tissue cells such as fibroblasts and smooth muscle cells as well as other cells such as capillary endothelial cells and neurons.The PDGF family of growth factors is composed of four different polypeptide chains encoded by four different genes. The classical PDGF chains, PDGF-A and PDGF-B, and more recently discovered PDGF-C and PDGF-D. The four PDGF chains assemble into disulphide-bonded dimers via homo- or heterodimerization, and five different dimeric isoforms have been described so far; PDGF-AA, PDGF-AB, PDGF-BB, PDGF-CC and PDGF-DD. It is notable that no heterodimers involving PDGF-C and PDGF-D chains have been described. PDGF exerts its effects by binding to, and activating, two protein tyrosine kinase (PTK) receptors, alpha and beta. These receptors dimerize and undergo autophosphorylation. The phosphorylation sites then attract downstream effectors to transduct the signal into the cell. More... | |
REACT_1695 | collagen mediated_activation_cascade | The GPVI receptor is a complex of the GPVI protein with Fc e...... The GPVI receptor is a complex of the GPVI protein with Fc epsilon R1 gamma (FcR). The Src family kinases Fyn and Lyn constitutively associate with the GPVI-FcR complex in platelets and initiate platelet activation through phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) in the FcR gamma chain, leading to binding and activation of the tyrosine kinase Syk. Downstream of Syk, a series of adapter molecules and effectors lead to platelet activation. The GPVI receptor signaling cascade is similar to that of T- and B-cell immune receptors, involving the formation of a signalosome composed of adapter and effector proteins. At the core of the T-cell receptor signalosome is the transmembrane adapter LAT and two cytosolic adapters SLP-76 and Gads. While LAT is essential for signalling to PLCgamma1 downstream of the T-cell receptor, the absence of LAT in platelets only impairs the activation of PLCgamma2, the response to collagen and GPVI receptor ligands remains sufficient to elicit a full aggregation response. In contrast, GPVI signalling is almost entirely abolished in the absence of SLP-76. More... | |
REACT_6900 | signaling in_immune_system | Humans are exposed to millions of potential pathogens daily,...... Humans are exposed to millions of potential pathogens daily, through contact, ingestion, and inhalation. Our ability to avoid infection depends on the adaptive immune system and during the first critical hours and days of exposure to a new pathogen, our innate immune system. More... | |
REACT_1230 | platelet adhesion_to_exposed_collagen | Initiation is the first step in the formation of the platele...... Initiation is the first step in the formation of the platelet plug. This occurs whenever circulating platelets are arrested and subsequently activated by exposed collagen and vWF. Several collagen binding proteins are expressed on platelets, including integrin Alpha2 Beta1, GP VI, and GP IV. Integrin Alpha2 Beta1, also known on leukocytes as VLA-2, is the major collagen receptor. It requires Mg2+ for interacting with collagen. Binding occurs via the alpha2 subunit I domain to a collagen motif with the sequence Gly-Phe-Hyp-Gly-Glu-Arg. Binding of collagen to Alpha2 Beta1 also generates the intracellular signals that contribute to platelet activation. These facilitate the engagement of the lower-affinity collagen receptor, GP VI. The second platelet receptor for collagen is GP VI. This is part of the immunoglobulin superfamily and is the most potent receptor that generates intracellular signals. Its signaling ability is strictly dependent on its association with the Fc receptor epsilon chain, which contains Immunoreceptor Tyrosine-based Activation Motifs (ITAM). GP VI is the key player in collagen-induced platelet activation. vWF protein is a polymeric structure of variable size. It is secreted in two directions by the endothelium - basolaterally and into the bloodstream. Shear-induced aggregation is achieved when vWF binds via its A1 domain to GPIb (part of GPIb - IX - V), and via its A3 domain mediating collagen binding to the subendothelium. The interaction between vWF and GPIb is regulated by shear force, an increase in the shear stress results in a corresponding increase in the affinity of vWF for GPIb. More... | |
REACT_12051 | cell surface_interactions_at_the_vascular_wall | Leukocyte extravasation is a rigorously controlled process t...... Leukocyte extravasation is a rigorously controlled process that guides white cell movement from the vascular lumen to sites of tissue inflammation. The powerful adhesive interactions that are required for leukocytes to withstand local flow at the vessel wall is a multistep process mediated by different adhesion molecules. Platelets adhered to injured vessel walls form strong adhesive substrates for leukocytes. For instance, the initial tethering and rolling of leukocytes over the site of injury are mediated by reversible binding of selectins to their cognate cell-surface glycoconjugates. Endothelial cells are tightly connected through various proteins, which regulate the organization of the junctional complex and bind to cytoskeletal proteins or cytoplasmic interaction partners that allow the transfer of intracellular signals. An important role for these junctional proteins in governing the transendothelial migration of leukocytes under normal or inflammatory conditions has been established. This pathway describes some of the key interactions that assist in the process of platelet and leukocyte interaction with the endothelium, in response to injury. More... | |
REACT_604 | hemostasis | Two principal mechanisms limit blood loss after vascular inj...... Two principal mechanisms limit blood loss after vascular injury. Initially, platelets are activated, adhere to the site of the injury, and aggregate into a plug that limits blood loss. Proteins and small molecules released from activated platelets stimulate the plug formation process, and fibrinogen from the plasma forms bridges between activated platelets. These events allow the initiation of the clotting cascade, the second mechanism to limit blood loss. Negatively charged phospholipids exposed on cell surfaces at the site of injury and on activated platelets interact with tissue factor, setting off a cascade of reactions leading to generation of fibrin and the formation of an insoluble fibrin clot that strengthens the platelet plug. More... | |
REACT_18266 | axon guidance | Axon guidance / axon pathfinding is the process by which neu...... Axon guidance / axon pathfinding is the process by which neurons send out axons to reach the correct targets. Growing axons have a highly motile structure at the growing tip called the growth cone, which senses the guidance cues in the environment through guidance cue receptors and responds by undergoing cytoskeletal changes that determine the direction of axon growth. Guidance cues present in the surrounding environment provide the necessary directional information for the trip. These extrinsic cues have been divided into attractive or repulsive signals that tell the growth cone where and where not to grow. Genetic and biochemical studies have led to the identification of highly conserved families of guidance molecules and their receptors that guide axons. These include netrins, Slits, semaphorins, and ephrins, and their cognate receptors, DCC and or uncoordinated-5 (UNC5), roundabouts (Robo), neuropilin and Eph. In addition, many other classes of adhesion molecules are also used by growth cones to navigate properly which include NCAM and L1CAM. 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... |

Gene | Interactor | Interactor in MK4MDD? | Experiment Type | PMID | |
---|---|---|---|---|---|
COL1A1 | MMP2 | No | in vitro | 11368514 | |
COL1A1 | CD93 | No | in vitro | 1377218 | |
COL1A1 | PRELP | No | in vitro | 11847210 | |
COL1A1 | TMPRSS6 | No | in vitro | 12149247 | |
COL1A1 | VWF | No | in vitro | 3490481 | |
COL1A1 | CAPN1 | No | yeast 2-hybrid | 12358155 | |
COL1A1 | BGN | No | in vitro | 7852349 | |
COL1A1 | CD44 | No | in vitro | 1730778 | |
COL1A1 | FGF7 | No | in vitro | 11973338 | |
COL1A1 | PAK1 | No | in vitro | 10772928 | |
COL1A1 | PDGFB | No | in vitro | 10446987 | |
COL1A1 | FN1 | No | in vivo | 8468356 | |
COL1A1 | DDR2 | No | in vitro | 9659899 | |
COL1A1 | TGFBI | No | in vitro | 12034705 , 11867580 | |
COL1A1 | ITGA2 | No | in vitro;in vivo | 11359786 , 11856343 , 2156854 | |
COL1A1 | MMP9 | No | in vivo | 9878537 | |
COL1A1 | COL7A1 | No | in vitro | 9169408 | |
COL1A1 | IGFBP3 | No | in vitro;in vivo;yeast 2-hybrid | 12735930 | |
COL1A1 | NID1 | No | in vitro | 9733643 | |
COL1A1 | SPARC | No | in vitro | 7034958 | |
COL1A1 | CD36 | No | in vitro | 2468670 | |
COL1A1 | THBS1 | No | in vitro | 3571333 | |
COL1A1 | DCN | No | in vitro | 9675033 , 1468447 | |
COL1A1 | BMP1 | No | in vivo | 11283002 | |
COL1A1 | HTRA1 | No | yeast 2-hybrid | 15101818 | |
COL1A1 | TXN | No | in vitro;yeast 2-hybrid | 12099690 | |
COL1A1 | ITGA5 | No | in vitro;in vivo | 1693626 | |
COL1A1 | MATN2 | No | in vitro;in vivo | 12180907 | |
COL1A1 | P4HB | No | in vitro | 1339453 |