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0FINC_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameFN1
DescriptionFibronectin precursor (fn) (cold-insoluble globulin) (cig).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005578 extracellular matrix (sensu Metazoa) (NAS)
0005518 collagen binding (NAS)
0005201 extracellular matrix structural constituent (NAS)
0008201 heparin binding (NAS)
0007155 cell adhesion (NAS)
0016477 cell migration (NAS)
0009611 response to wounding (NAS)
0007169 transmembrane receptor protein tyrosine kin... (NAS)

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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:
Fibronectin is a multi-domain glycoprotein.ound in a soluble form in plasma.nd in an insoluble form in looseconnective tissue and basement membranes.hat binds cell surfaces and various compounds including collagen.ibrin.eparin.NA.nd actin. Fibronectins are involved in a number of important functions e.g..oundhealing; cell adhesion; blood coagulation; cell differentiation and migration; maintenance of the cellularcytoskeleton; and tumour metastasis . The major part of the sequence of fibronectin consists of therepetition of three types of domains.hich are called type I.I.nd III . Type II domain isapproximately forty residues long.ontains four conserved cysteines involved in disulphide bonds and is part ofthe collagen-binding region of fibronectin. In fibronectin the type II domain is duplicated. Type II domains havealso been found in a range of proteins including blood coagulation factor XII; bovine seminal plasma proteinsPDC-109 (BSP-A1/A2) and BSP-A3 ; cation-independent mannose-6-phosphate receptor ;mannose receptor of macrophages ; 180 Kd secretory phospholipase A2 receptor . DEC-205receptor ; 72 Kd and 92 Kd type IV collagenase () ; and hepatocytegrowth factor activator .
  IPR000562:Type II fibronectin, collagen-binding
Fibronectin type I repeats are one of the three repeats found in the fibronectin protein. Fibronectin is a plasma protein that binds cell surfaces and various compounds including collagen.ibrin.eparin.NA.nd actin. Type I domain (FN1) is approximately 40 residues in length. Four conserved cysteines are involved in disulphide bonds. The 3D structure of the FN1 domain has been determined . It consists of two antiparallel beta-sheets.irst a double-stranded one.hat is linked by a disulphide bond to a triple-stranded beta-sheet. The second conserved disulphide bridge links the C-terminal adjacent strands of the domain. In human tissue plasminogen activator chain A the FN1 domain together with the following epidermal growth factor (EGF)-like domain are involved in fibrin-binding . It has been suggested that these two modules form a single structural and functional unit . The two domains keep their specific tertiary structure.ut interact intimately to bury a hydrophobic core; the inter-module linker makes up the third strand of the EGF-modules major beta-sheet.
  IPR000083:Fibronectin, type I
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
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.
  IPR003962:Fibronectin, type III subdomain
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
This entry represents proteins displaying a Kringle-like structure.hich consists of a nearly all-beta.isulphide-rich fold. Proteins displaying this fold include both Kringle modules as well as fibronectin type II modules.he latter displaying a shorter two-disulphide version of the Kringle module. Kringle modules occur in blood clotting and fibrinolytic proteins.uch as plasminogen.rothrombin.eizothrombin.nd urokinase-type plasminogen activator.s well as in apolipoprotein and hepatocyte growth factor. Kringle domains are believed to play a role in binding mediators (e.g..embranes.ther proteins or phospholipids).nd in the regulation of proteolytic activity .Fibronectin type II modules occur in fibronectin.s well as in gelatinase A (MMP-2).elatinase B (MMP-9).nd the collagen-binding domain of PDC-109. Fibronectin is a multi-domain glycoprotein.ound in a soluble form in plasma.nd in an insoluble form in loose connective tissue and basement membranes.hat binds cell surfaces and various compounds including collagen.ibrin.eparin.NA.nd actin . 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. Gelatinases A and B are members of the matrix metalloproteinase family that act as neutral proteinases in the breakdown and remodelling of the extracellular matrix. These gelatinases play important roles in the pathogenesis of inflammation.nfection and in neoplastic diseases . In gelatinase A.he three fibronectin-like modules are inserted within a catalytic domain.hese modules acting to target the enzyme to matrix macromolecules .
  IPR013806:Kringle-like fold
IPR000562:FN2 
Evalue:-29.1674910872938 
Location:353-401IPR000562:FN2 
Evalue:-29.0915149811213 
Location:413-461IPR003961:fn3 
Evalue:-27.9208183288574 
Location:1448-1530IPR003961:fn3 
Evalue:-26.2291488647461 
Location:811-889IPR003961:fn3 
Evalue:-25.1487407684326 
Location:1903-1982IPR003961:fn3 
Evalue:-23.2518119812012 
Location:907-986IPR003961:fn3 
Evalue:-23.180456161499 
Location:1358-1437IPR003961:fn3 
Evalue:-22.7212467193604 
Location:1267-1347IPR003961:fn3 
Evalue:-22.5686359405518 
Location:1814-1892IPR003961:fn3 
Evalue:-22.408935546875 
Location:1542-1621IPR003961:fn3 
Evalue:-21.9208183288574 
Location:997-1075IPR003961:fn3 
Evalue:-21.1674919128418 
Location:1722-1801IPR000083:fn1 
Evalue:-20.8860569000244 
Location:186-225IPR000083:FN1 
Evalue:-20.5850266520292 
Location:2251-2293IPR003961:fn3 
Evalue:-20.0604801177979 
Location:1174-1256IPR000083:fn1 
Evalue:-20.0087738037109 
Location:2206-2245IPR000083:fn1 
Evalue:-19.8538722991943 
Location:470-508IPR000083:fn1 
Evalue:-19.8239078521729 
Location:231-270IPR000083:FN1 
Evalue:-19.0604807473814 
Location:141-184IPR000083:fn1 
Evalue:-18.9208183288574 
Location:97-135IPR000083:fn1 
Evalue:-18.1487407684326 
Location:561-599IPR000083:FN1 
Evalue:-17.0969100130081 
Location:518-560IPR000083:FN1 
Evalue:-16.7695510786217 
Location:52-92IPR003961:fn3 
Evalue:-16.6020603179932 
Location:1632-1711IPR003961:fn3 
Evalue:-16.0043640136719 
Location:720-800IPR000083:FN1 
Evalue:-15.5528419686578 
Location:2295-2335IPR003961:fn3 
Evalue:-14 
Location:608-688IPR000083:FN1 
Evalue:-12.6777807052661 
Location:308-347IPR003961:fn3 
Evalue:-7.85387182235718 
Location:1096-1162IPR003961:fn3 
Evalue:-7.38721609115601 
Location:2132-2181
SequencesProtein: FINC_HUMAN (2386 aa)
mRNA: NM_212482
Local Annotation
Synapse Ontology
?
sdb:0265 cAMP mediated STP  (Evidence:keywords)
the mechanism by which the restiong potential is held.
sdb:0288 maintain membrane potential  (Evidence:keywords)
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentK05717
  Level 3 annotation:
    fibronectin 1
  Level 2 annotation:
    ECM-receptor interaction
    CAM ligands
    Regulation of actin cytoskeleton
    Focal adhesion
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 390 residues, 215933425-215934594Exon2: 39 residues, 215934936-215935047Exon3: 37 residues, 215937846-215937953Exon4: 44 residues, 215938472-215938598Exon5: 57 residues, 215940830-215940995Exon6: 48 residues, 215943261-215943400Exon7: 157 residues, 215944876-215945343Exon8: 32 residues, 215946289-215946379Exon9: 62 residues, 215948181-215948361Exon10: 32 residues, 215948596-215948686Exon11: 61 residues, 215949465-215949642Exon12: 31 residues, 215951142-215951230Exon13: 64 residues, 215952097-215952285Exon14: 92 residues, 215953778-215954048Exon15: 40 residues, 215955179-215955293Exon16: 54 residues, 215956295-215956451Exon17: 57 residues, 215956987-215957152Exon18: 41 residues, 215957827-215957944Exon19: 92 residues, 215959656-215959926Exon20: 32 residues, 215961179-215961269Exon21: 63 residues, 215964599-215964782Exon22: 93 residues, 215965898-215966171Exon23: 66 residues, 215967495-215967687Exon24: 31 residues, 215970104-215970191Exon25: 58 residues, 215970647-215970816Exon26: 33 residues, 215972224-215972319Exon27: 91 residues, 215977356-215977623Exon28: 93 residues, 215979205-215979478Exon29: 67 residues, 215980094-215980289Exon30: 32 residues, 215981075-215981165Exon31: 45 residues, 215981265-215981394Exon32: 61 residues, 215982530-215982707Exon33: 62 residues, 215982901-215983082Exon34: 42 residues, 215987804-215987926Exon35: 50 residues, 215992209-215992353Exon36: 45 residues, 215993640-215993769Exon37: 53 residues, 215995058-215995211Exon38: 61 residues, 215996317-215996494Exon39: 62 residues, 215997113-215997293Exon40: 66 residues, 215998061-215998253Exon41: 55 residues, 216001147-216001306Exon42: 48 residues, 216003682-216003820Exon43: 46 residues, 216004800-216004932Exon44: 48 residues, 216006291-216006429Exon45: 45 residues, 216007663-216007792Exon46: 140 residues, 216008622-216009036Exon47: 2 residues, -Jump to FINC_HUMAN  
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