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0CRUM1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCRB1
DescriptionCrumbs protein homolog 1 precursor.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0007267 cell-cell signaling (TAS)
0007163 establishment and/or maintenance of cell po... (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 assigned to SynO:
Laminins are large heterotrimeric glycoproteins involved in basement membrane function . The laminin globular (G) domain can be found in one to several copies in various laminin family members.ncluding a large number of extracellular proteins. The C-terminus of the laminin alpha chain contains a tandem repeat of five laminin G domains.hich are critical for heparin-binding and cell attachment activity . Laminin alpha4 is distributed in a variety of tissues including peripheral nerves.orsal root ganglion.keletal muscle and capillaries; in the neuromuscular junction.t is required for synaptic specialisation . The structure of the laminin-G domain has been predicted to resemble that of pentraxin .Laminin G domains can vary in their function.nd a variety of binding functions have been ascribed to different LamG modules. For example.he laminin alpha1 and alpha2 chains each have five C-teminal laminin G domains.here only domains LG4 and LG5 contain binding sites for heparin.ulphatides and the cell surface receptor dystroglycan . Laminin G-containing proteins appear to have a wide variety of roles in cell adhesion.ignalling.igration.ssembly and differentiation. Proteins with laminin-G domains include:Laminin.Merosin.Agrin.Neurexins.Vitamin K dependent protein S.Sex steroid binding protein SBP/SHBG.Drosophila proteins Slit.rumbs.at.several proteoglycan precursors.
  IPR001791:Laminin G
InterPro domains unassigned to SynO:
Laminins are large heterotrimeric glycoproteins involved in basement membrane function . The laminin globular (G) domain can be found in one to several copies in various laminin family members.ncluding a large number of extracellular proteins. The C-terminus of the laminin alpha chain contains a tandem repeat of five laminin G domains.hich are critical for heparin-binding and cell attachment activity . Laminin alpha4 is distributed in a variety of tissues including peripheral nerves.orsal root ganglion.keletal muscle and capillaries; in the neuromuscular junction.t is required for synaptic specialisation . The structure of the laminin-G domain has been predicted to resemble that of pentraxin . Laminin G domains can vary in their function.nd a variety of binding functions have been ascribed to different LamG modules. For example.he laminin alpha1 and alpha2 chains each have five C-teminal laminin G domains.here only domains LG4 and LG5 contain binding sites for heparin.ulphatides and the cell surface receptor dystroglycan . Laminin G-containing proteins appear to have a wide variety of roles in cell adhesion.ignalling.igration.ssembly and differentiation. This entry represents one subtype of laminin G domains.hich is sometimes found in association with thrombospondin-type laminin G domains ().
  IPR012680:Laminin G, subdomain 2
A sequence of about forty amino-acid residues found in epidermal growth factor (EGF) has been shown .o be present in a large number of membrane-bound and extracellular.ostly animal.roteins. Many of these proteins require calcium for their biological function and a calcium-binding site has been found at the N-terminus of some EGF-like domains . Calcium-binding may be crucial for numerous protein-protein interactions.For human coagulation factor IX it has been shown that the calcium-ligands form a pentagonal bipyramid. The first.hird and fourth conserved negatively charged or polar residues are side chain ligands. The latter is possibly hydroxylated (see aspartic acid and asparagine hydroxylation site) . A conserved aromatic residue.s well as the second conserved negative residue.re thought to be involved in stabilizing the calcium-binding site.As in non-calcium binding EGF-like domains.here are six conserved cysteines and the structure of both types is very similar as calcium-binding induces only strictly local structural changes .
  IPR001881:EGF-like calcium-binding
A sequence of about thirty to forty amino-acid residues long found in the sequence of epidermal growth factor (EGF)has been shown to be present.n a moreor less conserved form.n a large number of other.ostly animal proteins. The list of proteins currently known tocontain one or more copies of an EGF-like pattern is large and varied. The functional significance of EGF domains inwhat appear to be unrelated proteins is not yet clear. However. common feature is that these repeats are found inthe extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandinG/H synthase). The EGF domain includes six cysteine residues which have been shown (in EGF) to be involved in disulphidebonds. The main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet.Subdomains between the conserved cysteines vary in length.
  IPR006209:EGF-like
Epidermal growth factors and transforming growth factors belong to a general class of proteins that share a repeat pattern involving a number of conserved Cys residues. Growth factors are involved in cell recognition and division . The repeating pattern.specially of cysteines (the so-called EGF repeat).s thought to be important to the 3D structure of the proteins.nd hence its recognition by receptors and other molecules. The type 1 EGF signature includes six conserved cysteines believed to be involved in disulphide bond formation. The EGF motif is found frequently in nature.articularly in extracellular proteins.
  IPR006210:EGF
EGF-like repeats occur in coagulation factors.otch and xotch proteins.rotein Z.rokinases.lasminogen factors and the lin-12 protein . The repeat pattern is EGF-like in the sense that it does not share the exact Cys spacings of the type I EGF motif. The primary structures of many of the superfamily members contain regions that are dominated by multiple EGF-like repeats: these have been linked to some physiological role.hough the precise nature of this role is as yet unclear.The type II EGF-like signature is found in a variety of proteins having different functions and from a variety of sources.
  IPR001438:EGF-like, type 2
Lectins and glucanases exhibit the common property of reversibly binding to specific complex carbohydrates. The lectins/glucanases are a diverse group of proteins found in a wide range of species from prokaryotes to humans. The different family members all contain a concanavalin A-like domain.hich consists of a sandwich of 12-14 beta strands in two sheets with a complex topology. Members of this family are diverse.nd include the lectins: legume lectins.ereal lectins.iral lectins.nd animal lectins. Plant lectins function in the storage and transport of carbohydrates in seeds.he binding of nitrogen-fixing bacteria to root hairs.he inhibition of fungal growth or insect feeding.nd in hormonally regulated plant growth . Protein members include concanavalin A (Con A).avin.solectin I.ectin IV.oybean agglutinin and lentil lectin. Animal lectins include the galectins.hich are S-type lactose-binding and IgE-binding proteins such as S-lectin.LC protein.alectin1.alectin2.alectin3 CRD.nd Congerin I . Other members with a Con A-like domain include the glucanases and xylanases. Bacterial and fungal beta-glucanases.uch as Bacillus 1-3.-4-beta-glucanse.arry out the acid catalysis of beta-glucans found in microorganisms and plants . Similarly.appa-Carrageenase degrades kappa-carrageenans from marine red algae cell walls . Xylanase and cellobiohydrolase I degrade hemicellulose and cellulose.espectively . There are many Con A-like domains found in proteins involved in cell recognition and adhesion. For example.everal viral and bacterial toxins carry Con A-like domains. Examples include the Clostridium neurotoxins responsible for the neuroparalytic effects of botulism and tetanus . The Pseudomonas exotoxin A. virulence factor which is highly toxic to eukaryotic cells.ausing the arrest of protein synthesis.ontains a Con A-like domain involved in receptor binding . Cholerae neuraminidase can bind to cell surfaces.ossibly through their Con A-like domains.here they function as part of a mucinase complex to degrade the mucin layer of the gastrointestinal tract . The rotaviral outer capsid protein.P4.as a Con A-like sialic acid binding domain.hich functions in cell attachment and membrane penetration . Con A-like domains also play a role in cell recognition in eukaryotes. Proteins containing a Con A-like domain include the sex hormone-binding globulins which transport sex steroids in blood and regulate their access to target tissues .aminins which are large heterotrimeric glycoproteins involved in basement membrane architecture and function .eurexins which are expressed in hundreds of isoforms on the neuronal cell surface.here they may function as cell recognition molecules and sialidases that are found in both microorganisms and animals.nd function in cell adhesion and signal transduction . Other proteins containing a Con A-like domain include pentraxins and calnexins. The pentraxin PTX3 is a TNFalpha-induced.ecreted protein of adipose cells produced during inflammation . The calnexin family of molecular chaperones is conserved among plants.ungi.nd animals. Family members include Calnexin. type-I integral membrane protein in the endoplasmic reticulum which coordinates the processing of newly synthesized N-linked glycoproteins with their productive folding.almegin. type-I membrane protein expressed mainly in the spermatids of the testis.nd calreticulin. soluble ER lumenal paralog .
  IPR008985:Concanavalin A-like lectin/glucanase
Lectins and glucanases exhibit the common property of reversibly binding to specific complex carbohydrates. The lectins/glucanases are a diverse group of proteins found in a wide range of species from prokaryotes to humans. The different family members all contain a concanavalin A-like domain.hich consists of a sandwich of 12-14 beta strands in two sheets with a complex topology. Members of this family are diverse.nd include the lectins: legume lectins.ereal lectins.iral lectins.nd animal lectins. Plant lectins function in the storage and transport of carbohydrates in seeds.he binding of nitrogen-fixing bacteria to root hairs.he inhibition of fungal growth or insect feeding.nd in hormonally regulated plant growth . Protein members include concanavalin A (Con A).avin.solectin I.ectin IV.oybean agglutinin and lentil lectin. Animal lectins include the galectins.hich are S-type lactose-binding and IgE-binding proteins such as S-lectin.LC protein.alectin1.alectin2.alectin3 CRD.nd Congerin I . Other members with a Con A-like domain include the glucanases. Bacterial and fungal beta-glucanases.uch as Bacillus 1-3.-4-beta-glucanse.arry out the acid catalysis of beta-glucans found in microorganisms and plants . Similarly.appa-Carrageenase degrades kappa-carrageenans from marine red algae cell walls . This entry differs from () by omitting the xylanases and glycosyl hydrolases.
  IPR013320:Concanavalin A-like lectin/glucanase, subgroup
IPR012680:Laminin_G_2 
Evalue:-25.2291488647461 
Location:514-651IPR012680:Laminin_G_2 
Evalue:-23.3187580108643 
Location:980-1105IPR012680:Laminin_G_2 
Evalue:-21.7212467193604 
Location:743-860IPR001881:EGF_CA 
Evalue:-11.7447274948967 
Location:224-260IPR006209:EGF 
Evalue:-10.6197891235352 
Location:152-183IPR006209:EGF 
Evalue:-9.92081832885742 
Location:190-221IPR006209:EGF 
Evalue:-9.43179798126221 
Location:676-707IPR006209:EGF 
Evalue:-9.35654735565185 
Location:1143-1174IPR006209:EGF 
Evalue:-9.18045616149902 
Location:74-107IPR006209:EGF 
Evalue:-8.53760242462158 
Location:343-394IPR006209:EGF 
Evalue:-8.50863838195801 
Location:891-922IPR006209:EGF 
Evalue:-8.408935546875 
Location:1301-1332IPR001881:EGF_CA 
Evalue:-8.36653154442041 
Location:1177-1212IPR006209:EGF 
Evalue:-8.11350917816162 
Location:445-480IPR006209:EGF 
Evalue:-7.72124624252319 
Location:305-336IPR006209:EGF 
Evalue:-7.44369745254517 
Location:114-145IPR001881:EGF_CA 
Evalue:-7.05551732784983 
Location:262-299IPR001881:EGF_CA 
Evalue:-6.85387196432176 
Location:397-439IPR006209:EGF 
Evalue:-5.46852111816406 
Location:1218-1249IPR006210:EGF 
Evalue:-0.677780705266081 
Location:1258-1295IPR000742:EGF_3 
Evalue:0 
Location:30-68IPR000742:EGF_3 
Evalue:0 
Location:924-960
SequencesProtein: CRUM1_HUMAN (1406 aa)
mRNA: NM_012076 NM_201253
Local Annotation
Synapse Ontology
A neuromuscular junction is the junction of the axon terminal of a motoneuron with the motor end plate, the highly-excitable region of muscle fiber plasma membrane responsible for initiation of action potentials across the muscle's surface.
sdb:0024 neuromuscular junction  (Evidence:keywords,domains)
the mechanism by which the restiong potential is held.
sdb:0288 maintain membrane potential  (Evidence:keywords,domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 69 residues, 195504030-195504235Exon2: 196 residues, 195564174-195564756Exon3: 67 residues, 195580033-195580229Exon4: 48 residues, 195583092-195583232Exon5: 63 residues, 195592583-195592766Exon6: 321 residues, 195656752-195657709Exon7: 184 residues, 195663206-195663754Exon8: 57 residues, 195665201-195665367Exon9: 304 residues, 195670458-195671365Exon10: 45 residues, 195674299-195674428Exon11: 44 residues, 195677918-195678045Exon12: 265 residues, 195713416-195714207Exon13: 2 residues, -Jump to CRUM1_HUMANExon1: 69 residues, 195504030-195504235Exon2: 196 residues, 195564174-195564756Exon3: 67 residues, 195580033-195580229Exon4: 48 residues, 195583092-195583232Exon5: 63 residues, 195592583-195592766Exon6: 321 residues, 195656752-195657709Exon7: 184 residues, 195663206-195663754Exon8: 57 residues, 195665201-195665367Exon9: 304 residues, 195670458-195671365Exon10: 45 residues, 195674299-195674428Exon11: 125 residues, 195677918-195678287Exon12: 265 residues, 195713416-195714207Exon13: 2 residues, -Jump to CRUM1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2578 195504030-195714207 ~-210K 3598(CRB1)(+)Loci: 3856 195320076-195382190 ~-62K 3592(ASPM)(-)Link out to UCSC