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0EGF_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameEGF
DescriptionPro-epidermal growth factor precursor (egf) .
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005886 plasma membrane (TAS)
0005155 epidermal growth factor receptor activating... (TAS)
0000187 activation of MAPK activity (TAS)
0007001 chromosome organization and biogenesis (sen... (TAS)
0006260 DNA replication (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:
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 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 .
  IPR013091:EGF 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
The low-density lipoprotein receptor (LDLR) regulates cholesterol homeostasis in mammalian cells. LDLR binds cholesterol-carrying LDL.ssociates with clathrin-coated pits.nd is internalized into acidic endosomes where it separates from its ligand. The ligand is degraded in lysosomes.hile the receptor returns to the cell surface . The LDLR has several domains. The ligand-binding domain contains seven LDL receptor class A repeats.ach with three disulfide bonds and a coordinated Ca2+ ion. The second conserved region contains two EGF repeats.ollowed by six YWTD or LDL receptor class B repeats and another EGF repeat . This conserved region is critical for ligand release and recycling of the receptor . The structure of the six YWTD repeats of LDL receptor have been solved . The six YWTD repeats together fold into a six-bladed beta-propeller. Each blade of the propeller consists of four antiparallel beta-strands; the innermost strand of each blade is labeled 1 and the outermost strand.. The sequence repeats are offset with respect to the blades of the propeller.uch that any given 40-residue YWTD repeat spans strands 24 of one propeller blade and strand 1 of the subsequent blade. This offset ensures circularization of the propeller because the last strand of the final sequence repeat acts as an innermost strand 1 of the blade that harbors strands 24 from the first sequence repeat. The repeat is found in a variety of proteins that include.itellogenin receptor from Drosophila melanogaster.ow-density lipoprotein (LDL) receptor .reproepidermal growth factor.nd nidogen (entactin).
  IPR000033:Low-density lipoprotein receptor, YWTD repeat
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.
  IPR001336:EGF, type 1
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
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
IPR013091:EGF_CA 
Evalue:-13.7695512771606 
Location:870-910IPR000033:LY 
Evalue:-12.7958800173441 
Location:634-676IPR000033:LY 
Evalue:-11.4685210829577 
Location:547-589IPR000033:LY 
Evalue:-11.1938200260161 
Location:590-633IPR006209:EGF 
Evalue:-9.34678745269775 
Location:401-436IPR006209:EGF 
Evalue:-9.13076782226562 
Location:976-1012IPR006209:EGF 
Evalue:-7.85387182235718 
Location:835-868IPR001881:EGF_CA 
Evalue:-7.72124639904717 
Location:356-396IPR000033:LY 
Evalue:-7.2839966563652 
Location:504-546IPR013091:EGF_CA 
Evalue:-6.85387182235718 
Location:912-951IPR000033:LY 
Evalue:-6.31875876262441 
Location:677-718IPR006209:EGF 
Evalue:-5.16115093231201 
Location:745-780IPR006209:EGF 
Evalue:-5.00436496734619 
Location:318-354IPR000033:LY 
Evalue:-4.22184874961636 
Location:67-108IPR000033:LY 
Evalue:-2.29242982390206 
Location:151-192IPR000033:LY 
Evalue:-1.42021640338319 
Location:193-238IPR006210:EGF 
Evalue:-1.23657200643706 
Location:438-477IPR009030:Grow_fac_recept 
Evalue:0 
Location:20-39IPR000033:LY 
Evalue:0.7481880270062 
Location:110-150
SequencesProtein: EGF_HUMAN (1207 aa)
mRNA: NM_001963
Local Annotation
Synapse Ontology
?
sdb:0265 cAMP mediated STP  (Evidence:keywords)
KO assignmentK04357
  Level 3 annotation:
    epidermal growth factor
  Level 2 annotation:
    MAPK signaling pathway
    Cytokines
    Cytokine-cytokine receptor interaction
    Regulation of actin cytoskeleton
    Focal adhesion
    Gap junction
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 190 residues, 111053498-111054067Exon2: 68 residues, 111081550-111081750Exon3: 62 residues, 111083858-111084040Exon4: 78 residues, 111084446-111084674Exon5: 69 residues, 111085677-111085880Exon6: 44 residues, 111099916-111100042Exon7: 43 residues, 111101471-111101594Exon8: 43 residues, 111102467-111102590Exon9: 44 residues, 111103777-111103903Exon10: 47 residues, 111105005-111105142Exon11: 51 residues, 111109575-111109724Exon12: 37 residues, 111115307-111115412Exon13: 76 residues, 111116616-111116840Exon14: 58 residues, 111120576-111120744Exon15: 52 residues, 111121430-111121580Exon16: 42 residues, 111124026-111124146Exon17: 41 residues, 111128348-111128465Exon18: 44 residues, 111129188-111129314Exon19: 43 residues, 111133851-111133974Exon20: 51 residues, 111135337-111135485Exon21: 58 residues, 111140283-111140451Exon22: 41 residues, 111145109-111145227Exon23: 28 residues, 111148756-111148835Exon24: 356 residues, 111151806-111152868Exon25: 2 residues, -Jump to EGF_HUMAN  
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Loci Cluster (Details)Loci: 3424 111053498-111152868 ~-99K 28063(EGF)(+)Loci: 3423 110956114-110965340 ~-9K 28059(NOLA1)(+)Link out to UCSC