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InterPro: IPR006210 EGF-like
Protein matches
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UniProtKB Matches: 8827 proteins |
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Accession
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IPR006210 EGF-like |
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Secondary
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IPR000561
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Type
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Domain |
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Signatures
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InterPro Relationships
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Children
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IPR006209 EGF
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Found in
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IPR001438 EGF-like, type 2
IPR001881 EGF-like calcium-binding
IPR003056 GPCR, family 2, CD97 antigen
IPR009030 Growth factor, receptor
IPR010423 Plasmodium ookinete surface Pvs28
IPR011170 Growth factor, vaccinia C11R type
IPR012111 Hemolectin/hemocytin
IPR012224 Peptidase S1A, coagulation factor VII/IX/X/C/Z
IPR013091 EGF calcium-binding
IPR014394 Coagulation factor XII/hepatocyte growth factor activator
IPR015442 Integrin beta-8 subunit-like, C-terminal
IPR015447 Neurexin
IPR015497 Epidermal growth factor receptor ligand
IPR015781 Tyrosine-protein kinase, angiopoietin receptor
IPR017047 Teratocarcinoma-derived growth factor Cripto
IPR017048 Fibulin-1
IPR017369 SPAN protein/blastula protease 10
IPR017430 Glycoside hydrolase, family 56, Hyaluronidase
IPR018155 Hyaluronidase
IPR020696 Tyrosine-protein kinase, receptor Tie-1
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Contains
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IPR000152 EGF-type aspartate/asparagine hydroxylation site
IPR013032 EGF-like region, conserved site
IPR015149 Thrombomodulin-like, EGF-like
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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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 [1]. The repeating
pattern, especially of cysteines (the so-called EGF repeat), is thought to be important
to the 3D structure of the proteins, and 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,
particularly in extracellular proteins.
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Structural links
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Database links
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Interactions
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This domain has been experimentally proven to be involved in Protein:Protein interactions. Representative
data is shown with the following
example proteins:
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Example proteins
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O14944 Proepiregulin
O80977 Vacuolar-sorting receptor 3
P01132 Pro-epidermal growth factor
P07207 Neurogenic locus Notch protein
P14585 Protein lin-12
More proteins
Example Proteins Key
| InterPro entry accession number/name and structure databases |
Colour code |
| IPR013091 |
EGF calcium-binding |
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| IPR000800 |
Notch domain |
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| IPR006210 |
EGF-like |
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| IPR009030 |
Growth factor, receptor |
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| IPR008297 |
Notch |
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| IPR011656 |
Notch, NODP domain |
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| IPR013032 |
EGF-like region, conserved site |
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| IPR002110 |
Ankyrin repeat |
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| IPR018097 |
EGF-like calcium-binding, conserved site |
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| IPR003137 |
Protease-associated PA |
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| IPR016317 |
Pro-epidermal growth factor |
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| IPR001881 |
EGF-like calcium-binding |
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| IPR013111 |
EGF, extracellular |
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| IPR010660 |
Notch, NOD domain |
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| IPR020683 |
Ankyrin repeat-containing domain |
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| IPR011042 |
Six-bladed beta-propeller, TolB-like |
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| IPR000033 |
Low-density lipoprotein receptor, class B (YWTD) repeat |
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| IPR001438 |
EGF-like, type 2 |
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| IPR000152 |
EGF-type aspartate/asparagine hydroxylation site |
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| IPR000742 |
EGF-like, type 3 |
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| IPR001336 |
EGF, type 1 |
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| IPR006209 |
EGF |
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ModBase |
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SWISS-MODEL |
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PDB Chain |
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CATH Domain |
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SCOP Domain |
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Additional Reading
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Kwon HJ, Lagace TA, McNutt MC, Horton JD, Deisenhofer J.
Molecular basis for LDL receptor recognition by PCSK9.
Proc. Natl. Acad. Sci. U.S.A. 105 2008 1820-5
[PubMed: 18250299]
http://dx.doi.org/10.1073/pnas.0712064105
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Huai Q, Zhou A, Lin L, Mazar AP, Parry GC, Callahan J, Shaw DE, Furie B, Furie BC, Huang M.
Crystal structures of two human vitronectin, urokinase and urokinase receptor complexes.
Nat. Struct. Mol. Biol. 15 2008 422-3
[PubMed: 18376415]
http://dx.doi.org/10.1038/nsmb.1404
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Lee YK, Parks DJ, Lu T, Thieu TV, Markotan T, Pan W, McComsey DF, Milkiewicz KL, Crysler CS, Ninan N, Abad MC, Giardino EC, Maryanoff BE, Damiano BP, Player MR.
7-fluoroindazoles as potent and selective inhibitors of factor Xa.
J. Med. Chem. 51 2008 282-97
[PubMed: 18159923]
http://dx.doi.org/10.1021/jm701217r
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Baerga-Ortiz A, Bergqvist S, Mandell JG, Komives EA.
Two different proteins that compete for binding to thrombin have opposite kinetic and thermodynamic profiles.
Protein Sci. 13 2004 166-76
[PubMed: 14691232]
http://dx.doi.org/10.1110/ps.03120604
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Qiao JX, Cheney DL, Alexander RS, Smallwood AM, King SR, He K, Rendina AR, Luettgen JM, Knabb RM, Wexler RR, Lam PY.
Achieving structural diversity using the perpendicular conformation of alpha-substituted phenylcyclopropanes to mimic the bioactive conformation of ortho-substituted biphenyl P4 moieties: discovery of novel, highly potent inhibitors of Factor Xa.
Bioorg. Med. Chem. Lett. 18 2008 4118-23
[PubMed: 18550370]
http://dx.doi.org/10.1016/j.bmcl.2008.05.095
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Corte JR, Fang T, Pinto DJ, Han W, Hu Z, Jiang XJ, Li YL, Gauuan JF, Hadden M, Orton D, Rendina AR, Luettgen JM, Wong PC, He K, Morin PE, Chang CH, Cheney DL, Knabb RM, Wexler RR, Lam PY.
Structure-activity relationships of anthranilamide-based factor Xa inhibitors containing piperidinone and pyridinone P4 moieties.
Bioorg. Med. Chem. Lett. 18 2008 2845-9
[PubMed: 18424044]
http://dx.doi.org/10.1016/j.bmcl.2008.03.092
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