PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2698313-4 1989 The cDNA sequence indicated the presence of a Gly-Arg-Gly-Asp-Ser- (GRGDS) amino acid sequence identical to a cell binding sequence in fibronectin, and suggested that osteopontin might function as a cell attachment factor. Aspartic Acid 58-61 secreted phosphoprotein 1 Homo sapiens 167-178 33255056-2 2021 The arginine-glycine-aspartic acid (RGD) sequence is present in several ECM proteins, such as fibronectin, collagen type I, fibrinogen, laminin, vitronectin, and osteopontin. Aspartic Acid 21-34 secreted phosphoprotein 1 Homo sapiens 162-173 18228204-13 2008 NOR proteins and osteopontin are proteins containing aspartic acid rich regions that can bind Ag. Aspartic Acid 53-66 secreted phosphoprotein 1 Homo sapiens 17-28 30003880-1 2018 Osteopontin (OPN) is a highly phosphorylated glycophosphoprotein having acidic characteristics and rich in aspartic acid. Aspartic Acid 107-120 secreted phosphoprotein 1 Homo sapiens 0-11 30003880-1 2018 Osteopontin (OPN) is a highly phosphorylated glycophosphoprotein having acidic characteristics and rich in aspartic acid. Aspartic Acid 107-120 secreted phosphoprotein 1 Homo sapiens 13-16 24129963-6 2014 OPN has an arginine-glycine-aspartic acid (RGD) motif, and protease cleavage reveals a SVVYGLR motif. Aspartic Acid 28-41 secreted phosphoprotein 1 Homo sapiens 0-3 25419572-2 2014 OPN primarily exerts its functions through interaction with integrins via the Arg-Gly-Asp and Ser-Val-Val-Tyr-Gly-Leu-Arg sequences located in the N-terminal part of the protein. Aspartic Acid 86-89 secreted phosphoprotein 1 Homo sapiens 0-3 22179617-1 2012 Osteopontin (OPN) is a multifunctional phosphorylated protein containing the integrin binding sequence Arg-Gly-Asp through which it interacts with several integrin receptors, such as the alpha(V)beta(3)-integrin. Aspartic Acid 111-114 secreted phosphoprotein 1 Homo sapiens 0-11 22179617-1 2012 Osteopontin (OPN) is a multifunctional phosphorylated protein containing the integrin binding sequence Arg-Gly-Asp through which it interacts with several integrin receptors, such as the alpha(V)beta(3)-integrin. Aspartic Acid 111-114 secreted phosphoprotein 1 Homo sapiens 13-16 20071328-3 2010 Proteolytic cleavage by thrombin and matrix metalloproteinases close to the integrin-binding Arg-Gly-Asp sequence modulates the function of OPN and its integrin binding properties. Aspartic Acid 101-104 secreted phosphoprotein 1 Homo sapiens 140-143 19706414-3 2009 In vitro cleavage assays demonstrate that OPN is cleaved at Asp-135 and Asp-157 by caspase-8. Aspartic Acid 60-63 secreted phosphoprotein 1 Homo sapiens 42-45 19706414-3 2009 In vitro cleavage assays demonstrate that OPN is cleaved at Asp-135 and Asp-157 by caspase-8. Aspartic Acid 72-75 secreted phosphoprotein 1 Homo sapiens 42-45 18364727-1 2008 Osteopontin (OPN), a large secreted glycoprotein with an arginine, glycine, aspartate (RGD) motif, can bind and signal through cellular integrin receptors. Aspartic Acid 76-85 secreted phosphoprotein 1 Homo sapiens 0-11 18364727-1 2008 Osteopontin (OPN), a large secreted glycoprotein with an arginine, glycine, aspartate (RGD) motif, can bind and signal through cellular integrin receptors. Aspartic Acid 76-85 secreted phosphoprotein 1 Homo sapiens 13-16 18036861-10 2007 NOR proteins and osteopontin are proteins containing aspartic acid rich repeats that can bind Ag. Aspartic Acid 53-66 secreted phosphoprotein 1 Homo sapiens 17-28 7837791-2 1995 BACKGROUND: Osteopontin (OPN) is a phosphorylated glycoprotein that contains a functional Gly-Arg-Gly-Asp-Ser (GRGDS) cell-binding sequence. Aspartic Acid 102-105 secreted phosphoprotein 1 Homo sapiens 12-23 15643009-2 2005 Osteopontin (OPN) is a secreted acidic phosphoprotein containing an arginine-glycine-aspartate sequence and has been suggested to play an important role in early cellular immune responses. Aspartic Acid 85-94 secreted phosphoprotein 1 Homo sapiens 13-16 11696986-2 2001 The HA-binding properties of these proteins have been attributed to glutamic acid-rich sequences in BSP and aspartic acid-rich sequences in OPN. Aspartic Acid 108-121 secreted phosphoprotein 1 Homo sapiens 140-143 10449634-1 1999 The role of adhesion molecules like osteopontin and bone sialoprotein, both containing the Arg-Gly-Asp sequence have been shown to have a role in mineral formation, whereas fibronectin (FN), another adhesive protein, was never studied during the mineralization processes. Aspartic Acid 99-102 secreted phosphoprotein 1 Homo sapiens 36-47 9251683-2 1997 Osteopontin (OPN), a ligand for the alpha v beta 3 integrin, is a secreted glycoprotein with a glycine-arginine-glycine-aspartate-serine cell-binding domain. Aspartic Acid 120-129 secreted phosphoprotein 1 Homo sapiens 0-11 9251683-2 1997 Osteopontin (OPN), a ligand for the alpha v beta 3 integrin, is a secreted glycoprotein with a glycine-arginine-glycine-aspartate-serine cell-binding domain. Aspartic Acid 120-129 secreted phosphoprotein 1 Homo sapiens 13-16 15643009-2 2005 Osteopontin (OPN) is a secreted acidic phosphoprotein containing an arginine-glycine-aspartate sequence and has been suggested to play an important role in early cellular immune responses. Aspartic Acid 85-94 secreted phosphoprotein 1 Homo sapiens 0-11 15738658-11 2005 Interestingly, real-time RT-PCR analysis showed that hFOB cultured on hydrophobic substrata, which have downregulated alphav and beta3 integrin subunits, displayed greater steady state mRNA levels of osteopontin, an extracellular matrix (ECM) protein containing the Arg-Gly-Asp (RGD) integrin recognition sequence, than did cells cultured on hydrophilic substrata. Aspartic Acid 274-277 secreted phosphoprotein 1 Homo sapiens 200-211 11696986-9 2001 Poly(Asp) was able to displace a maximum of 100% of Poly(Glu), 99% of Poly(Asp), 95% of OPN and 89% of BSP. Aspartic Acid 5-9 secreted phosphoprotein 1 Homo sapiens 88-91 11696986-9 2001 Poly(Asp) was able to displace a maximum of 100% of Poly(Glu), 99% of Poly(Asp), 95% of OPN and 89% of BSP. Aspartic Acid 5-8 secreted phosphoprotein 1 Homo sapiens 88-91 10535747-4 1999 In contrast, an alphavbeta3 integrin-expressing cell line, SK-MEL-24, was able to adhere to OPN in an arginine-glycine-aspartic acid dependent manner. Aspartic Acid 119-132 secreted phosphoprotein 1 Homo sapiens 92-95 7837791-2 1995 BACKGROUND: Osteopontin (OPN) is a phosphorylated glycoprotein that contains a functional Gly-Arg-Gly-Asp-Ser (GRGDS) cell-binding sequence. Aspartic Acid 102-105 secreted phosphoprotein 1 Homo sapiens 25-28 1619654-6 1992 In intramolecular interactions, the aspartate favours a "side on" geometry, forming hydrogen bonds with N epsilon and N eta 2; in the intermolecular case, however, "end on" contacts involving N eta 1 and N eta 2 of the arginine are preferred. Aspartic Acid 36-45 secreted phosphoprotein 1 Homo sapiens 194-211 8010953-1 1994 Osteopontin is a phosphorylated sialoprotein containing a conserved sequence of contiguous aspartic acid residues. Aspartic Acid 91-104 secreted phosphoprotein 1 Homo sapiens 0-11 8010953-6 1994 The synthetic polypeptide poly(aspartic acid) was almost as effective an inhibitor of HA formation as osteopontin (IC50 0.11 microgram/ml), whereas poly(glutamic acid) was more than a thousand times less potent (IC50 155 micrograms/ml). Aspartic Acid 31-44 secreted phosphoprotein 1 Homo sapiens 102-113 8293561-7 1994 In addition, the peptide GRGDSP blocked adhesion to osteopontin, suggesting that integrins mediate Arg-Gly-Asp-dependent adhesion. Aspartic Acid 107-110 secreted phosphoprotein 1 Homo sapiens 52-63 8254036-1 1993 Osteopontin is a phosphorylated, sialic acid-rich, noncollagenous bone matrix protein containing the Arg-Gly-Asp-Ser amino acid sequence responsible for cell adhesion. Aspartic Acid 109-112 secreted phosphoprotein 1 Homo sapiens 0-11 2001376-8 1991 Features of this sequence which showed the greatest similarity to mammalian osteopontin included a region in which seven of nine consecutive residues are aspartic acid, a recognition sequence for integrin-mediated cell binding (-Arg-Gly-Asp), and four possible recognition sequences for phosphorylation by casein kinase II. Aspartic Acid 154-167 secreted phosphoprotein 1 Homo sapiens 76-87 2001376-8 1991 Features of this sequence which showed the greatest similarity to mammalian osteopontin included a region in which seven of nine consecutive residues are aspartic acid, a recognition sequence for integrin-mediated cell binding (-Arg-Gly-Asp), and four possible recognition sequences for phosphorylation by casein kinase II. Aspartic Acid 237-240 secreted phosphoprotein 1 Homo sapiens 76-87