RecName: Full=Phosphoinositide-3-kinase-interacting protein 1; AltName: Full=Kringle domain-containing protein HGFL; Flags: Precursor
inactive tyrosine-protein kinase transmembrane receptor ROR1( domain architecture ID 10639013)
inactive tyrosine-protein kinase transmembrane receptor ROR1 maybe a receptor for ligand WNT5A which activate downstream NFkB signaling pathway and may result in the inhibition of WNT3A-mediated signaling; has very low kinase activity in vitro
List of domain hits
Name | Accession | Description | Interval | E-value | |||
KR | smart00130 | Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ... |
24-101 | 4.91e-25 | |||
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides. : Pssm-ID: 214527 Cd Length: 83 Bit Score: 94.76 E-value: 4.91e-25
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Name | Accession | Description | Interval | E-value | |||
KR | smart00130 | Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ... |
24-101 | 4.91e-25 | |||
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides. Pssm-ID: 214527 Cd Length: 83 Bit Score: 94.76 E-value: 4.91e-25
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KR | cd00108 | Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ... |
24-99 | 1.55e-23 | |||
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides. Pssm-ID: 238056 Cd Length: 83 Bit Score: 90.90 E-value: 1.55e-23
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Kringle | pfam00051 | Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ... |
25-99 | 7.25e-20 | |||
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta. Pssm-ID: 395005 Cd Length: 79 Bit Score: 81.20 E-value: 7.25e-20
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Name | Accession | Description | Interval | E-value | |||
KR | smart00130 | Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ... |
24-101 | 4.91e-25 | |||
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides. Pssm-ID: 214527 Cd Length: 83 Bit Score: 94.76 E-value: 4.91e-25
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KR | cd00108 | Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ... |
24-99 | 1.55e-23 | |||
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides. Pssm-ID: 238056 Cd Length: 83 Bit Score: 90.90 E-value: 1.55e-23
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Kringle | pfam00051 | Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ... |
25-99 | 7.25e-20 | |||
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta. Pssm-ID: 395005 Cd Length: 79 Bit Score: 81.20 E-value: 7.25e-20
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Blast search parameters | ||||
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