about
CD9 moleculeIntegrin linked kinaseInsulin like growth factor 1CalreticulinFibronectin 1Von Willebrand factorInsulin-like growth factor 1Dystrophin, muscular dystrophyFibroblast growth factor 2Insulin-like growth factor 2Secreted phosphoprotein 1Fibroblast growth factor 1Neurofibromin 2Intercellular adhesion molecule 1Vascular cell adhesion molecule 1Thymus cell antigen 1, thetaPaxillinCollagen, type III, alpha 1Spleen tyrosine kinaseIntegrin binding sialoproteinCellular communication network factor 2Chemokine (C-X3-C motif) ligand 1A disintegrin and metallopeptidase domain 17Integrin beta 2Integrin beta 1 (fibronectin receptor beta)Integrin alpha 2Integrin alpha 3Erbb2 interacting proteinProtein kinase C, alphaIntegrin beta 3VitronectinInterleukin 1 betaCartilage oligomeric matrix proteinCalcium-sensing receptorLYN proto-oncogene, Src family tyrosine kinaseInsulin like growth factor 2Actinin alpha 4Actinin alpha 1Actinin alpha 2Actinin alpha 3
P680
Identification and characterization of a novel extracellular matrix protein nephronectin that is associated with integrin alpha8beta1 in the embryonic kidneyHuman endothelial-cell specific molecule-1 binds directly to the integrin CD11a/CD18 (LFA-1) and blocks binding to intercellular adhesion molecule-1Molecular cloning of ICAM-3, a third ligand for LFA-1, constitutively expressed on resting leukocytesActivation of human neutrophils induces an interaction between the integrin beta 2-subunit (CD18) and the actin binding protein alpha-actininDisruption of focal adhesions by integrin cytoplasmic domain-associated protein-1 alphaDisease-associated single amino acid mutation in the calf-1 domain of integrin α3 leads to defects in its processing and cell surface expressionJAM2 interacts with alpha4beta1. Facilitation by JAM3The CD9, CD81, and CD151 EC2 domains bind to the classical RGD-binding site of integrin αvβ3.Direct binding to integrins and loss of disulfide linkage in interleukin-1β (IL-1β) are involved in the agonistic action of IL-1β.Integrin alpha x stimulates cancer angiogenesis through PI3K/Akt signaling-mediated VEGFR2/VEGF-A overexpression in blood vessel endothelial cells
P921
Q1058190-709A823D-2ED8-4076-975A-A0C0671612A7Q1058190-89BE434E-2C9F-48EE-A54B-60548ED72E2DQ11913806-92695469-4CBD-4E66-86E8-C05A17A0DCF5Q1263065-7B096612-F640-4C85-A475-1D4CEEC9B72FQ14633944-7B53AE3C-57F3-4432-9929-2AB7050A9BBDQ14819493-0DBDA717-C2B8-4BCA-85FA-F8224DEC26F6Q14863680-FA92116D-5969-42A5-A4E2-B382057DF883Q14863723-EB349416-9258-449F-99B0-27EE0B3E8F55Q14864296-3EEA29ED-E50A-4F21-9F05-A7C8A85C5763Q14866180-5639BD43-5DA0-496A-A962-C6038CCFD0BEQ14874351-CDD4C631-6629-4BC1-ADBB-201B03F56DA8Q14876620-7F575F2B-8583-4BB4-B95A-E8F2ECDAE91EQ14889337-1BA1F820-7106-41C7-B549-14A7CC27DF6FQ14889820-EC708DAB-D9A6-4DB9-97D5-C9E4ED592B5CQ14891112-0DF419E9-64FA-487E-89DC-3BB47F994021Q14901868-0F3CFBD9-3C57-4CA6-928D-C191D4931FC0Q14901868-A8954AC6-2709-42BC-9482-3A7D5F6587CAQ14906181-4CBE93FA-7F60-496C-A93D-686872B34905Q14906181-9ACD210D-3597-4C0E-8A4D-AE736554B217Q14906595-10650D23-6782-4444-9ABE-5FA4267A2594Q14906850-C1274E19-64A3-4631-AD73-192D03C95CC7Q14907340-AA6CDB11-28C5-4DEF-AB5F-B3002B69F452Q14907673-2C9087D5-EFE1-406E-A7B5-A0415E9C6850Q14907754-4194D198-D7CB-4048-B017-FE0BE461E248Q14907754-6E1A2244-2445-414D-B165-06C3468B4501Q14907782-6A53A553-3677-4F35-96BD-332CCF456037Q14907944-2C241E02-1B81-48AA-97AC-BD8ADEDD664AQ14907944-A1A27C16-4025-41BF-816F-55BD5043A56CQ14912069-9E0CD4DC-3C52-48EE-BCE5-11C34AA1A76CQ14912087-5D31001C-5A69-4066-85E4-22BB667ECE02Q14912087-FDB2A700-90EF-434B-9B83-728C163DEA54Q14912138-85D6FBA0-713E-4E4C-BBEB-8D6699AC65EEQ14912138-D5871CA3-4480-4A7A-BEC8-1E2FB1CA1593Q14912141-8B289A58-5B8C-4704-9EEE-DA376FD1E1B6Q14912193-E164FF32-A3A2-4032-9CCD-94977067C116Q14912658-12A1F14E-7094-4C82-BFDF-F0D2B27464FCQ14913644-55590234-BFE4-4BFC-A347-780EE6CE3AFEQ14913644-8753D1D2-6D81-428E-9365-C8C904E0119BQ14916395-1295D9BB-2490-4FC8-869E-0F435783E3B8Q14916414-BB543D06-CBB7-4975-9CFC-F96B1658CD44
P680
Q24291483-FDC24E7E-A2F7-4821-96FE-A9C4AD3871B5Q24291650-806664E8-EF4B-4ADC-A3DF-C85CC2A97F11Q24294767-66BC5C6F-766A-4A9E-B141-F2E04606ACDDQ24322742-92B68CCC-0A90-493E-AFE9-0FE329370D98Q24324657-CD3F5BCA-629C-43A7-A15C-D77DBB57AD82Q24339572-9FC0EEA3-313D-42B0-B2E0-08FFA5D4067DQ28205206-0EE027C9-0719-4318-8B1F-CBF830F199D0Q40403704-21A9E7EE-6E7A-4F2E-BEC8-2B9D1B04F6E6Q46979263-C0CB2D26-C1F9-4559-BCDB-A7D2C3BB82F8Q92379771-EFBC74A7-621C-461E-B0F9-F11BF3391AA1
P921
description
Interacting selectively and non-covalently with an integrin.
@en
moleculaire functie
@nl
name
integrin binding
@en
קשירת אינטגרין
@he
type
label
integrin binding
@en
קשירת אינטגרין
@he
altLabel
GO:0005178
@en
prefLabel
integrin binding
@en
קשירת אינטגרין
@he
P279
P2888
P686
GO:0005178