about
Selectin, lymphocyteVascular cell adhesion molecule 1Protein tyrosine phosphatase, non-receptor type 11CD1d1 antigenDesmoplakinIntegrin beta 2Integrin beta 1 (fibronectin receptor beta)Integrin alpha 4Carboxypeptidase EIntegrin beta 3Fibroblast growth factor receptor 1Protein tyrosine phosphatase non-receptor type 6Claudin 7CD200 moleculeGlycophorin C (Gerbich blood group)Desmoglein 2Junction adhesion molecule likeNeuroligin 4 X-linkedNeuroligin 4 Y-linkedNeuroligin 3SRC proto-oncogene, non-receptor tyrosine kinaseIntegrin subunit alpha 5Immunoglobin superfamily member 21Calcium modulating ligandCatenin delta 1ADAM metallopeptidase domain 8Adhesion G protein-coupled receptor L1T cell immunoreceptor with Ig and ITIM domainsIntegrin subunit beta 7Transforming growth factor beta inducedCytotoxic and regulatory T cell moleculeHemicentin 1Leucine rich repeat containing 4CLeukocyte immunoglobulin-like receptor subfamily B member 2Plakophilin 3Teneurin transmembrane protein 4Teneurin transmembrane protein 2Teneurin transmembrane protein 3Teneurin transmembrane protein 1Neuroligin 1
P680
The human poliovirus receptor related 2 protein is a new hematopoietic/endothelial homophilic adhesion moleculeActivated endothelium binds lymphocytes through a novel binding site in the alternately spliced domain of vascular cell adhesion molecule-1The Arg451Cys-neuroligin-3 mutation associated with autism reveals a defect in protein processingRole of a novel EGF-like domain-containing gene NGX6 in cell adhesion modulation in nasopharyngeal carcinoma cellsThe most widespread desmosomal cadherin, desmoglein 2, is a novel target of caspase 3-mediated apoptotic machineryJAML, a novel protein with characteristics of a junctional adhesion molecule, is induced during differentiation of myeloid leukemia cellsStructural recognition of a novel fibrinogen gamma chain sequence (117-133) by intercellular adhesion molecule-1 mediates leukocyte-endothelium interactionA mitogenic action for fibrinogen mediated through intercellular adhesion molecule-1Identification of PVR (CD155) and Nectin-2 (CD112) as cell surface ligands for the human DNAM-1 (CD226) activating moleculeDisruption of the integrin alphaLbeta2 transmembrane domain interface by beta2 Thr-686 mutation activates alphaLbeta2 and promotes micro-clustering of the alphaL subunitsMutations in the N-terminal domains of nectin-1 and nectin-2 reveal differences in requirements for entry of various alphaherpesviruses and for nectin-nectin interactions.
P921
Q14901674-0CBFF68C-CDA1-4D36-AB4D-4CB69F98D3C1Q14901868-DF097A25-BBA4-4E80-8106-368D98BFE2E7Q14905498-1B0AE47E-8FD5-4EF0-9FD5-0BB0AAB0D86CQ14905534-E1A28A17-FE5A-436A-B3A1-EA94388AC14DQ14906114-297441D9-1C6C-463D-9E32-A3583D289446Q14912069-F6DEF6A4-4CA5-4D4D-9E63-B94CFCB8ED12Q14912087-2EC9C5D6-8037-4A07-A3E2-08C8FA19078EQ14912102-9B25EFF7-46F0-4A51-B5FA-1E51D4EA4731Q14913004-E587F1D8-F96A-4B21-B681-5D644EE6A010Q14913644-037C3CA8-72E5-4946-995B-3F6719ED87FBQ14914262-8972B484-2420-4185-B4A4-D31BA75D2735Q21100543-777C7E66-9E1B-4054-B7F6-F80CA905F2EDQ21100767-7C5B2A24-2916-4B34-A35A-E058A7EC553FQ21104677-802D4381-478F-41DE-932C-C61AEE32CCC2Q21106167-544D5F1F-D31A-405C-B1B4-EA5356078281Q21108549-CE85FDB7-0C57-437E-9847-96FE0366ED88Q21108774-21A2961C-6102-4D52-9A8C-080B782FE16BQ21109061-5C91BC1C-BE95-4C5F-8507-74D7CB419C45Q21109062-F15B2351-FC5D-4C8A-B26C-DC6E76B5A7EAQ21109066-97E7E97C-BB08-4138-881F-72F433BC9CA1Q21109354-31B390DC-CCAD-4DE2-8EBB-B29E092481CAQ21110097-1541080C-8205-4846-A78F-164882AA188EQ21111092-20C87A9C-04F2-41F9-B936-B3FE635E6628Q21111881-91297300-4F52-4C29-9CD7-102403ED4957Q21113069-C5F07753-6C80-4018-AD0F-C516B8608EF5Q21113736-EB29DE9F-A33A-4FB6-AB0B-D255D7152192Q21113825-05853FD8-2168-4FC8-BB5D-26735A42C3CBQ21114021-9F7087B7-4E6E-474C-AE6C-034DE6E6AF32Q21114531-94FC9CA3-B252-4D69-AAB3-8B9A59C61B51Q21116873-B0019C47-FC14-4095-8A0C-C0DFCB65F9F5Q21117323-940C8F33-A546-4588-A73F-737C01A5B8E2Q21118299-91F3F0CF-838E-4F80-890F-6FA4F0D0950FQ21119345-85B5E74A-1C3A-475A-8819-32497A00DF94Q21120800-860234F9-1485-4353-A4DF-BE9D8369D59DQ21122021-1E003D17-2D86-498E-8478-CD0A712ADA08Q21122176-68CA83F6-9335-4AB3-8221-602C78B2DEBBQ21122177-5CA0CD2F-7BE8-4D4A-9427-07CE8CA46282Q21122177-9B8191F2-FC78-4731-8BEB-F0D21BFBEA70Q21122178-01FCD064-0BBD-47B0-8B20-FE4FB27AF3D3Q21122179-BCEAEC2B-9045-4101-B1CE-4EDBC37D8C92
P680
Q22008517-EFC8DB7E-BD1F-4029-888B-3A3EA5D892CAQ24292864-8E56C256-CF6D-4304-95DF-521C538E9FBEQ24293639-5EFE43DD-EC7E-4E62-A39E-D77B323EB85CQ24308439-8FECB92A-BFB6-4045-B281-61032F381253Q24309080-F0C85D31-82B3-4AA4-9F60-77041DE45BD1Q24309293-626FF49B-5038-4901-90A7-9A8DF77A83D8Q24309459-E5888598-D9DA-40A8-A493-64B7E2E769A4Q24309485-C2C90A24-07DD-4F56-8A40-721A21BC4D2DQ24314704-73EC70F0-281D-438D-93FF-D968A8DBEB31Q24317338-9980344B-A100-4C1D-8FCC-1846C305B8DAQ24319105-E56438D7-5F4C-47C8-9D90-AE8390B1BE42
P921
description
Interacting selectively and non-covalently with a cell adhesion molecule.
@en
moleculaire functie
@nl
name
cell adhesion molecule binding
@en
type
label
cell adhesion molecule binding
@en
altLabel
CAM binding
@en
GO:0050839
@en
prefLabel
cell adhesion molecule binding
@en
P279
P2888
P686
GO:0050839