about
Mannose-binding lectin (protein C) 2Ceramide transporter 1Uncharacterized protein ARRDC1-AS1DAB2 interacting proteinWASH complex subunit 2CSorting nexin 3Pleckstrin homology domain containing A5ADP ribosylation factor interacting protein 2ADP ribosylation factor interacting protein 1LanC like 2Sorting nexin 5Junctophilin 2SH3 and PX domains 2AOxysterol binding proteinSAP30 likeSEC14 and spectrin domain containing 1Gasdermin DGasdermin BGasdermin AGasdermin CPleckstrin homology and FYVE domain containing 1Oxysterol binding protein like 8Oxysterol binding protein like 5Pleckstrin homology domain containing A3Sorting nexin 24Golgi phosphoprotein 3 likeSH3 and PX domains 2BGolgi phosphoprotein 3Pleckstrin homology domain containing A8WASH complex subunit 2`Mannose-binding lectin (protein A) 1Gasdermin C2Gasdermin A2Gasdermin C4Gasdermin A3Gasdermin C3LanC (bacterial lantibiotic synthetase component C)-like 2Collagen, type IV, alpha 3 (Goodpasture antigen) binding proteinPleckstrin homology domain containing, family F (with FYVE domain) member 1Pleckstrin homology domain containing, family A (phosphoinositide binding specific) member 8
P680
Recruitment of arfaptins to the trans-Golgi network by PI(4)P and their involvement in cargo exportMyristoylation of human LanC-like protein 2 (LANCL2) is essential for the interaction with the plasma membrane and the increase in cellular sensitivity to adriamycinGOLPH3L antagonizes GOLPH3 to determine Golgi morphologyFAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)PEssential Ca(2+)-independent role of the group IVA cytosolic phospholipase A(2) C2 domain for interfacial activity.Novel obscurins mediate cardiomyocyte adhesion and size via the PI3K/AKT/mTOR signaling pathway.
P921
Q14907668-8BF29B04-1EE8-4958-96FE-726F4A18CE1FQ21096462-68C66B6A-0D32-4FB4-9829-3430F68C3B23Q21096462-9C35A49E-8791-413F-8B25-2730C1C55333Q21102403-0BBD9764-9743-4E74-BBCF-F03552614CDDQ21105736-0EE7DC35-4A4B-4763-B824-90B9E3304DF9Q21106096-A034A103-AEA0-45C0-9B05-D9B3A1AFCBE6Q21106459-B4949372-4676-4E88-8CED-D70F456405EAQ21106556-778B4B07-0CC9-4168-AD07-EBD83B60ECDDQ21110420-54ED3A81-C768-4B3F-BBC1-A093E4B163C3Q21110422-AC012D37-EF47-4140-B443-5AED3346D133Q21111586-95CBA9F7-4601-4D24-80B1-92EA1743A057Q21111598-7535269D-7030-4C59-B172-4591552B692BQ21113470-519208D3-064A-4AF5-9B74-16D2C38EF8EFQ21113815-4804B578-22FE-40B0-9B0D-31BCA12838B4Q21115899-BEBBE579-B3BC-412D-B12C-4BF22D66BCC3Q21118302-72E11F78-5ED6-4C13-BE31-6CD1B1BD575AQ21119002-55D438B0-868A-42E5-9919-3799527C2C1FQ21119012-2A8FE45C-F8FC-4BF3-97A3-527A59D86749Q21119012-C99953F2-8A79-4807-9CFA-1B0FA50AE70BQ21119015-FCC9AD09-2658-4E7A-B7BA-B74066772A34Q21119016-8B9CA62D-F3EB-4F59-AB7E-BB183F4EBFC3Q21119017-263BFF91-0E63-4B84-997F-ABF9B55AE1AFQ21121586-98E56084-ACA2-4306-87FC-8C76F7619281Q21121786-34609EC2-6223-4C50-9273-79BBC161D37EQ21121790-EBA5CCE1-5C97-41AB-8C92-C189753C1878Q21122017-9C786434-A64C-4886-B4C5-02AE51DAD4C9Q21122017-C5A36BAF-7B7D-4105-9E87-A0CFE9CE67A8Q21125250-E626F629-6DD7-423C-8319-582E25D0C33FQ21130656-74DC6D70-D50D-4C45-969D-82ADF8E5E1E1Q21130656-B9E19D2A-0298-41D9-B8C3-3B51C31A5552Q21135654-BBA6C0BF-6B91-4A39-8F88-2164C092DD60Q21202979-46F1B62A-7CAE-4B62-BBE4-995F93A5535BQ21202979-7071F017-C6D0-49E9-AA7F-817A410AE4EDQ21207650-1E601524-6351-47D1-AF57-3F94D79E1D79Q21419801-C144959B-F223-45A5-8966-1EF625D14EB7Q21433554-06C5D660-D1FA-48DA-8B21-877134FAADE4Q21433633-82F0B064-09D3-480F-A6CB-3BC15B5C0B6BQ21433634-339F87D4-5D88-456B-A0C3-B3067AD5FB85Q21433635-6F0CC206-A1E1-44BE-9615-D9022B4521D6Q21433637-A8167253-BBC3-470B-A871-84F069CEDAFC
P680
description
Interacting selectively and no ...... phorylated at the 4' position.
@en
moleculaire functie
@nl
name
phosphatidylinositol-4-phosphate binding
@en
type
label
phosphatidylinositol-4-phosphate binding
@en
altLabel
GO:0070273
@en
prefLabel
phosphatidylinositol-4-phosphate binding
@en
P2888
P686
GO:0070273