about
Androgen receptorLymphocyte protein tyrosine kinaseEstrogen receptor 1 (alpha)BCL2 binding component 3FibrillarinTransient receptor potential cation channel, subfamily C, member 6Transient receptor potential cation channel, subfamily C, member 5Rac family small GTPase 1Ankyrin 1Ankyrin 2ATPase Na+/K+ transporting subunit beta 1ATPase Na+/K+ transporting subunit beta 2RuvB like AAA ATPase 2Polycystin 2, transient receptor potential cation channelProtein tyrosine phosphatase non-receptor type 3Methyltransferase like 21AValosin containing protein lysine methyltransferaseRAB4A, member RAS oncogene familySorting nexin 10Antioxidant 1 copper chaperoneATP synthase inhibitory factor subunit 1Phosphodiesterase 4DPIH1 domain containing 1RAB3A, member RAS oncogene familyBR serine/threonine kinase 2Cholinergic receptor, nicotinic, alpha polypeptide 7Adenylate cyclase 10DnaJ heat shock protein family (Hsp40) member C10RAS like proto-oncogene AGABA type A receptor associated protein like 2ATP binding cassette subfamily A member 1Nuclear receptor subfamily 1 group H member 2Syntrophin alpha 1ATPase Na+/K+ transporting subunit beta 3Caveolin 1Zinc finger HIT-type containing 6Nuclear FMR1 interacting protein 1Caseinolytic mitochondrial matrix peptidase proteolytic subunitATPase H+ transporting V0 subunit a2Torsin 1A interacting protein 1
P680
GATE-16, a membrane transport modulator, interacts with NSF and the Golgi v-SNARE GOS-28Targeting elements in the amino-terminal part direct the human 70-kDa peroxisomal integral membrane protein (PMP70) to peroxisomesThe influence of SRC-family tyrosine kinases on Na,K-ATPase activity in lens epitheliumSLC26A9 stimulates CFTR expression and function in human bronchial cell linesMutations in the peroxin Pex26p responsible for peroxisome biogenesis disorders of complementation group 8 impair its stability, peroxisomal localization, and interaction with the Pex1p x Pex6p complexNovel ATPase of SNF2-like protein family interacts with androgen receptor and modulates androgen-dependent transcriptionV1 and V0 domains of the human H+-ATPase are linked by an interaction between the G and a subunitsCa2+ -dependent interaction of S100A1 with the sarcoplasmic reticulum Ca2+ -ATPase2a and phospholamban in the human heartHistidine-rich Ca-binding protein interacts with sarcoplasmic reticulum Ca-ATPaseArresting a Torsin ATPase reshapes the endoplasmic reticulumAnkyrin binds to two distinct cytoplasmic domains of Na,K-ATPase alpha subunitERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stressSLC26A9 is a constitutively active, CFTR-regulated anion conductance in human bronchial epitheliaRecruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membraneThe sarcolemmal calcium pump inhibits the calcineurin/nuclear factor of activated T-cell pathway via interaction with the calcineurin A catalytic subunitDeletion of Tmtc4 activates the unfolded protein response and causes postnatal hearing loss
P921
Q14873035-0966A4FD-D29F-48AC-BC55-987987AC1CDAQ14885208-9D26F20C-D53A-4BC1-A4F2-7BD18B8595DDQ14902317-3E9FEBD6-7643-43ED-9BB3-3A190BA93981Q14907288-0FFADDAE-6781-4A29-8FA8-AC6B6AEE0173Q14914394-601F2B9F-043D-4718-8CEA-F6286BF1ED9DQ14914580-B6289598-0C7B-467F-8A23-350C31B69871Q15323071-E0E7E981-13B0-485C-AE7B-E3D926694C07Q15325768-1145379C-E337-4E8D-B2FD-33EA81092861Q21097227-8B11E751-ED2A-4764-95BF-05CF15D29BF4Q21097261-6647EB63-C88F-416A-AFFE-42E56B4657A2Q21097497-184303E0-8785-4E01-B710-7B2271343DABQ21097507-96BE5634-FF58-46EB-9550-354C20696C02Q21102282-9383F283-C9CC-4454-A542-A0420F8AE476Q21103321-4F040EF0-24D9-4941-8B6D-AA6312BE606CQ21105040-610F8F05-1C65-4614-9335-3D5F7706EFDAQ21105359-8E1C41E1-929A-4AB7-A038-F6224EFCCD6DQ21105874-A8CC02EC-7347-431D-8C3F-18D3F3462FF1Q21106139-9E8B1B36-18C5-4AFB-A3E3-B8769080F1A3Q21106527-7AF080E3-70E4-4746-B788-E0A93DBB0AEFQ21106530-DA320822-4DD7-40C9-97E6-7839795A9E9FQ21106657-248F6A9F-7A5C-4FC4-94F9-918C8642F86AQ21106657-491403D6-69E2-4DBD-BA73-E42D90C9A9F4Q21106795-608E90C4-963A-4052-A639-4B6F6C2852C7Q21106795-FAEE50CA-3653-48F0-9F2B-E69AB50E950FQ21107252-DE909CBF-1304-4FB2-9FC5-B0D63A66E507Q21108063-E88B6C9B-8661-4745-B282-7D6CA40BE5E8Q21110488-BAE02A5D-3824-4285-95BB-9ACC21FE0E29Q21111177-1BCD6168-BA45-4B4F-8DC0-6B7DC3D0B22EQ21111219-13B685BE-BFD4-4E90-A98E-87A9309B3988Q21112236-5822E899-87AD-4F25-86C0-A91A916419F5Q21114964-269EA664-38CA-4B31-B2A1-4B496E8C5358Q21115128-78D96A47-0236-44C9-B424-A62D313A4A9AQ21115210-1A9E1711-FF18-4445-A325-7883AA6D8578Q21115219-A5F8D115-E276-40A6-867D-EC8B7B858DE1Q21115228-CC4D3E1D-8ED1-4F5E-AB2C-71F1CC2A3B69Q21115336-837D73B2-4610-4A0E-9627-CFC935CB3722Q21115385-2D2256AE-00FA-471B-A50B-A5681DCAB810Q21116863-1EA598A6-FE8A-422F-8375-762F4A0E3E28Q21116870-B7E8CF5B-323D-45CE-8679-963FF1917E81Q21117239-B4C65730-2015-499E-BF14-91D053627EC4
P680
Q22253422-726AF51A-944D-4540-B929-BB29E0CD7297Q24291444-BACD0E36-0CC0-4EA2-9780-40EE44EB6C41Q24292765-4F2202A4-61F8-4AD0-A651-333797FD57A0Q24293056-0163F270-CE52-436F-B61C-4ED48412CA3FQ24293136-2CE129CF-ED1D-4FE9-B2D0-AB1D9AC2EE5AQ24299539-2F1327C1-77AC-4518-8976-611FD2E5AC1CQ24300220-8147929E-95FE-4DC1-9D48-F638B3407274Q24305007-BD798EDD-810D-4171-8B92-505C2D81FCB8Q24307062-F58563CE-7C7E-4F33-A1B1-D11F808B4519Q24310079-264251A4-63E7-4ECB-9555-27C5D820540DQ24310792-2FF65CF9-5992-40A3-937B-520C153842ACQ24314974-00C69866-A282-486B-86F8-E5D29C614D00Q24321913-78F40156-2A16-45CE-8CFE-725065BDEABBQ24336904-BACCE51B-DD95-47E5-A79A-544A39C5F5FAQ81850030-F94A452F-35EB-4AA0-950D-BBC24379B2CFQ91314340-38B77ADB-1146-4EC1-8B4F-78293144EC93
P921
description
Interacting selectively and no ...... talyzes the hydrolysis of ATP.
@en
moleculaire functie
@nl
name
ATPase binding
@en
liaison d'ATPase
@fr
type
label
ATPase binding
@en
liaison d'ATPase
@fr
altLabel
GO:0051117
@en
prefLabel
ATPase binding
@en
liaison d'ATPase
@fr
P279
P2888
P686
GO:0051117