about
ATPase H+ transporting V1 subunit E2Calpain small subunit 1NEDD4 E3 ubiquitin protein ligaseCyclin dependent kinase 5 regulatory subunit 1ATPase H+ transporting V1 subunit C1SH3 domain containing GRB2 like, endophilin B1Ubiquilin 2Sorting nexin 5ATPase H+ transporting V0 subunit cRegulatory associated protein of MTOR complex 1RB1 inducible coiled-coil 1Ubiquilin 1Protein kinase AMP-activated non-catalytic subunit beta 2Protein kinase AMP-activated non-catalytic subunit gamma 1Protein kinase AMP-activated catalytic subunit alpha 2Protein kinase AMP-activated catalytic subunit alpha 1ATPase cation transporting 13A2Protein kinase AMP-activated non-catalytic subunit gamma 3Protein kinase AMP-activated non-catalytic subunit gamma 2Protein kinase AMP-activated non-catalytic subunit beta 1Endoplasmic reticulum to nucleus signaling 1Calpain 1Unc-51 like autophagy activating kinase 1Cyclin dependent kinase 5ATPase H+ transporting V0 subunit a2Ras homolog, mTORC1 bindingATPase H+ transporting V1 subunit DLate endosomal/lysosomal adaptor, MAPK and MTOR activator 1MTOR associated protein, LST8 homologATPase H+ transporting V1 subunit G1Ras related GTP binding BRas related GTP binding ASolute carrier family 38 member 9Ras related GTP binding CATPase H+ transporting V1 subunit B2Late endosomal/lysosomal adaptor, MAPK and MTOR activator 5Late endosomal/lysosomal adaptor, MAPK and MTOR activator 4ATPase H+ transporting V0 subunit a1Sorting nexin 6Ras related GTP binding D
P682
RalB and the exocyst mediate the cellular starvation response by direct activation of autophagosome assemblyRegulation of autophagy by Beclin 1 in the heartFeedback regulation between autophagy and PKARetromer Ensures the Degradation of Autophagic Cargo by Maintaining Lysosome Function in DrosophilaThe calpain system as a modulator of stress/damage responseCdk5-mediated phosphorylation of endophilin B1 is required for induced autophagy in models of Parkinson's diseaseMitochondrial dysfunction associated with glucocerebrosidase deficiencyAMPK-Dependent Phosphorylation of GAPDH Triggers Sirt1 Activation and Is Necessary for Autophagy upon Glucose StarvationCaspase cleavage of Atg4D stimulates GABARAP-L1 processing and triggers mitochondrial targeting and apoptosis.ATP13A2 regulates mitochondrial bioenergetics through macroautophagyLipofuscin is formed independently of macroautophagy and lysosomal activity in stress-induced prematurely senescent human fibroblastsUCHL1 deficiency exacerbates human islet amyloid polypeptide toxicity in β-cells: evidence of interplay between the ubiquitin/proteasome system and autophagyNedd4 E3 ubiquitin ligase promotes cell proliferation and autophagy
P921
Q14876075-F4F94BFB-9294-4C16-A8A8-6228EA7FDE73Q21097401-985A7EBC-E696-4640-AF61-D020CC632346Q21097411-98C2A6A9-C6EA-48B3-A179-5D4AC91AA8AAQ21123467-C8F1A8E5-DE63-45E3-AC05-37FF6F72A99CQ22303863-D84C063F-12F5-4317-971B-AE238323853EQ22303979-3CE806F3-F7D6-4AAC-AD51-FF36ADA3E161Q22303982-981C1865-2DF3-48AE-9BC0-166BA4FBCED8Q26250122-5D48E9EF-5F46-4124-A21B-FE34EB4408CE
P279
Q21102396-61E27E68-E9D8-4266-90CD-FB36F9000E71Q21105302-943954C4-F5E9-4D01-94ED-7D37AAB46C5EQ21107331-F02BBE49-05B9-4A9B-B5A8-AC42BC7F1A4BQ21109701-F9DFA55A-2F14-48D2-BA86-AB6AE00450B9Q21110418-F48AA09E-F53D-4CBE-B409-E51630E97FCCQ21110722-3513AACD-A27A-453B-8398-418DC3C1D456Q21111235-15E1D98F-8A15-49D8-A5F6-77702B3BB14FQ21111235-E9AD3518-8902-4D40-81BD-27A9716CE0D5Q21111598-09222122-9992-4D54-9D78-A2E16EDF54D6Q21114090-18D61FA3-49F2-4D02-9DBF-99A58031B109Q21115067-384D45B4-6A38-436B-97D1-983A0EC51C11Q21115135-755B1EE1-67D9-4A1D-802A-82DD8C34568AQ21115143-B8FC7521-1F59-49D0-8D0E-87260077B5D9Q21115150-68A921B6-63E4-4A78-897D-09E00BF4C4F9Q21115161-F859F4D7-1AA5-483A-929D-2BA635E137A8Q21115165-34123851-D142-4ED3-8029-E5CCC5D90FECQ21115165-F37B837C-250E-4472-A20E-AB606507EBE9Q21115170-2455F07A-CF51-4ADC-B0FA-8C174E58A87BQ21115193-823D15C5-82A6-48BF-A2A8-34AE2EABD15CQ21115196-4B1ECF0F-B4BE-4D8B-AF7C-8F50206423C5Q21115198-BBD44997-3538-434D-AB62-48744BCBCD39Q21115204-74D34824-F0B9-4280-B669-C7515CFB2B35Q21115427-392D8E49-750E-418F-B166-AE85AB5C9FA4Q21115584-888B2F6E-7699-4998-84E1-E539796E785CQ21116760-4DDC1232-9B47-4709-B699-F9F66A1A90F0Q21116933-B2436C8A-AC51-48F8-A842-ABBDA86594E1Q21117465-FCAE5615-9047-4383-8932-465B18BF02BEQ21117636-B8442ABE-0544-4FE0-8F83-49CBDCC8C4E0Q21117771-1D17ABAC-EA71-4690-AB42-2773347947A2Q21117784-B0CF7D9C-DD09-4A1E-AAC8-83F73B575D48Q21117879-4FDA02CB-3995-4F6F-8F9E-1190790F851BQ21118930-C0FD9358-32AC-454E-815A-19031D7F3673Q21119281-938FE62E-3763-4758-B80E-3F422B221CBBQ21119361-51026B2D-064E-4B3B-82C8-34CCDA9B112BQ21119362-07E18FC5-3E32-4B43-81A1-85D7E225B797Q21120573-C053F85B-90E2-48EE-9BA7-88DF4A343D0DQ21121470-C1F53E93-50BF-4FC8-AF1B-00D06193711CQ21122340-D8F79710-3346-430B-9BCF-89BAD6942DC1Q21122342-BEE4F9F5-F4B7-4C35-BBF6-A1D3BA486D22Q21122938-BC0E21E8-BD51-4F4B-9C6D-11F5AF6D5FA2
P682
Q24337344-176B2DCE-185A-4900-8619-82EAE927F57BQ28114861-0B18FD47-6754-4262-92F8-E1365E06A31BQ28114959-44ADCD37-D8B3-4340-8A47-5F659D6CD2DAQ28115507-BFED3459-D631-48CC-B8AC-CBD85DC5EE27Q28115546-3F9A4508-9B34-4BE4-8815-1D59A045FE5DQ28115581-33B026EC-954B-4957-8533-BCA985AA787AQ28115678-9FA9721E-A117-4C67-A2EC-083DBE6163C2Q28116140-19405115-0D23-4834-B97E-69AC6A8D7C8CQ28116213-089D41F6-A756-4506-9804-1F564BDD4B64Q28116275-80490CD7-525B-4CCD-96E8-97EE0C8D2C31Q28118094-E3E857B9-0C73-4661-B286-09AF2A2B2A68Q28118734-946DBA96-ADD1-483F-99AB-E13D4DD11602Q28119201-393057FF-DF70-4E8F-9046-9559B8FA07D0
P921
description
Any process that modulates the frequency, rate or extent of macroautophagy.
@en
biologisch proces
@nl
name
regulation of macroautophagy
@en
type
label
regulation of macroautophagy
@en
altLabel
GO:0016241
@en
regulation of starvation-induced autophagy
@en
prefLabel
regulation of macroautophagy
@en
P128
P2888
P686
GO:0016241