{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9C0C7","secondaryAccessions":["A6XN33","D3DQP8","G3V193","Q86XD6","Q9H8Z0","Q9NXE7"],"uniProtkbId":"AMRA1_HUMAN","entryAudit":{"firstPublicDate":"2008-01-15","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2008-01-15","entryVersion":181,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"17589504"}],"value":"Activating molecule in BECN1-regulated autophagy protein 1"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"16949367"}],"value":"DDB1- and CUL4-associated factor 3"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"17589504"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:25990"}],"value":"AMBRA1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"16949367"}],"value":"DCAF3"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11214970"}],"value":"KIAA1736"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"A2AH22"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20921139"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21358617"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21753002"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23524951"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24587252"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25215947"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25438055"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25499913"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25803737"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30166453"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30217973"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30513302"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31123703"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32333458"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33854232"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33854235"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33854239"}],"value":"Substrate-recognition component of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex involved in cell cycle control and autophagy (PubMed:20921139, PubMed:23524951, PubMed:24587252, PubMed:32333458, PubMed:33854232, PubMed:33854235, PubMed:33854239). The DCX(AMBRA1) complex specifically mediates the polyubiquitination of target proteins such as BECN1, CCND1, CCND2, CCND3, ELOC and ULK1 (PubMed:23524951, PubMed:33854232, PubMed:33854235, PubMed:33854239). Acts as an upstream master regulator of the transition from G1 to S cell phase: AMBRA1 specifically recognizes and binds phosphorylated cyclin-D (CCND1, CCND2 and CCND3), leading to cyclin-D ubiquitination by the DCX(AMBRA1) complex and subsequent degradation (PubMed:33854232, PubMed:33854235, PubMed:33854239). By controlling the transition from G1 to S phase and cyclin-D degradation, AMBRA1 acts as a tumor suppressor that promotes genomic integrity during DNA replication and counteracts developmental abnormalities and tumor growth (PubMed:33854232, PubMed:33854235, PubMed:33854239). AMBRA1 also regulates the cell cycle by promoting MYC dephosphorylation and degradation independently of the DCX(AMBRA1) complex: acts via interaction with the catalytic subunit of protein phosphatase 2A (PPP2CA), which enhances interaction between PPP2CA and MYC, leading to MYC dephosphorylation and degradation (PubMed:25438055, PubMed:25803737). Acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes (PubMed:25499913, PubMed:30166453). Acts as a key regulator of autophagy by modulating the BECN1-PIK3C3 complex: controls protein turnover during neuronal development, and regulates normal cell survival and proliferation (PubMed:21358617). In normal conditions, AMBRA1 is tethered to the cytoskeleton via interaction with dyneins DYNLL1 and DYNLL2 (PubMed:20921139). Upon autophagy induction, AMBRA1 is released from the cytoskeletal docking site to induce autophagosome nucleation by mediating ubiquitination of proteins involved in autophagy (PubMed:20921139). The DCX(AMBRA1) complex mediates 'Lys-63'-linked ubiquitination of BECN1, increasing the association between BECN1 and PIK3C3 to promote PIK3C3 activity (By similarity). In collaboration with TRAF6, AMBRA1 mediates 'Lys-63'-linked ubiquitination of ULK1 following autophagy induction, promoting ULK1 stability and kinase activity (PubMed:23524951). Also activates ULK1 via interaction with TRIM32: TRIM32 stimulates ULK1 through unanchored 'Lys-63'-linked polyubiquitin chains (PubMed:31123703). Also acts as an activator of mitophagy via interaction with PRKN and LC3 proteins (MAP1LC3A, MAP1LC3B or MAP1LC3C); possibly by bringing damaged mitochondria onto autophagosomes (PubMed:21753002, PubMed:25215947). Also activates mitophagy by acting as a cofactor for HUWE1; acts by promoting HUWE1-mediated ubiquitination of MFN2 (PubMed:30217973). AMBRA1 is also involved in regulatory T-cells (Treg) differentiation by promoting FOXO3 dephosphorylation independently of the DCX(AMBRA1) complex: acts via interaction with PPP2CA, which enhances interaction between PPP2CA and FOXO3, leading to FOXO3 dephosphorylation and stabilization (PubMed:30513302). May act as a regulator of intracellular trafficking, regulating the localization of active PTK2/FAK and SRC (By similarity). Also involved in transcription regulation by acting as a scaffold for protein complexes at chromatin (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23524951"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30166453"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33854232"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33854235"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33854239"}],"value":"Protein modification; protein ubiquitination"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"A2AH22"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16949367"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20921139"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21358617"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23524951"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23954414"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25215947"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25438055"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25499913"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25803737"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30166453"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30217973"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30513302"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31123703"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33854232"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33854239"}],"value":"Component of the DCX(AMBRA1) E3 ubiquitin ligase complex, also named CRL4(AMBRA1), at least composed of CUL4 (CUL4A or CUL4B), DDB1, AMBRA1 and RBX1 (PubMed:16949367, PubMed:25499913, PubMed:30166453, PubMed:33854232, PubMed:33854239). Interacts with BECN1 (PubMed:21358617, PubMed:25438055). Probably forms a complex with BECN1 and PIK3C3 (By similarity). Interacts with BECN2 (PubMed:23954414). Interacts with BCL2; leading to prevent interaction with BCN1 and autophagy, interaction is disrupted upon autophagy induction (PubMed:21358617). Interacts with ULK1 (PubMed:25438055). Interacts (via PxP motifs) with PPP2CA; enhancing interaction between PPP2CA and MYC or FOXO3 (PubMed:25438055, PubMed:30513302). Forms a complex with PPP2CA and BECN1; AMBRA1 and BECN1 components of the complex regulate MYC stability via different pathways (PubMed:25803737). Interacts (TQT motifs) with DYNLL1 and DYNLL2; tethering AMBRA1 and the BECN1-PIK3C3 complex in absence of autophagy (PubMed:20921139). Interacts with TRAF6; interaction is required to mediate 'Lys-63'-linked ubiquitination of ULK1 (PubMed:23524951). Interacts with TRIM32; promoting activation of ULK1 by TRIM32 via unanchored 'Lys-63'-linked polyubiquitin chains (PubMed:31123703). Interacts with PRKN (By similarity). Interacts (via LIR motif) with LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C) (PubMed:25215947, PubMed:30217973). Interacts with HUWE1 (PubMed:30217973). Interacts with PTK2/FAK (By similarity). Interacts with SRC; required for SRC trafficking to autophagosomes (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q9C0C7","intActId":"EBI-2512975"},"interactantTwo":{"uniProtKBAccession":"P10415","geneName":"BCL2","intActId":"EBI-77694"},"numberOfExperiments":10,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9C0C7","intActId":"EBI-2512975"},"interactantTwo":{"uniProtKBAccession":"Q14457","geneName":"BECN1","intActId":"EBI-949378"},"numberOfExperiments":9,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9C0C7","intActId":"EBI-2512975"},"interactantTwo":{"uniProtKBAccession":"P30153","geneName":"PPP2R1A","intActId":"EBI-302388"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9C0C7","intActId":"EBI-2512975"},"interactantTwo":{"uniProtKBAccession":"O75385","geneName":"ULK1","intActId":"EBI-908831"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9C0C7","intActId":"EBI-2512975"},"interactantTwo":{"uniProtKBAccession":"P12504","geneName":"vif","intActId":"EBI-779991"},"numberOfExperiments":5,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"Q9C0C7-3","intActId":"EBI-16042318"},"interactantTwo":{"uniProtKBAccession":"Q9Y4K3","geneName":"TRAF6","intActId":"EBI-359276"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9C0C7-3","intActId":"EBI-16042318"},"interactantTwo":{"uniProtKBAccession":"O75385","geneName":"ULK1","intActId":"EBI-908831"},"numberOfExperiments":4,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"A2AH22"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20921139"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21358617"}],"value":"Localizes to the cytoskeleton in absence of autophagy induction (PubMed:20921139). Upon autophagy induction, AMBRA1 relocalizes to the endoplasmic reticulum to enable autophagosome nucleation (PubMed:20921139). Partially localizes at mitochondria in normal conditions (PubMed:21358617). Also localizes to discrete punctae along the ciliary axoneme (By similarity)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20921139"}],"value":"Endoplasmic reticulum","id":"SL-0095"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20921139"}],"value":"Cytoplasm, cytoskeleton","id":"SL-0090"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"A2AH22"}],"value":"Cytoplasmic vesicle, autophagosome","id":"SL-0023"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21358617"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25215947"}],"value":"Mitochondrion","id":"SL-0173"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"A2AH22"}],"value":"Cytoplasm, cytosol","id":"SL-0091"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32616651"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"A2AH22"}],"value":"Cell junction, focal adhesion","id":"SL-0118"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q9C0C7-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q9C0C7-2"],"sequenceIds":["VSP_030657"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"isoformIds":["Q9C0C7-3"],"sequenceIds":["VSP_030655"],"isoformSequenceStatus":"Described"},{"name":{"value":"4"},"isoformIds":["Q9C0C7-4"],"sequenceIds":["VSP_030654"],"isoformSequenceStatus":"Described"},{"name":{"value":"5"},"isoformIds":["Q9C0C7-5"],"sequenceIds":["VSP_030654","VSP_030656"],"isoformSequenceStatus":"Described"},{"name":{"value":"6"},"isoformIds":["Q9C0C7-6"],"sequenceIds":["VSP_030654","VSP_030655","VSP_045989","VSP_045990"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28059583"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30513302"}],"value":"Negatively regulated by microRNA 7-3HG (miR7-3HG), which targets the 3' untranslated (3'-UTR) region of AMBRA1 transcripts, leading to a decrease of AMBRA1 mRNA and protein levels, thereby inhibiting autophagy (PubMed:28059583). Strongly up-regulated during egulatory T-cells (Treg) differentiation (PubMed:30513302)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25438055"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30513302"}],"value":"The PxP motifs mediate interaction with the catalytic subunit of protein phosphatase 2A (PPP2CA)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20921139"}],"value":"The TQT motifs mediate interaction with the dynein light chain proteins DYNLL1 and DYNLL2, tethering AMBRA1 to the cytoskeleton in absence of autophagy"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25215947"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30217973"}],"value":"The LIR motif (LC3-interacting region) is required for the interaction with the ATG8 family proteins GABARAP and MAP1LC3B"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20921139"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23524951"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25438055"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30217973"}],"value":"Phosphorylation at Ser-52 by MTOR inhibits its ability to regulate autophagy and mediate ubiquitination of ULK1 (PubMed:23524951). Phosphorylation by ULK1 in response to autophagy induction abolishes interaction with DYNLL1 and DYNLL2, releasing AMBRA1 from the cytoskeletal docking site to induce autophagosome nucleation (PubMed:20921139). Phosphorylation by MTOR inhibits interaction with PPP2CA and subsequent dephosphorylation of MYC (PubMed:25438055). Phosphorylation at Ser-1043 by CHUK/IKKA promotes its interaction with ATG8 family proteins GABARAP and MAP1LC3B and its mitophagic activity (PubMed:30217973)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25499913"}],"value":"Ubiquitinated by RNF2 via 'Lys-48'-linkage in unstressed cells, leading to its degradation by the proteasome (PubMed:25499913). Induction of autophagy promotes stabilization via interaction with CUL4 (CUL4A or CUL4B) and DDB1 (PubMed:25499913). Upon prolonged starvation, ubiquitinated and degraded, terminating the autophagy response (PubMed:25499913)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22441670"}],"value":"Undergoes proteolytic processing by caspase-6 (CASP6), caspase-7 (CASP7) and caspase-8 (CASP8) during apoptosis, resulting in the dismantling of the autophagic machinery and the accomplishment of the programmed cell death program (PubMed:22441670). Also cleaved by calpains during apoptosis, which mediate a complete proteolytic degradation (PubMed:22441670)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the WD repeat AMBRA1 family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"BAA91067.1","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"BAB14457.1","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"BAB21827.1","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","molecule":"Isoform 6","sequenceCautionType":"Frameshift","sequence":"AL834190","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1298,"modifier":"EXACT"}},"description":"Activating molecule in BECN1-regulated autophagy protein 1","featureId":"PRO_0000315703"},{"type":"Repeat","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"WD 1"},{"type":"Repeat","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"WD 2"},{"type":"Repeat","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"WD 3"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"Interaction with 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