{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O75385","secondaryAccessions":["Q9UQ28"],"uniProtkbId":"ULK1_HUMAN","entryAudit":{"firstPublicDate":"1999-07-15","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2011-01-11","entryVersion":226,"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:0000305"}],"value":"Serine/threonine-protein kinase ULK1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18936157"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25126726"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28821708"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31123703"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37306101"}],"value":"2.7.11.1"}]},"alternativeNames":[{"fullName":{"value":"Autophagy-related protein 1 homolog"},"shortNames":[{"value":"ATG1"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21205641"}],"value":"hATG1"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9693035"}],"value":"Unc-51-like kinase 1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9693035"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:12558"}],"value":"ULK1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9872452"}],"value":"KIAA0722"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11146101"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18936157"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20921139"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21460634"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21795849"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23524951"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25040165"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25126726"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28821708"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29487085"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31123703"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37306101"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39384743"}],"value":"Serine/threonine-protein kinase involved in autophagy in response to starvation (PubMed:18936157, PubMed:21460634, PubMed:21795849, PubMed:23524951, PubMed:25040165, PubMed:29487085, PubMed:31123703). Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes (PubMed:18936157, PubMed:21460634, PubMed:21795849, PubMed:25040165, PubMed:39384743). Part of regulatory feedback loops in autophagy: acts both as a downstream effector and negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR (PubMed:21795849). Activated via phosphorylation by AMPK and also acts as a regulator of AMPK by mediating phosphorylation of AMPK subunits PRKAA1, PRKAB2 and PRKAG1, leading to negatively regulate AMPK activity (PubMed:21460634). May phosphorylate ATG13/KIAA0652 and RPTOR; however such data need additional evidence (PubMed:18936157). Plays a role early in neuronal differentiation and is required for granule cell axon formation (PubMed:11146101). Also phosphorylates SESN2 and SQSTM1 to regulate autophagy (PubMed:25040165, PubMed:37306101). Phosphorylates FLCN, promoting autophagy (PubMed:25126726). Phosphorylates AMBRA1 in response to autophagy induction, releasing AMBRA1 from the cytoskeletal docking site to induce autophagosome nucleation (PubMed:20921139). Phosphorylates ATG4B, leading to inhibit autophagy by decreasing both proteolytic activation and delipidation activities of ATG4B (PubMed:28821708)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17989"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:11604"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83421"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18936157"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25126726"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28821708"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31123703"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37306101"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:17990"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18936157"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25126726"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31123703"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37306101"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18936157"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:46609"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18936157"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O70405"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31123703"}],"value":"Acetylation by KAT5/TIP60 stimulates the protein kinase activity (By similarity). The protein kinase activity is activated by unanchored 'Lys-63'-linked polyubiquitin chains: unanchored 'Lys-63'-linked polyubiquitin chains are catalyzed by TRIM32 in an AMBRA1-dependent manner (PubMed:31123703)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11146101"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18936157"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19211835"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19287211"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19597335"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21795849"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22354037"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22613832"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25040165"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25127057"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25438055"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25891078"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26347139"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27334615"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28561066"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28890335"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31123703"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31806350"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39384743"}],"value":"Interacts with GABARAP and GABARAPL2 (PubMed:11146101). Interacts (via C-terminus) with ATG13 (PubMed:18936157). Part of a complex consisting of ATG13, ATG101, ULK1 and RB1CC1 (PubMed:19287211). Associates with the mammalian target of rapamycin complex 1 (mTORC1) through an interaction with RPTOR; the association depends on nutrient conditions and is reduced during starvation (PubMed:19211835, PubMed:21795849). Interacts with FEZ1; SCOC interferes with FEZ1-binding (PubMed:22354037). Interacts with TBC1D14 (PubMed:22613832). Interacts (phosphorylated form) with TRIM5 (PubMed:25127057). When phosphorylated at Ser-317, interacts with MEFV and BECN1 simultaneously (PubMed:26347139). Interacts with TRIM21 and IRF3, in the presence of TRIM21 (PubMed:26347139). Interacts with SESN2 (PubMed:25040165). Interacts with SQSTM1 (PubMed:25040165). Interacts with C9orf72 (PubMed:27334615). Interacts with WDR45 (PubMed:28561066). Interacts with ATG13; this interaction is increased in the absence of TMEM39A (PubMed:31806350). Interacts with WIPI2 (PubMed:28890335). Interacts with ATP2A2 (PubMed:28890335). Interacts with AMBRA1 (PubMed:25438055, PubMed:31123703). Interacts with IRGM; promoting the coassembly of ULK1 and BECN1 (PubMed:25891078). Interacts with FBXO16 (PubMed:39384743)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"Q9C0C7","geneName":"AMBRA1","intActId":"EBI-2512975"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"Q9C0C7-3","geneName":"AMBRA1","intActId":"EBI-16042318"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"O75143","geneName":"ATG13","intActId":"EBI-2798775"},"numberOfExperiments":15,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"Q96LT7-1","geneName":"C9orf72","intActId":"EBI-16693635"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"Q96LT7-2","geneName":"C9orf72","intActId":"EBI-16693673"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"Q9H0R8","geneName":"GABARAPL1","intActId":"EBI-746969"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"P60520","geneName":"GABARAPL2","intActId":"EBI-720116"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"P42858","geneName":"HTT","intActId":"EBI-466029"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"Q9GZQ8","geneName":"MAP1LC3B","intActId":"EBI-373144"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"Q9BXW4","geneName":"MAP1LC3C","intActId":"EBI-2603996"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"P42345","geneName":"MTOR","intActId":"EBI-359260"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"P04629","geneName":"NTRK1","intActId":"EBI-1028226"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"O15530","geneName":"PDPK1","intActId":"EBI-717097"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"P54646","geneName":"PRKAA2","intActId":"EBI-1383852"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"Q9Y478","geneName":"PRKAB1","intActId":"EBI-719769"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"Q8TDY2","geneName":"RB1CC1","intActId":"EBI-1047793"},"numberOfExperiments":13,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"Q8N122","geneName":"RPTOR","intActId":"EBI-1567928"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"Q9P2M4","geneName":"TBC1D14","intActId":"EBI-2797718"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"Q9Y4K3","geneName":"TRAF6","intActId":"EBI-359276"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75385","intActId":"EBI-908831"},"interactantTwo":{"uniProtKBAccession":"O75385","geneName":"ULK1","intActId":"EBI-908831"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formation of an autophagosome"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Cytoplasm, cytosol","id":"SL-0091"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Preautophagosomal structure","id":"SL-0220"}}]},{"texts":[{"value":"Ubiquitously expressed. Detected in the following adult tissues: skeletal muscle, heart, pancreas, brain, placenta, liver, kidney, and lung"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O70405"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21205641"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25891078"}],"value":"Autophosphorylated. Phosphorylated under nutrient-rich conditions; dephosphorylated during starvation or following treatment with rapamycin. Under nutrient sufficiency, phosphorylated by MTOR/mTOR, disrupting the interaction with AMPK and preventing activation of ULK1 (By similarity). In response to nutrient limitation, phosphorylated and activated by AMPK, leading to activate autophagy (PubMed:21205641, PubMed:25891078)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23524951"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29487085"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39384743"}],"value":"Ubiquitinated via 'Lys-63'-linkage by a complex composed of AMBRA1 and TRAF6 following autophagy induction, promoting ULK1 stability and kinase activity. Deubiquitinated by USP20; leading to ULK1 stability and autophagy initiation (PubMed:29487085). Ubiquitinated by the SCF-FBXO16 E3 ubiquitin ligase, leading to proteasomal degradation (PubMed:39384743)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O70405"}],"value":"Acetylated by KAT5/TIP60 under autophagy induction, promoting protein kinase activity"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00159"}],"value":"Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. APG1/unc-51/ULK1 subfamily"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"BAA34442.2","note":"Extended N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1050,"modifier":"EXACT"}},"description":"Serine/threonine-protein kinase ULK1","featureId":"PRO_0000086780"},{"type":"Domain","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":278,"modifier":"EXACT"}},"description":"Protein 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