{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O15169","secondaryAccessions":["Q4TT26","Q4TT27","Q86YA7","Q8WVW6","Q96S28"],"uniProtkbId":"AXIN1_HUMAN","entryAudit":{"firstPublicDate":"2000-12-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2002-05-10","entryVersion":251,"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":{"value":"Axin-1"}},"alternativeNames":[{"fullName":{"value":"Axis inhibition protein 1"},"shortNames":[{"value":"hAxin"}]}]},"genes":[{"geneName":{"value":"AXIN1"},"synonyms":[{"value":"AXIN"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O35625"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12192039"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16601693"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17210684"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27098453"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28546513"}],"value":"Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (PubMed:12192039, PubMed:27098453, PubMed:28829046). Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway (PubMed:12192039). In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B (PubMed:12192039). Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7 (PubMed:16601693). Also a component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development (PubMed:17210684). Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation (PubMed:17210684). Activates the AMP-activated protein kinase (AMPK) in response to calorie restriction by acting as a molecular adapter: recruited to late endosome membrane by the V-ATPase complex downstream of TULP3, and mediates association between STK11 and its AMPK substrates PRKAA1 and/or PRKAA2, leading to AMPK activation (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O35625"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O70239"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10811618"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11336703"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12192039"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12554650"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12805222"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15262978"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16601693"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17210684"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17318175"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19759537"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21478859"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21799911"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27098453"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28546513"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28829046"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9920888"}],"value":"Homodimer (By similarity). Interacts with ZBED3; the interaction is direct, enhanced by protein kinase GSK3B and casein kinase CSNK1E activities and decreases GSK3B-induced beta-catenin serine and threonine phosphorylations (By similarity). Component of the beta-catenin destruction complex, containing at least, CTNNB1, an axin and GSK3B, that regulates CTNNB1 protein levels through phosphorylation and ubiquitination. Interacts with CTNNB1 (via the armadillo repeats 2-7). Interacts with GSK3B; the interaction hyperphosphorylates CTNNB1 leading to its ubiquitination and destruction (PubMed:12554650, PubMed:17318175, PubMed:28546513). Component of the AXIN1-HIPK2-TP53 complex (PubMed:17210684). Interacts directly in the complex with TP53 and HIPK2 (PubMed:17210684). Interacts with DAXX; the interaction stimulates the interaction of DAXX with TP53, stimulates 'Ser-46' phosphorylation of TP53 and induces cell death on UV irradiation (PubMed:17210684). Also binds APC, SMAD6, SMAD7 and RNF111 (PubMed:10811618, PubMed:16601693). Interacts with DIXDC1; prevents interaction with MAP3K1 (PubMed:15262978). Interacts with MAP3K4 (PubMed:15262978). Interacts with ANKRD6 and AIDA (By similarity). Interacts with MDFI; the interaction decreases AXIN1-mediated JUN N-terminal kinase (JNK) activation (PubMed:12192039). Interacts with MDFIC; the interaction inhibits beta-cateninin-mediated signaling and AXIN1-mediated JUN N-terminal kinase (JNK) activation (PubMed:12192039). Interacts with LRP5 (via its phosphorylated PPPSP motifs); the interaction is stimulated by WNT1 and GSK3B and activates beta-catenin signaling (PubMed:11336703). Interacts (via the C-terminal) with PPP1CA; the interaction dephosphorylates AXIN1 and regulates interaction with GSK3B (PubMed:9920888). Interacts with PPP2CA; the interaction dephosphorylates AXIN1 (PubMed:9920888). Interacts with MACF1 (By similarity). Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B (By similarity). Interacts with TNKS (PubMed:19759537, PubMed:21478859, PubMed:21799911). Interacts with DAB2; the interaction is mutually exclusive with the AXIN1:PPP1CA interaction (PubMed:12805222). Interacts with WDR26 (PubMed:27098453). Interacts with GID8 (PubMed:28829046). Interacts with SIAH1 and SIAH2; both probably catalyze AXIN1 ubiquitination and subsequent proteasome-mediated ubiquitin-dependent degradation (PubMed:28546513). Interaction with GSK3B and AXIN1 is competitive (PubMed:28546513)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"Q5JTC6","geneName":"AMER1","intActId":"EBI-6169747"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"P39687","geneName":"ANP32A","intActId":"EBI-359234"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"Q02410","geneName":"APBA1","intActId":"EBI-368690"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"Q99767","geneName":"APBA2","intActId":"EBI-81711"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"P25054","geneName":"APC","intActId":"EBI-727707"},"numberOfExperiments":17,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"Q5T5U3","geneName":"ARHGAP21","intActId":"EBI-1642518"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"P49407","geneName":"ARRB1","intActId":"EBI-743313"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"O15169","geneName":"AXIN1","intActId":"EBI-710484"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"Q13137","geneName":"CALCOCO2","intActId":"EBI-739580"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"Q9H257-2","geneName":"CARD9","intActId":"EBI-11530605"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"Q2TAC2-2","geneName":"CCDC57","intActId":"EBI-10961624"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"Q14194","geneName":"CRMP1","intActId":"EBI-473101"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"P49674","geneName":"CSNK1E","intActId":"EBI-749343"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"P35222","geneName":"CTNNB1","intActId":"EBI-491549"},"numberOfExperiments":44,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"Q5VWQ8-2","geneName":"DAB2IP","intActId":"EBI-9543020"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"Q12959","geneName":"DLG1","intActId":"EBI-357481"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"Q92796","geneName":"DLG3","intActId":"EBI-80440"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"P78352","geneName":"DLG4","intActId":"EBI-80389"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"O14641","geneName":"DVL2","intActId":"EBI-740850"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"Q92997","geneName":"DVL3","intActId":"EBI-739789"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"Q9UKB1","geneName":"FBXW11","intActId":"EBI-355189"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"Q68DX3","geneName":"FRMPD2","intActId":"EBI-53993476"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15169","intActId":"EBI-710484"},"interactantTwo":{"uniProtKBAccession":"Q08379","geneName":"GOLGA2","intActId":"EBI-618309"},"numberOfExper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