{"metadata":{"accession":"IPR029421","entry_id":null,"type":"domain","go_terms":null,"source_database":"interpro","member_databases":{"pfam":{"PF14918":"MDM2-binding"}},"integrated":null,"hierarchy":{"accession":"IPR029421","name":"MDM2-binding protein, N-terminal domain","type":"Domain","children":[]},"name":{"name":"MDM2-binding protein, N-terminal domain","short":"MTBP_N"},"description":[{"text":"<p>This entry represents the N-terminal domain of the MDM2-binding protein (MTBP). MDM2 is an E3 ubiquitin-protein ligase that mediates ubiquitination of p53, leading to its degradation by the proteasome [[cite:PUB00068076]]. MTBP inhibits autoubiquitination of MDM2, thereby enhancing MDM2 stability, and this promotes MDM2-mediated ubiquitination of p53 and its subsequent degradation [[cite:PUB00068081]]. Mouse MTBP also inhibits cancer cell migration by interacting with alpha-actinin-4 (ACTN4) [[cite:PUB00070070]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00068076":{"PMID":14707283,"ISBN":null,"volume":"1","issue":"14","year":2003,"title":"The MDM2-p53 interaction.","URL":null,"raw_pages":"1001-8","medline_journal":"Mol Cancer Res","ISO_journal":"Mol. Cancer Res.","authors":["Moll UM","Petrenko O."],"DOI_URL":null},"PUB00070070":{"PMID":22370640,"ISBN":null,"volume":"32","issue":"4","year":2013,"title":"MTBP suppresses cell migration and filopodia formation by inhibiting ACTN4.","URL":null,"raw_pages":"462-70","medline_journal":"Oncogene","ISO_journal":"Oncogene","authors":["Agarwal N","Adhikari AS","Iyer SV","Hekmatdoost K","Welch DR","Iwakuma T."],"DOI_URL":"http://dx.doi.org/10.1038/onc.2012.69"},"PUB00068081":{"PMID":15632057,"ISBN":null,"volume":"25","issue":"2","year":2005,"title":"Regulation of p53 and MDM2 activity by MTBP.","URL":null,"raw_pages":"545-53","medline_journal":"Mol Cell Biol","ISO_journal":"Mol. Cell. Biol.","authors":["Brady M","Vlatkovic N","Boyd MT."],"DOI_URL":"http://dx.doi.org/10.1128/MCB.25.2.545-553.2005"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":18,"interactions":0,"matches":1002,"pathways":2,"proteins":988,"proteomes":627,"sets":0,"structural_models":{"alphafold":900,"bfvd":0},"structures":0,"taxa":2108},"entry_annotations":{"alignment:seed":9,"alignment:full":760},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}