{"metadata":{"accession":"PF04402","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR007497","hierarchy":null,"name":{"name":"Protein of unknown function (DUF541)","short":"SIMPL"},"description":[{"text":"<p>Members of this family have so far been found in bacteria and mouse SwissProt or TrEMBL entries.  However possible family members have also been identified in translated rat (Genbank:AW144450) and human (Genbank:AI478629) ESTs. A mouse family member has been named SIMPL (signalling molecule that associates with mouse pelle-like kinase).  SIMPL appears to facilitate and/or regulate complex formation between IRAK/mPLK (IL-1 receptor-associated kinase) and IKK (inhibitor of kappa-B kinase) containing complexes, and thus regulate NF-kappa-B activity [[cite:PUB00010115]]. Separate experiments demonstrate that a mouse family member (named LaXp180) binds the Listeria monocytogenes surface protein ActA, which is a virulence factor that induces actin polymerisation. It may also bind stathmin, a protein involved in signal transduction and in the regulation of microtubule dynamics [[cite:PUB00009982]]. In bacteria its function is unknown, but it is thought to be located in the periplasm or outer membrane.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00010115":{"PMID":11096118,"ISBN":null,"volume":"276","issue":"11","year":2001,"title":"SIMPL is a tumor necrosis factor-specific regulator of nuclear factor-kappaB activity.","URL":null,"raw_pages":"7859-66","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Vig E","Green M","Liu Y","Yu KY","Kwon HJ","Tian J","Goebl MG","Harrington MA."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M010399200"},"PUB00009982":{"PMID":11207567,"ISBN":null,"volume":"2","issue":"2","year":2000,"title":"LaXp180, a mammalian ActA-binding protein, identified with the yeast two-hybrid system, co-localizes with intracellular Listeria monocytogenes.","URL":null,"raw_pages":"101-14","medline_journal":"Cell Microbiol","ISO_journal":"Cell. Microbiol.","authors":["Pfeuffer T","Goebel W","Laubinger J","Bachmann M","Kuhn M."],"DOI_URL":"http://dx.doi.org/10.1046/j.1462-5822.2000.00034.x"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":17,"interactions":0,"matches":16828,"pathways":0,"proteins":16767,"proteomes":13193,"sets":0,"structural_models":{"alphafold":10934},"structures":3,"taxa":20114},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":465,"alignment:full":8519},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"7c50","name":"Crystal structure of a Simpl-like protein from Campylobacter jejuni (selenomethionine-incorporated protein)"}}}