{"metadata":{"accession":"cd16817","entry_id":null,"type":"domain","go_terms":null,"source_database":"cdd","member_databases":null,"integrated":null,"hierarchy":null,"name":{"name":"Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 157 (RNF157) and similar proteins","short":"mRING-HC-C3HC5_RNF157"},"description":[{"text":"<p>RNF157 is a cytoplasmic E3 ubiquitin ligase predominantly expressed in brain. It is a homolog of the E3 ligase mahogunin ring finger-1 (MGRN1). In cultured neurons, it promotes neuronal survival in an E3 ligase-dependent manner. In contrast, it supports growth and maintenance of dendrites independent of its E3 ligase activity. RNF157 interacts with and ubiquitinates the adaptor protein APBB1 (amyloid beta precursor protein-binding, family B, member 1 or Fe65), which regulates neuronal survival, but not dendritic growth downstream of RNF157. The nuclear localization of APBB1 together with its interaction partner RNA-binding protein SART3 (squamous cell carcinoma antigen recognized by T cells 3 or Tip110) is crucial to trigger apoptosis. RNF157 contains a modified C3HC5-type RING-HC finger, and a functionally uncharacterized region, known as domain associated with RING2 (DAR2), N-terminal to the RING finger. The C3HC5-type RING-HC finger is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain. [[cite:PUB00098244]]</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00098244":{"PMID":25342469,"ISBN":null,"volume":"22","issue":"4","year":2015,"title":"Regulation of neuronal survival and morphology by the E3 ubiquitin ligase RNF157.","URL":null,"raw_pages":"626-42","medline_journal":"Cell Death Differ","ISO_journal":"Cell Death Differ","authors":["Matz A","Lee SJ","Schwedhelm-Domeyer N","Zanini D","Holubowska A","Kannan M","Farnworth M","Jahn O","Gopfert MC","Stegmuller J."],"DOI_URL":null}},"set_info":{"accession":"cl17238","name":"RING_Ubox"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":0,"interactions":0,"matches":1293,"pathways":0,"proteins":1293,"proteomes":553,"sets":1,"structural_models":{"alphafold":1175,"bfvd":0},"structures":0,"taxa":1819},"entry_annotations":{},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}