{"metadata":{"accession":"PTHR10666","entry_id":null,"type":"family","go_terms":null,"source_database":"panther","member_databases":null,"integrated":"IPR050158","hierarchy":null,"name":{"name":"Ubiquitin and ubiquitin-like","short":"Ubiquitin_ubiquitin-like"},"description":[{"text":"The ubiquitin family is characterized by its role in post-translational modification, where ubiquitin or ubiquitin-like proteins are covalently attached to target proteins, influencing their stability, localization, or activity. Ubiquitination involves the conjugation of ubiquitin to lysine residues on substrates through an isopeptide bond, often leading to proteasomal degradation. However, ubiquitin also participates in non-proteolytic functions such as DNA repair, cell cycle regulation, endocytosis, and signal transduction. Polyubiquitin chains linked through different lysine residues or linearly through the N-terminal methionine can have distinct cellular roles. Some family members are involved in ribosome biogenesis as fusion proteins with ribosomal proteins, contributing to the structure and function of ribosomes. The family includes ubiquitin-like modifiers such as NEDD8, which regulate cell cycle and embryogenesis by modifying cullins and other proteins to alter E3 ligase activity.","llm":true,"checked":false,"updated":false}],"wikipedia":null,"literature":null,"set_info":null,"overlaps_with":null,"counters":{"subfamilies":81,"domain_architectures":0,"interactions":0,"matches":30062,"pathways":0,"proteins":30062,"proteomes":3375,"sets":0,"structural_models":{"alphafold":26882,"bfvd":31},"structures":1322,"taxa":11306},"entry_annotations":{"hmm":0,"logo":0},"cross_references":{},"is_llm":true,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"6q00","name":"TDP2 UBA Domain Bound to Ubiquitin at 0.85 Angstroms Resolution, Crystal Form 1"}}}