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Proteasome Endopeptidase ComplexCysteine EndopeptidasesMultienzyme ComplexesNegative StainingProtease InhibitorsProteasome InhibitorsEndopeptidasesMolecular Sequence DataNeprilysinAmino Acid SequenceSerine EndopeptidasesPituitary GlandElectrophoresis, Polyacrylamide GelThiorphanCysteine Proteinase InhibitorsSerine Proteinase InhibitorsCattleLeupeptinsLiverPHEX Phosphate Regulating Neutral EndopeptidasePeptide HydrolasesMetalloendopeptidasesSubstrate SpecificityBoronic AcidsPyrazinesEndopeptidase KCathepsinsHydrolysisThrombectomyOligopeptidesKineticsChymotrypsinUbiquitinsHemostatic DisordersCathepsin BBase SequencePapainalpha 1-AntitrypsinMyeloblastinGlycopeptidesProtein Processing, Post-TranslationalCystatinsTrypsin InhibitorsDipeptidesMultilocus Sequence TypingCathepsin LPancreatic ElastaseProteolysisSequence Homology, Amino AcidPeptide FragmentsPepstatinsRecombinant ProteinsMolecular WeightPeptidesNeurotensinBinding SitesLysostaphinHydrogen-Ion ConcentrationAspartic Acid EndopeptidasesCloning, MolecularEnzyme PrecursorsAcetylcysteineCarboxypeptidasesUbiquitinationCell LineDiazomethanealpha-MacroglobulinsTrypsinChromatography, GelChromatography, High Pressure LiquidCathepsin GSerpinsTime FactorsProtein PrecursorsProtein BindingSubtilisinsAminopeptidasesSequence Analysis, DNAProteinsCaseinsDrug Resistance, Multiple, BacterialLeukocyte ElastaseBlotting, WesternAtrial Natriuretic FactorMutationEnzyme ActivationPolyubiquitinEnzyme StabilityThiazepinesSequence AlignmentProtein ConformationProtein Structure, TertiaryThermolysinModels, MolecularAmino AcidsCalpainCells, CulturedCathepsin DChromatography, Ion ExchangeProteinase Inhibitory Proteins, Secretory
ProteinCYSTEINE ENDOPEPTIDASESProteinsBindsActivity
Protein1
  • The encoded protein is a member of the proteasome B-type family, also known as the T1B family, and is a 20S core beta subunit in the proteasome. (antibodies-online.com)
CYSTEINE ENDOPEPTIDASES1
Proteins4
  • A large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. (bvsalud.org)
  • The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme. (bvsalud.org)
  • Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. (nih.gov)
  • The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. (nih.gov)
Binds2
  • Carfilzomib irreversibly and selectively binds to N-terminal threonine-containing active sites of the 20S proteasome, the proteolytic core particle within the 26S proteasome. (drugbank.com)
  • P61959.1 MADEKPKEGVKTENNDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCERQGLSMRQIRFRFDGQPINETDTPAQLEMEDEDTIDVFQQQTGGVY 1367453_at NP_446195 6.64 hsp90 co-chaperone Cdc37 Cdc37 Rattus norvegicus " Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp9N/A complex, resulting in stabilization and promotion of their activity. (nih.gov)
Activity2
  • Intravenous carfilzomib administration resulted in suppression of proteasome chymotrypsin-like activity when measured in blood 1 hour after the first dose. (drugbank.com)
  • the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). (nih.gov)