CHIP E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation. Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation. Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner. Likely mediates polyubiquitination and downregulates plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation. May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation. Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation. Expressed in differentiated myotubes (at protein level) (PubMed:17369820). Highly expressed in skeletal muscle, heart, pancreas, brain and placenta (PubMed:10330192, PubMed:11435423). Detected in kidney, liver and lung (PubMed:10330192, PubMed:11435423). 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Adaptor/scaffold; EC 6.3.2.-; EC 6.3.2.19; Ligase; Ubiquitin conjugating system; Ubiquitin ligase
Chromosomal Location of human Ortholog: 16p13.3
Cellular Component:  cytoplasm; cytosol; endoplasmic reticulum; nuclear inclusion body; nucleoplasm; nucleus; protein folding chaperone complex; ubiquitin conjugating enzyme complex; ubiquitin ligase complex; Z disc
Molecular Function:  enzyme binding; G protein-coupled receptor binding; heat shock protein binding; Hsp70 protein binding; Hsp90 protein binding; kinase binding; misfolded protein binding; protein binding; protein homodimerization activity; protein-folding chaperone binding; protein-macromolecule adaptor activity; SMAD binding; tau protein binding; TPR domain binding; ubiquitin protein ligase activity; ubiquitin protein ligase binding; ubiquitin-protein transferase activity; ubiquitin-ubiquitin ligase activity
Biological Process:  cellular response to heat; cellular response to hypoxia; cellular response to misfolded protein; chaperone-mediated autophagy; DNA repair; endoplasmic reticulum unfolded protein response; ERBB2 signaling pathway; negative regulation of protein binding; negative regulation of transforming growth factor beta receptor signaling pathway; positive regulation of chaperone-mediated protein complex assembly; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; positive regulation of protein ubiquitination; positive regulation of proteolysis; positive regulation of ubiquitin-protein transferase activity; proteasome-mediated ubiquitin-dependent protein catabolic process; protein autoubiquitination; protein K63-linked ubiquitination; protein maturation; protein monoubiquitination; protein polyubiquitination; protein quality control for misfolded or incompletely synthesized proteins; protein stabilization; protein ubiquitination; regulation of glucocorticoid metabolic process; regulation of protein stability; response to ischemia; ubiquitin-dependent ERAD pathway; ubiquitin-dependent protein catabolic process
Disease: Spinocerebellar Ataxia 48; Spinocerebellar Ataxia, Autosomal Recessive 16
Reference #:  Q9UNE7 (UniProtKB)
Alt. Names/Synonyms: Antigen NY-CO-7; Carboxy terminus of Hsp70-interacting protein; CHIP; CLL-associated antigen KW-8; E3 ubiquitin-protein ligase CHIP; heat shock protein A binding protein 2 (c-terminal); HSPABP2; NY-CO-7; RING-type E3 ubiquitin transferase CHIP; SCA48; SCAR16; SDCCAG7; serologically defined colon cancer antigen 7; STIP1 homology and U box-containing protein 1; STIP1 homology and U-box containing protein 1; STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase; STUB1; UBOX1
Gene Symbols: STUB1
Molecular weight: 34,856 Da
Basal Isoelectric point: 5.61  Predict pI for various phosphorylation states
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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CHIP

Protein Structure Not Found.


Cross-references to other databases:  AlphaFold  |  STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  InnateDB  |  Ensembl Protein