NP_001280126.1
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
27,067 Da
NCBI Official Full Name
E3 ubiquitin-protein ligase CHIP isoform b
NCBI Official Synonym Full Names
STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase
NCBI Official Synonym Symbols
CHIP; UBOX1; SCAR16; HSPABP2; NY-CO-7; SDCCAG7 [Similar Products]
NCBI Protein Information
E3 ubiquitin-protein ligase CHIP; CLL-associated antigen KW-8; antigen NY-CO-7; carboxy terminus of Hsp70-interacting protein; heat shock protein A binding protein 2 (c-terminal); serologically defined colon cancer antigen 7
UniProt Protein Name
E3 ubiquitin-protein ligase CHIP
UniProt Synonym Protein Names
Antigen NY-CO-7; CLL-associated antigen KW-8; Carboxy terminus of Hsp70-interacting protein; STIP1 homology and U box-containing protein 1
UniProt Entry Name
CHIP_HUMAN
NCBI Summary for STUB1
This gene encodes a protein containing tetratricopeptide repeat and a U-box that functions as a ubiquitin ligase/cochaperone. The encoded protein binds to and ubiquitinates shock cognate 71 kDa protein (Hspa8) and DNA polymerase beta (Polb), among other targets. Mutations in this gene cause spinocerebellar ataxia, autosomal recessive 16. Alternative splicing results in multiple transcript variants. There is a pseudogene for this gene on chromosome 2. [provided by RefSeq, Jun 2014]
UniProt Comments for STUB1
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. Homodimer. Interacts with BAG2, and with the E2 ubiquitin conjugating enzymes UBE2D1, UBE2D2 and UBE2D3. Interacts with the C-terminal domains of HSPA8 and HSPA1A. Detected in a ternary complex containing STUB1, HSPA1A and HSPBP1. Interacts with MKKS. Interacts with DYX1C1 and POLB. Interacts (via TPR repeats) with HSP90AA1. Interacts (when monoubiquitinated) with ATXN3. Interacts with UBE2W. Interacts (via the U-box domain) with the UBE2V2- UBE2N heterodimer; the complex has a specific 'Lys-63'-linked polyubiquitination activity. Interacts with DNAJB6. Highly expressed in skeletal muscle, heart, pancreas, brain and placenta. Detected in kidney, liver and lung. 2 isoforms of the human protein are produced by alternative splicing.
Protein type: Adaptor/scaffold; Ligase; Ubiquitin conjugating system; EC 6.3.2.19; Ubiquitin ligase; EC 6.3.2.-
Chromosomal Location of Human Ortholog: 16p13.3
Cellular Component: nucleoplasm; intermediate filament cytoskeleton; endoplasmic reticulum; ubiquitin conjugating enzyme complex; cytoplasm; plasma membrane; cytosol; ubiquitin ligase complex; nuclear inclusion body
Molecular Function: protein binding, bridging; protein binding; protein homodimerization activity; enzyme binding; G-protein-coupled receptor binding; TPR domain binding; ubiquitin protein ligase binding; ubiquitin-protein ligase activity; misfolded protein binding; Hsp70 protein binding; Hsp90 protein binding; SMAD binding; kinase binding; ligase activity
Biological Process: ubiquitin-dependent protein catabolic process; proteasomal ubiquitin-dependent protein catabolic process; protein autoubiquitination; protein polyubiquitination; unfolded protein response; protein maturation; misfolded or incompletely synthesized protein catabolic process; DNA repair; ubiquitin-dependent SMAD protein catabolic process; positive regulation of protein ubiquitination; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; positive regulation of ubiquitin-protein ligase activity; transforming growth factor beta receptor signaling pathway; regulation of glucocorticoid metabolic process; negative regulation of protein binding; negative regulation of transforming growth factor beta receptor signaling pathway
Disease: Spinocerebellar Ataxia, Autosomal Recessive 16
Research Articles on STUB1
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Products associated with STUB1 recombinant protein
Pathways associated with STUB1 recombinant protein
Diseases associated with STUB1 recombinant protein
Organs/Tissues associated with STUB1 recombinant protein
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