Aliases for STUB1 Gene
- STIP1 Homology And U-Box Containing Protein 1, E3 Ubiquitin Protein Ligase 2 3
- CHIP 3 4 6
- Carboxy Terminus Of Hsp70-Interacting Protein 3 4
- CLL-Associated Antigen KW-8 3 4
- Antigen NY-CO-7 3 4
- Heat Shock Protein A Binding Protein 2 (C-Terminal) 3
- STIP1 Homology And U-Box Containing Protein 1 2
- STIP1 Homology And U Box-Containing Protein 1 4
- Serologically Defined Colon Cancer Antigen 7 3
External Ids for STUB1 Gene
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]
GeneCards Summary for STUB1 Gene
STUB1 (STIP1 Homology And U-Box Containing Protein 1, E3 Ubiquitin Protein Ligase) is a Protein Coding gene. Diseases associated with STUB1 include spinocerebellar ataxia, autosomal recessive 16 and cerebellar ataxia and hypogonadotropic hypogonadism. Among its related pathways are Signaling by FGFR and Signaling by GPCR. GO annotations related to this gene include protein homodimerization activity and enzyme binding.
UniProtKB/Swiss-Prot for STUB1 Gene
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. 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 (PubMed:23973223).