STUB1

STUB1 (STIP1 homology and U-Box containing protein 1) is a human gene that codes for the protein CHIP (C terminus of HSC70-Interacting Protein).^[5][6]

STUB1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4KBQ
Identifiers
Aliases	STUB1, CHIP, HSPABP2, NY-CO-7, SCAR16, SDCCAG7, UBOX1, STIP1 homology and U-box containing protein 1, SCA48
External IDs	OMIM: 607207; MGI: 1891731; HomoloGene: 4281; GeneCards: STUB1; OMA:STUB1 - orthologs
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16p13.3 Start 680,224 bp[1] End 682,870 bp[1]
Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17 A3.3|17 12.93 cM Start 26,049,479 bp[2] End 26,052,378 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in lateral nuclear group of thalamus postcentral gyrus pars compacta external globus pallidus pars reticulata spinal ganglia superior vestibular nucleus ventral tegmental area parotid gland pons Top expressed in neural tube lens bone marrow islet of Langerhans mesencephalon adrenal gland rhombencephalon striatum of neuraxis hypothalamus urinary bladder More reference expression data BioGPS More reference expression data
Gene ontology Molecular function Hsp90 protein binding protein-macromolecule adaptor activity protein homodimerization activity misfolded protein binding ubiquitin protein ligase activity ubiquitin-protein transferase activity ubiquitin-ubiquitin ligase activity kinase binding protein binding enzyme binding TPR domain binding G protein-coupled receptor binding ubiquitin protein ligase binding transferase activity Hsp70 protein binding SMAD binding heat shock protein binding tau protein binding chaperone binding Cellular component cytoplasm ubiquitin ligase complex nucleoplasm Z discdkac endoplasmic reticulum nuclear inclusion body extracellular exosome ubiquitin conjugating enzyme complex nucleus cytosol chaperone complex Biological process positive regulation of chaperone-mediated protein complex assembly regulation of protein stability ubiquitin-dependent protein catabolic process regulation of glucocorticoid metabolic process protein K63-linked ubiquitination protein maturation protein polyubiquitination protein quality control for misfolded or incompletely synthesized proteins negative regulation of protein binding ubiquitin-dependent SMAD protein catabolic process cellular response to DNA damage stimulus endoplasmic reticulum unfolded protein response positive regulation of ubiquitin-protein transferase activity protein ubiquitination positive regulation of protein ubiquitination positive regulation of proteasomal ubiquitin-dependent protein catabolic process DNA repair proteasome-mediated ubiquitin-dependent protein catabolic process protein autoubiquitination cellular response to misfolded protein ERBB2 signaling pathway negative regulation of transforming growth factor beta receptor signaling pathway ubiquitin-dependent ERAD pathway response to ischemia cellular response to heat chaperone-mediated autophagy cellular response to hypoxia Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10273 56424 Ensembl ENSG00000103266 ENSMUSG00000039615 UniProt Q9UNE7 Q9WUD1 RefSeq (mRNA) NM_005861 NM_001293197 NM_019719 RefSeq (protein) NP_001280126 NP_005852 NP_062693 Location (UCSC) Chr 16: 0.68 – 0.68 Mb Chr 17: 26.05 – 26.05 Mb PubMed search [3] [4]
Wikidata
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Function

The CHIP protein encoded by this gene binds to and inhibits the ATPase activity of the chaperone proteins HSC70 and HSP70 and blocks the forward reaction of the HSC70-HSP70 substrate-binding cycle.^[6] In addition, CHIP possesses E3 ubiquitin ligase activity and promotes ubiquitylation,^[7] mainly of chaperone-bound misfolded proteins.

CHIP enhances HSP70 induction during acute stress and also mediates its turnover during the stress recovery process. Hence CHIP appears to maintain protein homeostasis by controlling chaperone levels during stress and recovery.^[8]

Mutations in STUB1 cause spinocerebellar ataxia type 16.^{[9][failed verification]}

Interactions

STUB1 has been shown to interact with:

• C-Raf,^[10]
• DNAJB1,^[6]
• HSPA1A,^[6][11]
• HSPA4,^[6]
• HSPA8,^[6]
• Parkin (ligase),^[11] and
• RUNX2.^[12]