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STUB1, or CHIP, is a ubiquitin ligase/cochaperone that participates in protein quality control by targeting a broad range of chaperone protein substrates for degradation (Min et al., 2008 [PubMed 18411298]).[supplied by OMIM, Jul 2009].. Additionally we are shipping STIP1 Homology and U-Box Containing Protein 1 Antibodies (110) and STIP1 Homology and U-Box Containing Protein 1 Kits (11) and many more products for this protein.
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Through selective degradation of Clp subunits, AtCHIP could positively regulate homeostasis of Clp proteolytic subunits and maximize the production of functional chloroplasts. Similar results were obtained from transgenic tobacco plants.
we propose that CHIP and NBR1 (show NBR1 Proteins) mediate two distinct but complementary anti-proteotoxic pathways and protein's propensity to aggregate under stress conditions is one of the critical factors for pathway selection of protein degradation
Hsc70-4 and CHIP were highly induced in ppi2 mutant plants, where they mediated the degradation of chloroplast-targeted precursors through the ubiquitin-26S proteasome (show Psmd4 Proteins) system.
AtCHIP, an E3 ubiquitin liagase, functions upstream of protein phosphatase 2A in stress-responsive signal transduction pathways under conditions of low temperature or in the dark. [AtCHIP]
The interaction of CHIP with FtsH1 in vitro, in normal and in CHIP-over-expressing plants is reported.
CHIP is a negative regulator of RIPK1 (show RIPK1 Proteins) and RIPK3 (show RIPK3 Proteins), thus inhibiting necroptosis.
our study demonstrated that over-expressing miR (show MLXIP Proteins)-21 in UCBMSCs could improve neovascularization in Critical limb ischemia (CLI (show CLU Proteins)) through enhancing HIF-1alpha (show HIF1A Proteins) activity by targeting CHIP, which may hold great therapeutic promise in treating CLI (show CLU Proteins)
PABPN1 (show PABPN1 Proteins) interacts with and is stabilized by heat shock protein 90 (show HSP90 Proteins).
CHIP targets Osx (show SP7 Proteins) for ubiquitination and degradation in osteoblasts after chronic exposure to TNF-alpha (show TNF Proteins).
CHIP/TRAF3 (show TRAF3 Proteins)/NIK (show MAP4K4 Proteins) interactions recruit NIK (show MAP4K4 Proteins) to E3 ligase complexes for ubiquitination and degradation, thus maintaining NIK (show MAP4K4 Proteins) at low levels
Cbl-b, together with Stub1, ubiquitinate Foxp3 (show FOXP3 Proteins), and regulate tTreg development.
CHIP regulates the levels of FMR1 (show FMR1 Proteins) as an E3 ubiquitin ligase (show MUL1 Proteins) in phosphorylation-dependent manner, suggesting that CHIP regulates FMR1 (show FMR1 Proteins)-mediated translational repression by regulating the levels of FMR1 (show FMR1 Proteins).
The cardiac CHIP appears to play a role in regulating autophagy during the development of cardiac hypertrophy, possibly by its role in supporting Akt (show AKT1 Proteins) signalling, induced by voluntary running in vivo.
Ebp1 (show NFKB1 Proteins) p42 (show EPB42 Proteins) isoform regulates the proteasomal degradation of the p85 (show ECM1 Proteins) regulatory subunit of PI3K by recruiting a chaperone-E3 ligase complex HSP70 (show HSP70 Proteins)/CHIP.
CHIP as a novel causative gene for autosomal recessive cerebellar ataxia (show USP14 Proteins)
Cdk5 (show CDK5 Proteins)-mediated phosphorylation of CHIP negatively regulates its neuroprotective function, thereby contributing to neuronal cell death progression following neurotoxic stimuli.
CHIP is a bona fide negative regulator of the RIPK1 (show RIPK1 Proteins)-RIPK3 (show RIPK3 Proteins) necrosome formation leading to desensitization of TNF (show TNF Proteins)-mediated necroptosis
Protein-protein interactions modulate the docking-dependent E3-ubiquitin ligase (show MUL1 Proteins) activity of CHIP.
Data show that the E3 ubiquitin ligase (show MUL1 Proteins) CHIP interacts with protein arginine methyltransferase-5 (PRMT5 (show PRMT5 Proteins)) both in vivo and in vitro.
These results indicate that CHIP decreases the Kv1.5 (show KCNA5 Proteins) protein level and functional channel by facilitating its degradation in concert with chaperone Hsc70 (show HSPA8 Proteins)
detailed and systematic investigation to characterize if there are significant differences in the CHIP in vitro ubiquitination of human Hsp70 (show HSP70 Proteins) and Hsc70 (show HSPA8 Proteins).
CHIP stabilizes amyloid precursor protein (show APP Proteins) via proteasomal degradation and p53 (show TP53 Proteins)-mediated trans-repression of BACE1 (show BACE Proteins).
Our findings demonstrate for the first time that CHIP may be involved in RCC (show XRCC1 Proteins) angiogenesis through regulating VEGF (show VEGFA Proteins) secretion and expression of VEGFR2 (show KDR Proteins).
results indicate that the post-endocytic ubiquitination of CFTR (show CFTR Proteins) by CHIP is a critical step in the peripheral quality control of cell surface DeltaF508 CFTR (show CFTR Proteins)
CHIP docks onto Hsp70/Hsc70 and defines a bipartite mode of interaction between TPR domains and their binding partners.
STUB1, or CHIP, is a ubiquitin ligase/cochaperone that participates in protein quality control by targeting a broad range of chaperone protein substrates for degradation (Min et al., 2008
STIP1 homology and U-box containing protein 1
, STIP1 homology and U box-containing protein 1
, E3 ubiquitin-protein ligase CHIP
, carboxy terminus of Hsp70-interacting protein
, CLL-associated antigen KW-8
, antigen NY-CO-7
, heat shock protein A binding protein 2 (c-terminal)
, serologically defined colon cancer antigen 7
, STIP1 homology and U-Box containing protein 1