STUB1

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STUB1
Protein STUB1 PDB 2c2l.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases STUB1, CHIP, HSPABP2, NY-CO-7, SCAR16, SDCCAG7, UBOX1, STIP1 homology and U-box containing protein 1
External IDs MGI: 1891731 HomoloGene: 4281 GeneCards: 10273
RNA expression pattern
PBB GE STUB1 217934 x at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_005861
NM_001293197

NM_019719

RefSeq (protein)

NP_001280126.1
NP_005852.2

NP_062693.1

Location (UCSC) Chr 16: 0.68 – 0.68 Mb Chr 17: 25.83 – 25.83 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

STUB1 (STIP1 homology and U-Box containing protein 1), also known as CHIP (C terminus of HSC70-Interacting Protein), is a human gene.[1][2]

Function[edit]

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.[2] In addition, CHIP possesses E3 ubiquitin ligase activity and promotes ubiquitylation.[3] 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.[4]

Mutations in STUB1 cause ataxia .[5]

Interactions[edit]

STUB1 has been shown to interact with:

References[edit]

  1. ^ "Entrez Gene: STUB1 STIP1 homology and U-box containing protein 1". 
  2. ^ a b c d e f Ballinger CA, Connell P, Wu Y, Hu Z, Thompson LJ, Yin LY, Patterson C (Jun 1999). "Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions". Molecular and Cellular Biology 19 (6): 4535–45. doi:10.1128/mcb.19.6.4535. PMC 104411. PMID 10330192. 
  3. ^ Jiang J, Ballinger CA, Wu Y, Dai Q, Cyr DM, Höhfeld J, Patterson C (Nov 2001). "CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation". The Journal of Biological Chemistry 276 (46): 42938–44. doi:10.1074/jbc.M101968200. PMID 11557750. 
  4. ^ Qian SB, McDonough H, Boellmann F, Cyr DM, Patterson C (Mar 2006). "CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70". Nature 440 (7083): 551–5. doi:10.1038/nature04600. PMID 16554822. 
  5. ^ Synofzik M, Schüle R, Schulze M, Gburek-Augustat J, Schweizer R, Schirmacher A, Krägeloh-Mann I, Gonzalez M, Young P, Züchner S, Schöls L, Bauer P (2014). "Phenotype and frequency of STUB1 mutations: next-generation screenings in Caucasian ataxia and spastic paraplegia cohorts". Orphanet Journal of Rare Diseases 9 (1): 57. doi:10.1186/1750-1172-9-57. PMC 4021831. PMID 24742043. 
  6. ^ Dogan T, Harms GS, Hekman M, Karreman C, Oberoi TK, Alnemri ES, Rapp UR, Rajalingam K (Dec 2008). "X-linked and cellular IAPs modulate the stability of C-RAF kinase and cell motility". Nature Cell Biology 10 (12): 1447–55. doi:10.1038/ncb1804. PMID 19011619. 
  7. ^ a b Imai Y, Soda M, Hatakeyama S, Akagi T, Hashikawa T, Nakayama KI, Takahashi R (Jul 2002). "CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity". Molecular Cell 10 (1): 55–67. doi:10.1016/s1097-2765(02)00583-x. PMID 12150907. 
  8. ^ Li X, Huang M, Zheng H, Wang Y, Ren F, Shang Y, Zhai Y, Irwin DM, Shi Y, Chen D, Chang Z (Jun 2008). "CHIP promotes Runx2 degradation and negatively regulates osteoblast differentiation". The Journal of Cell Biology 181 (6): 959–72. doi:10.1083/jcb.200711044. PMC 2426947. PMID 18541707. 

Further reading[edit]

External links[edit]