Heat Shock 70kDa Binding Protein 1 (HSPBP1)

FES1; Hsp70 Interacting Protein; Hsp70 Binding Protein,Cytoplasmic Cochaperone 1; Heat shock protein-binding protein 1; Hsp70-interacting protein 1

SPN	R943
HGNC	24989
MGI	1913495
PubMed	15694338
RGD	628677
UniProt	Q9NZL4
Wiki	HSPBP1

Using the ATPase domain of human HSP70 as bait in a yeast 2-hybrid screen of a human heart cDNA library, Raynes and Guerriero (1998) cloned HSPBP1. The deduced 459-amino acid protein has a calculated molecular mass of 39.3 kD and contains 6 consecutive glycines near its N terminus. Northern blot analysis detected a 1.7-kb HSPBP1 transcript in all tissues examined, with highest expression in heart and skeletal muscle.

Raynes and Guerriero (1998) also identified an HSPBP1 variant that they called HSPBP2, which has 2 polyadenylation signals rather than the single polyadenylation signal of HSPBP1. The deduced HSPBP2 protein is identical to HSPBP1 except that it has 9 consecutive glycines near the N terminus.

Reference

"Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein."
J. Biol. Chem. 273:32883-32888(1998) [PubMed] [Europe PMC] [Abstract]

"Isolation and characterization of isoforms of HspBP1, inhibitors of Hsp70."
Biochim. Biophys. Acta 1490:203-207(2000) [PubMed] [Europe PMC] [Abstract]

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"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domain."
J. Biol. Chem. 278:19017-19022(2003) [PubMed] [Europe PMC] [Abstract]

"The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator."
Mol. Biol. Cell 15:4003-4010(2004) [PubMed] [Europe PMC] [Abstract]

"A quantitative atlas of mitotic phosphorylation."
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]

"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]

"Initial characterization of the human central proteome."
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]

"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]

"Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange."
Mol. Cell 17:367-379(2005) [PubMed] [Europe PMC] [Abstract]