Property Summary

NCBI Gene PubMed Count 14
PubMed Score 7.42
PubTator Score 4.23

Knowledge Summary


No data available


  Disease Relevance (1)

Disease Z-score Confidence
Huntington's disease 72 4.563 2.3


Accession Q9NX55 C9JKJ0 O75408 Q8WUW8 Q9P024
Symbols HSPC136


Gene RIF (6)

25446099 specific interaction of HYPK with HTT-N17 is crucial for the chaperone activity of HYPK
25116620 By virtue of its flexibility and nascent peptide binding activity, HYPK may play an important role in assisting protein (re)folding.
24465598 Chaperone-like protein HYPK is induced by cellular stress and is under transcriptional regulation by HSF1.
24361604 maintenance of HYPK expression by HSF1 is necessary for the survival of cells under thermal stress conditions
23272104 HYPK has roles in regulating cell growth, cell cycle, unfolded protein response and cell death
17947297 The present study, has confirmed, by confocal microscopy and immunoprecipitation, that HYPK interacts with the N-terminal of Htt.

AA Sequence


Text Mined References (20)

PMID Year Title
25446099 2015 Chaperone protein HYPK interacts with the first 17 amino acid region of Huntingtin and modulates mutant HTT-mediated aggregation and cytotoxicity.
25416956 2014 A proteome-scale map of the human interactome network.
25116620 2014 Conserved C-terminal nascent peptide binding domain of HYPK facilitates its chaperone-like activity.
24465598 2014 Transcription regulation of HYPK by Heat Shock Factor 1.
24361604 2014 Heat shock transcription factor HSF1 regulates the expression of the Huntingtin-interacting protein HYPK.
24275569 2014 An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
23272104 2012 Identification of HYPK-interacting proteins reveals involvement of HYPK in regulating cell growth, cell cycle, unfolded protein response and cell death.
23186163 2013 Toward a comprehensive characterization of a human cancer cell phosphoproteome.
21269460 2011 Initial characterization of the human central proteome.
20154145 2010 The chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregation.