Search Keyword:


Search option:


IID01024
 UniprotQ9NX55
ProteinHuntingtin-interacting protein K
GeneHYPK
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
121
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 27-121 Hetero trimer : P41227,Q9BXJ9
 Evidence X-RAY 6c95 D Reference
       Region 6c95 D 27-121 order
SeqProS possible 27-52 The N-terminal region (1-52) had almost no secondary structure (CD, pmid=18076027). Hetero trimer : P41227,Q9BXJ9
       Region 6c95 D 27-121 order
Seqphosphorylation
    30-30 Phosphoserine
 
Prediction
NeProc
Disorder 1-62
Order 63-121
ProS 25-62
AlphaFold
Disorder 1-40,49-49,52-52,65-86
Order 41-48,50-51,53-64,87-129
SEG 62-79
Function
Function in SwissProt
Component of several N-terminal acetyltransferase complexes (PubMed:20154145, PubMed:29754825, PubMed:32042062). Inhibits the N-terminal acetylation activity of the N-terminal acetyltransferase NAA10-NAA15 complex (also called the NatA complex) (PubMed:29754825, PubMed:32042062). Has chaperone-like activity preventing polyglutamine (polyQ) aggregation of HTT in neuronal cells probably while associated with the NatA complex (PubMed:17947297, PubMed:20154145). May play a role in the NatA complex-mediated N-terminal acetylation of PCNP (PubMed:20154145).
Biological Process
Diagram with PDB data
HYPK/NAA10/NAA15The Human NatA (Naa10/Naa15) amino-terminal acetyltransferase complex bound to HYPK