20250201 IID01024 Huntingtin-interacting protein K Huntingtin yeast partner K Homo sapiens 121 Q9NX55 C9JKJ0 O75408 Q8WUW8 Q9P024 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). 0 0 Phosphoserine 30 30 HYPK Huntingtin-interacting protein K MATEGDVELELETETSGPERPPEKPRKHDSGAADLERVTDYAEEKEIQSSNLETAMSVIGDRRSREQKAKQEREKELAKVTIKKEDLELIMTEMEISRAAAERSLREHMGNVVEALIALTN 2 6c95D 27 121 order 1 1 6c95 X-RAY 293K 6.5 29754825 L.GOTTLIEB,R.MARMORSTEIN STRUCTURE OF HUMAN NATA AND ITS REGULATION BY THE HUNTINGTIN INTERACTING PROTEIN HYPK. 2018 STRUCTURE 26 925 x-ray 6c95 D 27 121 100 0 1 6c95 5062 Hetero trimer 6c95D Q9NX55 IID01024 6c95B P41227 6c95A Q9BXJ9 6c95A-6c95B 6c95B-6c95D 6c95A-6c95D ProS 1 possible 2 27 52 The N-terminal region (1-52) had almost no secondary structure (CD, pmid=18076027).
Q9NX55-1 HYPK/NAA10/NAA15 The Human NatA (Naa10/Naa15) amino-terminal acetyltransferase complex bound to HYPK
41-48,50-51,53-64,87-129 1-40,49-49,52-52,65-86 63-121 1-62 25-62 62-79