Q2PFU1 · HYPK_MACFA

Function

function

Component of several N-terminal acetyltransferase complexes (By similarity).
Inhibits the N-terminal acetylation activity of the N-terminal acetyltransferase NAA10-NAA15 complex (also called the NatA complex) (By similarity).
Has chaperone-like activity preventing polyglutamine (polyQ) aggregation of HTT in neuronal cells probably while associated with the NatA complex (By similarity).
May play a role in the NatA complex-mediated N-terminal acetylation of PCNP (By similarity).

Caution

Regulator of the N-terminal acetyltransferase NAA10-NAA15 complex, however it is unclear if it acts as an activator or inhibitor of the complex (By similarity).
Has been shown in one study to be required for efficient N-terminal acetylation of NAA10-NAA15 complex substrates in vivo and in vitro (By similarity).
Another study, however, has shown that it acts in vitro as an inhibitor of NAA10-NAA15 complex-mediated N-terminal acetylation (By similarity).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Biological Processnegative regulation of apoptotic process
Biological Processprotein stabilization

Names & Taxonomy

Protein names

  • Recommended name
    Huntingtin-interacting protein K
  • Alternative names
    • Huntingtin yeast partner K

Gene names

    • Name
      HYPK
    • ORF names
      QnpA-10575

Organism names

Accessions

  • Primary accession
    Q2PFU1

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Cytoplasm
Note: Within the NatA/HYPK complex, may localize to ribosomes.

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002746061-121Huntingtin-interacting protein K
Modified residue30Phosphoserine

Keywords

Interaction

Subunit

Component of the N-terminal acetyltransferase A (NatA)/HYPK complex at least composed of NAA10, NAA15 and HYPK, which has N-terminal acetyltransferase activity (By similarity).
Within the complex interacts with NAA10 (By similarity).
Within the complex interacts with NAA15 (By similarity).
Predominantly interacts with NAA15 in the NAA10-NAA15 complex (also called the NatA complex); the interaction with the NatA complex reduces the acetylation activity of the NatA complex (By similarity).
Interacts with HTT (via N-terminus) (By similarity).
The NatA complex is required for HYPK stability and for reducing polyQ aggregation of HTT (By similarity).
Component of the N-terminal acetyltransferase E (NatE)/HYPK complex at least composed of NAA10, NAA15, NAA50 and HYPK (By similarity).
Within the complex interacts with NAA10 and NAA15 (By similarity).
Does not interact with NAA50 (By similarity).
Interaction with NAA15 reduces the capacity of NAA15 to interact with NAA50 (By similarity).
Its capacity to interact with the NatA complex is reduced by NAA50 (By similarity).
Does not interact with the N-terminal acetyltransferase B (NatB) complex component NAA25 or the N-terminal acetyltransferase C (NatC) complex component NAA35 (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, coiled coil.

TypeIDPosition(s)Description
Region1-75Disordered
Compositional bias13-47Basic and acidic residues
Region52-121Required for association with the NAA10-NAA15 complex
Compositional bias59-75Basic and acidic residues
Coiled coil62-107

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    121
  • Mass (Da)
    13,651
  • Last updated
    2022-02-23 v2
  • Checksum
    27028987B3FE6EE8
MATEGDVELELETETSGPERPPEKPRKHDSGAADLERVTDYAEEKEIQSSNLETAMSVIGDRRSREQKAKQEREKELAKVTIKKEDLELIMTEMEISRAAAERSLREHMGNVVEALIALTN

Sequence caution

The sequence BAE73029.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias13-47Basic and acidic residues
Compositional bias59-75Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB220496
EMBL· GenBank· DDBJ
BAE73029.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Similar Proteins

Disclaimer

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