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GenomicsExpression data from Arabidopsis thaliana depleted of HYPK or NAA10
Expression data from Arabidopsis thaliana depleted of HYPK or NAA10
PRJNA665720 | ENA
ProteomicsLC-MS/MS analysis of immunoprecipitated NAA15-V5 variants
The human N-terminal acetyltransferase E (NatE) including its associated NatA co-translationally acetylates the N-terminus of about 40-60% of the proteome to mediate diverse biological processes including protein half-life, localization and protein interaction. In eukaryotes, the NatE complex contai...
ORGANISM(S): Homo sapiens (Human) 
2020-03-13 | PXD017031 | Pride
Lc-ms/ms N-terminal acetylation Nate Naa15 Naa10 Hypk Naa50 
TranscriptomicsExpression data from Arabidopsis thaliana depleted of HYPK or NAA10
N-alpha terminal acetylation is an abundant protein modification in eukaryotes. The NatA (N-alpha acetyltransferase A) complex is responsible for N-terminal acetylation of majority of the cytosolic proteins and its core is composed of NAA10 and NAA15 subunit. HYPK has been shown to interact with Nat...
ORGANISM(S): Arabidopsis thaliana 
2022-05-20 | GSE158586 | GEO
ProteomicsMass-spectrometry based quantification of HYPK, NAA10 and NAA15 protein steady-state levels in Arabidopsis thaliana mutants carrying a T-DNA insertion in the HYPK gene.
N-alpha terminal acetylation is one of the major protein modifications in eukaryotes carried out by distinct Nats (N-alpha acetyltransferases). The core NatA complex is composed of the catalytic NAA10 and the auxiliary NAA15 subunit and co-translationally acetylates majority of the cytosolic protein...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2022-08-12 | PXD023599 | Pride
Arabidopsis thaliana Hypk Nata complex N-alpha terminal acetylation 
UnknownTranscription regulation of HYPK by Heat Shock Factor 1.
Not available
S-EPMC3897489 | biostudies-literature
UnknownIdentification of HYPK-interacting proteins reveals involvement of HYPK in regulating cell growth, cell cycle, unfolded protein response and cell death.
Not available
S-EPMC3525516 | biostudies-literature
ProteomicsHYPK controls stability and catalytic activity of the N-terminal acetyltransferase A in Arabidopsis thaliana
The ribosome-tethered N-terminal acetyltransferase A (NatA) acetylates 52% of soluble proteins in Arabidopsis thaliana. This co-translational shielding of the N-terminus stabilizes diverse cytosolic plant proteins. The Huntingtin yeast partner K (HYPK) facilitates NatA activity in planta, but in vit...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2024-01-22 | PXD043600 | Pride
Co-translational protein modification N-terminal acetylation Nata Hypk Drought resistance 
ProteomicsHYPK controls stability and catalytic activity of the N-terminal acetyltransferase A in Arabidopsis thaliana
The ribosome-tethered N-terminal acetyltransferase A (NatA) acetylates 52% of soluble proteins in Arabidopsis thaliana. This co-translational shielding of the N-terminus stabilizes diverse cytosolic plant proteins. The Huntingtin yeast partner K (HYPK) facilitates NatA activity in planta, but in vit...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2024-01-22 | PXD047700 | Pride
Co-translational protein modification N-terminal acetylation Nata Hypk Drought resistance 
UnknownHYPK promotes N-terminal protein acetylation through rapid ribosome exchange of NatA.
Not available
S-EPMC12699156 | biostudies-literature
UnknownStructural basis of HypK regulating N-terminal acetylation by the NatA complex.
Not available
S-EPMC5467210 | biostudies-literature
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