Q9CR41 · HYPK_MOUSE
- ProteinHuntingtin-interacting protein K
- GeneHypk
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids121 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
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).
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).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Biological Process | negative regulation of apoptotic process | |
Biological Process | protein stabilization |
Names & Taxonomy
Protein names
- Recommended nameHuntingtin-interacting protein K
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9CR41
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000274607 | 1-121 | Huntingtin-interacting protein K | |||
Sequence: MATEGDVELELETETSGPERPPEKPRKHDSGAADLERVTDYAEEKEIQSSNLETAMSVIGDRRSREQKAKQEREKELAKVTIKKEDLELIMTEMEISRAAAERSLREHMGNVVEALIALTN | ||||||
Modified residue | 30 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
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).
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
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-75 | Disordered | ||||
Sequence: MATEGDVELELETETSGPERPPEKPRKHDSGAADLERVTDYAEEKEIQSSNLETAMSVIGDRRSREQKAKQEREK | ||||||
Compositional bias | 13-47 | Basic and acidic residues | ||||
Sequence: TETSGPERPPEKPRKHDSGAADLERVTDYAEEKEI | ||||||
Region | 52-121 | Required for association with the NAA10-NAA15 complex | ||||
Sequence: LETAMSVIGDRRSREQKAKQEREKELAKVTIKKEDLELIMTEMEISRAAAERSLREHMGNVVEALIALTN | ||||||
Compositional bias | 59-75 | Basic and acidic residues | ||||
Sequence: IGDRRSREQKAKQEREK | ||||||
Coiled coil | 62-107 | |||||
Sequence: RRSREQKAKQEREKELAKVTIKKEDLELIMTEMEISRAAAERSLRE |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9CR41-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length121
- Mass (Da)13,651
- Last updated2022-02-23 v3
- Checksum27028987B3FE6EE8
Q9CR41-2
- Name2
- Differences from canonical
- 74-121: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8Q0PQH5 | A0A8Q0PQH5_MOUSE | Hypk | 129 |
Sequence caution
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 13-47 | Basic and acidic residues | ||||
Sequence: TETSGPERPPEKPRKHDSGAADLERVTDYAEEKEI | ||||||
Compositional bias | 59-75 | Basic and acidic residues | ||||
Sequence: IGDRRSREQKAKQEREK | ||||||
Alternative sequence | VSP_022833 | 74-121 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK003580 EMBL· GenBank· DDBJ | BAB22870.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK009109 EMBL· GenBank· DDBJ | BAB26075.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK168506 EMBL· GenBank· DDBJ | BAE40389.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC021588 EMBL· GenBank· DDBJ | AAH21588.1 EMBL· GenBank· DDBJ | mRNA | ||
BC038469 EMBL· GenBank· DDBJ | AAH38469.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |