HYPK_MACFA
ID HYPK_MACFA Reviewed; 121 AA.
AC Q2PFU1;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Huntingtin-interacting protein K {ECO:0000250|UniProtKB:Q9NX55};
DE AltName: Full=Huntingtin yeast partner K;
GN Name=HYPK {ECO:0000250|UniProtKB:Q9NX55}; ORFNames=QnpA-10575;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Parietal cortex;
RA Kobayashi M., Tanuma R., Hirata M., Osada N., Kusuda J., Sugano S.,
RA Hashimoto K.;
RT "Analysis of gene expression in cynomolgus monkey tissues by macaque cDNA
RT oligo-chips.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of several N-terminal acetyltransferase complexes
CC (By similarity). Inhibits the N-terminal acetylation activity of the N-
CC terminal acetyltransferase NAA10-NAA15 complex (also called the NatA
CC complex) (By similarity). Has chaperone-like activity preventing
CC polyglutamine (polyQ) aggregation of HTT in neuronal cells probably
CC while associated with the NatA complex (By similarity). May play a role
CC in the NatA complex-mediated N-terminal acetylation of PCNP (By
CC similarity). {ECO:0000250|UniProtKB:Q9NX55}.
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase A (NatA)/HYPK
CC complex at least composed of NAA10, NAA15 and HYPK, which has N-
CC terminal acetyltransferase activity (By similarity). Within the complex
CC interacts with NAA10 (By similarity). Within the complex interacts with
CC NAA15 (By similarity). Predominantly interacts with NAA15 in the NAA10-
CC NAA15 complex (also called the NatA complex); the interaction with the
CC NatA complex reduces the acetylation activity of the NatA complex (By
CC similarity). Interacts with HTT (via N-terminus) (By similarity). The
CC NatA complex is required for HYPK stability and for reducing polyQ
CC aggregation of HTT (By similarity). Component of the N-terminal
CC acetyltransferase E (NatE)/HYPK complex at least composed of NAA10,
CC NAA15, NAA50 and HYPK (By similarity). Within the complex interacts
CC with NAA10 and NAA15 (By similarity). Does not interact with NAA50 (By
CC similarity). Interaction with NAA15 reduces the capacity of NAA15 to
CC interact with NAA50 (By similarity). Its capacity to interact with the
CC NatA complex is reduced by NAA50 (By similarity). Does not interact
CC with the N-terminal acetyltransferase B (NatB) complex component NAA25
CC or the N-terminal acetyltransferase C (NatC) complex component NAA35
CC (By similarity). {ECO:0000250|UniProtKB:Q9NX55}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NX55}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9NX55}. Note=Within the NatA/HYPK complex, may
CC localize to ribosomes. {ECO:0000250|UniProtKB:Q9NX55}.
CC -!- CAUTION: Regulator of the N-terminal acetyltransferase NAA10-NAA15
CC complex, however it is unclear if it acts as an activator or inhibitor
CC of the complex (By similarity). Has been shown in one study to be
CC required for efficient N-terminal acetylation of NAA10-NAA15 complex
CC substrates in vivo and in vitro (By similarity). Another study,
CC however, has shown that it acts in vitro as an inhibitor of NAA10-NAA15
CC complex-mediated N-terminal acetylation (By similarity).
CC {ECO:0000250|UniProtKB:Q9NX55}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE73029.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB220496; BAE73029.1; ALT_INIT; mRNA.
DR RefSeq; NP_001274614.1; NM_001287685.1.
DR AlphaFoldDB; Q2PFU1; -.
DR SMR; Q2PFU1; -.
DR STRING; 9541.XP_005559440.1; -.
DR GeneID; 102116290; -.
DR CTD; 25764; -.
DR VEuPathDB; HostDB:ENSMFAG00000038315; -.
DR eggNOG; KOG3450; Eukaryota.
DR OMA; SAEADWN; -.
DR OrthoDB; 1512609at2759; -.
DR Proteomes; UP000233100; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR CDD; cd14361; UBA_HYPK; 1.
DR InterPro; IPR038922; HYPK_UBA.
DR InterPro; IPR044034; NAC-like_UBA.
DR Pfam; PF19026; HYPK_UBA; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..121
FT /note="Huntingtin-interacting protein K"
FT /id="PRO_0000274606"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..121
FT /note="Required for association with the NAA10-NAA15
FT complex"
FT /evidence="ECO:0000250|UniProtKB:Q9NX55"
FT COILED 62..107
FT /evidence="ECO:0000255"
FT COMPBIAS 13..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX55"
SQ SEQUENCE 121 AA; 13651 MW; 27028987B3FE6EE8 CRC64;
MATEGDVELE LETETSGPER PPEKPRKHDS GAADLERVTD YAEEKEIQSS NLETAMSVIG
DRRSREQKAK QEREKELAKV TIKKEDLELI MTEMEISRAA AERSLREHMG NVVEALIALT
N
