HYPK_MOUSE
ID HYPK_MOUSE Reviewed; 121 AA.
AC Q9CR41; Q3TH09; Q8VDK6;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Huntingtin-interacting protein K {ECO:0000305};
DE AltName: Full=Huntingtin yeast partner K;
GN Name=Hypk {ECO:0000312|EMBL:BAB22870.2};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Heart, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary gland, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CR41-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CR41-2; Sequence=VSP_022833;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH38469.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB22870.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB26075.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE40389.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK003580; BAB22870.2; ALT_INIT; mRNA.
DR EMBL; AK009109; BAB26075.2; ALT_INIT; mRNA.
DR EMBL; AK168506; BAE40389.1; ALT_INIT; mRNA.
DR EMBL; BC021588; AAH21588.1; -; mRNA.
DR EMBL; BC038469; AAH38469.1; ALT_INIT; mRNA.
DR RefSeq; NP_080594.2; NM_026318.3. [Q9CR41-1]
DR AlphaFoldDB; Q9CR41; -.
DR SMR; Q9CR41; -.
DR BioGRID; 212372; 6.
DR STRING; 10090.ENSMUSP00000117946; -.
DR iPTMnet; Q9CR41; -.
DR PhosphoSitePlus; Q9CR41; -.
DR EPD; Q9CR41; -.
DR MaxQB; Q9CR41; -.
DR PaxDb; Q9CR41; -.
DR PeptideAtlas; Q9CR41; -.
DR PRIDE; Q9CR41; -.
DR ProteomicsDB; 273065; -. [Q9CR41-1]
DR ProteomicsDB; 273066; -. [Q9CR41-2]
DR Antibodypedia; 65071; 7 antibodies from 5 providers.
DR GeneID; 67693; -.
DR KEGG; mmu:67693; -.
DR UCSC; uc008lzf.2; mouse. [Q9CR41-1]
DR CTD; 25764; -.
DR MGI; MGI:1914943; Hypk.
DR VEuPathDB; HostDB:ENSMUSG00000027245; -.
DR eggNOG; KOG3450; Eukaryota.
DR HOGENOM; CLU_128817_1_1_1; -.
DR InParanoid; Q9CR41; -.
DR OMA; SAEADWN; -.
DR OrthoDB; 1512609at2759; -.
DR PhylomeDB; Q9CR41; -.
DR TreeFam; TF325606; -.
DR BioGRID-ORCS; 67693; 24 hits in 77 CRISPR screens.
DR ChiTaRS; Hypk; mouse.
DR PRO; PR:Q9CR41; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CR41; protein.
DR Bgee; ENSMUSG00000027245; Expressed in yolk sac and 163 other tissues.
DR Genevisible; Q9CR41; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR CDD; cd14361; UBA_HYPK; 1.
DR InterPro; IPR038922; HYPK_UBA.
DR InterPro; IPR044034; NAC-like_UBA.
DR Pfam; PF19026; HYPK_UBA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..121
FT /note="Huntingtin-interacting protein K"
FT /id="PRO_0000274607"
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"
FT VAR_SEQ 74..121
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022833"
SQ SEQUENCE 121 AA; 13651 MW; 27028987B3FE6EE8 CRC64;
MATEGDVELE LETETSGPER PPEKPRKHDS GAADLERVTD YAEEKEIQSS NLETAMSVIG
DRRSREQKAK QEREKELAKV TIKKEDLELI MTEMEISRAA AERSLREHMG NVVEALIALT
N
