Full text data of HYPK
HYPK
(C15orf63)
[Confidence: low (only semi-automatic identification from reviews)]
Huntingtin-interacting protein K (Huntingtin yeast partner K)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Huntingtin-interacting protein K (Huntingtin yeast partner K)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NX55
ID HYPK_HUMAN Reviewed; 129 AA.
AC Q9NX55; C9JKJ0; O75408; Q8WUW8; Q9P024;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 08-MAR-2011, sequence version 2.
DT 22-JAN-2014, entry version 76.
DE RecName: Full=Huntingtin-interacting protein K;
DE AltName: Full=Huntingtin yeast partner K;
GN Name=HYPK; Synonyms=C15orf63; ORFNames=HSPC136;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human
RT chromosome 15.";
RL Nature 440:671-675(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-129 (ISOFORM 2), AND
RP VARIANT PRO-105.
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-129 (ISOFORM 2), AND POSSIBLE
RP INTERACTION WITH HTT.
RC TISSUE=Testis;
RX PubMed=9700202; DOI=10.1093/hmg/7.9.1463;
RA Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F.,
RA MacDonald M.E.;
RT "Huntingtin interacts with a family of WW domain proteins.";
RL Hum. Mol. Genet. 7:1463-1474(1998).
RN [6]
RP FUNCTION, INTERACTION WITH HTT, AND SUBCELLULAR LOCATION.
RX PubMed=17947297; DOI=10.1093/hmg/ddm301;
RA Raychaudhuri S., Sinha M., Mukhopadhyay D., Bhattacharyya N.P.;
RT "HYPK, a Huntingtin interacting protein, reduces aggregates and
RT apoptosis induced by N-terminal Huntingtin with 40 glutamines in
RT Neuro2a cells and exhibits chaperone-like activity.";
RL Hum. Mol. Genet. 17:240-255(2008).
RN [7]
RP FUNCTION, INTERACTION WITH NAA15, ASSOCIATION WITH NAA10-NAA15
RP COMPLEX, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=20154145; DOI=10.1128/MCB.01199-09;
RA Arnesen T., Starheim K.K., Van Damme P., Evjenth R., Dinh H.,
RA Betts M.J., Ryningen A., Vandekerckhove J., Gevaert K., Anderson D.;
RT "The chaperone-like protein HYPK acts together with NatA in
RT cotranslational N-terminal acetylation and prevention of Huntingtin
RT aggregation.";
RL Mol. Cell. Biol. 30:1898-1909(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Has a chaperone-like activity preventing polyglutamine
CC (polyQ) aggregation of HTT. Protects against HTT polyQ-mediated
CC apoptosis in Neuro2a neuronal cells. Required for optimal NAA10-
CC NAA15 complex-mediated N-terminal acetylation.
CC -!- SUBUNIT: Interacts with HTT (via N-terminus). Associates with the
CC NAA10-NAA15 complex and with the ribosome; the NAA10-NAA15 complex
CC is required for HYPK stability and for reducing polyQ aggregation
CC of HTT. Interacts with NAA15.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q9NX55-2; Sequence=Displayed;
CC Name=3;
CC IsoId=Q9NX55-3; Sequence=VSP_040677, VSP_040678;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29100.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAA91165.1; Type=Miscellaneous discrepancy; Note=Readthrough transcript SERF2-HYPK/C15orf63;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK000438; BAA91165.1; ALT_SEQ; mRNA.
DR EMBL; AK022435; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC018512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019262; AAH19262.2; -; mRNA.
DR EMBL; AF161485; AAF29100.1; ALT_INIT; mRNA.
DR EMBL; AF049613; AAC26849.1; -; mRNA.
DR RefSeq; NP_001186814.1; NM_001199885.1.
DR RefSeq; NP_057484.3; NM_016400.3.
DR UniGene; Hs.730672; -.
DR DisProt; DP00546; -.
DR ProteinModelPortal; Q9NX55; -.
DR SMR; Q9NX55; 85-127.
DR IntAct; Q9NX55; 2.
DR MINT; MINT-1374304; -.
DR STRING; 9606.ENSP00000384474; -.
DR PhosphoSite; Q9NX55; -.
DR DMDM; 74719419; -.
DR PaxDb; Q9NX55; -.
DR PRIDE; Q9NX55; -.
DR Ensembl; ENST00000406925; ENSP00000384474; ENSG00000242028.
DR Ensembl; ENST00000442995; ENSP00000401155; ENSG00000242028.
DR GeneID; 25764; -.
DR KEGG; hsa:25764; -.
DR UCSC; uc001ztb.3; human.
DR CTD; 25764; -.
DR GeneCards; GC15P044092; -.
DR HGNC; HGNC:18418; HYPK.
DR HPA; HPA055252; -.
DR MIM; 612784; gene.
DR neXtProt; NX_Q9NX55; -.
DR PharmGKB; PA165478509; -.
DR eggNOG; NOG312666; -.
DR HOGENOM; HOG000189569; -.
DR HOVERGEN; HBG060491; -.
DR InParanoid; Q9NX55; -.
DR OrthoDB; EOG7TBC4C; -.
DR ChiTaRS; C15orf63; human.
DR GenomeRNAi; 25764; -.
DR NextBio; 46884; -.
DR PRO; PR:Q9NX55; -.
DR ArrayExpress; Q9NX55; -.
DR Bgee; Q9NX55; -.
DR Genevestigator; Q9NX55; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW Nucleus; Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 129 Huntingtin-interacting protein K.
FT /FTId=PRO_0000274605.
FT COILED 70 115 Potential.
FT MOD_RES 38 38 Phosphoserine.
FT VAR_SEQ 63 82 AMSVIGDRRSREQKAKQERE -> GERTGKSHYQEGRSGAN
FT SEW (in isoform 3).
FT /FTId=VSP_040677.
FT VAR_SEQ 86 129 Missing (in isoform 3).
FT /FTId=VSP_040678.
FT VARIANT 105 105 S -> P (in dbSNP:rs12702).
FT /FTId=VAR_030335.
SQ SEQUENCE 129 AA; 14665 MW; 50AA7E49B1996948 CRC64;
MRRRGEIDMA TEGDVELELE TETSGPERPP EKPRKHDSGA ADLERVTDYA EEKEIQSSNL
ETAMSVIGDR RSREQKAKQE REKELAKVTI KKEDLELIMT EMEISRAAAE RSLREHMGNV
VEALIALTN
//
ID HYPK_HUMAN Reviewed; 129 AA.
AC Q9NX55; C9JKJ0; O75408; Q8WUW8; Q9P024;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 08-MAR-2011, sequence version 2.
DT 22-JAN-2014, entry version 76.
DE RecName: Full=Huntingtin-interacting protein K;
DE AltName: Full=Huntingtin yeast partner K;
GN Name=HYPK; Synonyms=C15orf63; ORFNames=HSPC136;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human
RT chromosome 15.";
RL Nature 440:671-675(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-129 (ISOFORM 2), AND
RP VARIANT PRO-105.
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-129 (ISOFORM 2), AND POSSIBLE
RP INTERACTION WITH HTT.
RC TISSUE=Testis;
RX PubMed=9700202; DOI=10.1093/hmg/7.9.1463;
RA Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F.,
RA MacDonald M.E.;
RT "Huntingtin interacts with a family of WW domain proteins.";
RL Hum. Mol. Genet. 7:1463-1474(1998).
RN [6]
RP FUNCTION, INTERACTION WITH HTT, AND SUBCELLULAR LOCATION.
RX PubMed=17947297; DOI=10.1093/hmg/ddm301;
RA Raychaudhuri S., Sinha M., Mukhopadhyay D., Bhattacharyya N.P.;
RT "HYPK, a Huntingtin interacting protein, reduces aggregates and
RT apoptosis induced by N-terminal Huntingtin with 40 glutamines in
RT Neuro2a cells and exhibits chaperone-like activity.";
RL Hum. Mol. Genet. 17:240-255(2008).
RN [7]
RP FUNCTION, INTERACTION WITH NAA15, ASSOCIATION WITH NAA10-NAA15
RP COMPLEX, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=20154145; DOI=10.1128/MCB.01199-09;
RA Arnesen T., Starheim K.K., Van Damme P., Evjenth R., Dinh H.,
RA Betts M.J., Ryningen A., Vandekerckhove J., Gevaert K., Anderson D.;
RT "The chaperone-like protein HYPK acts together with NatA in
RT cotranslational N-terminal acetylation and prevention of Huntingtin
RT aggregation.";
RL Mol. Cell. Biol. 30:1898-1909(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Has a chaperone-like activity preventing polyglutamine
CC (polyQ) aggregation of HTT. Protects against HTT polyQ-mediated
CC apoptosis in Neuro2a neuronal cells. Required for optimal NAA10-
CC NAA15 complex-mediated N-terminal acetylation.
CC -!- SUBUNIT: Interacts with HTT (via N-terminus). Associates with the
CC NAA10-NAA15 complex and with the ribosome; the NAA10-NAA15 complex
CC is required for HYPK stability and for reducing polyQ aggregation
CC of HTT. Interacts with NAA15.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q9NX55-2; Sequence=Displayed;
CC Name=3;
CC IsoId=Q9NX55-3; Sequence=VSP_040677, VSP_040678;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29100.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAA91165.1; Type=Miscellaneous discrepancy; Note=Readthrough transcript SERF2-HYPK/C15orf63;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK000438; BAA91165.1; ALT_SEQ; mRNA.
DR EMBL; AK022435; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC018512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019262; AAH19262.2; -; mRNA.
DR EMBL; AF161485; AAF29100.1; ALT_INIT; mRNA.
DR EMBL; AF049613; AAC26849.1; -; mRNA.
DR RefSeq; NP_001186814.1; NM_001199885.1.
DR RefSeq; NP_057484.3; NM_016400.3.
DR UniGene; Hs.730672; -.
DR DisProt; DP00546; -.
DR ProteinModelPortal; Q9NX55; -.
DR SMR; Q9NX55; 85-127.
DR IntAct; Q9NX55; 2.
DR MINT; MINT-1374304; -.
DR STRING; 9606.ENSP00000384474; -.
DR PhosphoSite; Q9NX55; -.
DR DMDM; 74719419; -.
DR PaxDb; Q9NX55; -.
DR PRIDE; Q9NX55; -.
DR Ensembl; ENST00000406925; ENSP00000384474; ENSG00000242028.
DR Ensembl; ENST00000442995; ENSP00000401155; ENSG00000242028.
DR GeneID; 25764; -.
DR KEGG; hsa:25764; -.
DR UCSC; uc001ztb.3; human.
DR CTD; 25764; -.
DR GeneCards; GC15P044092; -.
DR HGNC; HGNC:18418; HYPK.
DR HPA; HPA055252; -.
DR MIM; 612784; gene.
DR neXtProt; NX_Q9NX55; -.
DR PharmGKB; PA165478509; -.
DR eggNOG; NOG312666; -.
DR HOGENOM; HOG000189569; -.
DR HOVERGEN; HBG060491; -.
DR InParanoid; Q9NX55; -.
DR OrthoDB; EOG7TBC4C; -.
DR ChiTaRS; C15orf63; human.
DR GenomeRNAi; 25764; -.
DR NextBio; 46884; -.
DR PRO; PR:Q9NX55; -.
DR ArrayExpress; Q9NX55; -.
DR Bgee; Q9NX55; -.
DR Genevestigator; Q9NX55; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW Nucleus; Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 129 Huntingtin-interacting protein K.
FT /FTId=PRO_0000274605.
FT COILED 70 115 Potential.
FT MOD_RES 38 38 Phosphoserine.
FT VAR_SEQ 63 82 AMSVIGDRRSREQKAKQERE -> GERTGKSHYQEGRSGAN
FT SEW (in isoform 3).
FT /FTId=VSP_040677.
FT VAR_SEQ 86 129 Missing (in isoform 3).
FT /FTId=VSP_040678.
FT VARIANT 105 105 S -> P (in dbSNP:rs12702).
FT /FTId=VAR_030335.
SQ SEQUENCE 129 AA; 14665 MW; 50AA7E49B1996948 CRC64;
MRRRGEIDMA TEGDVELELE TETSGPERPP EKPRKHDSGA ADLERVTDYA EEKEIQSSNL
ETAMSVIGDR RSREQKAKQE REKELAKVTI KKEDLELIMT EMEISRAAAE RSLREHMGNV
VEALIALTN
//
MIM
612784
*RECORD*
*FIELD* NO
612784
*FIELD* TI
*612784 HUNTINGTIN-INTERACTING PROTEIN K
;;HUNTINGTIN YEAST 2-HYBRID PROTEIN K; HYPK
read more*FIELD* TX
CLONING
Huntington disease (HD; 143100) is caused by expansion of a CAG
trinucleotide repeat encoding an N-terminal polyglutamine region in
huntingtin (HTT; 613004) to more than 34 units. Using N-terminal domains
of HTT containing 58 or 62 glutamines in a yeast 2-hybrid assay of a
testis cDNA library, Faber et al. (1998) obtained a partial HYPK clone.
By PCR of a Burkitt B-cell lymphoma cell line, Raychaudhuri et al.
(2008) cloned full-length HYPK.
GENE FUNCTION
By coexpressing human proteins in a mouse neuroblastoma cell line,
Raychaudhuri et al. (2008) showed that HYPK interacted with the isolated
N-terminal region of human huntingtin containing either 16 (H16) or 40
(H40) glutamines. Coexpression of HYPK reduced H40 aggregate formation
and H40-induced apoptosis. Purified recombinant HYPK showed
chaperone-like activity in vitro against temperature-induced protein
aggregates and in vivo against heat-denatured proteins. In cells
expressing HYPK and H40, the chaperone-like activity of HYPK against
other protein substrates was reduced compared with cells expressing HYPK
and H16, apparently due to interaction of HYPK with H40 protein
aggregates.
MAPPING
Hartz (2009) mapped the HYPK gene to chromosome 15q15.3 based on an
alignment of the HYPK sequence (GenBank GENBANK AF049613) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Faber, P. W.; Barnes, G. T.; Srinidhi, J.; Chen, J.; Gusella, J.
F.; MacDonald, M. E.: Huntingtin interacts with a family of WW domain
proteins. Hum. Molec. Genet. 7: 1463-1474, 1998.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 5/13/2009.
3. Raychaudhuri, S.; Sinha, M.; Mukhopadhyay, D.; Bhattacharyya, N.
P.: HYPK, a Huntingtin interacting protein, reduces aggregates and
apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a
cells and exhibits chaperone-like activity. Hum. Molec. Genet. 17:
240-255, 2008.
*FIELD* CD
Patricia A. Hartz: 5/13/2009
*FIELD* ED
carol: 09/15/2009
mgross: 5/13/2009
*RECORD*
*FIELD* NO
612784
*FIELD* TI
*612784 HUNTINGTIN-INTERACTING PROTEIN K
;;HUNTINGTIN YEAST 2-HYBRID PROTEIN K; HYPK
read more*FIELD* TX
CLONING
Huntington disease (HD; 143100) is caused by expansion of a CAG
trinucleotide repeat encoding an N-terminal polyglutamine region in
huntingtin (HTT; 613004) to more than 34 units. Using N-terminal domains
of HTT containing 58 or 62 glutamines in a yeast 2-hybrid assay of a
testis cDNA library, Faber et al. (1998) obtained a partial HYPK clone.
By PCR of a Burkitt B-cell lymphoma cell line, Raychaudhuri et al.
(2008) cloned full-length HYPK.
GENE FUNCTION
By coexpressing human proteins in a mouse neuroblastoma cell line,
Raychaudhuri et al. (2008) showed that HYPK interacted with the isolated
N-terminal region of human huntingtin containing either 16 (H16) or 40
(H40) glutamines. Coexpression of HYPK reduced H40 aggregate formation
and H40-induced apoptosis. Purified recombinant HYPK showed
chaperone-like activity in vitro against temperature-induced protein
aggregates and in vivo against heat-denatured proteins. In cells
expressing HYPK and H40, the chaperone-like activity of HYPK against
other protein substrates was reduced compared with cells expressing HYPK
and H16, apparently due to interaction of HYPK with H40 protein
aggregates.
MAPPING
Hartz (2009) mapped the HYPK gene to chromosome 15q15.3 based on an
alignment of the HYPK sequence (GenBank GENBANK AF049613) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Faber, P. W.; Barnes, G. T.; Srinidhi, J.; Chen, J.; Gusella, J.
F.; MacDonald, M. E.: Huntingtin interacts with a family of WW domain
proteins. Hum. Molec. Genet. 7: 1463-1474, 1998.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 5/13/2009.
3. Raychaudhuri, S.; Sinha, M.; Mukhopadhyay, D.; Bhattacharyya, N.
P.: HYPK, a Huntingtin interacting protein, reduces aggregates and
apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a
cells and exhibits chaperone-like activity. Hum. Molec. Genet. 17:
240-255, 2008.
*FIELD* CD
Patricia A. Hartz: 5/13/2009
*FIELD* ED
carol: 09/15/2009
mgross: 5/13/2009