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Protein

Huntingtin-interacting protein K

Gene

HYPK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Has a chaperone-like activity preventing polyglutamine (polyQ) aggregation of HTT. Protects against HTT polyQ-mediated apoptosis in Neuro2a neuronal cells. Required for optimal NAA10-NAA15 complex-mediated N-terminal acetylation.2 Publications

Names & Taxonomyi

Protein namesi
Recommended name:
Huntingtin-interacting protein K
Alternative name(s):
Huntingtin yeast partner K
Gene namesi
Name:HYPK
Synonyms:C15orf63
ORF Names:HSPC136
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:18418. HYPK.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165478509.

Polymorphism and mutation databases

BioMutaiHYPK.
DMDMi325511335.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 129129Huntingtin-interacting protein KPRO_0000274605Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NX55.
MaxQBiQ9NX55.
PaxDbiQ9NX55.
PeptideAtlasiQ9NX55.
PRIDEiQ9NX55.
TopDownProteomicsiQ9NX55-2. [Q9NX55-2]

PTM databases

iPTMnetiQ9NX55.
PhosphoSiteiQ9NX55.

Expressioni

Gene expression databases

BgeeiQ9NX55.
ExpressionAtlasiQ9NX55. baseline and differential.
GenevisibleiQ9NX55. HS.

Organism-specific databases

HPAiHPA055252.

Interactioni

Subunit structurei

Interacts with HTT (via N-terminus). Associates with the NAA10-NAA15 complex and with the ribosome; the NAA10-NAA15 complex is required for HYPK stability and for reducing polyQ aggregation of HTT. Interacts with NAA15.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAGEA1P433553EBI-1048743,EBI-740978
TXLNAP402223EBI-1048743,EBI-359793

Protein-protein interaction databases

BioGridi117304. 21 interactions.
IntActiQ9NX55. 9 interactions.
MINTiMINT-1374304.
STRINGi9606.ENSP00000384474.

Structurei

3D structure databases

DisProtiDP00546.
ProteinModelPortaliQ9NX55.
SMRiQ9NX55. Positions 85-127.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili70 – 11546Sequence analysisAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3450. Eukaryota.
ENOG4111M4G. LUCA.
GeneTreeiENSGT00390000008502.
HOGENOMiHOG000189569.
HOVERGENiHBG060491.
InParanoidiQ9NX55.
OMAiNCTGKPA.
OrthoDBiEOG7TBC4C.
PhylomeDBiQ9NX55.
TreeFamiTF325606.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: Q9NX55-2) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MRRRGEIDMA TEGDVELELE TETSGPERPP EKPRKHDSGA ADLERVTDYA
60 70 80 90 100
EEKEIQSSNL ETAMSVIGDR RSREQKAKQE REKELAKVTI KKEDLELIMT
110 120
EMEISRAAAE RSLREHMGNV VEALIALTN
Length:129
Mass (Da):14,665
Last modified:March 8, 2011 - v2
Checksum:i50AA7E49B1996948
GO
Isoform 3 (identifier: Q9NX55-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     63-82: AMSVIGDRRSREQKAKQERE → GERTGKSHYQEGRSGANSEW
     86-129: Missing.

Show »
Length:85
Mass (Da):9,619
Checksum:i4069C34590473DAB
GO

Sequence cautioni

The sequence AAF29100.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA91165.1 differs from that shown.Readthrough transcript SERF2-HYPK/C15orf63.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051S → P.1 Publication
Corresponds to variant rs12702 [ dbSNP | Ensembl ].
VAR_030335

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei63 – 8220AMSVI…KQERE → GERTGKSHYQEGRSGANSEW in isoform 3. 1 PublicationVSP_040677Add
BLAST
Alternative sequencei86 – 12944Missing in isoform 3. 1 PublicationVSP_040678Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000438 mRNA. Translation: BAA91165.1. Sequence problems.
AK022435 mRNA. No translation available.
AC018512 Genomic DNA. No translation available.
BC019262 mRNA. Translation: AAH19262.2.
AF161485 mRNA. Translation: AAF29100.1. Different initiation.
AF049613 mRNA. Translation: AAC26849.1.
CCDSiCCDS10104.1. [Q9NX55-2]
RefSeqiNP_001186814.1. NM_001199885.1.
NP_057484.3. NM_016400.3. [Q9NX55-2]
UniGeneiHs.730672.

Genome annotation databases

EnsembliENST00000406925; ENSP00000384474; ENSG00000242028. [Q9NX55-2]
ENST00000442995; ENSP00000401155; ENSG00000242028. [Q9NX55-2]
GeneIDi25764.
KEGGihsa:25764.
UCSCiuc059inn.1. human. [Q9NX55-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000438 mRNA. Translation: BAA91165.1. Sequence problems.
AK022435 mRNA. No translation available.
AC018512 Genomic DNA. No translation available.
BC019262 mRNA. Translation: AAH19262.2.
AF161485 mRNA. Translation: AAF29100.1. Different initiation.
AF049613 mRNA. Translation: AAC26849.1.
CCDSiCCDS10104.1. [Q9NX55-2]
RefSeqiNP_001186814.1. NM_001199885.1.
NP_057484.3. NM_016400.3. [Q9NX55-2]
UniGeneiHs.730672.

3D structure databases

DisProtiDP00546.
ProteinModelPortaliQ9NX55.
SMRiQ9NX55. Positions 85-127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117304. 21 interactions.
IntActiQ9NX55. 9 interactions.
MINTiMINT-1374304.
STRINGi9606.ENSP00000384474.

PTM databases

iPTMnetiQ9NX55.
PhosphoSiteiQ9NX55.

Polymorphism and mutation databases

BioMutaiHYPK.
DMDMi325511335.

Proteomic databases

EPDiQ9NX55.
MaxQBiQ9NX55.
PaxDbiQ9NX55.
PeptideAtlasiQ9NX55.
PRIDEiQ9NX55.
TopDownProteomicsiQ9NX55-2. [Q9NX55-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000406925; ENSP00000384474; ENSG00000242028. [Q9NX55-2]
ENST00000442995; ENSP00000401155; ENSG00000242028. [Q9NX55-2]
GeneIDi25764.
KEGGihsa:25764.
UCSCiuc059inn.1. human. [Q9NX55-2]

Organism-specific databases

CTDi25764.
GeneCardsiHYPK.
HGNCiHGNC:18418. HYPK.
HPAiHPA055252.
MIMi612784. gene.
neXtProtiNX_Q9NX55.
PharmGKBiPA165478509.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3450. Eukaryota.
ENOG4111M4G. LUCA.
GeneTreeiENSGT00390000008502.
HOGENOMiHOG000189569.
HOVERGENiHBG060491.
InParanoidiQ9NX55.
OMAiNCTGKPA.
OrthoDBiEOG7TBC4C.
PhylomeDBiQ9NX55.
TreeFamiTF325606.

Miscellaneous databases

GenomeRNAii25764.
PROiQ9NX55.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NX55.
ExpressionAtlasiQ9NX55. baseline and differential.
GenevisibleiQ9NX55. HS.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  2. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  4. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-129 (ISOFORM 2), VARIANT PRO-105.
    Tissue: Umbilical cord blood.
  5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-129 (ISOFORM 2), POSSIBLE INTERACTION WITH HTT.
    Tissue: Testis.
  6. "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."
    Raychaudhuri S., Sinha M., Mukhopadhyay D., Bhattacharyya N.P.
    Hum. Mol. Genet. 17:240-255(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HTT, SUBCELLULAR LOCATION.
  7. "The chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregation."
    Arnesen T., Starheim K.K., Van Damme P., Evjenth R., Dinh H., Betts M.J., Ryningen A., Vandekerckhove J., Gevaert K., Anderson D.
    Mol. Cell. Biol. 30:1898-1909(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NAA15, ASSOCIATION WITH NAA10-NAA15 COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiHYPK_HUMAN
AccessioniPrimary (citable) accession number: Q9NX55
Secondary accession number(s): C9JKJ0
, O75408, Q8WUW8, Q9P024
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: March 8, 2011
Last modified: July 6, 2016
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.