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Reviewed, UniProtKB/Swiss-Prot Q96PU8 (QKI_HUMAN)

Last modified July 22, 2008. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Protein quaking
Alternative name(s):
    HqkI
      Short name=Hqk
Gene names
Name: QKI
Synonyms: HKQ
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

RNA-binding protein that plays a central role in myelinization. Binds to the 5'-NACUAAY-N(1,20)-UAAY-3' RNA core sequence. Acts by regulating pre-mRNA splicing, mRNA export, mRNA stability and protein translation. Required to protect and promote stability of mRNAs such as MBP and CDKN1B which promotes oligodendrocyte differentiation. Participates in mRNA transport by regulating the nuclear export of MBP mRNA. Also involved in regulation of mRNA splicing of MAG pre-mRNA. Acts as a translational repressor By similarity.

Subunit structure

Homodimer. Does not require RNA to homodimerize. Able to heterodimerize with BICC1 By similarity.

Subcellular location

NucleusBy similarity. CytoplasmBy similarity.

Tissue specificity

Expressed in the frontal cortex of brain.

Post-translational modification

Methylated by PRMT1 By similarity.

Tyrosine phosphorylated at its C-terminus, probably by FYN. Phosphorylation leads to decreased mRNA-binding affinity, affecting transport and/or stabilization of MBP mRNA By similarity.

Involvement in disease

May play a role in genetic susceptibility to schizophrenia. QKI levels of some isoforms such as isoform 6, are frequently down-regulated in schizophrenic patients.

Deletion of the QKI gene may play a role in astrocytic tumors.

Sequence similarities

Contains 1 KH domain.

Sequence caution

The sequence AAF63412.1 differs from that shown. Reason: Miscellaneous discrepancy. Chimeric cDNA.

The sequence AAF63415.1 differs from that shown. Reason: Miscellaneous discrepancy. Chimeric cDNA.

The sequence AAF63416.1 differs from that shown. Reason: Miscellaneous discrepancy. Chimeric cDNA.

Ontologies

Keywords

   Biological processDifferentiation
Translation regulation
Transport
mRNA processing
mRNA splicing
mRNA transport
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSH3-binding
   LigandRNA-binding
   Molecular functionDevelopmental protein
   PTMMethylation
Phosphoprotein

Gene Ontology (GO)

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96PU8-1)

Also known as: HQK-5; QKI-5;

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.
Isoform 2 (identifier: Q96PU8-2)

Also known as: HQK-6;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLSLSSLRRNSGRNSGSCGAWNM
     312-341: GAVATKVRRHDMRVHPYQRIVTADRAATGN → GMAFPTKG
Isoform 3 (identifier: Q96PU8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     213-220: Missing.
Isoform 4 (identifier: Q96PU8-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLSLSSLRRNSGRNSGSCGAWNM
Isoform 5 (identifier: Q96PU8-5)

The sequence of this isoform differs from the canonical sequence as follows:
     213-220: Missing.
     312-341: GAVATKVRRHDMRVHPYQRIVTADRAATGN → EWIEMPVMPDISAH
Isoform 6 (identifier: Q96PU8-6)

Also known as: HQK-7;

The sequence of this isoform differs from the canonical sequence as follows:
     312-341: GAVATKVRRHDMRVHPYQRIVTADRAATGN → EWIEMPVMPDISAH
Isoform 7 (identifier: Q96PU8-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLSLSSLRRNSGRNSGSCGAWNM
     312-341: GAVATKVRRHDMRVHPYQRIVTADRAATGN → EWIEMPVMPDISAH
Isoform 8 (identifier: Q96PU8-8)

Also known as: HQK-7B;

The sequence of this isoform differs from the canonical sequence as follows:
     312-341: GAVATKVRRHDMRVHPYQRIVTADRAATGN → GKFFSPWG

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 341341Protein quaking

Regions

Domain87 – 15367KH
Motif276 – 2794SH3-binding
Motif324 – 3307Nuclear localization signal By similarity

Natural variations

Alternative sequence11M → MLSLSSLRRNSGRNSGSCGA WNM in isoform 2, isoform 4 and isoform 7.
Alternative sequence213 – 2208Missing in isoform 3 and isoform 5.
Alternative sequence312 – 34130GAVAT…AATGN → GMAFPTKG in isoform 2.
Alternative sequence312 – 34130GAVAT…AATGN → EWIEMPVMPDISAH in isoform 5, isoform 6 and isoform 7.
Alternative sequence312 – 34130GAVAT…AATGN → GKFFSPWG in isoform 8.
Natural variant3361R → Q in a colorectal cancer sample; somatic mutation.

Experimental info

Sequence conflict301S → G in ABC88600. Ref.3
Sequence conflict2081N → D in AAH12222. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (HQK-5) (QKI-5) [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 43E7F3A426A494C4

FASTA34137,671
        10         20         30         40         50         60 
MVGEMETKEK PKPTPDYLMQ LMNDKKLMSS LPNFCGIFNH LERLLDEEIS RVRKDMYNDT 

        70         80         90        100        110        120 
LNGSTEKRSA ELPDAVGPIV QLQEKLYVPV KEYPDFNFVG RILGPRGLTA KQLEAETGCK 

       130        140        150        160        170        180 
IMVRGKGSMR DKKKEEQNRG KPNWEHLNED LHVLITVEDA QNRAEIKLKR AVEEVKKLLV 

       190        200        210        220        230        240 
PAAEGEDSLK KMQLMELAIL NGTYRDANIK SPALAFSLAA TAQAAPRIIT GPAPVLPPAA 

       250        260        270        280        290        300 
LRTPTPAGPT IMPLIRQIQT AVMPNGTPHP TAAIVPPGPE AGLIYTPYEY PYTLAPATSI 

       310        320        330        340 
LEYPIEPSGV LGAVATKVRR HDMRVHPYQR IVTADRAATG N 

« Hide

Isoform 2 (HQK-6) [UniParc].

Checksum: 8925D705A2F8C64A
Show »

34137,466
Isoform 3 [UniParc].

Checksum: 920353FF3C2B7403
Show »

33336,926
Isoform 4 [UniParc].

Checksum: B80BADA6E99380B3
Show »

36340,006
Isoform 5 [UniParc].

Checksum: DB23E1D2573820DF
Show »

31735,233
Isoform 6 (HQK-7) [UniParc].

Checksum: B4B2DA898F0145B3
Show »

32535,978
Isoform 7 [UniParc].

Checksum: 56F472815F85EDD4
Show »

34738,313
Isoform 8 (HQK-7B) [UniParc].

Checksum: D152389660BB4147
Show »

31935,248

References

« Hide 'large scale' references
[1]"Expression of Hqk encoding a KH RNA binding protein is altered in human glioma."
Li Z.Z., Kondo T., Murata T., Ebersole T.A., Nishi T., Tada K., Ushio Y., Yamamura K., Abe K.
Jpn. J. Cancer Res. 93:167-177(2002) [PubMed: 11856480] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 6 AND 8).
Tissue: Brain.
[2]"Molecular cloning of human QUAKING gene."
Xia J.-H., Xiao J.-F., He Y.-G., Yu K.-P., Pan Q., Dai H.-P.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4 AND 7), NUCLEOTIDE SEQUENCE [MRNA] OF 5-341 (ISOFORM 9).
[3]Li H., Nong W., Zhou G., Ke R., Shen C., Zhong G., Liang M., Tang Z., Huang B., Lin L., Yang S.
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-341 (ISOFORM 5).
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta and Skin.
[6]"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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-341.
Tissue: Embryo.
[7]"Human QKI, a new candidate gene for schizophrenia involved in myelination."
Aeberg K., Saetre P., Lindholm E., Ekholm B., Pettersson U., Adolfsson R., Jazin E.
Am. J. Med. Genet. B Neuropsychiatr. Genet. 141:84-90(2006) [PubMed: 16342280] [Abstract]
Cited for: POSSIBLE INVOLVEMENT IN SCHIZOPHRENIA.
[8]"Small regions of overlapping deletions on 6q26 in human astrocytic tumours identified using chromosome 6 tile path array-CGH."
Ichimura K., Mungall A.J., Fiegler H., Pearson D.M., Dunham I., Carter N.P., Collins V.P.
Oncogene 25:1261-1271(2006) [PubMed: 16205629] [Abstract]
Cited for: POSSIBLE INVOLVEMENT IN ASTROCYTIC TUMORS.
[9]"Human QKI, a potential regulator of mRNA expression of human oligodendrocyte-related genes involved in schizophrenia."
Aberg K., Saetre P., Jareborg N., Jazin E.
Proc. Natl. Acad. Sci. U.S.A. 103:7482-7487(2006) [PubMed: 16641098] [Abstract]
Cited for: POSSIBLE INVOLVEMENT IN SCHIZOPHRENIA.
[10]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-336.
+Additional computationally mapped references.

Cross-references

Sequence databases

AB067798 mRNA. Translation: BAB69496.1.
AB067799 mRNA. Translation: BAB69497.1.
AB067800 mRNA. Translation: BAB69498.1.
AB067801 mRNA. Translation: BAB69499.1.
AB067808 Genomic DNA. Translation: BAB69681.1.
AF142417 mRNA. Translation: AAF63412.1. Sequence problems.
AF142418 mRNA. Translation: AAF63413.1.
AF142419 mRNA. Translation: AAF63414.1.
AF142420 mRNA. Translation: AAF63415.1.
AF142421 mRNA. Translation: AAF63416.1. Sequence problems.
AF142422 mRNA. Translation: AAF63417.1.
AY780788 mRNA. Translation: AAV98358.1.
DQ323998 mRNA. Translation: ABC88600.1.
AL356119, AL031781 Genomic DNA. Translation: CAI23022.1.
AL356119, AL031781 Genomic DNA. Translation: CAI23023.1.
AL356119, AL031781 Genomic DNA. Translation: CAI23024.1.
AL031781, AL356119 Genomic DNA. Translation: CAI21651.1.
AL031781, AL356119 Genomic DNA. Translation: CAI21652.1.