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Protein

Protein quaking

Gene

Qki

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. cell differentiation Source: UniProtKB-KW
  2. mRNA processing Source: UniProtKB-KW
  3. mRNA transport Source: UniProtKB-KW
  4. multicellular organismal development Source: UniProtKB-KW
  5. regulation of translation Source: UniProtKB-KW
  6. RNA splicing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, mRNA processing, mRNA splicing, mRNA transport, Translation regulation, Transport

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein quaking
Short name:
RqkI
Gene namesi
Name:Qki
Synonyms:Qk
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi1584886. Qk.

Subcellular locationi

Nucleus By similarity. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341Protein quakingPRO_0000239376Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei242 – 2421Asymmetric dimethylarginine; by CARM1By similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

PRIDEiQ91XU1.

PTM databases

PhosphoSiteiQ91XU1.

Expressioni

Tissue specificityi

Present in myelinating oligodendrocytes (at protein level).1 Publication

Gene expression databases

GenevestigatoriQ91XU1.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ91XU1.
SMRiQ91XU1. Positions 81-214.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini87 – 15367KHAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi276 – 2794SH3-binding
Motifi324 – 3307Nuclear localization signalBy similarity

Sequence similaritiesi

Contains 1 KH domain.Curated

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiCOG5176.
HOGENOMiHOG000019831.
HOVERGENiHBG093883.
InParanoidiQ91XU1.
PhylomeDBiQ91XU1.

Family and domain databases

Gene3Di3.30.1370.10. 1 hit.
InterProiIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamiPF00013. KH_1. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 1 hit.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 1 hit.

Sequencei

Sequence statusi: Complete.

Q91XU1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVGEMETKEN PNPTPDYLMQ LMNDKKLMSS LPNFCGIFNH LERLLDEEIS
60 70 80 90 100
RVRKDMYNDT LNGSTEKRSA ELPDAVGPIV QLQEKLYVPV KEYPDFNFVG
110 120 130 140 150
RILGPRGLTA KQLEAETGCK IMVRGKGSMR DKKKEEQNRG KPNWEHLNED
160 170 180 190 200
LHVLITVEDA QNRAEIKLKR AVEEVKKLLV PAAEGEDSLK KMQLMELAIL
210 220 230 240 250
NGTYRDANIK SPALAFSLAA TAQAAPRIIT GPAPVLPPAA LRTPTPAGPT
260 270 280 290 300
IMPLIRQIQT AVMPNGTPHP TAAIVPPGPE AGLIYTPYEY PYTLAPATSI
310 320 330 340
LEYPIEPSGV LGAVATKVRR HDMRVHPYQR IVTADRAATG N
Length:341
Mass (Da):37,643
Last modified:June 13, 2006 - v2
Checksum:i41B066F1711771C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03000138 Genomic DNA. No translation available.
AB054997 mRNA. Translation: BAB62175.1.
UniGeneiRn.228876.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03000138 Genomic DNA. No translation available.
AB054997 mRNA. Translation: BAB62175.1.
UniGeneiRn.228876.

3D structure databases

ProteinModelPortaliQ91XU1.
SMRiQ91XU1. Positions 81-214.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ91XU1.

Proteomic databases

PRIDEiQ91XU1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi1584886. Qk.

Phylogenomic databases

eggNOGiCOG5176.
HOGENOMiHOG000019831.
HOVERGENiHBG093883.
InParanoidiQ91XU1.
PhylomeDBiQ91XU1.

Miscellaneous databases

PROiQ91XU1.

Gene expression databases

GenevestigatoriQ91XU1.

Family and domain databases

Gene3Di3.30.1370.10. 1 hit.
InterProiIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamiPF00013. KH_1. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 1 hit.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Differentially expressed genes."
    Leng S., Tsutsumi M., Takase S., Abe S., Yamamoto Y., Fukunaga T., Saijoh K.
    Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 98-302.
    Tissue: Brain.
  3. "Expression of QKI proteins and MAP1B identifies actively myelinating oligodendrocytes in adult rat brain."
    Wu H.Y., Dawson M.R.L., Reynolds R., Hardy R.J.
    Mol. Cell. Neurosci. 17:292-302(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiQKI_RAT
AccessioniPrimary (citable) accession number: Q91XU1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: June 13, 2006
Last modified: January 7, 2015
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.