E9Q3L2 · PI4KA_MOUSE

  • Protein
    Phosphatidylinositol 4-kinase alpha
  • Gene
    Pi4ka
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate.

Catalytic activity

Activity regulation

Activated by Triton X-100, insensitive to inhibition by adenosine and inhibited by wortmannin (By similarity).
The PI4K complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns4P) synthesis. Interaction with TMEM150A regulates PtdIns4P synthesis (By similarity).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular ComponentGolgi-associated vesicle membrane
Cellular Componentplasma membrane
Molecular Function1-phosphatidylinositol 4-kinase activity
Molecular FunctionATP binding
Molecular Functionkinase activity
Biological Processmodulation by host of viral process
Biological Processphosphatidylinositol phosphate biosynthetic process
Biological Processphosphatidylinositol-mediated signaling
Biological Processphosphorylation
Biological Processreorganization of cellular membranes to establish viral sites of replication

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosphatidylinositol 4-kinase alpha
  • EC number
  • Short names
    PI4-kinase alpha; PI4K-alpha; PtdIns-4-kinase alpha

Gene names

    • Name
      Pi4ka
    • Synonyms
      Pik4, Pik4ca

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    E9Q3L2
  • Secondary accessions
    • Q3UVT5
    • Q6DIC7
    • Q7TNG2
    • Q80Y45

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Cell membrane
Note: Localization to the plasma membrane is mediated by the PI4K complex and association with EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and HYCC (HYCC1 or HYCC2). Localization to the plasma membrane is regulated by TMEM150A.

Keywords

Phenotypes & Variants

Disruption phenotype

Early embryonic lethality. Conditional knockout mice show a dramatic depletion of cellular phosphatidylinositol 4-phosphate (PtdIns4P).

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 103 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004356321-2105Phosphatidylinositol 4-kinase alpha
Modified residue233Phosphoserine
Modified residue259Phosphoserine
Modified residue260Phosphoserine
Modified residue262Phosphoserine
Modified residue263Phosphoserine
Modified residue265Phosphoserine
Modified residue268Phosphoserine
Modified residue432Phosphoserine
Modified residue1439Phosphoserine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Component of a phosphatidylinositol 4-kinase (PI4K) complex, composed of PI4KA, EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and HYCC (HYCC1 or HYCC2). Interacts with TMEM150A; regulating recruitment to the plasma membrane. Interacts with TTC7A.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-24Disordered
Domain1533-1721PIK helical
Domain1811-2089PI3K/PI4K catalytic
Region1817-1823G-loop
Region1957-1965Catalytic loop
Region1976-2000Activation loop

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,105
  • Mass (Da)
    237,042
  • Last updated
    2016-02-17 v2
  • Checksum
    25EB66874330ED51
MAAAGARGGGGGGGGGGGGGSGSSSGSSTSRGFYFNTVLSLARSLAVQRPASLEKVQKLLCMCPVDFHGIFQLDERRRDAVIALGIFLIESDLQHKDCVVPYLLRLLRGLPKVYWVEESTARKGRGNLPVAESFSFCLVTLLSDVACRDPSLRDEILEAILQVLHVLLGMCQALEIQEKEYLCKYAIPCLIGISRSFGRYSNSEESLLSKLFPKVSPHSLRIPEELEGVRRRSFNDFRSILPSNLLTVCQEGTLKRKTSSVSSISQVSPERGIPPPSSPGGSAFHYFEASCLPDGTALEPEYYFSTISSSFSISPLFNGITYKEFCIPLEMLRELLNLVKKIVEEPVLKSLDAIVAGVMEANPSADLYYTTFSDPLYLTMFKMLRDTLYYMKDLPTSFVKEIHDFVLEQFNMSQGELQKILHDADRIHSEMSPLKLRCQANAACVDLMVWAVKDEQGAENLCIKLSEKLQSKTSSKVIIAHLPLLICCLQGLGRLCERFPVVVHSVTPSLRDFLVIPSPVLVKLYKYHSQYHTVAGSDIKISVTNEHSESTLNVLPGKKNQPSMYEQLRDIAIDNICRCLKAGLTVDPVIVEAFLASLSNRLYISQESDKDAHLIPDHTIRALGHIAVALRDTPKVMEPILQILQQKFCQPPSPLDVLIIDQLGCLVITGNQYIYQEVWNLFQQISVKASSVVYSATKDYKDHGYRHCSLAVINALANIAANIQEEHLVDELLMNLLELFVQLGLEGKRASERASEKGPALKASSSAGNLGVLIPVIAVLTRRLPPIKEAKPRLQKLFRDFWLYSVLMGFAVEGSGLWPEEWYEGVCEIATKSPLLTFPSKEPLRSVLQYNSAMKNDTVTPAELSELRSTIINLLDPPPEVSALINKLDFAMSTYLLSVYRLEYMRVLRSTDPDRFQVMFCYFEDKAIQKDKSGMMQCVIAVADKVFDAFLNMMAEKAKTKENEEELERHAQFLLVNFNHIHKRIRRVADKYLSGLVDKFPHLLWSGTVLKTMLDILQTLSLSLSADIHKDQPYYDIPDAPYRITVPDTYEARESIVKDFAARCGMILQEAMKWAPTVTKSHLQEYLNKHQNWVSGLSQHTGLAMATESILHFAGYNKQNTTLGATQLTERPACVKKDYSNFMASLNLRNRYAGEVHGMIRFSGATGQMSDLNKMMVQDLITALDHSHPQHYTQAMFKLTAMLISSKDCDPQLLHHLCWGPLRMFNEHGMETALACWEWLLAGKNGVEVPFMREMAGAWHMTVEQKFGLFSVETKEADPLAASEASQPRPCPPEVTPHYIWIDFLVQRFEIAKYCSSDQVEIFSSLLQRSMSLNIGGARGSMNRHVAAIGPRFKLLTLGLSLLHADVVPNATIRNVLREKIYSTAFDYFSCPPKFPTQGEKRLREDISIMIKFWTAMFSDKKYLTASQLVPPDNQDTRSNLDITVGSRQQATQGWINTYPLSSGMSTISKKSGMSKKTNRGSQLHKYYMKRRTLLLSLLATEIERLITWYNPLSAPELELDQAGENSVANWRSKYISLSEKQWKDNVNLAWSISPYLAVQLPARFKNTEAIGNEVTRLVRLDPGAVSDVPEAIKFLVTWHTIDADAPELSHVLCWAPTDPPTGLSYFSSMYPPHPLTAQYGVKVLRSFPPDAILFYIPQIVQALRYDKMGYVREYILWAAAKSQLLAHQFIWNMKTNIYLDEEGHQKDPDIGDLLEQLVEEITGSLSGPAKDFYQREFDFFNKITNVSAIIKPYPKGDERKKACLSALSEVKVQPGCYLPSNPEAIVLDIDYKSGTPMQSAAKAPYLAKFKVKRCGVSELEKEGLQCRSDAEDECFSQEADGKKICWQAAIFKVGDDCRQDMLALQIIDLFKNIFQLVGLDLFVFPYRVVATAPGCGVIECIPDCTSRDQLGRQTDFGMYDYFTRQYGDESTLAFQQARYNFIRSMAAYSLLLFLLQIKDRHNGNIMLDKKGHIIHIDFGFMFESSPGGNLGWEPDIKLTDEMVMIMGGKMEATPFKWFMEMCVRGYLAVRPYMDAVVSLVTLMLDTGLPCFRGQTIKLLKHRFSPNMTEREAANFIMKVIQNCFLSNRSRTYDMIQYYQNDIPY

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A140T8I9A0A140T8I9_MOUSEPi4ka2044
A0A338P7D3A0A338P7D3_MOUSEPi4ka319
A0A338P6S0A0A338P6S0_MOUSEPi4ka153
A0A338P6F9A0A338P6F9_MOUSEPi4ka74

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict861in Ref. 2; AAH75629

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC110573
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC049252
EMBL· GenBank· DDBJ
AAH49252.1
EMBL· GenBank· DDBJ
mRNA
BC055479
EMBL· GenBank· DDBJ
AAH55479.1
EMBL· GenBank· DDBJ
mRNA
BC075629
EMBL· GenBank· DDBJ
AAH75629.1
EMBL· GenBank· DDBJ
mRNA
AK136942
EMBL· GenBank· DDBJ
BAE23184.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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