Q8IIT5 · PTKL_PLAF7

Function

Caution

Although it belongs to the kinase superfamily, contains an asparagine residue at the position of the canonical catalytic aspartic acid and does not have kinase activity (PubMed:31148576).
However, can bind ATP (PubMed:31148576).

Features

Showing features for binding site.

115012004006008001,0001,2001,400
TypeIDPosition(s)Description
Binding site836-844ATP (UniProtKB | ChEBI)
Binding site864ATP (UniProtKB | ChEBI)

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 Componenthost cell plasma membrane
Cellular Componenthost cytoskeleton
Cellular Componentmembrane
Cellular Componentsymbiont-containing vacuole
Molecular FunctionATP binding
Molecular Functionprotein serine/threonine kinase activity
Biological Processprotein phosphorylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Inactive protein tyrosine kinase pTKL
  • Alternative names
    • PfpTKL
    • Pseudo-tyrosine kinase-like protein

Gene names

    • Name
      pTKL
    • ORF names
      PF3D7_1106800

Organism names

  • Taxonomic identifier
  • Strain
    • 3D7
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)

Accessions

  • Primary accession
    Q8IIT5

Proteomes

Organism-specific databases

Subcellular Location

Host cell membrane
; Peripheral membrane protein
Host cytoplasm
Note: During the trophozoite stages, secreted into the parasitophorous vacuole and into the host erythrocyte cytoplasm. At the schizont stage, localizes to the parasitophorous vacuole but not to the host erythrocyte cytoplasm.

Keywords

PTM/Processing

Features

Showing features for chain, glycosylation, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00004501981-1501UniProtInactive protein tyrosine kinase pTKL
Glycosylation64UniProtN-linked (GlcNAc...) asparagine
Glycosylation128UniProtN-linked (GlcNAc...) asparagine
Glycosylation133UniProtN-linked (GlcNAc...) asparagine
Glycosylation239UniProtN-linked (GlcNAc...) asparagine
Glycosylation242UniProtN-linked (GlcNAc...) asparagine
Glycosylation258UniProtN-linked (GlcNAc...) asparagine
Glycosylation327UniProtN-linked (GlcNAc...) asparagine
Glycosylation448UniProtN-linked (GlcNAc...) asparagine
Glycosylation463UniProtN-linked (GlcNAc...) asparagine
Glycosylation471UniProtN-linked (GlcNAc...) asparagine
Modified residue (large scale data)473PTMeXchangePhosphoserine
Modified residue (large scale data)485PTMeXchangePhosphoserine
Glycosylation506UniProtN-linked (GlcNAc...) asparagine
Modified residue (large scale data)528PTMeXchangePhosphoserine
Modified residue (large scale data)649PTMeXchangePhosphoserine
Glycosylation652UniProtN-linked (GlcNAc...) asparagine
Glycosylation681UniProtN-linked (GlcNAc...) asparagine
Glycosylation712UniProtN-linked (GlcNAc...) asparagine
Glycosylation737UniProtN-linked (GlcNAc...) asparagine
Glycosylation811UniProtN-linked (GlcNAc...) asparagine
Glycosylation819UniProtN-linked (GlcNAc...) asparagine
Modified residue (large scale data)821PTMeXchangePhosphoserine
Modified residue (large scale data)1015PTMeXchangePhosphothreonine
Glycosylation1024UniProtN-linked (GlcNAc...) asparagine
Glycosylation1031UniProtN-linked (GlcNAc...) asparagine
Glycosylation1074UniProtN-linked (GlcNAc...) asparagine
Glycosylation1157UniProtN-linked (GlcNAc...) asparagine
Modified residue (large scale data)1162PTMeXchangePhosphoserine
Modified residue (large scale data)1167PTMeXchangePhosphothreonine
Modified residue (large scale data)1182PTMeXchangePhosphoserine
Glycosylation1382UniProtN-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts (via RVxF motif 1 and/or 2) with phosphatase PP1C (PubMed:31148576).
May interact (via SAM domain) with SERA5 (via C-terminus) (PubMed:31148576).

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region, domain, coiled coil, motif.

TypeIDPosition(s)Description
Compositional bias204-221Basic residues
Region204-223Disordered
Compositional bias257-272Basic and acidic residues
Region257-276Disordered
Domain301-366SAM
Region392-425Disordered
Compositional bias398-425Basic residues
Coiled coil399-433
Motif483-486RVxF motif 1
Compositional bias543-575Polar residues
Region543-607Disordered
Region659-678Disordered
Compositional bias662-677Basic and acidic residues
Domain1088-1483Protein kinase
Motif1238-1241RVxF motif 2

Domain

The protein kinase domain is predicted to be catalytically inactive (By similarity).
There is a second N-terminal lobe-like kinase domain at residues 830-1095 that contains functional ATP binding sites (PubMed:31148576).

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,501
  • Mass (Da)
    176,120
  • Last updated
    2009-09-22 v2
  • Checksum
    E517CBE251A2999F
MGNTLDSNKPKNFVTYADYKYIGKLNNKNEHHGIGIILYNSGESFYGSFINGKKEGKGIYIDKNLTRYINTWVDNKVFGKVKVVPYNSNRVYYFYYKNYMIEKCIYFDNNINNKESHHKNNIYNNYDNNSYNNNSCDDEEKRKYPIGVTKFKEDLSNYIHSTHIMKKNNKLFNKNDNEYNIFSSSLSYSSDSENINLLDILKKKKNKKNKKNKKKKNKKTKNTQILSCTQHKMYEHNMNESNFTKKDNVNCEHTDKMNISLHEKNDKKNEKKNEKKNKKKKLFKYFSNNIENLIIENYQTWSLREVIQWLMLCNVPVKWLISFYKNNITGDKLKYININTIRNELGIIAYGHAIKILQLIKNLQVMAYNKKFNNLIQIEEYKNYIRQKENTNKNIKKGKNIKKEKKKKKEKNIKKEKKKKKKETKKFNNMDKKYIDLAIHKNVKNIQNDTFYNKHENIYNCKNQTNFIYQNDSEIKKIMNKKKVSFEYDNNEEKKKKNIIKFIKNNKSLQNSNGEYYLINHLSKGICSDSIFYKSSQSKSSSQLSSPLSSPLSSPSPSSSPSSSPSSSPSSSPSSSPSPSSSPSPSSSPSSSPSSSPSSPPSPLSYKDNFPISSSCSSLERLPSYEKKLLSSSQSNIEHIKNLPLDVLSNNNSSANIKIKKSKSKYNNDKKEQKKLPLILNKSSSEFSPSHSYTSKSYHYNIKPSLQSSSNNSSDSSYSISSTCSSSSSYVSSLYSNRSNDILNFYRNKIIKYCNNIYMNTKLAYSYMNGFIIPHEDLIFIHPIENYYMDNTNEKNNINNPYTKEKIMNHNFSFNTKNNTSFIDINTNIFSSNKQQNINNFGKYKKMKSRMFKGKYMGKEVAIKILVGKIKNFKKLHQILYNLYNLRHSNLVLIMGVSIHYPFVFIIYEYMKNKCLFSYLHCIKYKHVYISTFLQRYKTLLHITQQEKIKKTNNINNNNNINHNNINNNNINHNNINHNNINNNNINNNNINYNKDYNNKKKKEDEQHNIEHQDTFIDLPEKSNISSDDNNSTDISQIQKENFHFLNKKIEENKNIIYDDHTSTLSDHSIHNINKSYDNVYKNKMNIFHYQHNVLCGAYDNNDNNINDNDIYCNNIYDNNINDNHIYCNNINDNHIYCNNINDNHIYCNNIYDHHKNTSLNSKEQNTDHNIEQINECNKYASETKYNIKKSNLKNNIISHKNFQKCNQIQMNQPYTFPPYQKELSSYLKNEKIKRKRKVLFSYLKTHIHFNSQQINDQHNRLSVQKIMKIITDVTLACTYLEKEKMSPINLKPTNILLDESLNAKISDFGISKIENCLDMNIDYSYKISSNSVIKINKKEYEQKKAKKIKIVNKNNNDLLYLYDHNNNVYKYNTQYIDVTYNNSYPSIFYWTPPEILRGKKNKKFYSDIYAFGIILWEMLSNDIPYNYPFASHIMAVVGYANEELSFNNIPVSIQSLIKACVNRNKYKRPTFEHILKTISTLYQKANTKVEDALISFMDGT

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias204-221Basic residues
Compositional bias257-272Basic and acidic residues
Compositional bias398-425Basic residues
Compositional bias543-575Polar residues
Compositional bias662-677Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LN999945
EMBL· GenBank· DDBJ
CZT98734.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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