Q8IIT5 · PTKL_PLAF7
- ProteinInactive protein tyrosine kinase pTKL
- GenepTKL
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1501 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | host cell plasma membrane | |
Cellular Component | host cytoskeleton | |
Cellular Component | membrane | |
Cellular Component | symbiont-containing vacuole | |
Molecular Function | ATP binding | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | protein phosphorylation |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInactive protein tyrosine kinase pTKL
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)
Accessions
- Primary accessionQ8IIT5
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Host cell membrane ; Peripheral membrane protein
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
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000450198 | 1-1501 | UniProt | Inactive protein tyrosine kinase pTKL | |||
Sequence: MGNTLDSNKPKNFVTYADYKYIGKLNNKNEHHGIGIILYNSGESFYGSFINGKKEGKGIYIDKNLTRYINTWVDNKVFGKVKVVPYNSNRVYYFYYKNYMIEKCIYFDNNINNKESHHKNNIYNNYDNNSYNNNSCDDEEKRKYPIGVTKFKEDLSNYIHSTHIMKKNNKLFNKNDNEYNIFSSSLSYSSDSENINLLDILKKKKNKKNKKNKKKKNKKTKNTQILSCTQHKMYEHNMNESNFTKKDNVNCEHTDKMNISLHEKNDKKNEKKNEKKNKKKKLFKYFSNNIENLIIENYQTWSLREVIQWLMLCNVPVKWLISFYKNNITGDKLKYININTIRNELGIIAYGHAIKILQLIKNLQVMAYNKKFNNLIQIEEYKNYIRQKENTNKNIKKGKNIKKEKKKKKEKNIKKEKKKKKKETKKFNNMDKKYIDLAIHKNVKNIQNDTFYNKHENIYNCKNQTNFIYQNDSEIKKIMNKKKVSFEYDNNEEKKKKNIIKFIKNNKSLQNSNGEYYLINHLSKGICSDSIFYKSSQSKSSSQLSSPLSSPLSSPSPSSSPSSSPSSSPSSSPSSSPSPSSSPSPSSSPSSSPSSSPSSPPSPLSYKDNFPISSSCSSLERLPSYEKKLLSSSQSNIEHIKNLPLDVLSNNNSSANIKIKKSKSKYNNDKKEQKKLPLILNKSSSEFSPSHSYTSKSYHYNIKPSLQSSSNNSSDSSYSISSTCSSSSSYVSSLYSNRSNDILNFYRNKIIKYCNNIYMNTKLAYSYMNGFIIPHEDLIFIHPIENYYMDNTNEKNNINNPYTKEKIMNHNFSFNTKNNTSFIDINTNIFSSNKQQNINNFGKYKKMKSRMFKGKYMGKEVAIKILVGKIKNFKKLHQILYNLYNLRHSNLVLIMGVSIHYPFVFIIYEYMKNKCLFSYLHCIKYKHVYISTFLQRYKTLLHITQQEKIKKTNNINNNNNINHNNINNNNINHNNINHNNINNNNINNNNINYNKDYNNKKKKEDEQHNIEHQDTFIDLPEKSNISSDDNNSTDISQIQKENFHFLNKKIEENKNIIYDDHTSTLSDHSIHNINKSYDNVYKNKMNIFHYQHNVLCGAYDNNDNNINDNDIYCNNIYDNNINDNHIYCNNINDNHIYCNNINDNHIYCNNIYDHHKNTSLNSKEQNTDHNIEQINECNKYASETKYNIKKSNLKNNIISHKNFQKCNQIQMNQPYTFPPYQKELSSYLKNEKIKRKRKVLFSYLKTHIHFNSQQINDQHNRLSVQKIMKIITDVTLACTYLEKEKMSPINLKPTNILLDESLNAKISDFGISKIENCLDMNIDYSYKISSNSVIKINKKEYEQKKAKKIKIVNKNNNDLLYLYDHNNNVYKYNTQYIDVTYNNSYPSIFYWTPPEILRGKKNKKFYSDIYAFGIILWEMLSNDIPYNYPFASHIMAVVGYANEELSFNNIPVSIQSLIKACVNRNKYKRPTFEHILKTISTLYQKANTKVEDALISFMDGT | |||||||
Glycosylation | 64 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 128 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 133 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 239 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 242 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 258 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 327 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 448 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 463 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 471 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 473 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 485 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 506 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 528 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 649 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 652 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 681 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 712 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 737 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 811 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 819 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 821 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1015 | PTMeXchange | Phosphothreonine | ||||
Sequence: T | |||||||
Glycosylation | 1024 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1031 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1074 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1157 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 1162 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1167 | PTMeXchange | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1182 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 1382 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, coiled coil, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 204-221 | Basic residues | ||||
Sequence: KKNKKNKKNKKKKNKKTK | ||||||
Region | 204-223 | Disordered | ||||
Sequence: KKNKKNKKNKKKKNKKTKNT | ||||||
Compositional bias | 257-272 | Basic and acidic residues | ||||
Sequence: MNISLHEKNDKKNEKK | ||||||
Region | 257-276 | Disordered | ||||
Sequence: MNISLHEKNDKKNEKKNEKK | ||||||
Domain | 301-366 | SAM | ||||
Sequence: WSLREVIQWLMLCNVPVKWLISFYKNNITGDKLKYININTIRNELGIIAYGHAIKILQLIKNLQVM | ||||||
Region | 392-425 | Disordered | ||||
Sequence: NKNIKKGKNIKKEKKKKKEKNIKKEKKKKKKETK | ||||||
Compositional bias | 398-425 | Basic residues | ||||
Sequence: GKNIKKEKKKKKEKNIKKEKKKKKKETK | ||||||
Coiled coil | 399-433 | |||||
Sequence: KNIKKEKKKKKEKNIKKEKKKKKKETKKFNNMDKK | ||||||
Motif | 483-486 | RVxF motif 1 | ||||
Sequence: KVSF | ||||||
Compositional bias | 543-575 | Polar residues | ||||
Sequence: QLSSPLSSPLSSPSPSSSPSSSPSSSPSSSPSS | ||||||
Region | 543-607 | Disordered | ||||
Sequence: QLSSPLSSPLSSPSPSSSPSSSPSSSPSSSPSSSPSPSSSPSPSSSPSSSPSSSPSSPPSPLSYK | ||||||
Region | 659-678 | Disordered | ||||
Sequence: IKKSKSKYNNDKKEQKKLPL | ||||||
Compositional bias | 662-677 | Basic and acidic residues | ||||
Sequence: SKSKYNNDKKEQKKLP | ||||||
Domain | 1088-1483 | Protein kinase | ||||
Sequence: FHYQHNVLCGAYDNNDNNINDNDIYCNNIYDNNINDNHIYCNNINDNHIYCNNINDNHIYCNNIYDHHKNTSLNSKEQNTDHNIEQINECNKYASETKYNIKKSNLKNNIISHKNFQKCNQIQMNQPYTFPPYQKELSSYLKNEKIKRKRKVLFSYLKTHIHFNSQQINDQHNRLSVQKIMKIITDVTLACTYLEKEKMSPINLKPTNILLDESLNAKISDFGISKIENCLDMNIDYSYKISSNSVIKINKKEYEQKKAKKIKIVNKNNNDLLYLYDHNNNVYKYNTQYIDVTYNNSYPSIFYWTPPEILRGKKNKKFYSDIYAFGIILWEMLSNDIPYNYPFASHIMAVVGYANEELSFNNIPVSIQSLIKACVNRNKYKRPTFEHILKTISTLY | ||||||
Motif | 1238-1241 | RVxF motif 2 | ||||
Sequence: KVLF |
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).
There is a second N-terminal lobe-like kinase domain at residues 830-1095 that contains functional ATP binding sites (PubMed:31148576).
Sequence similarities
Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,501
- Mass (Da)176,120
- Last updated2009-09-22 v2
- ChecksumE517CBE251A2999F
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 204-221 | Basic residues | ||||
Sequence: KKNKKNKKNKKKKNKKTK | ||||||
Compositional bias | 257-272 | Basic and acidic residues | ||||
Sequence: MNISLHEKNDKKNEKK | ||||||
Compositional bias | 398-425 | Basic residues | ||||
Sequence: GKNIKKEKKKKKEKNIKKEKKKKKKETK | ||||||
Compositional bias | 543-575 | Polar residues | ||||
Sequence: QLSSPLSSPLSSPSPSSSPSSSPSSSPSSSPSS | ||||||
Compositional bias | 662-677 | Basic and acidic residues | ||||
Sequence: SKSKYNNDKKEQKKLP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LN999945 EMBL· GenBank· DDBJ | CZT98734.1 EMBL· GenBank· DDBJ | Genomic DNA |