UniProt ID | DYR1A_RAT | |
---|---|---|
UniProt AC | Q63470 | |
Protein Name | Dual specificity tyrosine-phosphorylation-regulated kinase 1A | |
Gene Name | Dyrk1a | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 763 | |
Subcellular Localization | Nucleus speckle . | |
Protein Description | Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. May play a role in a signaling pathway regulating nuclear functions of cell proliferation. Modulates alternative splicing by phosphorylating the splice factor SRSF6 (By similarity). Exhibits a substrate preference for proline at position P+1 and arginine at position P-3. Has pro-survival function and negatively regulates the apoptotic process. Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1. This in turn inhibits TP53 activity and apoptosis (By similarity).. | |
Protein Sequence | MHTGGETSACKPSSVRLAPSFSFHAAGLQMAAQMPHSHQYSDRRQPNISDQQVSALSYSDQIQQPLTNQVMPDIVMLQRRMPQTFRDPATAPLRKLSVDLIKTYKHINEVYYAKKKRRHQQGQGDDSSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDGTWSLKKTKDGKREYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKKTADEGTNTSNSVSTSPAMEQSQSSGTTSSTSSSSGGSSGTSNSGRARSDPTHQHRHSGGHFAAAVQAMDCETHSPQVRQQFPAPLGWSGTEAPTQVTVETHPVQETTFHVAPQQNALHHHHGNSSHHHHHHHHHHHHHGQQALGNRTRPRVYNSPTNSSSTQDSMEVGHSHHSMTSLSSSTTSSSTSSSSTGNQGNQAYQNRPVAANTLDFGQNGAMDVNLTVYSNPRQETGIAGHPTYQFSANTGPAHYMTEGHLTMRQGADREESPMTGVCVQQSPVASS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
14 | Phosphorylation | TSACKPSSVRLAPSF CCCCCCCCCCCCCCC | 21.56 | - | |
104 | Phosphorylation | SVDLIKTYKHINEVY CHHHHHHHHHHHHHH | 8.79 | - | |
105 | Acetylation | VDLIKTYKHINEVYY HHHHHHHHHHHHHHH | 43.15 | 22902405 | |
111 | Phosphorylation | YKHINEVYYAKKKRR HHHHHHHHHHHHHHH | 7.48 | - | |
140 | Phosphorylation | RKVYNDGYDDDNYDY HHCCCCCCCCCCCCE | 21.04 | - | |
145 | Phosphorylation | DGYDDDNYDYIVKNG CCCCCCCCCEEEECC | 19.67 | - | |
147 | Phosphorylation | YDDDNYDYIVKNGEK CCCCCCCEEEECCCC | 9.39 | - | |
159 | Phosphorylation | GEKWMDRYEIDSLIG CCCEECCEECHHHCC | 16.99 | - | |
177 | Phosphorylation | FGQVVKAYDRVEQEW HHHHHHHHHHHHHEE | 9.88 | - | |
219 | Phosphorylation | KHDTEMKYYIVHLKR HCCCHHHHHHHHHHH | 9.34 | 8631952 | |
310 | Phosphorylation | IKIVDFGSSCQLGQR EEEEECCCCCHHHHH | 28.12 | - | |
319 | Phosphorylation | CQLGQRIYQYIQSRF CHHHHHHHHHHHHHH | 9.46 | 27097102 | |
321 | Phosphorylation | LGQRIYQYIQSRFYR HHHHHHHHHHHHHCC | 5.51 | 23712012 | |
324 | Phosphorylation | RIYQYIQSRFYRSPE HHHHHHHHHHCCCHH | 18.13 | 27097102 | |
402 | Phosphorylation | FEKLPDGTWSLKKTK HHCCCCCCCCEEECC | 21.18 | - | |
449 | Phosphorylation | SGHTVADYLKFKDLI CCCCHHHHHHHHHHH | 11.31 | - | |
489 | Phosphorylation | TADEGTNTSNSVSTS CCCCCCCCCCCCCCC | 29.17 | 28689409 | |
496 | Phosphorylation | TSNSVSTSPAMEQSQ CCCCCCCCCHHHCHH | 11.80 | 28689409 | |
529 | Phosphorylation | SNSGRARSDPTHQHR CCCCCCCCCCCCCCC | 47.13 | 29779826 | |
532 | Phosphorylation | GRARSDPTHQHRHSG CCCCCCCCCCCCCCC | 38.88 | 25575281 | |
538 | Phosphorylation | PTHQHRHSGGHFAAA CCCCCCCCCCHHHHH | 46.56 | 28432305 | |
553 | Phosphorylation | VQAMDCETHSPQVRQ HHHHCCCCCCHHHHH | 33.70 | 28432305 | |
555 | Phosphorylation | AMDCETHSPQVRQQF HHCCCCCCHHHHHHC | 25.17 | 28432305 | |
748 | Phosphorylation | QGADREESPMTGVCV CCCCCCCCCCCCEEE | 18.41 | 27097102 | |
751 | Phosphorylation | DREESPMTGVCVQQS CCCCCCCCCEEEECC | 29.82 | 27097102 | |
758 | Phosphorylation | TGVCVQQSPVASS-- CCEEEECCCCCCC-- | 12.30 | 27097102 | |
762 | Phosphorylation | VQQSPVASS------ EECCCCCCC------ | 36.49 | 27097102 | |
763 | Phosphorylation | QQSPVASS------- ECCCCCCC------- | 34.21 | 27097102 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
97 | S | Phosphorylation | Kinase | DYRK1A | Q63470 | GPS |
111 | Y | Phosphorylation | Kinase | DYRK1A | Q63470 | GPS |
219 | Y | Phosphorylation | Kinase | DYRK1A | Q63470 | PSP |
319 | Y | Phosphorylation | Kinase | DYRK1A | Q63470 | GPS |
321 | Y | Phosphorylation | Kinase | DYRK1A | Q63470 | PSP |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DYR1A_RAT !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of DYR1A_RAT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
DCAF7_HUMAN | DCAF7 | physical | 27307198 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Dyrk, a dual specificity protein kinase with unique structuralfeatures whose activity is dependent on tyrosine residues betweensubdomains VII and VIII."; Kentrup H., Becker W., Heukelbach J., Wilmes A., Schuermann A.,Huppertz C., Kainulainen H., Joost H.-G.; J. Biol. Chem. 271:3488-3495(1996). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), FUNCTION, TISSUESPECIFICITY, AUTOPHOSPHORYLATION AT TYR-219; TYR-319 AND TYR-321, ANDMUTAGENESIS OF LYS-188; TYR-219; TYR-319 AND TYR-321. |