DYR1A_RAT - dbPTM
DYR1A_RAT - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
14PhosphorylationTSACKPSSVRLAPSF
CCCCCCCCCCCCCCC
21.56-
104PhosphorylationSVDLIKTYKHINEVY
CHHHHHHHHHHHHHH
8.79-
105AcetylationVDLIKTYKHINEVYY
HHHHHHHHHHHHHHH
43.1522902405
111PhosphorylationYKHINEVYYAKKKRR
HHHHHHHHHHHHHHH
7.48-
140PhosphorylationRKVYNDGYDDDNYDY
HHCCCCCCCCCCCCE
21.04-
145PhosphorylationDGYDDDNYDYIVKNG
CCCCCCCCCEEEECC
19.67-
147PhosphorylationYDDDNYDYIVKNGEK
CCCCCCCEEEECCCC
9.39-
159PhosphorylationGEKWMDRYEIDSLIG
CCCEECCEECHHHCC
16.99-
177PhosphorylationFGQVVKAYDRVEQEW
HHHHHHHHHHHHHEE
9.88-
219PhosphorylationKHDTEMKYYIVHLKR
HCCCHHHHHHHHHHH
9.348631952
310PhosphorylationIKIVDFGSSCQLGQR
EEEEECCCCCHHHHH
28.12-
319PhosphorylationCQLGQRIYQYIQSRF
CHHHHHHHHHHHHHH
9.4627097102
321PhosphorylationLGQRIYQYIQSRFYR
HHHHHHHHHHHHHCC
5.5123712012
324PhosphorylationRIYQYIQSRFYRSPE
HHHHHHHHHHCCCHH
18.1327097102
402PhosphorylationFEKLPDGTWSLKKTK
HHCCCCCCCCEEECC
21.18-
449PhosphorylationSGHTVADYLKFKDLI
CCCCHHHHHHHHHHH
11.31-
489PhosphorylationTADEGTNTSNSVSTS
CCCCCCCCCCCCCCC
29.1728689409
496PhosphorylationTSNSVSTSPAMEQSQ
CCCCCCCCCHHHCHH
11.8028689409
529PhosphorylationSNSGRARSDPTHQHR
CCCCCCCCCCCCCCC
47.1329779826
532PhosphorylationGRARSDPTHQHRHSG
CCCCCCCCCCCCCCC
38.8825575281
538PhosphorylationPTHQHRHSGGHFAAA
CCCCCCCCCCHHHHH
46.5628432305
553PhosphorylationVQAMDCETHSPQVRQ
HHHHCCCCCCHHHHH
33.7028432305
555PhosphorylationAMDCETHSPQVRQQF
HHCCCCCCHHHHHHC
25.1728432305
748PhosphorylationQGADREESPMTGVCV
CCCCCCCCCCCCEEE
18.4127097102
751PhosphorylationDREESPMTGVCVQQS
CCCCCCCCCEEEECC
29.8227097102
758PhosphorylationTGVCVQQSPVASS--
CCEEEECCCCCCC--
12.3027097102
762PhosphorylationVQQSPVASS------
EECCCCCCC------
36.4927097102
763PhosphorylationQQSPVASS-------
ECCCCCCC-------
34.2127097102

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
97SPhosphorylationKinaseDYRK1AQ63470
GPS
111YPhosphorylationKinaseDYRK1AQ63470
GPS
219YPhosphorylationKinaseDYRK1AQ63470
PSP
319YPhosphorylationKinaseDYRK1AQ63470
GPS
321YPhosphorylationKinaseDYRK1AQ63470
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DYR1A_RAT !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DCAF7_HUMANDCAF7physical
27307198

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DYR1A_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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