Dyrk1a
entrez
25255
canonical
uniprot
Q63470
canonical
ensembl
ENSRNOG00000001662
resolver
ensembl
ENSRNOG00055016511
resolver
ensembl
ENSRNOG00060019663
resolver
ensembl
ENSRNOG00065013664
resolver
ensp
ENSRNOP00000042446
resolver
ensp
ENSRNOP00000096172
resolver
genesymbol
Dyrk1a
resolver
genesymbol_syn
Dyrk
resolver
uniprot_entry
DYR1A_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by RANBP9 (By similarity). Inhibited by harmine, leucettamine B and leucettine L41 (PubMed:22998443). {ECO:0000250|UniProtKB:Q13627, ECO:0000269|PubMed:22998443}.
uniprot
proteins
amino_acid_sequence
MHTGGETSACKPSSVRLAPSFSFHAAGLQMAAQMPHSHQYSDRRQPNISDQQVSALSYSDQIQQPLTNQVMPDIVMLQRRMPQTFRDPATAPLRKLSVDLIKTYKHINEVYYAKKKRRHQQGQGDDSSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDGTWSLKKTKDGKREYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKKTADEGTNTSNSVSTSPAMEQSQSSGTTSSTSSSSGGSSGTSNSGRARSDPTHQHRHSGGHFAAAVQAMDCETHSPQVRQQFPAPLGWSGTEAPTQVTVETHPVQETTFHVAPQQNALHHHHGNSSHHHHHHHHHHHHHGQQALGNRTRPRVYNSPTNSSSTQDSMEVGHSHHSMTSLSSSTTSSSTSSSSTGNQGNQAYQNRPVAANTLDFGQNGAMDVNLTVYSNPRQETGIAGHPTYQFSANTGPAHYMTEGHLTMRQGADREESPMTGVCVQQSPVASS
uniprot
proteins
ec_number
2.7.11.23
uniprot
proteins
ec_number
2.7.12.1
uniprot
proteins
function
FUNCTION: Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities (PubMed:18938227, PubMed:22998443, PubMed:8631952, PubMed:9748265). Exhibits a substrate preference for proline at position P+1 and arginine at position P-3 (By similarity). Plays an important role in double-strand breaks (DSBs) repair following DNA damage (By similarity). Mechanistically, phosphorylates RNF169 and increases its ability to block accumulation of TP53BP1 at the DSB sites thereby promoting homologous recombination repair (HRR) (By similarity). Also acts as a positive regulator of transcription by acting as a CTD kinase that mediates phosphorylation of the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A (By similarity). May play a role in a signaling pathway regulating nuclear functions of cell proliferation (By similarity). Modulates alternative splicing by phosphorylating the splice factor SRSF6 (PubMed:22767602). Has pro-survival function and negatively regulates the apoptotic process. Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1. This in turn inhibits p53/TP53 activity and apoptosis (By similarity). Phosphorylates SEPTIN4, SEPTIN5 and SF3B1 at 'Thr-434' (PubMed:18938227). {ECO:0000250|UniProtKB:Q13627, ECO:0000250|UniProtKB:Q61214, ECO:0000269|PubMed:18938227, ECO:0000269|PubMed:22767602, ECO:0000269|PubMed:22998443, ECO:0000269|PubMed:8631952, ECO:0000269|PubMed:9748265}.
uniprot
proteins
mass_dalton
85541
uniprot
proteins
mutagenesis
MUTAGEN 188; /note="K->R: Abolishes autophosphorylation. Retains marginal kinase activity towards histones."; /evidence="ECO:0000269|PubMed:22767602, ECO:0000269|PubMed:8631952"; MUTAGEN 219; /note="Y->F: Reduced autophosphorylation on tyrosine, but retains some kinase activity towards histones."; /evidence="ECO:0000269|PubMed:8631952"; MUTAGEN 319; /note="Y->F: Suppressed autophosphorylation on tyrosine and reduced tyrosine, threonine and serine kinase activity towards histones; when associated with F-321."; /evidence="ECO:0000269|PubMed:8631952"; MUTAGEN 321; /note="Y->F: Suppressed autophosphorylation on tyrosine and reduced tyrosine, threonine and serine kinase activity towards histones; when associated with F-319."; /evidence="ECO:0000269|PubMed:8631952
uniprot
proteins
post_translational_modification
PTM: Can also autophosphorylate on serine and threonine residues (in vitro) (By similarity). Autophosphorylated on numerous tyrosine residues (PubMed:8631952). {ECO:0000250|UniProtKB:Q13627, ECO:0000269|PubMed:8631952}.
uniprot
proteins
protein_family
CMGC Ser/Thr protein kinase family
uniprot
proteins
protein_family
MNB/DYRK subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
18938227
uniprot
proteins
pubmed
22767602
uniprot
proteins
pubmed
22998443
uniprot
proteins
pubmed
8631952
uniprot
proteins
pubmed
9748265
uniprot
proteins
sequence_length
763
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:22767602, ECO:0000269|PubMed:9748265}.
uniprot
proteins