UniProt Accession

 DYR1A_HUMAN; Q13627; O60769; Q92582; Q92810; Q9UNM5 

Genbank Protein ID

 U58496; U52373; D85759; D86550; AF108830; AJ001870 

Genbank Nucleotide ID

 AAC50939.1; AAB18639.1; BAA12866.1; BAA13110.1; AAD31169.1; CAA05059.1 

Protein Name

 Dual specificity tyrosine-phosphorylation-regulated kinase 1A 

Protein Synonyms/Alias

 Dual specificity YAK1-related kinase; HP86; Protein kinase minibrain homolog; MNBH; hMNB 

Gene Name

 DYRK1A 

Gene Synonyms/Alias

 DYRK; MNB; MNBH 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
105	VDLIKTYKHINEVYY	acetylation	[1]
167	EIDSLIGKGSFGQVV	ubiquitination	[2]
453	VADYLKFKDLILRML	ubiquitination	[2, 3, 4]

Reference

 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 

Functional Description

 May play a role in a signaling pathway regulating nuclear functions of cell proliferation. Phosphorylates serine, threonine and tyrosine residues in its sequence and in exogenous substrates such as CRY2, FOXO1 and SIRT1. 

Sequence Annotation

 DOMAIN 159 479 Protein kinase.
 NP_BIND 165 173 ATP (By similarity).
 MOTIF 117 134 Bipartite nuclear localization signal
 ACT_SITE 287 287 Proton acceptor (By similarity).
 BINDING 188 188 ATP (By similarity).
 MOD_RES 145 145 Phosphotyrosine.
 MOD_RES 219 219 Phosphotyrosine; by autocatalysis (By
 MOD_RES 319 319 Phosphotyrosine; by autocatalysis (By
 MOD_RES 321 321 Phosphotyrosine; by autocatalysis.
 MOD_RES 748 748 Phosphoserine.
 MOD_RES 758 758 Phosphoserine.  

Keyword

 3D-structure; Alternative splicing; ATP-binding; Complete proteome; Kinase; Mental retardation; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 763 AA 

Protein Sequence

Gene Ontology

 GO:0016607; C:nuclear speck; ISS:UniProtKB.
 GO:0030529; C:ribonucleoprotein complex; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:MGI.
 GO:0043621; F:protein self-association; ISS:UniProtKB.
 GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
 GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:EC.
 GO:0048156; F:tau protein binding; ISS:BHF-UCL.
 GO:0007623; P:circadian rhythm; ISS:UniProtKB.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; ISS:BHF-UCL.
 GO:0007399; P:nervous system development; TAS:ProtInc.
 GO:0018107; P:peptidyl-threonine phosphorylation; ISS:BHF-UCL.
 GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
 GO:0090312; P:positive regulation of protein deacetylation; ISS:BHF-UCL.
 GO:0046777; P:protein autophosphorylation; ISS:UniProtKB. 

Interpro

 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS. 

Pfam

 PF00069; Pkinase 

SMART

 SM00220; S_TKc 

PROSITE

 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 

PRINTS