DYRK1A (dual-specificity tyrosine- (Y)-phosphorylation regulated kinase 1A)

Written2010-09Maria L Arbonés, Susana de la Luna
Center for Genomic Regulation (CRG), Centro de Investigacion Biomedica en Red de Enfermedades Raras (CIBERER), Barcelona, Spain (MLA, SDLL); Institucio Catalana de Recerca i Estudis Avancats (ICREA), Barcelona, Spain (SDLL)

(Note : for Links provided by Atlas : click)

1. Identity

General Information
dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 1A
dual specificity tyrosine-(Y)-phosphorylation regulated kinase 1A
Other aliasHP86
LocusID (NCBI) 1859
Atlas_Id 43234
Location 21q22.13  [Link to chromosome band 21q22]
Location_base_pair Starts at 37420299 and ends at 37515376 bp from pter ( according to hg19-Feb_2009)  [Mapping DYRK1A.png]
Local_order Genes surrounding DYRK1A and their chromosome locations ordered from centromere to telomere (according to NCBI Map Viewer):
- TTC3 (tetratricopeptide repeat domain 3). Location 21q22.13.
- DSCR9 (Down syndrome critical region gene 9; miscRNA, non-protein coding). Location 21q22.13.
- DSCR3 (Down syndrome critical region gene 3). Location 21q22.13.
- DYRK1A. Location 21q22.13.
- LOC100289229 (hypothetical gene). Location 21q22.13.
- KCNJ6 (potassium inwardly-rectifying channel, subfamily J, member 6). Location: 21q22.1; 21q22.1.
- DSCR4 (Down syndrome critical region gene 4). Location 21q22.2.
- DSCR8 (Down syndrome critical region gene 8; miscRNA). Location 21q22.2.
  Map of the Chromosomal region in 21q22.13 - 21q22.2 where DYRK1A is located. Genes (in green) and predicted gene (in black) surrounding DYRK1A are depicted according to the chromosomal position in NCBI Map Viewer (version released in August 2009). Direction of the arrowhead indicates the orientation of the gene.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
BRWD1 (21q22.2) / DYRK1A (21q22.13)DYRK1A (21q22.13) / ACOXL (2q13)DYRK1A (21q22.13) / BRWD1 (21q22.2)
DYRK1A (21q22.13) / CLK3 (15q24.1)DYRK1A (21q22.13) / KDM4B (19p13.3)DYRK1A (21q22.13) / MRPS6 (21q22.11)
DYRK1A (21q22.13) / MTMR1 (Xq28)DYRK1A (21q22.13) / PRRC2C (1q24.3)DYRK1A (21q22.13) / RUNX1 (21q22.12)
DYRK1A (21q22.13) / TTC3 (21q22.13)DYRK1A (21q22.13) / ZBTB46 (20q13.33)ERG (21q22.2) / DYRK1A (21q22.13)
NQO1 (16q22.1) / DYRK1A (21q22.13)RUNX1 (21q22.12) / DYRK1A (21q22.13)YWHAZ (8q22.3) / DYRK1A (21q22.13)
Note The chromosomal region depicted in the above figure is part of the "critical region" for Down syndrome, commonly named Down syndrome critical region (DSCR). This region, which encompasses 5.4 Mb of chromosome 21 and contains around 30 genes, has been defined in phenotype-genotype correlation studies of individuals with partial trisomy 21 (Delabar et al., 1993). Similar correlation studies of patients with partial monosomy 21 have defined a common region within DSCR that when deleted causes microcephaly and developmental delay. This region expands 1.2 Mb and contains 10 genes including DYRK1A (Matsumoto et al., 1997). The identification of two unrelated patients with microcephaly carrying a DYRK1A truncated mutation in hemizygosis (see bellow; Moller et al., 2007) indicates that haploinsufficiency of DYRK1A is most likely the cause of the common features presented by these two patients and by patients with partial monosomy 21.


  Schematic representation of the exon-intron organization of human DYRK1A gene. The size of introns and exons is in kb. Exons (boxes) are numbered and drawn to scale: in orange, coding exons; in blue, alternative first exons. The position of major transcription start sites (TSSs) according to Maenz et al. (2008) is indicated with blue arrows. Alternative splicing events are shown with dotted lines and numbered from a-e.
Description The DYRK1A gene contains at least 12 exons spanning approximately 149.7 kb of genomic DNA.
Transcription Several transcripts have been identified as result of alternative splicing (Wang et al., 1998; Guimerá et al., 1999; Maenz et al., 2008). The use of two alternative first exons, controlled by different promoter sequences, does not affect the open reading frame (alternative splicing events a and b). These two promoters differ in their strength and regulation by the transcription factor E2F1 (Maenz et al., 2008). Exclusion of exon 2 would give rise to a N-terminal truncated protein (alternative splicing event c). The use of an alternative acceptor site within exon 4 (alternative splicing events d and e) generates two protein variants that differ by the inclusion/exclusion of 9 amino acids in the N-terminal region (Kentrup et al., 1996; Guimerá et al., 1999). No functional differences have been associated to any of these variants. Further splice variants, affecting the C-terminal region, were identified by PCR cloning (Guimerá et al., 1999), although the existence of the protein isoforms encoded by these transcripts has not yet been confirmed.
Pseudogene No pseudogene reported.

3. Protein

  Schematic representation of DYRK1A protein. NLS: nuclear localization signal. DH: DYRK-homology box. PEST: Pest motif. His: Polyhistidine stretch. S/T: Serine and threonine-rich region. The line shows the alternatively spliced segment of 9 amino acids.
Description The DYRK1A gene encodes two main protein isoforms of 763 and 754 amino acids. DYRK1A is a protein kinase that belongs to the DYRK family of dual-specificity protein kinases (CMGC group: DYRK family: DYRK subfamily). The kinase domain is located centrally in the primary structure of the protein. DYRK1A shares with the other DYRKs a conserved motif N-terminal to the kinase domain known as DYRK homology (DH)-box. It also harbors a functional, bipartite nuclear localization signal (NLS) N-terminal to the DH-box, a second NLS between subdomains X and XI within the kinase domain, a C-terminal PEST motif, and a polyhistidine tract that acts as a nuclear speckle targeting signal. When analyzed by Western blot with antibodies raised against the C-terminal, the protein appears as three bands around 90 kDa.
Expression At the RNA level, DYRK1A is expressed as an approximately 6 kb transcript in many fetal and adult tissues including brain, heart, lung and skeletal muscle (Guimerá et al., 1996; Shindoh et al., 1996; Song et al., 1996). At the protein level, human DYRK1A expression has been mainly studied in the central nervous system, where it is detected in cortex, hippocampus, amygdala, thalamus and substantia nigra (Wegiel et al., 2004). The number of DYRK1A immunopositive neurons increases with maturation of human brain and an increase in the number of DYRK1A-positive astrocytes in aged people has also been observed (Weigel et al., 2004). Work done in mice has led to the proposal that Dyrk1a is expressed in sequential phases of central nervous system development; i) scattered expression in individual pre-neurogenic progenitors; ii) throughout the cell cycle in neurogenic progenitors; ii) down-regulated in post-mitotic neurons as they migrate radially; and iv) sustained expression in late differentiating neurons (Hammerle et al., 2008). Based on these observations, DYRK1A has been suggested to be critical for the coupling of the sequential events required for proper neuronal development.
The analysis of the human DYRK1A promoter found two promoter regions that respond differentially to the cell cycle-related transcription factor E2F1 (Maenz et al., 2008). Binding of the AP4-geminin complex to the human DYRK1A promoter has been shown by chromatin immunoprecipitation assays; moreover, the DYRK1A promoter is downregulated by AP4 overexpression in gene reporter assays, suggesting that the AP4-geminin repressor complex could be responsible of the DYRK1A downregulation in non-neuronal cells (Kim et al., 2004). In mice, Dyrk1a is transcriptionally induced by the receptor activator of nuclear factor kappa-B ligand (RANKL) cytokine through the activity of the nuclear factor of activated T-cells (NFAT) transcription factors (Lee et al., 2009).
Localisation When overexpressed in mammalian cells, DYRK1A protein mainly localizes in the nucleus and shows a punctuated staining that it is compatible with its accumulation in nuclear speckles (or splicing factor compartment) (Becker et al., 1998; Alvarez et al., 2003). Two nuclear localization signals contribute to DYRK1A nuclear translocation and the histidine stretch is responsible for the accumulation of the protein in nuclear speckles (Alvarez et al., 2003). Endogenous DYRK1A is detected in both the nucleus and the cytosol of human neurons, but only in the cytosol of astrocytes (Wegiel et al., 2004). Within the cytosol, DYRK1A accumulates in the cell bodies, dendrites and synapses (Wegiel et al., 2004). Similar behaviour has been described for mouse and chicken Dyrk1a (Marti et al., 2003; Hammerle et al., 2003; Laguna et al., 2008). These findings also correlate with the observed nuclear-cytosolic partitioning of Dyrk1a in mouse brain by biochemical fractionation (Aranda et al., 2008).
In certain pathological situations like the neurodegeneration associated to sporadic Alzheimer's disease and Down syndrome, DYRK1A is detected in neurofibrillary tangles, in granules in granulovacuolar degeneration and in corpora amylacea (Wegiel et al., 2008).
Function DYRK1A is a dual-specificity protein kinase that autophosphorylates on tyrosine serine and threonine residues, but phosphorylate substrates only on serine or threonine residues. Autophosphorylation of Tyr 312/321 (754/763 variants) in the activation loop is required for full catalytic activity (Himpel et al., 2001; Lochhed et al., 2005). A full list of the residues phosphorylated in DYRK1A can be found at PhoSphositePlus. A consensus phosphorylation sequence has been proposed for DYRK1A (RPXS/TP) (Himpel et al., 2000), although some phosphorylation sites have been found that do not fit within the consensus such as in the case of LTAT(434)P in SF3B1/SAP155 or RPAS(640)V in glycogen synthase (Skurat et al., 2004; de Graaf et al., 2006).
The phenotypic analysis of a loss-of-function mouse model has provided information about DYRK1A functional roles. Null Dyrk1a embryos present a severe developmental delay and die around embryonic day 10.5, and the analysis of the heterozygous animals has indicated that DYRK1A plays a role in brain development (Fotaki et al., 2002). In this context, DYRK1A has been shown to participate in neuritogenesis (Benavides-Piccione et al., 2005; Gockler et al., 2009; Lepagnol-Bestel et al., 2009; Scales et al., 2009), and DYRK1A overexpression potentiates nerve growth factor (NGF)-mediated neuronal differentiation in PC12 cells through an enhancement of Ras/MAPK signalling (Kelly and Ramahni, 2005) or exit from the cell cycle in neuronal progenitors (Park et al., 2010; Yabut et al., 2010). Furthermore, an increase in DYRK1A gene dosage alters the levels of neuron-restrictive silencer factor (NRSF or REST), a key regulator of neuronal differentiation (Canzonetta et al., 2008). In the adult brain, DYRK1A regulates epidermal growth factor (EGF) signalling in stem cell daughters and reduced levels of DYRK1A compromise stem cell longevity (Ferron et al., 2010). These evidences together with DYRK1A overexpression in Down syndrome individuals (Dowjat et al., 2007) and the phenotype of mouse models of overexpression (Smith et al., 1997; Altafaj et al., 2001; Ahn et al., 2006), have led to the proposal of DYRK1A as a main contributor to Down syndrome neurological alterations (reviewed in Park et al., 2009a). Finally, there are increasing evidences of a link of DYRK1A with neurodegeneration, given that it phosphorylates several proteins related to this cellular process including tau, alpha-synuclein, septin-4, presenilin or amyloid beta precursor protein (APP) and accumulates in amyloid lesions (reviewed in Park et al., 2009b).
Additionally, the participation of DYRK1A in different cellular processes and signal transduction pathways has been inferred from the activity of its interactors and substrates. Functional activities include apoptosis, exerting a protective role through phosphorylation of caspase-9 or the deactelylase sirtuin-1 (SIRT1) (Seifert et al., 2008; Laguna et al., 2008; Guo et al., 2010); endocytosis, through the interaction and phosphorylation of the GTPase dynamin-1, the phosphatase synaptojanin-1 or the scaffold protein amphiphysin-1 (Murakami et al., 2009; and references therein); cytoskeletal-related processes, through phosphorylation of tau or microtubule-associated protein 1B (MAP1B) (Woods et al., 2001; Scales et al., 2009); receptor tyrosine kinase-dependent signalling, through the interaction with the kinase B-Raf (NGF) or the inhibitor Sprouty-2 (FGF) (Kelly and Rahmani, 2005; Aranda et al., 2008).
A relevant group of DYRK1A substrates are chromatin regulators and transcription factors suggesting a role for DYRK1A in the regulation of gene expression programs. When assayed in gene reporter assays, DYRK1A works as an activator of cAMP responsive element binding protein 1 (CREB1) (Yang et al., 2001), Gli1 (Mao et al., 2002), forkhead box protein O1 (FOXO1/FKHR) (von Groote-Bidlingmaier et al., 2003) or androgen receptor-interacting protein 4 (ARIP4/RAD54L2) (Sitz et al., 2004) and as an inhibitor of Notch-dependent transcription (Fernandez-Martinez et al., 2009). DYRK1A acts as negative regulator of NFAT transcription factors in distinct cellular environments by inducing their translocation to the cytosol (Arron et al., 2006; Kuhn et al., 2009; Lee et al., 2009). DYRK1A cooperation with glycogen synthase kinase 3 (GSK3) promotes the degradation of cryptochrome 2 (CRY2), thus contributing to the internal cellular clock (Kurabayashi et al., 2010). Another DYRK1A target is the tumour protein p53, either by being a direct DYRK1A substrate or indirectly through the phosphorylation by DYRK1A of the p53 deactelylase SIRT1 (Guo et al., 2010; Park et al., 2010). Finally, DYRK1A has been proposed as a regulator of splicing based on DYRK1A localization in nuclear speckles (Alvarez et al., 2003) and on having several splicing factors such SF3b1 or ASF as substrates (de Graaf et al., 2006; Shi et al., 2008). In fact, DYRK1A phosphorylation of the alternative splicing factor ASF prevents ASF-mediated inclusion of the alternatively spliced exon 10 in tau mRNA (Shi et al., 2008).
Homology Mouse and human DYRK1A show a high degree of homology at the amino acid level (99%). The Drosophila DYRK1A orthologue is the minibrain gene (Tejedor et al., 1995). Within the DYRK family of kinases, the closest paralogous is DYRK1B.

4. Mutations

Note A truncated mutation in DYRK1A gene has been identified in two unrelated patients that present prenatal onset of microcephaly, intrauterine growth retardation, developmental delay, severe feeding problems and febrile seizures. In both patients, truncation of DYRK1A results from a de novo balanced translocation involving chromosome 21, t(9;21)(p12;q22) in one patient and t(2;21)(q22;q22) in the other (Moller et al., 2008). Location of the breakpoints within DYRK1A is depicted in the diagram bellow.
  Schematic representation of DYRK1A gene indicating the location of the breakpoints in chromosome 21 (vertical arrows) of the reported patients with a de novo balanced translocation.

5. Implicated in

Entity Various types of cancer and disease
Disease There are evidences suggesting a role of DYRK1A in several human diseases. All the evidences, with the exception of those reported in Moller et al. (2008) regarding microcephaly, are based on in vitro molecular and biochemical studies, on RNA expression studies and on studies in model organisms, mainly in the mouse. The list of human diseases includes Down syndrome (reviewed in Hammerle et al., 2003; Park et al., 2009a), early onset microcephaly (Moller et al., 2008), Alzheimer and Huntington diseases (reviewed in Park et al., 2009b), several cancer types (Baek et al., 2009; de Wit et al., 2002) and cardiac hypertrophy (Khun at al., 2009; Raaf et al., 2009).
Oncogenesis Experiments performed in the Ts65Dn trisomic mouse model for Down syndrome have shown that overexpression of DYRK1A contributes to the attenuation of the calcineurin pathway induced by the increased dosage of RCAN1 (also named DSCR1), a chromosome 21 gene that like DYRK1A is triplicated in this model (Baek et al., 2009). The reduction in calcineurin signalling leads to a significant reduction of angiogenesis and tumour growth. Because the incidence of many cancer types is significantly reduced in people with Down syndrome (complete trisomy of chromosome 21), the results obtained in mice suggest that small differences in the amount of DYRK1A kinase could, through the calcineurin-dependent regulation of angiogenesis, modify the growth of some type of tumours also in humans (Pussegoda et al., 2010). By contrary, phosphorylation of caspase-9 by DYRK1A may have a negative role in cancer because a reduction of caspase-9 apoptotic activity protects mitotic cells from apoptosis and promotes cell survival during tumorigenesis (Allan and Clarke, 2007).
DYRK1A has been shown to interact with two viral oncoproteins, adenovirus E1A and human papilloma virus (HPV) E7 (Zhang et al., 2001; Liang et al., 2008; Komorek et al., 2010), which could be suggestive of the involvement of DYRK1A in oncogenic transformation.
Entity Melanoma
Note DYRK1A mRNA levels in a melanoma cell line with high metastatic potential (Mel57) are lower than in a melanoma cell line (1F6) with poor metastatic potential. DYRK1A mRNA levels are down-regulated in vivo during melanocytic tumour progression, and in tumour samples from lung, oesophagus, colon, pancreas and testis when compared to normal samples from the same tissues (de Wit et al., 2002).
Entity Cervical cancer
Note HPV type 16 (HPV16) is a tumorigenic virus that causes the development of cervical cancer. DYRK1A is present in HPV16 immortalized keratinocytes but not in primary keratynocytes; moreover, malignant cervical lesions contain more DYRK1A than normal tissue (Chang et al., 2007). Biochemical data lead to the suggestion that the increased expression of DYRK1A in immortalized keratinocytes and in cervical tissues acts as an antiapoptotic factor in the FKHR-dependent pathway leading to tumour development (Chang et al., 2007). Additionally, DYRK1A interacts and phosphorylates the HPV16 protein E7 leading to its stabilization and to an increase in its capacity for forming clones in a colony-formation assay (Liang et al., 2008).
Entity Pancreatic endocrine neoplasms
Note Microarray hybridization data showed up-regulation of DYRK1A in metastatic pancreatic endocrine neoplasms when compared with nonmetastatic pancreatic endocrine neoplasms (Hansel et al., 2004).

6. Bibliography

DYRK1A BAC transgenic mice show altered synaptic plasticity with learning and memory defects.
Ahn KJ, Jeong HK, Choi HS, Ryoo SR, Kim YJ, Goo JS, Choi SY, Han JS, Ha I, Song WJ.
Neurobiol Dis. 2006 Jun;22(3):463-72. Epub 2006 Feb 7.
PMID 16455265
Phosphorylation of caspase-9 by CDK1/cyclin B1 protects mitotic cells against apoptosis.
Allan LA, Clarke PR.
Mol Cell. 2007 Apr 27;26(2):301-10.
PMID 17466630
Neurodevelopmental delay, motor abnormalities and cognitive deficits in transgenic mice overexpressing Dyrk1A (minibrain), a murine model of Down's syndrome.
Altafaj X, Dierssen M, Baamonde C, Marti E, Visa J, Guimera J, Oset M, Gonzalez JR, Florez J, Fillat C, Estivill X.
Hum Mol Genet. 2001 Sep 1;10(18):1915-23.
PMID 11555628
DYRK1A accumulates in splicing speckles through a novel targeting signal and induces speckle disassembly.
Alvarez M, Estivill X, de la Luna S.
J Cell Sci. 2003 Aug 1;116(Pt 15):3099-107. Epub 2003 Jun 10.
PMID 12799418
Sprouty2-mediated inhibition of fibroblast growth factor signaling is modulated by the protein kinase DYRK1A.
Aranda S, Alvarez M, Turro S, Laguna A, de la Luna S.
Mol Cell Biol. 2008 Oct;28(19):5899-911. Epub 2008 Aug 4.
PMID 18678649
NFAT dysregulation by increased dosage of DSCR1 and DYRK1A on chromosome 21.
Arron JR, Winslow MM, Polleri A, Chang CP, Wu H, Gao X, Neilson JR, Chen L, Heit JJ, Kim SK, Yamasaki N, Miyakawa T, Francke U, Graef IA, Crabtree GR.
Nature. 2006 Jun 1;441(7093):595-600. Epub 2006 Mar 22.
PMID 16554754
Down's syndrome suppression of tumour growth and the role of the calcineurin inhibitor DSCR1.
Baek KH, Zaslavsky A, Lynch RC, Britt C, Okada Y, Siarey RJ, Lensch MW, Park IH, Yoon SS, Minami T, Korenberg JR, Folkman J, Daley GQ, Aird WC, Galdzicki Z, Ryeom S.
Nature. 2009 Jun 25;459(7250):1126-30. Epub 2009 May 20.
PMID 19458618
Sequence characteristics, subcellular localization, and substrate specificity of DYRK-related kinases, a novel family of dual specificity protein kinases.
Becker W, Weber Y, Wetzel K, Eirmbter K, Tejedor FJ, Joost HG.
J Biol Chem. 1998 Oct 2;273(40):25893-902.
PMID 9748265
Alterations in the phenotype of neocortical pyramidal cells in the Dyrk1A+/- mouse.
Benavides-Piccione R, Dierssen M, Ballesteros-Yanez I, Martinez de Lagran M, Arbones ML, Fotaki V, DeFelipe J, Elston GN.
Neurobiol Dis. 2005 Oct;20(1):115-22.
PMID 16137572
DYRK1A-dosage imbalance perturbs NRSF/REST levels, deregulating pluripotency and embryonic stem cell fate in Down syndrome.
Canzonetta C, Mulligan C, Deutsch S, Ruf S, O'Doherty A, Lyle R, Borel C, Lin-Marq N, Delom F, Groet J, Schnappauf F, De Vita S, Averill S, Priestley JV, Martin JE, Shipley J, Denyer G, Epstein CJ, Fillat C, Estivill X, Tybulewicz VL, Fisher EM, Antonarakis SE, Nizetic D.
Am J Hum Genet. 2008 Sep;83(3):388-400. Epub 2008 Sep 4.
PMID 18771760
Increased expression of Dyrk1a in HPV16 immortalized keratinocytes enable evasion of apoptosis.
Chang HS, Lin CH, Yang CH, Yen MS, Lai CR, Chen YR, Liang YJ, Yu WC.
Int J Cancer. 2007 Jun 1;120(11):2377-85.
PMID 17294446
Molecular mapping of twenty-four features of Down syndrome on chromosome 21.
Delabar JM, Theophile D, Rahmani Z, Chettouh Z, Blouin JL, Prieur M, Noel B, Sinet PM.
Eur J Hum Genet. 1993;1(2):114-24.
PMID 8055322
Trisomy-driven overexpression of DYRK1A kinase in the brain of subjects with Down syndrome.
Dowjat WK, Adayev T, Kuchna I, Nowicki K, Palminiello S, Hwang YW, Wegiel J.
Neurosci Lett. 2007 Feb 8;413(1):77-81. Epub 2006 Dec 4.
PMID 17145134
Attenuation of Notch signalling by the Down-syndrome-associated kinase DYRK1A.
Fernandez-Martinez J, Vela EM, Tora-Ponsioen M, Ocana OH, Nieto MA, Galceran J.
J Cell Sci. 2009 May 15;122(Pt 10):1574-83. Epub 2009 Apr 21.
PMID 19383720
Regulated segregation of kinase Dyrk1A during asymmetric neural stem cell division is critical for EGFR-mediated biased signaling.
Ferron SR, Pozo N, Laguna A, Aranda S, Porlan E, Moreno M, Fillat C, de la Luna S, Sanchez P, Arbones ML, Farinas I.
Cell Stem Cell. 2010 Sep 3;7(3):367-79.
PMID 20804972
Dyrk1A haploinsufficiency affects viability and causes developmental delay and abnormal brain morphology in mice.
Fotaki V, Dierssen M, Alcantara S, Martinez S, Marti E, Casas C, Visa J, Soriano E, Estivill X, Arbones ML.
Mol Cell Biol. 2002 Sep;22(18):6636-47.
PMID 12192061
Harmine specifically inhibits protein kinase DYRK1A and interferes with neurite formation.
Gockler N, Jofre G, Papadopoulos C, Soppa U, Tejedor FJ, Becker W.
FEBS J. 2009 Nov;276(21):6324-37. Epub 2009 Oct 1.
PMID 19796173
Human minibrain homologue (MNBH/DYRK1): characterization, alternative splicing, differential tissue expression, and overexpression in Down syndrome.
Guimera J, Casas C, Estivill X, Pritchard M.
Genomics. 1999 May 1;57(3):407-18.
PMID 10329007
DYRK1A and DYRK3 promote cell survival through phosphorylation and activation of SIRT1.
Guo X, Williams JG, Schug TT, Li X.
J Biol Chem. 2010 Apr 23;285(17):13223-32. Epub 2010 Feb 18.
PMID 20167603
The spatio-temporal and subcellular expression of the candidate Down syndrome gene Mnb/Dyrk1A in the developing mouse brain suggests distinct sequential roles in neuronal development.
Hammerle B, Elizalde C, Tejedor FJ.
Eur J Neurosci. 2008 Mar;27(5):1061-74.
PMID 18364031
Met proto-oncogene and insulin-like growth factor binding protein 3 overexpression correlates with metastatic ability in well-differentiated pancreatic endocrine neoplasms.
Hansel DE, Rahman A, House M, Ashfaq R, Berg K, Yeo CJ, Maitra A.
Clin Cancer Res. 2004 Sep 15;10(18 Pt 1):6152-8.
PMID 15448002
Identification of the autophosphorylation sites and characterization of their effects in the protein kinase DYRK1A.
Himpel S, Panzer P, Eirmbter K, Czajkowska H, Sayed M, Packman LC, Blundell T, Kentrup H, Grotzinger J, Joost HG, Becker W.
Biochem J. 2001 Nov 1;359(Pt 3):497-505.
PMID 11672423
Specificity determinants of substrate recognition by the protein kinase DYRK1A.
Himpel S, Tegge W, Frank R, Leder S, Joost HG, Becker W.
J Biol Chem. 2000 Jan 28;275(4):2431-8.
PMID 10644696
DYRK1A enhances the mitogen-activated protein kinase cascade in PC12 cells by forming a complex with Ras, B-Raf, and MEK1.
Kelly PA, Rahmani Z.
Mol Biol Cell. 2005 Aug;16(8):3562-73. Epub 2005 May 25.
PMID 15917294
Dyrk, a dual specificity protein kinase with unique structural features whose activity is dependent on tyrosine residues between subdomains VII and VIII.
Kentrup H, Becker W, Heukelbach J, Wilmes A, Schurmann A, Huppertz C, Kainulainen H, Joost HG.
J Biol Chem. 1996 Feb 16;271(7):3488-95.
PMID 8631952
A repressor complex, AP4 transcription factor and geminin, negatively regulates expression of target genes in nonneuronal cells.
Kim MY, Jeong BC, Lee JH, Kee HJ, Kook H, Kim NS, Kim YH, Kim JK, Ahn KY, Kim KK.
Proc Natl Acad Sci U S A. 2006 Aug 29;103(35):13074-9. Epub 2006 Aug 21.
PMID 16924111
Adenovirus type 5 E1A and E6 proteins of low-risk cutaneous beta-human papillomaviruses suppress cell transformation through interaction with FOXK1/K2 transcription factors.
Komorek J, Kuppuswamy M, Subramanian T, Vijayalingam S, Lomonosova E, Zhao LJ, Mymryk JS, Schmitt K, Chinnadurai G.
J Virol. 2010 Mar;84(6):2719-31. Epub 2010 Jan 6.
PMID 20053746
DYRK1A is a novel negative regulator of cardiomyocyte hypertrophy.
Kuhn C, Frank D, Will R, Jaschinski C, Frauen R, Katus HA, Frey N.
J Biol Chem. 2009 Jun 19;284(25):17320-7. Epub 2009 Apr 16.
PMID 19372220
DYRK1A and glycogen synthase kinase 3beta, a dual-kinase mechanism directing proteasomal degradation of CRY2 for circadian timekeeping.
Kurabayashi N, Hirota T, Sakai M, Sanada K, Fukada Y.
Mol Cell Biol. 2010 Apr;30(7):1757-68. Epub 2010 Feb 1.
PMID 20123978
The protein kinase DYRK1A regulates caspase-9-mediated apoptosis during retina development.
Laguna A, Aranda S, Barallobre MJ, Barhoum R, Fernandez E, Fotaki V, Delabar JM, de la Luna S, de la Villa P, Arbones ML.
Dev Cell. 2008 Dec;15(6):841-53.
PMID 19081073
Negative feedback Inhibition of NFATc1 by DYRK1A regulates bone homeostasis.
Lee Y, Ha J, Kim HJ, Kim YS, Chang EJ, Song WJ, Kim HH.
J Biol Chem. 2009 Nov 27;284(48):33343-51. Epub 2009 Oct 2.
PMID 19801542
DYRK1A interacts with the REST/NRSF-SWI/SNF chromatin remodelling complex to deregulate gene clusters involved in the neuronal phenotypic traits of Down syndrome.
Lepagnol-Bestel AM, Zvara A, Maussion G, Quignon F, Ngimbous B, Ramoz N, Imbeaud S, Loe-Mie Y, Benihoud K, Agier N, Salin PA, Cardona A, Khung-Savatovsky S, Kallunki P, Delabar JM, Puskas LG, Delacroix H, Aggerbeck L, Delezoide AL, Delattre O, Gorwood P, Moalic JM, Simonneau M.
Hum Mol Genet. 2009 Apr 15;18(8):1405-14. Epub 2009 Feb 12.
PMID 19218269
DYRK1A stabilizes HPV16E7 oncoprotein through phosphorylation of the threonine 5 and threonine 7 residues.
Liang YJ, Chang HS, Wang CY, Yu WC.
Int J Biochem Cell Biol. 2008;40(11):2431-41. Epub 2008 Apr 6.
PMID 18468476
Activation-loop autophosphorylation is mediated by a novel transitional intermediate form of DYRKs.
Lochhead PA, Sibbet G, Morrice N, Cleghon V.
Cell. 2005 Jun 17;121(6):925-36.
PMID 15960979
Characterization of the human DYRK1A promoter and its regulation by the transcription factor E2F1.
Maenz B, Hekerman P, Vela EM, Galceran J, Becker W.
BMC Mol Biol. 2008 Mar 26;9:30.
PMID 18366763
Regulation of Gli1 transcriptional activity in the nucleus by Dyrk1.
Mao J, Maye P, Kogerman P, Tejedor FJ, Toftgard R, Xie W, Wu G, Wu D.
J Biol Chem. 2002 Sep 20;277(38):35156-61. Epub 2002 Jul 22.
PMID 12138125
Dyrk1A expression pattern supports specific roles of this kinase in the adult central nervous system.
Marti E, Altafaj X, Dierssen M, de la Luna S, Fotaki V, Alvarez M, Perez-Riba M, Ferrer I, Estivill X.
Brain Res. 2003 Feb 28;964(2):250-63.
PMID 12576186
Possible narrowed assignment of the loci of monosomy 21-associated microcephaly and intrauterine growth retardation to a 1.2-Mb segment at 21q22.2.
Matsumoto N, Ohashi H, Tsukahara M, Kim KC, Soeda E, Niikawa N.
Am J Hum Genet. 1997 Apr;60(4):997-9.
PMID 9106547
Truncation of the Down syndrome candidate gene DYRK1A in two unrelated patients with microcephaly.
Moller RS, Kubart S, Hoeltzenbein M, Heye B, Vogel I, Hansen CP, Menzel C, Ullmann R, Tommerup N, Ropers HH, Tumer Z, Kalscheuer VM.
Am J Hum Genet. 2008 May;82(5):1165-70. Epub 2008 Apr 10.
PMID 18405873
Dyrk1A binds to multiple endocytic proteins required for formation of clathrin-coated vesicles.
Murakami N, Bolton D, Hwang YW.
Biochemistry. 2009 Oct 6;48(39):9297-305.
PMID 19722700
Dyrk1A phosphorylates p53 and inhibits proliferation of embryonic neuronal cells.
Park J, Oh Y, Yoo L, Jung MS, Song WJ, Lee SH, Seo H, Chung KC.
J Biol Chem. 2010 Oct 8;285(41):31895-906. Epub 2010 Aug 9.
PMID 20696760
Function and regulation of Dyrk1A: towards understanding Down syndrome.
Park J, Song WJ, Chung KC.
Cell Mol Life Sci. 2009b Oct;66(20):3235-40. Epub 2009 Aug 14. (REVIEW)
PMID 19685005
Down's syndrome patients are less likely to develop cancer.
Pussegoda KA.
Clin Genet. 2010 Jul;78(1):35-7.
PMID 20597922
Hyperhomocysteinemia-induced Dyrk1a downregulation results in cardiomyocyte hypertrophy in rats.
Raaf L, Noll C, Cherifi M, Benazzoug Y, Delabar JM, Janel N.
Int J Cardiol. 2009 Nov 9. [Epub ahead of print]
PMID 19906449
Nonprimed and DYRK1A-primed GSK3 beta-phosphorylation sites on MAP1B regulate microtubule dynamics in growing axons.
Scales TM, Lin S, Kraus M, Goold RG, Gordon-Weeks PR.
J Cell Sci. 2009 Jul 15;122(Pt 14):2424-35. Epub 2009 Jun 23.
PMID 19549690
DYRK1A phosphorylates caspase 9 at an inhibitory site and is potently inhibited in human cells by harmine.
Seifert A, Allan LA, Clarke PR.
FEBS J. 2008 Dec;275(24):6268-80. Epub 2008 Nov 7.
PMID 19016842
Increased dosage of Dyrk1A alters alternative splicing factor (ASF)-regulated alternative splicing of tau in Down syndrome.
Shi J, Zhang T, Zhou C, Chohan MO, Gu X, Wegiel J, Zhou J, Hwang YW, Iqbal K, Grundke-Iqbal I, Gong CX, Liu F.
J Biol Chem. 2008 Oct 17;283(42):28660-9. Epub 2008 Jul 24.
PMID 18658135
Cloning of a human homolog of the Drosophila minibrain/rat Dyrk gene from "the Down syndrome critical region" of chromosome 21.
Shindoh N, Kudoh J, Maeda H, Yamaki A, Minoshima S, Shimizu Y, Shimizu N.
Biochem Biophys Res Commun. 1996 Aug 5;225(1):92-9.
PMID 8769099
Dyrk1A potentiates steroid hormone-induced transcription via the chromatin remodeling factor Arip4.
Sitz JH, Tigges M, Baumgartel K, Khaspekov LG, Lutz B.
Mol Cell Biol. 2004 Jul;24(13):5821-34.
PMID 15199138
Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family protein kinases.
Skurat AV, Dietrich AD.
J Biol Chem. 2004 Jan 23;279(4):2490-8. Epub 2003 Oct 30.
PMID 14593110
Functional screening of 2 Mb of human chromosome 21q22.2 in transgenic mice implicates minibrain in learning defects associated with Down syndrome.
Smith DJ, Stevens ME, Sudanagunta SP, Bronson RT, Makhinson M, Watabe AM, O'Dell TJ, Fung J, Weier HU, Cheng JF, Rubin EM.
Nat Genet. 1997 May;16(1):28-36.
PMID 9140392
Isolation of human and murine homologues of the Drosophila minibrain gene: human homologue maps to 21q22.2 in the Down syndrome "critical region".
Song WJ, Sternberg LR, Kasten-Sportes C, Keuren ML, Chung SH, Slack AC, Miller DE, Glover TW, Chiang PW, Lou L, Kurnit DM.
Genomics. 1996 Dec 15;38(3):331-9.
PMID 8975710.
minibrain: a new protein kinase family involved in postembryonic neurogenesis in Drosophila.
Tejedor F, Zhu XR, Kaltenbach E, Ackermann A, Baumann A, Canal I, Heisenberg M, Fischbach KF, Pongs O.
Neuron. 1995 Feb;14(2):287-301.
PMID 7857639
Identification of two novel 5' noncoding exons in human MNB/DYRK gene and alternatively spliced transcripts.
Wang J, Kudoh J, Shintani A, Minoshima S, Shimizu N.
Biochem Biophys Res Commun. 1998 Sep 29;250(3):704-10.
PMID 9784410
The role of overexpressed DYRK1A protein in the early onset of neurofibrillary degeneration in Down syndrome.
Wegiel J, Dowjat K, Kaczmarski W, Kuchna I, Nowicki K, Frackowiak J, Mazur Kolecka B, Wegiel J, Silverman WP, Reisberg B, Deleon M, Wisniewski T, Gong CX, Liu F, Adayev T, Chen-Hwang MC, Hwang YW.
Acta Neuropathol. 2008 Oct;116(4):391-407. Epub 2008 Aug 12.
PMID 18696092
Cell type- and brain structure-specific patterns of distribution of minibrain kinase in human brain.
Wegiel J, Kuchna I, Nowicki K, Frackowiak J, Dowjat K, Silverman WP, Reisberg B, DeLeon M, Wisniewski T, Adayev T, Chen-Hwang MC, Hwang YW.
Brain Res. 2004 Jun 4;1010(1-2):69-80.
PMID 15126119
The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bepsilon at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase.
Woods YL, Cohen P, Becker W, Jakes R, Goedert M, Wang X, Proud CG.
Biochem J. 2001 May 1;355(Pt 3):609-15.
PMID 11311121.
Dyrk1A overexpression inhibits proliferation and induces premature neuronal differentiation of neural progenitor cells.
Yabut O, Domogauer J, D'Arcangelo G.
J Neurosci. 2010 Mar 17;30(11):4004-14.
PMID 20237271
Protein kinase Dyrk1 activates cAMP response element-binding protein during neuronal differentiation in hippocampal progenitor cells.
Yang EJ, Ahn YS, Chung KC.
J Biol Chem. 2001 Oct 26;276(43):39819-24. Epub 2001 Aug 22.
PMID 11518709
Interaction of the E1A oncoprotein with Yak1p, a novel regulator of yeast pseudohyphal differentiation, and related mammalian kinases.
Zhang Z, Smith MM, Mymryk JS.
Mol Biol Cell. 2001 Mar;12(3):699-710.
PMID 11251081
The protein kinase DYRK1A phosphorylates the splicing factor SF3b1/SAP155 at Thr434, a novel in vivo phosphorylation site.
de Graaf K, Czajkowska H, Rottmann S, Packman LC, Lilischkis R, Luscher B, Becker W.
BMC Biochem. 2006 Mar 2;7:7.
PMID 16512921
Differentially expressed genes identified in human melanoma cell lines with different metastatic behaviour using high density oligonucleotide arrays.
de Wit NJ, Burtscher HJ, Weidle UH, Ruiter DJ, van Muijen GN.
Melanoma Res. 2002 Feb;12(1):57-69.
PMID 11828259
DYRK1 is a co-activator of FKHR (FOXO1a)-dependent glucose-6-phosphatase gene expression.
von Groote-Bidlingmaier F, Schmoll D, Orth HM, Joost HG, Becker W, Barthel A.
Biochem Biophys Res Commun. 2003 Jan 17;300(3):764-9.
PMID 12507516

7. Citation

This paper should be referenced as such :
Arbonés, ML ; de, la Luna S
DYRK1A (dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 1A)
Atlas Genet Cytogenet Oncol Haematol. 2011;15(5):443-449.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://atlasgeneticsoncology.usal.es/classic/Genes/DYRK1AID43234ch21q22.html

8. Other Leukemias implicated (Data extracted from papers in the Atlas) [ 2 ]

9. External links

HGNC (Hugo)DYRK1A   3091
Entrez_Gene (NCBI)DYRK1A  1859  dual specificity tyrosine phosphorylation regulated kinase 1A
AliasesDYRK; DYRK1; HP86; MNB; 
GeneCards (Weizmann)DYRK1A
Ensembl hg19 (Hinxton)ENSG00000157540 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000157540 [Gene_View] &nbspENSG00000157540 [Sequence]  chr21:37420299-37515376 [Contig_View]  DYRK1A [Vega]
ICGC DataPortalENSG00000157540
Genatlas (Paris)DYRK1A
SOURCE (Princeton)DYRK1A
Genetics Home Reference (NIH)DYRK1A
Genomic and cartography
GoldenPath hg38 (UCSC)DYRK1A  -     chr21:37420299-37515376 +  21q22.13   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)DYRK1A  -     21q22.13   [Description]    (hg19-Feb_2009)
EnsemblDYRK1A - 21q22.13 [CytoView hg19]  DYRK1A - 21q22.13 [CytoView hg38]
Mapping of homologs : NCBIDYRK1A [Mapview hg19]  DYRK1A [Mapview hg38]
OMIM600855   614104   
Gene and transcription
Genbank (Entrez)AB015282 AB015283 AB015284 AF108830 AJ001870
RefSeq transcript (Entrez)NM_001347721 NM_001347722 NM_001347723 NM_001396 NM_101395 NM_130436 NM_130437 NM_130438
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)DYRK1A
Cluster EST : UnigeneHs.368240 [ NCBI ]
CGAP (NCI)Hs.368240
Alternative Splicing GalleryENSG00000157540
Gene ExpressionDYRK1A [ NCBI-GEO ]   DYRK1A [ EBI - ARRAY_EXPRESS ]   DYRK1A [ SEEK ]   DYRK1A [ MEM ]
Gene Expression Viewer (FireBrowse)DYRK1A [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets] &nbsp [Normal Tissue Atlas] &nbsp[carcinoma Classsification] &nbsp[NCI60]
GenevestigatorExpression in : [tissues] &nbsp[cell-lines] &nbsp[cancer] &nbsp[perturbations] &nbsp
BioGPS (Tissue expression)1859
GTEX Portal (Tissue expression)DYRK1A
Human Protein AtlasENSG00000157540-DYRK1A [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ13627   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ13627  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ13627
Splice isoforms : SwissVarQ13627
Domaine pattern : Prosite (Expaxy)PROTEIN_KINASE_ATP (PS00107)    PROTEIN_KINASE_DOM (PS50011)    PROTEIN_KINASE_ST (PS00108)   
Domains : Interpro (EBI)DYRK1A/MNB    Kinase-like_dom_sf    Prot_kinase_dom    Protein_kinase_ATP_BS    Ser/Thr_kinase_AS   
Domain families : Pfam (Sanger)Pkinase (PF00069)   
Domain families : Pfam (NCBI)pfam00069   
Domain families : Smart (EMBL)S_TKc (SM00220)  
Conserved Domain (NCBI)DYRK1A
DMDM Disease mutations1859
Blocks (Seattle)DYRK1A
PDB (RSDB)2VX3    2WO6    3ANQ    3ANR    4AZE    4MQ1    4MQ2    4NCT    4YLJ    4YLK    4YLL    4YU2    5A3X    5A4E    5A4L    5A4Q    5A4T    5A54    5AIK   
PDB Europe2VX3    2WO6    3ANQ    3ANR    4AZE    4MQ1    4MQ2    4NCT    4YLJ    4YLK    4YLL    4YU2    5A3X    5A4E    5A4L    5A4Q    5A4T    5A54    5AIK   
PDB (PDBSum)2VX3    2WO6    3ANQ    3ANR    4AZE    4MQ1    4MQ2    4NCT    4YLJ    4YLK    4YLL    4YU2    5A3X    5A4E    5A4L    5A4Q    5A4T    5A54    5AIK   
PDB (IMB)2VX3    2WO6    3ANQ    3ANR    4AZE    4MQ1    4MQ2    4NCT    4YLJ    4YLK    4YLL    4YU2    5A3X    5A4E    5A4L    5A4Q    5A4T    5A54    5AIK   
Structural Biology KnowledgeBase2VX3    2WO6    3ANQ    3ANR    4AZE    4MQ1    4MQ2    4NCT    4YLJ    4YLK    4YLL    4YU2    5A3X    5A4E    5A4L    5A4Q    5A4T    5A54    5AIK   
SCOP (Structural Classification of Proteins)2VX3    2WO6    3ANQ    3ANR    4AZE    4MQ1    4MQ2    4NCT    4YLJ    4YLK    4YLL    4YU2    5A3X    5A4E    5A4L    5A4Q    5A4T    5A54    5AIK   
CATH (Classification of proteins structures)2VX3    2WO6    3ANQ    3ANR    4AZE    4MQ1    4MQ2    4NCT    4YLJ    4YLK    4YLL    4YU2    5A3X    5A4E    5A4L    5A4Q    5A4T    5A54    5AIK   
Human Protein Atlas [tissue]ENSG00000157540-DYRK1A [tissue]
Peptide AtlasQ13627
IPIIPI00014344   IPI00219250   IPI00219251   IPI00219252   IPI00182717   IPI00941492   IPI00796059   IPI00796684   
Protein Interaction databases
IntAct (EBI)Q13627
Ontologies - Pathways
Ontology : AmiGOregulation of alternative mRNA splicing, via spliceosome  protein kinase activity  protein serine/threonine kinase activity  protein serine/threonine kinase activity  protein serine/threonine kinase activity  protein serine/threonine/tyrosine kinase activity  protein tyrosine kinase activity  non-membrane spanning protein tyrosine kinase activity  protein binding  ATP binding  nucleus  nucleus  nucleoplasm  cytoplasm  cytoplasm  cytoskeleton  protein phosphorylation  protein phosphorylation  nervous system development  circadian rhythm  viral process  nuclear speck  nuclear speck  peptidyl-serine phosphorylation  peptidyl-serine phosphorylation  peptidyl-threonine phosphorylation  peptidyl-tyrosine phosphorylation  peptidyl-tyrosine phosphorylation  axon  dendrite  negative regulation of microtubule polymerization  positive regulation of RNA splicing  amyloid-beta formation  peptidyl-serine autophosphorylation  peptidyl-tyrosine autophosphorylation  peptidyl-tyrosine autophosphorylation  identical protein binding  negative regulation of DNA damage response, signal transduction by p53 class mediator  protein self-association  protein autophosphorylation  negative regulation of mRNA splicing, via spliceosome  tau protein binding  tau protein binding  tau-protein kinase activity  positive regulation of protein deacetylation  ribonucleoprotein complex  
Ontology : EGO-EBIregulation of alternative mRNA splicing, via spliceosome  protein kinase activity  protein serine/threonine kinase activity  protein serine/threonine kinase activity  protein serine/threonine kinase activity  protein serine/threonine/tyrosine kinase activity  protein tyrosine kinase activity  non-membrane spanning protein tyrosine kinase activity  protein binding  ATP binding  nucleus  nucleus  nucleoplasm  cytoplasm  cytoplasm  cytoskeleton  protein phosphorylation  protein phosphorylation  nervous system development  circadian rhythm  viral process  nuclear speck  nuclear speck  peptidyl-serine phosphorylation  peptidyl-serine phosphorylation  peptidyl-threonine phosphorylation  peptidyl-tyrosine phosphorylation  peptidyl-tyrosine phosphorylation  axon  dendrite  negative regulation of microtubule polymerization  positive regulation of RNA splicing  amyloid-beta formation  peptidyl-serine autophosphorylation  peptidyl-tyrosine autophosphorylation  peptidyl-tyrosine autophosphorylation  identical protein binding  negative regulation of DNA damage response, signal transduction by p53 class mediator  protein self-association  protein autophosphorylation  negative regulation of mRNA splicing, via spliceosome  tau protein binding  tau protein binding  tau-protein kinase activity  positive regulation of protein deacetylation  ribonucleoprotein complex  
REACTOMEQ13627 [protein]
REACTOME PathwaysR-HSA-1538133 [pathway]   
NDEx NetworkDYRK1A
Atlas of Cancer Signalling NetworkDYRK1A
Wikipedia pathwaysDYRK1A
Orthology - Evolution
GeneTree (enSembl)ENSG00000157540
Phylogenetic Trees/Animal Genes : TreeFamDYRK1A
Homologs : HomoloGeneDYRK1A
Homology/Alignments : Family Browser (UCSC)DYRK1A
Gene fusions - Rearrangements
Fusion : MitelmanBRWD1/DYRK1A [21q22.2/21q22.13] &nbsp[t(21;21)(q22;q22)]  
Fusion : MitelmanDYRK1A/BRWD1 [21q22.13/21q22.2] &nbsp[t(21;21)(q22;q22)]  
Fusion : MitelmanDYRK1A/KDM4B [21q22.13/19p13.3] &nbsp[t(19;21)(p13;q22)]  
Fusion : MitelmanDYRK1A/MRPS6 [21q22.13/21q22.11] &nbsp[t(21;21)(q22;q22)]  
Fusion : MitelmanDYRK1A/RUNX1 [21q22.13/21q22.12] &nbsp[t(21;21)(q22;q22)]  
Fusion : MitelmanDYRK1A/TTC3 [21q22.13/21q22.13] &nbsp[t(21;21)(q22;q22)]  
Fusion : MitelmanDYRK1A/ZBTB46 [21q22.13/20q13.33] &nbsp[t(20;21)(q13;q22)]  
Fusion PortalBRWD1 21q22.2 DYRK1A 21q22.13 BRCA
Fusion PortalDYRK1A 21q22.13 BRWD1 21q22.2 BRCA
Fusion PortalDYRK1A 21q22.13 KDM4B 19p13.3 BRCA
Fusion PortalDYRK1A 21q22.13 MRPS6 21q22.11 BRCA
Fusion PortalDYRK1A 21q22.13 RUNX1 21q22.12 HNSC
Fusion PortalDYRK1A 21q22.13 TTC3 21q22.13 LUAD
Fusion PortalDYRK1A 21q22.13 ZBTB46 20q13.33 BRCA
Fusion : QuiverDYRK1A
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerDYRK1A [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)DYRK1A
Exome Variant ServerDYRK1A
ExAC (Exome Aggregation Consortium)ENSG00000157540
GNOMAD BrowserENSG00000157540
Varsome BrowserDYRK1A
Genetic variants : HAPMAP1859
Genomic Variants (DGV)DYRK1A [DGVbeta]
DECIPHERDYRK1A [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisDYRK1A 
ICGC Data PortalDYRK1A 
TCGA Data PortalDYRK1A 
Broad Tumor PortalDYRK1A
OASIS PortalDYRK1A [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICDYRK1A  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDDYRK1A
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch DYRK1A
DgiDB (Drug Gene Interaction Database)DYRK1A
DoCM (Curated mutations)DYRK1A (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)DYRK1A (select a term)
NCG5 (London)DYRK1A
Cancer3DDYRK1A(select the gene name)
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
OMIM600855    614104   
Genetic Testing Registry DYRK1A
NextProtQ13627 [Medical]
Target ValidationDYRK1A
Huge Navigator DYRK1A [HugePedia]
snp3D : Map Gene to Disease1859
ClinGenDYRK1A (curated)
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD1859
Chemical/Pharm GKB GenePA27545
Clinical trialDYRK1A
canSAR (ICR)DYRK1A (select the gene name)
DataMed IndexDYRK1A
Other databaseSignaling Gateway
Other databasePhosphosite
PubMed175 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

Search in all EBI   NCBI

© Atlas of Genetics and Cytogenetics in Oncology and Haematology
indexed on : Thu Jan 17 18:53:38 CET 2019

For comments and suggestions or contributions, please contact us atlasgeneticsoncology@usal.es.