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Q13627 (DYR1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity tyrosine-phosphorylation-regulated kinase 1A

EC=2.7.12.1
Alternative name(s):
Dual specificity YAK1-related kinase
HP86
Protein kinase minibrain homolog
Short name=MNBH
Short name=hMNB
Gene names
Name:DYRK1A
Synonyms:DYRK, MNB, MNBH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length763 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Phosphorylates serine, threonine and tyrosine residues in its sequence and in exogenous substrates such as CRY2, FOXO1, SRSF6 and SIRT1. Ref.3 Ref.15 Ref.18

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.15 Ref.16 Ref.17 Ref.18

Enzyme regulation

Inhibited by RANBP9. Inhibited by harmine, leucettamine B and leucettine L41. Ref.7 Ref.16

Subunit structure

Interacts RAD54L2/ARIP4. Interacts with CRY2 By similarity. Interacts with RANBP9. Interacts with WDR68. Interacts with SRSF6. Ref.7 Ref.8 Ref.14

Subcellular location

Nucleus speckle.

Tissue specificity

Ubiquitous. Highest levels in skeletal muscle, testis, fetal lung and fetal kidney. Ref.1 Ref.2 Ref.3 Ref.5

Developmental stage

Expressed in the developing central nervous system. Overexpressed 1.5-fold in fetal Down syndrome brain. Ref.3

Domain

The polyhistidine repeats act as targeting signals to nuclear speckles (Ref.11).

Post-translational modification

Autophosphorylated on numerous tyrosine residues. Can also autophosphorylate on serine and threonine residues (in vitro). Ref.18

Involvement in disease

Mental retardation, autosomal dominant 7 (MRD7) [MIM:614104]: A disease characterized by primary microcephaly, severe mental retardation without speech, anxious autistic behavior, and dysmorphic features, including bitemporal narrowing, deep-set eyes, large simple ears, and a pointed nasal tip. Mental retardation is characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseMental retardation
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcircadian rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from sequence or structural similarity PubMed 20736167. Source: BHF-UCL

nervous system development

Traceable author statement Ref.3. Source: ProtInc

peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

peptidyl-threonine phosphorylation

Inferred from sequence or structural similarity PubMed 20736167. Source: BHF-UCL

peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein deacetylation

Inferred from sequence or structural similarity PubMed 20736167. Source: BHF-UCL

protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentnuclear speck

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

ribonucleoprotein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from direct assay PubMed 9748265. Source: MGI

protein binding

Inferred from physical interaction PubMed 17229891. Source: IntAct

protein kinase activity

Traceable author statement Ref.3Ref.1. Source: ProtInc

protein self-association

Inferred from sequence or structural similarity. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein serine/threonine/tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

tau protein binding

Inferred from sequence or structural similarity PubMed 20736167. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform Long (identifier: Q13627-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1 (identifier: Q13627-2)

The sequence of this isoform differs from the canonical sequence as follows:
     70-78: Missing.
Isoform 2 (identifier: Q13627-3)

The sequence of this isoform differs from the canonical sequence as follows:
     516-529: GGSSGTSNSGRARS → GASAISCSSWLVRH
     530-763: Missing.
Isoform 3 (identifier: Q13627-4)

The sequence of this isoform differs from the canonical sequence as follows:
     516-540: GGSSGTSNSGRARSDPTHQHRHSGG → VEQHWMPGAFRMTVSFTLEVHDVPV
     541-763: Missing.
Isoform 4 (identifier: Q13627-5)

The sequence of this isoform differs from the canonical sequence as follows:
     559-584: RQQFPAPLGWSGTEAPTQVTVETHPV → SSHVVHLLVSPAILRWSSTGCQVPLE
     585-763: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 763763Dual specificity tyrosine-phosphorylation-regulated kinase 1A
PRO_0000085931

Regions

Domain159 – 479321Protein kinase
Nucleotide binding165 – 1739ATP Probable
Nucleotide binding238 – 2414ATP Probable
Motif117 – 13418Bipartite nuclear localization signal Potential
Compositional bias509 – 5157Poly-Ser
Compositional bias599 – 6024Poly-His
Compositional bias607 – 61913Poly-His
Compositional bias656 – 67217Ser/Thr-rich
Compositional bias664 – 6718Poly-Ser

Sites

Active site2871Proton acceptor Probable
Binding site1881ATP Probable

Amino acid modifications

Modified residue1111Phosphotyrosine; by autocatalysis Ref.18
Modified residue1401Phosphotyrosine; by autocatalysis Ref.18
Modified residue1451Phosphotyrosine Ref.12
Modified residue1591Phosphotyrosine; by autocatalysis Ref.18
Modified residue1771Phosphotyrosine; by autocatalysis Ref.18
Modified residue2191Phosphotyrosine; by autocatalysis By similarity
Modified residue3101Phosphoserine; by autocatalysis Ref.18
Modified residue3191Phosphotyrosine; by autocatalysis Ref.18
Modified residue3211Phosphotyrosine; by autocatalysis Ref.18
Modified residue4021Phosphothreonine; by autocatalysis Ref.18
Modified residue4491Phosphotyrosine; by autocatalysis Ref.18
Modified residue7481Phosphoserine Ref.10
Modified residue7581Phosphoserine Ref.10

Natural variations

Alternative sequence70 – 789Missing in isoform 1.
VSP_004917
Alternative sequence516 – 54025GGSSG…RHSGG → VEQHWMPGAFRMTVSFTLEV HDVPV in isoform 3.
VSP_004920
Alternative sequence516 – 52914GGSSG…GRARS → GASAISCSSWLVRH in isoform 2.
VSP_004918
Alternative sequence530 – 763234Missing in isoform 2.
VSP_004919
Alternative sequence541 – 763223Missing in isoform 3.
VSP_004921
Alternative sequence559 – 58426RQQFP…ETHPV → SSHVVHLLVSPAILRWSSTG CQVPLE in isoform 4.
VSP_004922
Alternative sequence585 – 763179Missing in isoform 4.
VSP_004923
Natural variant4151Y → F. Ref.5
VAR_009395
Natural variant6791A → P. Ref.1 Ref.19
Corresponds to variant rs55720916 [ dbSNP | Ensembl ].
VAR_040453
Natural variant6811Q → H. Ref.5
VAR_009396

Experimental info

Mutagenesis1881K → R: Abolishes kinase activity. Ref.18
Mutagenesis3211Y → F: Mildly reduces kinase activity. Does not abolish autophosphorylation on tyrosine residues. Ref.18
Sequence conflict321G → A in AAC50939. Ref.1
Sequence conflict471N → S in AAC50939. Ref.1
Sequence conflict571S → P in AAC50939. Ref.1
Sequence conflict1231Q → R in AAC50939. Ref.1
Sequence conflict2661A → V in CAA05059. Ref.6
Sequence conflict3571G → R in CAA05059. Ref.6
Sequence conflict3971K → N in AAC50939. Ref.1
Sequence conflict5921A → G in AAC50939. Ref.1

Secondary structure

............................................................... 763
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 7C3A52A3CBB04FB5

FASTA76385,584
        10         20         30         40         50         60 
MHTGGETSAC KPSSVRLAPS FSFHAAGLQM AGQMPHSHQY SDRRQPNISD QQVSALSYSD 

        70         80         90        100        110        120 
QIQQPLTNQV MPDIVMLQRR MPQTFRDPAT APLRKLSVDL IKTYKHINEV YYAKKKRRHQ 

       130        140        150        160        170        180 
QGQGDDSSHK KERKVYNDGY DDDNYDYIVK NGEKWMDRYE IDSLIGKGSF GQVVKAYDRV 

       190        200        210        220        230        240 
EQEWVAIKII KNKKAFLNQA QIEVRLLELM NKHDTEMKYY IVHLKRHFMF RNHLCLVFEM 

       250        260        270        280        290        300 
LSYNLYDLLR NTNFRGVSLN LTRKFAQQMC TALLFLATPE LSIIHCDLKP ENILLCNPKR 

       310        320        330        340        350        360 
SAIKIVDFGS SCQLGQRIYQ YIQSRFYRSP EVLLGMPYDL AIDMWSLGCI LVEMHTGEPL 

       370        380        390        400        410        420 
FSGANEVDQM NKIVEVLGIP PAHILDQAPK ARKFFEKLPD GTWNLKKTKD GKREYKPPGT 

       430        440        450        460        470        480 
RKLHNILGVE TGGPGGRRAG ESGHTVADYL KFKDLILRML DYDPKTRIQP YYALQHSFFK 

       490        500        510        520        530        540 
KTADEGTNTS NSVSTSPAME QSQSSGTTSS TSSSSGGSSG TSNSGRARSD PTHQHRHSGG 

       550        560        570        580        590        600 
HFTAAVQAMD CETHSPQVRQ QFPAPLGWSG TEAPTQVTVE THPVQETTFH VAPQQNALHH 

       610        620        630        640        650        660 
HHGNSSHHHH HHHHHHHHHG QQALGNRTRP RVYNSPTNSS STQDSMEVGH SHHSMTSLSS 

       670        680        690        700        710        720 
STTSSSTSSS STGNQGNQAY QNRPVAANTL DFGQNGAMDV NLTVYSNPRQ ETGIAGHPTY 

       730        740        750        760 
QFSANTGPAH YMTEGHLTMR QGADREESPM TGVCVQQSPV ASS 

« Hide

Isoform 1 [UniParc].

Checksum: 59518E25F1D4FF96
Show »

FASTA75484,556
Isoform 2 [UniParc].

Checksum: F639B3152ACC7750
Show »

FASTA52960,330
Isoform 3 [UniParc].

Checksum: E02CE08DF1AE0AED
Show »

FASTA54061,770
Isoform 4 [UniParc].

Checksum: BA2480B34BAB2878
Show »

FASTA58466,099

References

« Hide 'large scale' references
[1]"Isolation of human and murine homologues of the Drosophila minibrain gene: human homologue maps to 21q22.2 in the Down syndrome 'critical region'."
Song W.J., Sternberg L.R., Kasten-Sportes C., van Keuren M.L., Chung S.H., Slack A.C., Miller D.E., Glover T.W., Chiang P.W., Lou L., Kurnit D.W.
Genomics 38:331-339(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT PRO-679, TISSUE SPECIFICITY.
Tissue: Fetal brain.
[2]"A human homologue of Drosophila minibrain (MNB) is expressed in the neuronal regions affected in Down syndrome and maps to the critical region."
Guimera J., Casas C., Pucharcos C., Solans A., Domenech A., Planas A.M., Ashley J., Lovett M., Estivill X., Pritchard M.A.
Hum. Mol. Genet. 5:1305-1310(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), TISSUE SPECIFICITY, POSSIBLE INVOLVEMENT IN DOWN SYNDROME.
[3]"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. 225:92-99(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Fetal brain.
[4]"Gene identification in 1.6-Mb region of the Down syndrome region on chromosome 21."
Ohira M., Seki N., Nagase T., Suzuki E., Nomura N., Ohara O., Hattori M., Sakaki Y., Eki T., Murakami Y., Saito T., Ichikawa H., Ohki M.
Genome Res. 7:47-58(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Promyelocytic leukemia.
[5]"Human minibrain homologue (MNBH/DYRK1): characterization, alternative splicing, differential tissue expression, and overexpression in Down syndrome."
Guimera J., Casas C., Estivill X., Pritchard M.A.
Genomics 57:407-418(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, POSSIBLE INVOLVEMENT IN DOWN SYNDROME, VARIANTS PHE-415 AND HIS-681, ALTERNATIVE SPLICING.
[6]"Transcriptional map of the 2.5-Mb CBR-ERG region of chromosome 21 involved in Down syndrome."
Dahmane N., Ait-Ghezala G., Gosset P., Chamoun Z., Dufresne-Zacharia M.-C., Lopes C., Rabatel N., Gassanova-Maugenre S., Chettouh Z., Abramowski V., Fayet E., Yaspo M.-L., Korn B., Blouin J.-L., Lehrach H., Poustka A., Antonarakis S.E., Sinet P.-M., Creau N., Delabar J.-M.
Genomics 48:12-23(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 234-380.
Tissue: Fetal brain.
[7]"Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell migration and is negatively regulated by the Met adaptor Ran-binding protein M."
Zou Y., Lim S., Lee K., Deng X., Friedman E.
J. Biol. Chem. 278:49573-49581(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RANBP9, ENZYME REGULATION.
[8]"Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family protein kinases."
Skurat A.V., Dietrich A.D.
J. Biol. Chem. 279:2490-2498(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WDR68.
[9]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-748 AND SER-758, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Genome-wide analysis of histidine repeats reveals their role in the localization of human proteins to the nuclear speckles compartment."
Salichs E., Ledda A., Mularoni L., Alba M.M., de la Luna S.
PLoS Genet. 5:E1000397-E1000397(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: POLY-HISTIDINE REPEATS.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Intragenic deletion in DYRK1A leads to mental retardation and primary microcephaly."
van Bon B.W., Hoischen A., Hehir-Kwa J., de Brouwer A.P., Ruivenkamp C., Gijsbers A.C., Marcelis C.L., de Leeuw N., Veltman J.A., Brunner H.G., de Vries B.B.
Clin. Genet. 79:296-299(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MRD7.
[14]"Dual-specificity tyrosine phosphorylation-regulated kinase 1A (Dyrk1A) modulates serine/arginine-rich protein 55 (SRp55)-promoted Tau exon 10 inclusion."
Yin X., Jin N., Gu J., Shi J., Zhou J., Gong C.X., Iqbal K., Grundke-Iqbal I., Liu F.
J. Biol. Chem. 287:30497-30506(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SRSF6.
[15]"Development of a novel selective inhibitor of the Down syndrome-related kinase Dyrk1A."
Ogawa Y., Nonaka Y., Goto T., Ohnishi E., Hiramatsu T., Kii I., Yoshida M., Ikura T., Onogi H., Shibuya H., Hosoya T., Ito N., Hagiwara M.
Nat. Commun. 1:86-86(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 126-490 IN COMPLEXES WITH THE SYNTHETIC INHIBITORS HARMINE AND INDY, CATALYTIC ACTIVITY, FUNCTION.
[16]"Selectivity, cocrystal structures, and neuroprotective properties of leucettines, a family of protein kinase inhibitors derived from the marine sponge alkaloid leucettamine B."
Tahtouh T., Elkins J.M., Filippakopoulos P., Soundararajan M., Burgy G., Durieu E., Cochet C., Schmid R.S., Lo D.C., Delhommel F., Oberholzer A.E., Pearl L.H., Carreaux F., Bazureau J.P., Knapp S., Meijer L.
J. Med. Chem. 55:9312-9330(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 128-485, CATALYTIC ACTIVITY, ENZYME REGULATION.
[17]"Pyrido[2,3-d]pyrimidines: discovery and preliminary SAR of a novel series of DYRK1B and DYRK1A inhibitors."
Anderson K., Chen Y., Chen Z., Dominique R., Glenn K., He Y., Janson C., Luk K.C., Lukacs C., Polonskaia A., Qiao Q., Railkar A., Rossman P., Sun H., Xiang Q., Vilenchik M., Wovkulich P., Zhang X.
Bioorg. Med. Chem. Lett. 23:6610-6615(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 127-485 IN COMPLEX WITH SYNTHETIC INHIBITOR, CATALYTIC ACTIVITY.
[18]"Structures of Down syndrome kinases, DYRKs, reveal mechanisms of kinase activation and substrate recognition."
Soundararajan M., Roos A.K., Savitsky P., Filippakopoulos P., Kettenbach A.N., Olsen J.V., Gerber S.A., Eswaran J., Knapp S., Elkins J.M.
Structure 21:986-996(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 127-485 IN COMPLEXES WITH PEPTIDE SUBSTRATE AND INHIBITOR DJM2005, CATALYTIC ACTIVITY, FUNCTION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-188 AND TYR-321, PHOSPHORYLATION AT TYR-111; TYR-140; TYR-159; TYR-177; SER-310; TYR-319; TYR-321; THR-402 AND TYR-449, ACTIVE SITE, IDENTIFICATION BY MASS SPECTROMETRY.
[19]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-679.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U58496 mRNA. Translation: AAC50939.1.
U52373 mRNA. Translation: AAB18639.1.
D85759 mRNA. Translation: BAA12866.1.
D86550 mRNA. Translation: BAA13110.1.
AF108830 mRNA. Translation: AAD31169.1.
AJ001870 mRNA. Translation: CAA05059.1.
CCDSCCDS13653.1. [Q13627-2]
CCDS13654.1. [Q13627-3]
CCDS42925.1. [Q13627-1]
CCDS42926.1. [Q13627-5]
PIRJC4898.
RefSeqNP_001387.2. NM_001396.3. [Q13627-1]
NP_567824.1. NM_101395.2. [Q13627-5]
NP_569120.1. NM_130436.2. [Q13627-2]
NP_569122.1. NM_130438.2. [Q13627-3]
XP_006724039.1. XM_006723976.1. [Q13627-1]
XP_006724040.1. XM_006723977.1. [Q13627-1]
XP_006724041.1. XM_006723978.1. [Q13627-1]
XP_006724042.1. XM_006723979.1. [Q13627-2]
UniGeneHs.368240.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VX3X-ray2.40A/B/C/D127-485[»]
2WO6X-ray2.50A/B127-485[»]
3ANQX-ray2.60A/B/C/D126-490[»]
3ANRX-ray2.60A/B/C/D126-490[»]
4AZEX-ray3.15A/B/C128-485[»]
4MQ1X-ray2.35A/B/C/D127-485[»]
4MQ2X-ray2.80A/B/C/D127-485[»]
ProteinModelPortalQ13627.
SMRQ13627. Positions 148-480.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108192. 55 interactions.
DIPDIP-39750N.
IntActQ13627. 32 interactions.
MINTMINT-1205413.
STRING9606.ENSP00000381932.

Chemistry

BindingDBQ13627.
ChEMBLCHEMBL2292.
GuidetoPHARMACOLOGY2009.

PTM databases

PhosphoSiteQ13627.

Polymorphism databases

DMDM3219996.

Proteomic databases

MaxQBQ13627.
PaxDbQ13627.
PRIDEQ13627.

Protocols and materials databases

DNASU1859.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338785; ENSP00000342690; ENSG00000157540. [Q13627-5]
ENST00000339659; ENSP00000340373; ENSG00000157540. [Q13627-2]
ENST00000398956; ENSP00000381929; ENSG00000157540. [Q13627-3]
ENST00000398960; ENSP00000381932; ENSG00000157540. [Q13627-1]
ENST00000451934; ENSP00000416089; ENSG00000157540. [Q13627-5]
GeneID1859.
KEGGhsa:1859.
UCSCuc002ywi.3. human. [Q13627-5]
uc002ywj.3. human. [Q13627-2]
uc002ywk.3. human. [Q13627-1]
uc002ywm.3. human. [Q13627-3]

Organism-specific databases

CTD1859.
GeneCardsGC21P038739.
HGNCHGNC:3091. DYRK1A.
HPAHPA015323.
HPA015810.
MIM600855. gene.
614104. phenotype.
neXtProtNX_Q13627.
Orphanet178469. Autosomal dominant nonsyndromic intellectual disability.
PharmGKBPA27545.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000220863.
HOVERGENHBG051425.
InParanoidQ13627.
KOK08825.
OMALTNQRRM.
OrthoDBEOG77127N.
PhylomeDBQ13627.
TreeFamTF314624.

Enzyme and pathway databases

BRENDA2.7.12.1. 2681.
ReactomeREACT_115566. Cell Cycle.
SignaLinkQ13627.

Gene expression databases

ArrayExpressQ13627.
BgeeQ13627.
CleanExHS_DYRK1A.
GenevestigatorQ13627.

Family and domain databases

InterProIPR028318. DYRK1A.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR24058:SF28. PTHR24058:SF28. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDYRK1A. human.
EvolutionaryTraceQ13627.
GeneWikiDYRK1A.
GenomeRNAi1859.
NextBio7615.
PROQ13627.
SOURCESearch...

Entry information

Entry nameDYR1A_HUMAN
AccessionPrimary (citable) accession number: Q13627
Secondary accession number(s): O60769 expand/collapse secondary AC list , Q92582, Q92810, Q9UNM5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1998
Last modified: July 9, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM