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UniProtKB/Swiss-Prot entry Q13627


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DYR1A_HUMAN
Primary accession number Q13627
Secondary accession numbers O60769 Q92582 Q92810 Q9UNM5
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on July 15, 1998 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 93)
Name and origin of the protein
Protein name Dual specificity tyrosine-phosphorylation-regulated kinase 1A
Synonyms EC 2.7.12.1
Protein kinase minibrain homolog
MNBH
hMNB
HP86
Dual specificity YAK1-related kinase
Gene name
Name: DYRK1A
Synonyms: DYRK, MNB, MNBH
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT PRO-679, AND TISSUE SPECIFICITY.
TISSUE=Fetal brain;
DOI=10.1006/geno.1996.0636; PubMed=8975710 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Isolation of human and murine homologues of the Drosophila minibrain gene: human homologue maps to 21q22.2 in the Down syndrome 'critical region'.";
Genomics 38:331-339(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), TISSUE SPECIFICITY, AND POSSIBLE INVOLVEMENT IN DOWN SYNDROME.
DOI=10.1093/hmg/5.9.1305; PubMed=8872470 [NCBI, ExPASy, EBI, Israel, Japan]
Guimera J., Casas C., Pucharcos C., Solans A., Domenech A., Planas A.M., Ashley J., Lovett M., Estivill X., Pritchard M.A.;
"A human homologue of Drosophila minibrain (MNB) is expressed in the neuronal regions affected in Down syndrome and maps to the critical region.";
Hum. Mol. Genet. 5:1305-1310(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
TISSUE=Fetal brain;
DOI=10.1006/bbrc.1996.1135; PubMed=8769099 [NCBI, ExPASy, EBI, Israel, Japan]
Shindoh N., Kudoh J., Maeda H., Yamaki A., Minoshima S., Shimizu Y., Shimizu N.;
"Cloning of a human homolog of the Drosophila minibrain/rat Dyrk gene from 'the Down syndrome critical region' of chromosome 21.";
Biochem. Biophys. Res. Commun. 225:92-99(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Promyelocytic leukemia;
PubMed=9037601 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Gene identification in 1.6-Mb region of the Down syndrome region on chromosome 21.";
Genome Res. 7:47-58(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, POSSIBLE INVOLVEMENT IN DOWN SYNDROME, VARIANTS PHE-415 AND HIS-681, AND ALTERNATIVE SPLICING.
DOI=10.1006/geno.1999.5775; PubMed=10329007 [NCBI, ExPASy, EBI, Israel, Japan]
Guimera J., Casas C., Estivill X., Pritchard M.A.;
"Human minibrain homologue (MNBH/DYRK1): characterization, alternative splicing, differential tissue expression, and overexpression in Down syndrome.";
Genomics 57:407-418(1999).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 234-380.
TISSUE=Fetal brain;
DOI=10.1006/geno.1997.5146; PubMed=9503011 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Transcriptional map of the 2.5-Mb CBR-ERG region of chromosome 21 involved in Down syndrome.";
Genomics 48:12-23(1998).
[7]
INTERACTION WITH RANBP9, AND ENZYME REGULATION.
DOI=10.1074/jbc.M307556200; PubMed=14500717 [NCBI, ExPASy, EBI, Israel, Japan]
Zou Y., Lim S., Lee K., Deng X., Friedman E.;
"Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell migration and is negatively regulated by the Met adaptor Ran-binding protein M.";
J. Biol. Chem. 278:49573-49581(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145 AND TYR-321, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan]
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.;
"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry.";
Mol. Cell. Proteomics 6:537-547(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321; SER-748 AND SER-758, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
VARIANT [LARGE SCALE ANALYSIS] PRO-679.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U58496; AAC50939.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U52373; AAB18639.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D85759; BAA12866.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D86550; BAA13110.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF108830; AAD31169.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ001870; CAA05059.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC4898; JC4898.
RefSeq NP_001387.2; -.
NP_567824.1; -.
NP_569120.1; -.
NP_569121.1; -.
NP_569122.1; -.
UniGene Hs.705437
3D structure databases
PDB
2VX3; X-ray; 2.40 A; A/B/C/D=127-485.[ExPASy / RCSB / EBI]
PDBsum 2VX3; -.
ModBase Q13627.
Protein-protein interaction databases
IntAct Q13627; 5.
PTM databases
PhosphoSite Q13627; -.
Organism-specific databases
GeneCards GC21P037661; -.
H-InvDB HIX0040839; -.
HGNC HGNC:3091; DYRK1A.
GenAtlas DYRK1A.
HPA HPA015323; -.
HPA015810; -.
MIM 600855; gene. [NCBI / EBI]
PharmGKB PA27545; -.
GeneCards Q13627.
Gene expression databases
ArrayExpress Q13627; -.
CleanEx HS_DYRK1A; -.
GermOnline ENSG00000157540; Homo sapiens.
Ontologies
GO
GO:0016607; Cellular component: nuclear speck (inferred from sequence or structural similarity from UniProtKB).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004715; Molecular function: non-membrane spanning protein tyrosine kinase activity (inferred from direct assay from MGI).
GO:0043621; Molecular function: protein self-association (inferred from sequence or structural similarity from UniProtKB).
GO:0004674; Molecular function: protein serine/threonine kinase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0007399; Biological process: nervous system development (traceable author statement from ProtInc).
GO:0018108; Biological process: peptidyl-tyrosine phosphorylation (inferred from sequence or structural similarity from UniProtKB).
GO:0046777; Biological process: protein amino acid autophosphorylation (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE Q13627; -.
Genome annotation databases
Ensembl ENSG00000157540; Homo sapiens. [Contig view]
GeneID 1859; -.
KEGG hsa:1859; -.
Phylogenomic databases
HOGENOM Q13627; -.
HOVERGEN Q13627; -.
Other
NextBio 7615; -.
SOURCE DYRK1A; Homo sapiens.
ProtoNet Q13627.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   763  763     Dual specificity tyrosine-phosphorylation-regulated kinase 1A. PRO_0000085931
DOMAIN   159   479  321     Protein kinase. 
NP_BIND   165   173  9     ATP (By similarity). 
MOTIF   117   134  18     Bipartite nuclear localization signal (Potential). 
COMPBIAS   509   515  7     Poly-Ser. 
COMPBIAS   599   602  4     Poly-His. 
COMPBIAS   607   619  13     Poly-His. 
COMPBIAS   656   672  17     Ser/Thr-rich. 
COMPBIAS   664   671  8     Poly-Ser. 
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 similarity). 
MOD_RES   319   319        Phosphotyrosine; by autocatalysis (By similarity). 
MOD_RES   321   321        Phosphotyrosine; by autocatalysis. 
MOD_RES   748   748        Phosphoserine. 
MOD_RES   758   758        Phosphoserine. 
VAR_SEQ   70    78        Missing (in isoform 1). VSP_004917
VAR_SEQ   516   540        GGSSGTSNSGRARSDPTHQHRHSGG -> VEQHWMPGAFRMTVSFTLEVHDVPV (in isoform 3). VSP_004920
VAR_SEQ   516   529        GGSSGTSNSGRARS -> GASAISCSSWLVRH (in isoform 2). VSP_004918
VAR_SEQ   530   763        Missing (in isoform 2). VSP_004919
VAR_SEQ   541   763        Missing (in isoform 3). VSP_004921
VAR_SEQ   559   584        RQQFPAPLGWSGTEAPTQVTVETHPV -> SSHVVHLLVSPAILRWSSTGCQVPLE (in isoform 4). VSP_004922
VAR_SEQ   585   763        Missing (in isoform 4). VSP_004923
VARIANT   415   415  1     Y -> F. VAR_009395 
VARIANT   679   679  1     A -> P. VAR_040453 
VARIANT   681   681  1     Q -> H. VAR_009396 
CONFLICT   32    32        G -> A (in Ref. 1; AAC50939). 
CONFLICT   47    47        N -> S (in Ref. 1; AAC50939). 
CONFLICT   57    57        S -> P (in Ref. 1; AAC50939). 
CONFLICT   123   123        Q -> R (in Ref. 1; AAC50939). 
CONFLICT   266   266        A -> V (in Ref. 6; CAA05059). 
CONFLICT   357   357        G -> R (in Ref. 6; CAA05059). 
CONFLICT   397   397        K -> N (in Ref. 1; AAC50939). 
CONFLICT   592   592        A -> G (in Ref. 1; AAC50939). 
Sequence information
Length: 763 AA [This is the length of the unprocessed precursor] Molecular weight: 85584 Da [This is the MW of the unprocessed precursor] CRC64: 7C3A52A3CBB04FB5 [This is a checksum on the sequence]
        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 

Q13627 in FASTA format

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