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Q61214

- DYR1A_MOUSE

UniProt

Q61214 - DYR1A_MOUSE

Protein

Dual specificity tyrosine-phosphorylation-regulated kinase 1A

Gene

Dyrk1a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    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.By similarity1 Publication

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Inhibited by RANBP9.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei188 – 1881ATPPROSITE-ProRule annotation
    Active sitei287 – 2871Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi165 – 1739ATPPROSITE-ProRule annotation
    Nucleotide bindingi238 – 2414ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. non-membrane spanning protein tyrosine kinase activity Source: MGI
    4. protein binding Source: UniProtKB
    5. protein self-association Source: UniProtKB
    6. protein serine/threonine/tyrosine kinase activity Source: UniProtKB-EC
    7. protein serine/threonine kinase activity Source: UniProtKB
    8. protein tyrosine kinase activity Source: UniProtKB
    9. tau protein binding Source: BHF-UCL

    GO - Biological processi

    1. circadian rhythm Source: UniProtKB
    2. negative regulation of DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
    3. peptidyl-serine phosphorylation Source: UniProtKB
    4. peptidyl-threonine phosphorylation Source: BHF-UCL
    5. peptidyl-tyrosine phosphorylation Source: UniProtKB
    6. positive regulation of protein deacetylation Source: BHF-UCL
    7. protein autophosphorylation Source: UniProtKB
    8. protein phosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.12.1. 3474.
    ReactomeiREACT_199110. G0 and Early G1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity tyrosine-phosphorylation-regulated kinase 1A (EC:2.7.12.1)
    Alternative name(s):
    Dual specificity YAK1-related kinase
    MP86
    Protein kinase minibrain homolog
    Short name:
    MNBH
    Gene namesi
    Name:Dyrk1a
    Synonyms:Dyrk
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:1330299. Dyrk1a.

    Subcellular locationi

    Nucleus speckle 1 Publication

    GO - Cellular componenti

    1. nuclear speck Source: UniProtKB
    2. nucleus Source: UniProtKB
    3. ribonucleoprotein complex Source: MGI

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 763763Dual specificity tyrosine-phosphorylation-regulated kinase 1APRO_0000085932Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei111 – 1111Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei140 – 1401Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei145 – 1451Phosphotyrosine1 Publication
    Modified residuei159 – 1591Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei177 – 1771Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei219 – 2191Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei310 – 3101Phosphoserine; by autocatalysisBy similarity
    Modified residuei319 – 3191Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei321 – 3211Phosphotyrosine; by autocatalysis
    Modified residuei402 – 4021Phosphothreonine; by autocatalysisBy similarity
    Modified residuei449 – 4491Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei748 – 7481PhosphoserineBy similarity
    Modified residuei758 – 7581PhosphoserineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ61214.
    PaxDbiQ61214.
    PRIDEiQ61214.

    PTM databases

    PhosphoSiteiQ61214.

    Expressioni

    Tissue specificityi

    Detected in brain (at protein level). Expressed in a variety of embryonic and adult tissues. Expressed abundantly in neurons of the brain, spinal cord, and retina in developing embryos.2 Publications

    Gene expression databases

    ArrayExpressiQ61214.
    BgeeiQ61214.
    GenevestigatoriQ61214.

    Interactioni

    Subunit structurei

    Interacts with RANBP9 By similarity. Interacts with RAD54L2/ARIP4. Interacts with WDR68 By similarity. Interacts with CRY2.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-80344,EBI-80344
    RCAN1P53805-25EBI-80344,EBI-1541912From a different organism.
    Rcan1Q9JHG62EBI-80344,EBI-644061
    Sirt1Q923E44EBI-80344,EBI-1802585

    Protein-protein interaction databases

    BioGridi199347. 2 interactions.
    IntActiQ61214. 4 interactions.
    MINTiMINT-1205474.

    Structurei

    3D structure databases

    ProteinModelPortaliQ61214.
    SMRiQ61214. Positions 148-481.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini159 – 479321Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi117 – 13418Bipartite nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi509 – 5157Poly-Ser
    Compositional biasi599 – 6024Poly-His
    Compositional biasi607 – 61913Poly-HisAdd
    BLAST
    Compositional biasi656 – 67217Ser/Thr-richAdd
    BLAST
    Compositional biasi664 – 6718Poly-Ser

    Domaini

    The polyhistidine repeats act as targeting signals to nuclear speckles.By similarity

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117228.
    HOGENOMiHOG000220863.
    HOVERGENiHBG051425.
    InParanoidiQ61214.
    KOiK08825.
    OMAiLTNQRRM.
    OrthoDBiEOG77127N.
    PhylomeDBiQ61214.
    TreeFamiTF314624.

    Family and domain databases

    InterProiIPR028318. 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]
    PANTHERiPTHR24058:SF28. PTHR24058:SF28. 1 hit.
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q61214-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHTGGETSAC KPSSVRLAPS FSFHAAGLQM AAQMPHSHQY SDRRQPSISD    50
    QQVSALPYSD QIQQPLTNQV MPDIVMLQRR MPQTFRDPAT APLRKLSVDL 100
    IKTYKHINEV YYAKKKRRHQ QGQGDDSSHK KERKVYNDGY DDDNYDYIVK 150
    NGEKWMDRYE IDSLIGKGSF GQVVKAYDRV EQEWVAIKII KNKKAFLNQA 200
    QIEVRLLELM NKHDTEMKYY IVHLKRHFMF RNHLCLVFEM LSYNLYDLLR 250
    NTNFRGVSLN LTRKFAQQMC TALLFLATPE LSIIHCDLKP ENILLCNPKR 300
    SAIKIVDFGS SCQLGQRIYQ YIQSRFYRSP EVLLGMPYDL AIDMWSLGCI 350
    LVEMHTGEPL FSGANEVDQM NKIVEVLGIP PAHILDQAPK ARKFFEKLPD 400
    GTWSLKKTKD GKREYKPPGT RKLHNILGVE TGGPGGRRAG ESGHTVADYL 450
    KFKDLILRML DYDPKTRIQP YYALQHSFFK KTADEGTNTS NSVSTSPAME 500
    QSQSSGTTSS TSSSSGGSSG TSNSGRARSD PTHQHRHSGG HFAAAVQAMD 550
    CETHSPQVRQ QFPAPLGWSG TEAPTQVTVE THPVQETTFH VAPQQNALHH 600
    HHGNSSHHHH HHHHHHHHHG QQALGNRTRP RVYNSPTNSS STQDSMEVGH 650
    SHHSMTSLSS STTSSSTSSS STGNQGNQAY QNRPVAANTL DFGQNGAMDV 700
    NLTVYSNPRQ ETGIAGHPTY QFSANTGPAH YMTEGHLAMR QGADREESPM 750
    TGVCVQQSPV ASS 763
    Length:763
    Mass (Da):85,494
    Last modified:November 1, 1996 - v1
    Checksum:iE117DDD6C5E8C74F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58497 mRNA. Translation: AAC52994.1.
    CCDSiCCDS28350.1.
    RefSeqiNP_001106860.1. NM_001113389.1.
    NP_031916.1. NM_007890.2.
    UniGeneiMm.310973.

    Genome annotation databases

    EnsembliENSMUST00000023614; ENSMUSP00000023614; ENSMUSG00000022897.
    ENSMUST00000119878; ENSMUSP00000113660; ENSMUSG00000022897.
    GeneIDi13548.
    KEGGimmu:13548.
    UCSCiuc008abg.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58497 mRNA. Translation: AAC52994.1 .
    CCDSi CCDS28350.1.
    RefSeqi NP_001106860.1. NM_001113389.1.
    NP_031916.1. NM_007890.2.
    UniGenei Mm.310973.

    3D structure databases

    ProteinModelPortali Q61214.
    SMRi Q61214. Positions 148-481.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199347. 2 interactions.
    IntActi Q61214. 4 interactions.
    MINTi MINT-1205474.

    Chemistry

    BindingDBi Q61214.
    ChEMBLi CHEMBL4750.

    PTM databases

    PhosphoSitei Q61214.

    Proteomic databases

    MaxQBi Q61214.
    PaxDbi Q61214.
    PRIDEi Q61214.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000023614 ; ENSMUSP00000023614 ; ENSMUSG00000022897 .
    ENSMUST00000119878 ; ENSMUSP00000113660 ; ENSMUSG00000022897 .
    GeneIDi 13548.
    KEGGi mmu:13548.
    UCSCi uc008abg.2. mouse.

    Organism-specific databases

    CTDi 1859.
    MGIi MGI:1330299. Dyrk1a.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117228.
    HOGENOMi HOG000220863.
    HOVERGENi HBG051425.
    InParanoidi Q61214.
    KOi K08825.
    OMAi LTNQRRM.
    OrthoDBi EOG77127N.
    PhylomeDBi Q61214.
    TreeFami TF314624.

    Enzyme and pathway databases

    BRENDAi 2.7.12.1. 3474.
    Reactomei REACT_199110. G0 and Early G1.

    Miscellaneous databases

    NextBioi 284158.
    PROi Q61214.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61214.
    Bgeei Q61214.
    Genevestigatori Q61214.

    Family and domain databases

    InterProi IPR028318. 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 ]
    PANTHERi PTHR24058:SF28. PTHR24058:SF28. 1 hit.
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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], TISSUE SPECIFICITY.
      Strain: Swiss Webster / NIH.
      Tissue: Embryo.
    2. "The murine Dyrk protein maps to chromosome 16, localizes to the nucleus, and can form multimers."
      Song W.J., Chung S.H., Kurnit D.M.
      Biochem. Biophys. Res. Commun. 231:640-644(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SUBUNIT.
    3. "Dyrk1A potentiates steroid hormone-induced transcription via the chromatin remodeling factor Arip4."
      Sitz J.H., Tigges M., Baumgaertel K., Khaspekov L.G., Lutz B.
      Mol. Cell. Biol. 24:5821-5834(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD54L2.
    4. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    5. "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. 30:1757-1768(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CRY2.
    6. "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: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiDYR1A_MOUSE
    AccessioniPrimary (citable) accession number: Q61214
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 138 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3