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Q13627

- DYR1A_HUMAN

UniProt

Q13627 - DYR1A_HUMAN

Protein

Dual specificity tyrosine-phosphorylation-regulated kinase 1A

Gene

DYRK1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      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 similarity3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.4 Publications

    Enzyme regulationi

    Inhibited by RANBP9. Inhibited by harmine, leucettamine B and leucettine L41.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei188 – 1881ATPCurated
    Active sitei287 – 2871Proton acceptor1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi165 – 1739ATPCurated
    Nucleotide bindingi238 – 2414ATPCurated

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. non-membrane spanning protein tyrosine kinase activity Source: MGI
    3. protein binding Source: IntAct
    4. protein kinase activity Source: ProtInc
    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. mitotic cell cycle Source: Reactome
    3. negative regulation of DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
    4. nervous system development Source: ProtInc
    5. peptidyl-serine phosphorylation Source: Ensembl
    6. peptidyl-threonine phosphorylation Source: BHF-UCL
    7. peptidyl-tyrosine phosphorylation Source: UniProtKB
    8. positive regulation of protein deacetylation Source: BHF-UCL
    9. protein autophosphorylation Source: UniProtKB
    10. 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. 2681.
    ReactomeiREACT_111214. G0 and Early G1.
    SignaLinkiQ13627.

    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
    HP86
    Protein kinase minibrain homolog
    Short name:
    MNBH
    Short name:
    hMNB
    Gene namesi
    Name:DYRK1A
    Synonyms:DYRK, MNB, MNBH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:3091. DYRK1A.

    Subcellular locationi

    GO - Cellular componenti

    1. nuclear speck Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB
    4. ribonucleoprotein complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi188 – 1881K → R: Abolishes kinase activity. 1 Publication
    Mutagenesisi321 – 3211Y → F: Mildly reduces kinase activity. Does not abolish autophosphorylation on tyrosine residues. 1 Publication

    Keywords - Diseasei

    Mental retardation

    Organism-specific databases

    MIMi614104. phenotype.
    Orphaneti178469. Autosomal dominant nonsyndromic intellectual disability.
    PharmGKBiPA27545.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 763763Dual specificity tyrosine-phosphorylation-regulated kinase 1APRO_0000085931Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei111 – 1111Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei140 – 1401Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei145 – 1451Phosphotyrosine1 Publication
    Modified residuei159 – 1591Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei177 – 1771Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei219 – 2191Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei310 – 3101Phosphoserine; by autocatalysis1 Publication
    Modified residuei319 – 3191Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei321 – 3211Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei402 – 4021Phosphothreonine; by autocatalysis1 Publication
    Modified residuei449 – 4491Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei748 – 7481Phosphoserine1 Publication
    Modified residuei758 – 7581Phosphoserine1 Publication

    Post-translational modificationi

    Autophosphorylated on numerous tyrosine residues. Can also autophosphorylate on serine and threonine residues (in vitro).3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13627.
    PaxDbiQ13627.
    PRIDEiQ13627.

    PTM databases

    PhosphoSiteiQ13627.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highest levels in skeletal muscle, testis, fetal lung and fetal kidney.4 Publications

    Developmental stagei

    Expressed in the developing central nervous system. Overexpressed 1.5-fold in fetal Down syndrome brain.1 Publication

    Gene expression databases

    ArrayExpressiQ13627.
    BgeeiQ13627.
    CleanExiHS_DYRK1A.
    GenevestigatoriQ13627.

    Organism-specific databases

    HPAiHPA015323.
    HPA015810.

    Interactioni

    Subunit structurei

    Interacts RAD54L2/ARIP4. Interacts with CRY2 By similarity. Interacts with RANBP9. Interacts with WDR68. Interacts with SRSF6.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DCAF7P619623EBI-1053596,EBI-359808
    LZTS2Q9BRK43EBI-1053596,EBI-741037
    RB1P064003EBI-1053596,EBI-491274
    RBL1P287493EBI-1053596,EBI-971402
    TROAPQ128153EBI-1053596,EBI-2349743
    YWHABP319463EBI-1053621,EBI-359815

    Protein-protein interaction databases

    BioGridi108192. 56 interactions.
    DIPiDIP-39750N.
    IntActiQ13627. 32 interactions.
    MINTiMINT-1205413.
    STRINGi9606.ENSP00000381932.

    Structurei

    Secondary structure

    1
    763
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi137 – 1393
    Turni156 – 1583
    Beta strandi159 – 16810
    Beta strandi171 – 1788
    Turni179 – 1824
    Beta strandi183 – 1908
    Helixi194 – 21118
    Helixi216 – 2205
    Beta strandi224 – 2307
    Beta strandi233 – 2397
    Helixi245 – 2517
    Turni252 – 2543
    Helixi259 – 27618
    Turni279 – 2813
    Helixi290 – 2923
    Beta strandi293 – 2975
    Beta strandi303 – 3053
    Helixi308 – 3103
    Beta strandi312 – 3165
    Helixi325 – 3273
    Helixi330 – 3334
    Helixi341 – 35616
    Helixi366 – 37712
    Helixi382 – 3854
    Helixi391 – 3944
    Beta strandi395 – 3973
    Beta strandi403 – 4053
    Helixi423 – 4264
    Turni427 – 4326
    Helixi434 – 4363
    Turni437 – 4404
    Helixi446 – 45914
    Turni464 – 4663
    Helixi470 – 4745
    Helixi477 – 4793

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ13627.
    SMRiQ13627. Positions 148-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13627.

    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.1 Publication

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000220863.
    HOVERGENiHBG051425.
    InParanoidiQ13627.
    KOiK08825.
    OMAiLTNQRRM.
    OrthoDBiEOG77127N.
    PhylomeDBiQ13627.
    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]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform Long (identifier: Q13627-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MHTGGETSAC KPSSVRLAPS FSFHAAGLQM AGQMPHSHQY SDRRQPNISD    50
    QQVSALSYSD 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
    GTWNLKKTKD GKREYKPPGT RKLHNILGVE TGGPGGRRAG ESGHTVADYL 450
    KFKDLILRML DYDPKTRIQP YYALQHSFFK KTADEGTNTS NSVSTSPAME 500
    QSQSSGTTSS TSSSSGGSSG TSNSGRARSD PTHQHRHSGG HFTAAVQAMD 550
    CETHSPQVRQ QFPAPLGWSG TEAPTQVTVE THPVQETTFH VAPQQNALHH 600
    HHGNSSHHHH HHHHHHHHHG QQALGNRTRP RVYNSPTNSS STQDSMEVGH 650
    SHHSMTSLSS STTSSSTSSS STGNQGNQAY QNRPVAANTL DFGQNGAMDV 700
    NLTVYSNPRQ ETGIAGHPTY QFSANTGPAH YMTEGHLTMR QGADREESPM 750
    TGVCVQQSPV ASS 763
    Length:763
    Mass (Da):85,584
    Last modified:July 15, 1998 - v2
    Checksum:i7C3A52A3CBB04FB5
    GO
    Isoform 1 (identifier: Q13627-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         70-78: Missing.

    Show »
    Length:754
    Mass (Da):84,556
    Checksum:i59518E25F1D4FF96
    GO
    Isoform 2 (identifier: Q13627-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         516-529: GGSSGTSNSGRARS → GASAISCSSWLVRH
         530-763: Missing.

    Show »
    Length:529
    Mass (Da):60,330
    Checksum:iF639B3152ACC7750
    GO
    Isoform 3 (identifier: Q13627-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         516-540: GGSSGTSNSGRARSDPTHQHRHSGG → VEQHWMPGAFRMTVSFTLEVHDVPV
         541-763: Missing.

    Show »
    Length:540
    Mass (Da):61,770
    Checksum:iE02CE08DF1AE0AED
    GO
    Isoform 4 (identifier: Q13627-5) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:584
    Mass (Da):66,099
    Checksum:iBA2480B34BAB2878
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321G → A in AAC50939. (PubMed:8975710)Curated
    Sequence conflicti47 – 471N → S in AAC50939. (PubMed:8975710)Curated
    Sequence conflicti57 – 571S → P in AAC50939. (PubMed:8975710)Curated
    Sequence conflicti123 – 1231Q → R in AAC50939. (PubMed:8975710)Curated
    Sequence conflicti266 – 2661A → V in CAA05059. (PubMed:9503011)Curated
    Sequence conflicti357 – 3571G → R in CAA05059. (PubMed:9503011)Curated
    Sequence conflicti397 – 3971K → N in AAC50939. (PubMed:8975710)Curated
    Sequence conflicti592 – 5921A → G in AAC50939. (PubMed:8975710)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti415 – 4151Y → F.1 Publication
    VAR_009395
    Natural varianti679 – 6791A → P.2 Publications
    Corresponds to variant rs55720916 [ dbSNP | Ensembl ].
    VAR_040453
    Natural varianti681 – 6811Q → H.1 Publication
    VAR_009396

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei70 – 789Missing in isoform 1. 2 PublicationsVSP_004917
    Alternative sequencei516 – 54025GGSSG…RHSGG → VEQHWMPGAFRMTVSFTLEV HDVPV in isoform 3. CuratedVSP_004920Add
    BLAST
    Alternative sequencei516 – 52914GGSSG…GRARS → GASAISCSSWLVRH in isoform 2. CuratedVSP_004918Add
    BLAST
    Alternative sequencei530 – 763234Missing in isoform 2. CuratedVSP_004919Add
    BLAST
    Alternative sequencei541 – 763223Missing in isoform 3. CuratedVSP_004921Add
    BLAST
    Alternative sequencei559 – 58426RQQFP…ETHPV → SSHVVHLLVSPAILRWSSTG CQVPLE in isoform 4. 1 PublicationVSP_004922Add
    BLAST
    Alternative sequencei585 – 763179Missing in isoform 4. 1 PublicationVSP_004923Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS13653.1. [Q13627-2]
    CCDS13654.1. [Q13627-3]
    CCDS42925.1. [Q13627-1]
    CCDS42926.1. [Q13627-5]
    PIRiJC4898.
    RefSeqiNP_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]
    UniGeneiHs.368240.

    Genome annotation databases

    EnsembliENST00000338785; ENSP00000342690; ENSG00000157540. [Q13627-5]
    ENST00000339659; ENSP00000340373; ENSG00000157540. [Q13627-2]
    ENST00000398956; ENSP00000381929; ENSG00000157540. [Q13627-3]
    ENST00000398960; ENSP00000381932; ENSG00000157540. [Q13627-1]
    GeneIDi1859.
    KEGGihsa:1859.
    UCSCiuc002ywi.3. human. [Q13627-5]
    uc002ywj.3. human. [Q13627-2]
    uc002ywk.3. human. [Q13627-1]
    uc002ywm.3. human. [Q13627-3]

    Polymorphism databases

    DMDMi3219996.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS13653.1. [Q13627-2 ]
    CCDS13654.1. [Q13627-3 ]
    CCDS42925.1. [Q13627-1 ]
    CCDS42926.1. [Q13627-5 ]
    PIRi JC4898.
    RefSeqi NP_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 ]
    UniGenei Hs.368240.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VX3 X-ray 2.40 A/B/C/D 127-485 [» ]
    2WO6 X-ray 2.50 A/B 127-485 [» ]
    3ANQ X-ray 2.60 A/B/C/D 126-490 [» ]
    3ANR X-ray 2.60 A/B/C/D 126-490 [» ]
    4AZE X-ray 3.15 A/B/C 128-485 [» ]
    4MQ1 X-ray 2.35 A/B/C/D 127-485 [» ]
    4MQ2 X-ray 2.80 A/B/C/D 127-485 [» ]
    ProteinModelPortali Q13627.
    SMRi Q13627. Positions 148-480.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108192. 56 interactions.
    DIPi DIP-39750N.
    IntActi Q13627. 32 interactions.
    MINTi MINT-1205413.
    STRINGi 9606.ENSP00000381932.

    Chemistry

    BindingDBi Q13627.
    ChEMBLi CHEMBL2292.
    GuidetoPHARMACOLOGYi 2009.

    PTM databases

    PhosphoSitei Q13627.

    Polymorphism databases

    DMDMi 3219996.

    Proteomic databases

    MaxQBi Q13627.
    PaxDbi Q13627.
    PRIDEi Q13627.

    Protocols and materials databases

    DNASUi 1859.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338785 ; ENSP00000342690 ; ENSG00000157540 . [Q13627-5 ]
    ENST00000339659 ; ENSP00000340373 ; ENSG00000157540 . [Q13627-2 ]
    ENST00000398956 ; ENSP00000381929 ; ENSG00000157540 . [Q13627-3 ]
    ENST00000398960 ; ENSP00000381932 ; ENSG00000157540 . [Q13627-1 ]
    GeneIDi 1859.
    KEGGi hsa:1859.
    UCSCi uc002ywi.3. human. [Q13627-5 ]
    uc002ywj.3. human. [Q13627-2 ]
    uc002ywk.3. human. [Q13627-1 ]
    uc002ywm.3. human. [Q13627-3 ]

    Organism-specific databases

    CTDi 1859.
    GeneCardsi GC21P038739.
    HGNCi HGNC:3091. DYRK1A.
    HPAi HPA015323.
    HPA015810.
    MIMi 600855. gene.
    614104. phenotype.
    neXtProti NX_Q13627.
    Orphaneti 178469. Autosomal dominant nonsyndromic intellectual disability.
    PharmGKBi PA27545.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000220863.
    HOVERGENi HBG051425.
    InParanoidi Q13627.
    KOi K08825.
    OMAi LTNQRRM.
    OrthoDBi EOG77127N.
    PhylomeDBi Q13627.
    TreeFami TF314624.

    Enzyme and pathway databases

    BRENDAi 2.7.12.1. 2681.
    Reactomei REACT_111214. G0 and Early G1.
    SignaLinki Q13627.

    Miscellaneous databases

    ChiTaRSi DYRK1A. human.
    EvolutionaryTracei Q13627.
    GeneWikii DYRK1A.
    GenomeRNAii 1859.
    NextBioi 7615.
    PROi Q13627.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13627.
    Bgeei Q13627.
    CleanExi HS_DYRK1A.
    Genevestigatori Q13627.

    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] (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. 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. 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. 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.
      , 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.

    Entry informationi

    Entry nameiDYR1A_HUMAN
    AccessioniPrimary (citable) accession number: Q13627
    Secondary accession number(s): O60769
    , Q92582, Q92810, Q9UNM5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 156 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 21
      Human chromosome 21: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3