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Q61214

- DYR1A_MOUSE

UniProt

Q61214 - DYR1A_MOUSE

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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

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. Exhibits a sugstrate preference for proline at position P+1 and arginine at position P-3.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 self-association Source: UniProtKB
  5. protein serine/threonine/tyrosine kinase activity Source: UniProtKB-EC
  6. protein serine/threonine kinase activity Source: UniProtKB
  7. protein tyrosine kinase activity Source: UniProtKB
  8. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ61214.
ExpressionAtlasiQ61214. baseline and differential.
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.
GeneTreeiENSGT00760000119032.
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.
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

        10         20         30         40         50
MHTGGETSAC KPSSVRLAPS FSFHAAGLQM AAQMPHSHQY SDRRQPSISD
60 70 80 90 100
QQVSALPYSD QIQQPLTNQV MPDIVMLQRR MPQTFRDPAT APLRKLSVDL
110 120 130 140 150
IKTYKHINEV YYAKKKRRHQ QGQGDDSSHK KERKVYNDGY DDDNYDYIVK
160 170 180 190 200
NGEKWMDRYE IDSLIGKGSF GQVVKAYDRV EQEWVAIKII KNKKAFLNQA
210 220 230 240 250
QIEVRLLELM NKHDTEMKYY IVHLKRHFMF RNHLCLVFEM LSYNLYDLLR
260 270 280 290 300
NTNFRGVSLN LTRKFAQQMC TALLFLATPE LSIIHCDLKP ENILLCNPKR
310 320 330 340 350
SAIKIVDFGS SCQLGQRIYQ YIQSRFYRSP EVLLGMPYDL AIDMWSLGCI
360 370 380 390 400
LVEMHTGEPL FSGANEVDQM NKIVEVLGIP PAHILDQAPK ARKFFEKLPD
410 420 430 440 450
GTWSLKKTKD GKREYKPPGT RKLHNILGVE TGGPGGRRAG ESGHTVADYL
460 470 480 490 500
KFKDLILRML DYDPKTRIQP YYALQHSFFK KTADEGTNTS NSVSTSPAME
510 520 530 540 550
QSQSSGTTSS TSSSSGGSSG TSNSGRARSD PTHQHRHSGG HFAAAVQAMD
560 570 580 590 600
CETHSPQVRQ QFPAPLGWSG TEAPTQVTVE THPVQETTFH VAPQQNALHH
610 620 630 640 650
HHGNSSHHHH HHHHHHHHHG QQALGNRTRP RVYNSPTNSS STQDSMEVGH
660 670 680 690 700
SHHSMTSLSS STTSSSTSSS STGNQGNQAY QNRPVAANTL DFGQNGAMDV
710 720 730 740 750
NLTVYSNPRQ ETGIAGHPTY QFSANTGPAH YMTEGHLAMR QGADREESPM
760
TGVCVQQSPV ASS
Length:763
Mass (Da):85,494
Last modified:November 1, 1996 - v1
Checksum:iE117DDD6C5E8C74F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 ENSGT00760000119032.
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

Bgeei Q61214.
ExpressionAtlasi Q61214. baseline and differential.
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.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 140 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