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Protein

Dual specificity tyrosine-phosphorylation-regulated kinase 3

Gene

Dyrk3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. Negative regulator of EPO-dependent erythropoiesis, may place an upper limit on red cell production during stress erythropoiesis. Inhibits cell death due to cytokine withdrawal in hematopoietic progenitor cells (By similarity). May act by regulating CREB/CRE signaling (PubMed:12356771). Stabilizes and prevents stress granule disassembly thereby regulating mTORC1 signaling during cellular stress. During stressful conditions, DYRK3 partitions to the stress granule from the cytosol, as well as mTORC1 components, which prevents mTORC1 signaling. When stress signals are gone, the kinase activity of DYRK3 is required for the dissolution of stress granule and mTORC1 relocation to the cytosol, and promotes the phosphorylation of the mTORC1 inhibitor, AKT1S1, allowing full reactivation of mTORC1 signaling. Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1. This in turn inhibits TP53 activity and apoptosis (By similarity).By similarity1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.2 Publications

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei237ATPPROSITE-ProRule annotation1 Publication1
Active sitei334Proton acceptorPROSITE-ProRule annotationBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi214 – 222ATPPROSITE-ProRule annotationBy similarity9
Nucleotide bindingi287 – 290ATPPROSITE-ProRule annotation4

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • protein kinase activity Source: UniProtKB
  • protein serine/threonine/tyrosine kinase activity Source: UniProtKB-EC
  • protein serine/threonine kinase activity Source: UniProtKB
  • protein tyrosine kinase activity Source: MGI

GO - Biological processi

  • erythrocyte differentiation Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  • peptidyl-tyrosine phosphorylation Source: MGI
  • protein phosphorylation Source: UniProtKB
  • regulation of cellular response to stress Source: UniProtKB
  • regulation of TORC1 signaling Source: UniProtKB
  • stress granule disassembly Source: UniProtKB

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.12.1. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity tyrosine-phosphorylation-regulated kinase 3 (EC:2.7.12.12 Publications)
Gene namesi
Name:Dyrk3Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1330300. Dyrk3.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasmic granule By similarity

  • Note: Shuttles between cytoplasm and stress granules. Localized predominantly on distinct speckles distributed throughout the cytoplasm of the cell. At low concentration, showns a homogeneous distribution throughout the cytoplasm and does not condense in speckles. During oxidative and osmotic stress, localizes to stress granules (By similarity).By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice exhibit unperturbed steady-state erythropoiesis but significantly increased reticulocyte production during stress erythropoiesis and appear to be partially protected against anemia.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi237K → A: Loss of kinase activity. 1 Publication1
Mutagenesisi366Y → A: Minimal loss of kinase activity. 1 Publication1
Mutagenesisi366Y → E: Minimal loss of kinase activity; when associated with E-368. 1 Publication1
Mutagenesisi368Y → A: Loss of kinase activity. 1 Publication1
Mutagenesisi368Y → E: Minimal loss of kinase activity; when associated with E-366. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002915371 – 586Dual specificity tyrosine-phosphorylation-regulated kinase 3Add BLAST586

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei368Phosphotyrosine1 Publication1

Post-translational modificationi

Autophosphorylated on tyrosine residues.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ922Y0.
PRIDEiQ922Y0.

PTM databases

iPTMnetiQ922Y0.
PhosphoSitePlusiQ922Y0.

Expressioni

Gene expression databases

BgeeiENSMUSG00000016526.
ExpressionAtlasiQ922Y0. baseline and differential.
GenevisibleiQ922Y0. MM.

Interactioni

Subunit structurei

Interacts with SIRT1 (PubMed:20167603).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Sirt1Q923E47EBI-5242007,EBI-1802585

Protein-protein interaction databases

BioGridi230510. 1 interactor.
IntActiQ922Y0. 2 interactors.
STRINGi10090.ENSMUSP00000016670.

Structurei

3D structure databases

ProteinModelPortaliQ922Y0.
SMRiQ922Y0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini208 – 521Protein kinasePROSITE-ProRule annotationAdd BLAST314

Domaini

The N-terminal domain is required for stress granule localization.By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0667. Eukaryota.
ENOG410XPET. LUCA.
GeneTreeiENSGT00760000119032.
HOGENOMiHOG000220863.
HOVERGENiHBG051426.
InParanoidiQ922Y0.
KOiK18669.
OMAiLKQYKHH.
OrthoDBiEOG091G0Q46.
PhylomeDBiQ922Y0.
TreeFamiTF314624.

Family and domain databases

InterProiView protein in InterPro
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
PfamiView protein in Pfam
PF00069. Pkinase. 1 hit.
SMARTiView protein in SMART
SM00220. S_TKc. 1 hit.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiView protein in PROSITE
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.

Sequencei

Sequence statusi: Complete.

Q922Y0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGAARDRGR KDAALPGAGL PPQQRRLGDG VYDTFMMIDE TKGPPYSDTF
60 70 80 90 100
SNPSEAPVSR RLNITTEPLT RGHTQHFVNG SEMKVEQLFQ EFGNRRSNTL
110 120 130 140 150
QSDGISNSEK SSPASQGKSS ESLSAVKCNL SSRPSKVLPL TPEQALKQYK
160 170 180 190 200
HHLTAYEKLE IVSYPEIYFV GPNAKKRQGV IGGPNNGGYD DADGAYIHVP
210 220 230 240 250
RDHLAYRYEV LKIIGKGSFG QVARVYDHKL RQYVALKMVR NEKRFHRQAA
260 270 280 290 300
EEIRILEHLK KQDKTGSMNV IHMLESFTFR NHVCMAFELL SIDLYELIKK
310 320 330 340 350
NKFQGFSVQL VRKFAQSILQ SLDALHKNKI IHCDLKPENI LLKHHGRSAT
360 370 380 390 400
KVIDFGSSCF EYQKLYTYIQ SRFYRAPEII LGCRYSTPID IWSFGCILAE
410 420 430 440 450
LLTGQPLFPG EDEGDQLACM IELLGMPPQK LLEQSKRAKY FINSKGLPRY
460 470 480 490 500
CSVSTQTDGR VVLLGGRSRR GKKRGPPGSK DWATALKGCG DYLFIEFLKR
510 520 530 540 550
CLQWDPSARL TPAQALRHPW ISKSTPKPLT MDKVPGKRVV NPTNAFQGLG
560 570 580
SKLPPVVGIA SKLKANLMSE TSGSIPLCSV LPKLIS
Length:586
Mass (Da):65,572
Last modified:December 1, 2001 - v1
Checksum:i0097F7584726AB55
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC006704 mRNA. Translation: AAH06704.1.
AK035114 mRNA. Translation: BAC28949.1.
CCDSiCCDS15267.1.
RefSeqiNP_663483.1. NM_145508.2.
UniGeneiMm.39299.

Genome annotation databases

EnsembliENSMUST00000016670; ENSMUSP00000016670; ENSMUSG00000016526.
GeneIDi226419.
KEGGimmu:226419.
UCSCiuc007cmw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC006704 mRNA. Translation: AAH06704.1.
AK035114 mRNA. Translation: BAC28949.1.
CCDSiCCDS15267.1.
RefSeqiNP_663483.1. NM_145508.2.
UniGeneiMm.39299.

3D structure databases

ProteinModelPortaliQ922Y0.
SMRiQ922Y0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230510. 1 interactor.
IntActiQ922Y0. 2 interactors.
STRINGi10090.ENSMUSP00000016670.

PTM databases

iPTMnetiQ922Y0.
PhosphoSitePlusiQ922Y0.

Proteomic databases

PaxDbiQ922Y0.
PRIDEiQ922Y0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000016670; ENSMUSP00000016670; ENSMUSG00000016526.
GeneIDi226419.
KEGGimmu:226419.
UCSCiuc007cmw.1. mouse.

Organism-specific databases

CTDi8444.
MGIiMGI:1330300. Dyrk3.

Phylogenomic databases

eggNOGiKOG0667. Eukaryota.
ENOG410XPET. LUCA.
GeneTreeiENSGT00760000119032.
HOGENOMiHOG000220863.
HOVERGENiHBG051426.
InParanoidiQ922Y0.
KOiK18669.
OMAiLKQYKHH.
OrthoDBiEOG091G0Q46.
PhylomeDBiQ922Y0.
TreeFamiTF314624.

Enzyme and pathway databases

BRENDAi2.7.12.1. 3474.

Miscellaneous databases

PROiPR:Q922Y0.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000016526.
ExpressionAtlasiQ922Y0. baseline and differential.
GenevisibleiQ922Y0. MM.

Family and domain databases

InterProiView protein in InterPro
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
PfamiView protein in Pfam
PF00069. Pkinase. 1 hit.
SMARTiView protein in SMART
SM00220. S_TKc. 1 hit.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiView protein in PROSITE
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDYRK3_MOUSE
AccessioniPrimary (citable) accession number: Q922Y0
Secondary accession number(s): Q8BM34
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: December 1, 2001
Last modified: May 10, 2017
This is version 113 of the entry and version 1 of the sequence. See 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.