Dual specificity tyrosine-phosphorylation-regulated kinase 1A

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Q61214 (DYR1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 111. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	Dyrk1a
Synonyms:	Dyrk

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	763 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in a signaling pathway regulating nuclear functions of cell proliferation. Phosphorylates serine, threonine and tyrosine residues in its sequence and in exogenous substrates.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Inhibited by RANBP9 By similarity.
Subunit structure	Interacts with RANBP9 By similarity. Interacts with RAD54L2/ARIP4. Interacts with WDR68 By similarity. Ref.2 Ref.4
Subcellular location	Nucleus speckle Ref.2.
Tissue specificity	Expressed in a variety of embryonic and adult tissues. Expressed abundantly in neurons of the brain, spinal cord, and retina in developing embryos. Ref.1
Post-translational modification	Autophosphorylated on tyrosine residues By similarity. Ref.3 Ref.5 Ref.6
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	peptidyl-tyrosine phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB protein autophosphorylation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	nuclear speck Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein self-association Inferred from physical interaction Ref.2. Source: UniProtKB protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB protein serine/threonine/tyrosine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Sirt1	Q923E4	4	EBI-80344,EBI-1802585

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 763

763

Dual specificity tyrosine-phosphorylation-regulated kinase 1A

PRO_0000085932

Regions

Domain

159 – 479

321

Protein kinase

Nucleotide binding

165 – 173

ATP By similarity

Motif

117 – 134

Bipartite nuclear localization signal Potential

Compositional bias

509 – 515

Poly-Ser

Compositional bias

599 – 602

Poly-His

Compositional bias

607 – 619

Poly-His

Compositional bias

656 – 672

Ser/Thr-rich

Compositional bias

664 – 671

Poly-Ser

Sites

Active site

287

Proton acceptor By similarity

Binding site

188

ATP By similarity

Amino acid modifications

Modified residue

145

Phosphotyrosine Ref.6

Modified residue

219

Phosphotyrosine; by autocatalysis By similarity

Modified residue

319

Phosphotyrosine; by autocatalysis By similarity

Modified residue

321

Phosphotyrosine; by autocatalysis Ref.3 Ref.5

Modified residue

324

Phosphoserine By similarity

Modified residue

748

Phosphoserine By similarity

Modified residue

758

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q61214 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E117DDD6C5E8C74F
Show »

FASTA

763

85,494

        10         20         30         40         50         60 
MHTGGETSAC KPSSVRLAPS FSFHAAGLQM AAQMPHSHQY SDRRQPSISD QQVSALPYSD 

        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 GTWSLKKTKD 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 
HFAAAVQAMD 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 YMTEGHLAMR QGADREESPM TGVCVQQSPV ASS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8975710] [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: 9070862] [Abstract] Cited for: SUBCELLULAR LOCATION, SUBUNIT.
[3]	"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry." Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C. Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003) [PubMed: 12522270] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321, MASS SPECTROMETRY.
[4]	"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: 15199138] [Abstract] Cited for: INTERACTION WITH RAD54L2.
[5]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321, MASS SPECTROMETRY.
[6]	"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: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, MASS SPECTROMETRY. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U58497 mRNA. Translation: AAC52994.1.
IPI	IPI00118849.
RefSeq	NP_001106860.1. NM_001113389.1. NP_031916.1. NM_007890.2.
UniGene	Mm.310973.
3D structure databases
ProteinModelPortal	Q61214.
SMR	Q61214. Positions 148-481.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q61214. 4 interactions.
MINT	MINT-1205474.
STRING	Q61214.
PTM databases
PhosphoSite	Q61214.
Proteomic databases
PRIDE	Q61214.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000023614; ENSMUSP00000023614; ENSMUSG00000022897. ENSMUST00000119878; ENSMUSP00000113660; ENSMUSG00000022897.
GeneID	13548.
KEGG	mmu:13548.
Organism-specific databases
CTD	1859.
MGI	MGI:1330299. Dyrk1a.
Phylogenomic databases
HOGENOM	HBG755340.
HOVERGEN	HBG051425.
InParanoid	Q61214.
OMA	HRHSGGH.
OrthoDB	EOG4MW85K.
PhylomeDB	Q61214.
Enzyme and pathway databases
BRENDA	2.7.12.1. 3474.
Gene expression databases
ArrayExpress	Q61214.
Bgee	Q61214.
Genevestigator	Q61214.
GermOnline	ENSMUSG00000022897. Mus musculus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K08825.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	284158.
SOURCE	Search...

Entry information

Entry name

DYR1A_MOUSE

Accession

Primary (citable) accession number: Q61214

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents