Reviewed, UniProtKB/Swiss-Prot Q922Y0 (DYRK3_MOUSE)

Names and origin

Protein names

Recommended name:
    Dual specificity tyrosine-phosphorylation-regulated kinase 3
    EC=2.7.12.1

Gene names

Name:

Dyrk3

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

Protein attributes

Sequence length	586 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. May act by regulating CREB/CRE signaling. Ref.3 UniProtKB O43781
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.3
Cofactor	Magnesium By similarity. Ref.3
Subcellular location	Nucleus By similarity UniProtKB O43781.
Post-translational modification	Autophosphorylated on tyrosine residues By similarity. UniProtKB O43781
Disruption phenotype	Mice exhibit unperturbed steady-state erythropoiesis but significantly increased reticulocyte production during stress erythropoiesis and appear to be partially protected against anemia. Ref.4
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 Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	erythrocyte differentiation Ref.4 Inferred from direct assay. Source: UniProtKB protein amino acid phosphorylation Ref.3 Inferred from direct assay. Source: UniProtKB
Cellular component	nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Ref.3 Inferred from direct assay. Source: UniProtKB magnesium ion binding Ref.3 Inferred from direct assay. Source: UniProtKB protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein tyrosine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 586	586	Dual specificity tyrosine-phosphorylation-regulated kinase 3		PRO_0000291537
Regions
	Domain	208 – 521	314	Protein kinase
	Nucleotide binding	214 – 222	9	ATP By similarity UniProtKB P28523
Sites
	Active site	334	1	Proton acceptor By similarity UniProtKB P28523
	Binding site	237	1	ATP Ref.3
Amino acid modifications
	Modified residue	208	1	Phosphotyrosine By similarity UniProtKB O43781
	Modified residue	317	1	Phosphoserine Ref.5
	Modified residue	368	1	Phosphotyrosine Ref.3
Experimental info
	Mutagenesis	237	1	K → A: Loss of kinase activity. Ref.3
	Mutagenesis	366	1	Y → A: Minimal loss of kinase activity. Ref.3
	Mutagenesis	366	1	Y → E: Minimal loss of kinase activity; when associated with E-368. Ref.3
	Mutagenesis	368	1	Y → A: Loss of kinase activity. Ref.3
	Mutagenesis	368	1	Y → E: Minimal loss of kinase activity; when associated with E-366. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q922Y0-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 0097F7584726AB55	FASTA	586	65,572
	10 20 30 40 50 60 MGGAARDRGR KDAALPGAGL PPQQRRLGDG VYDTFMMIDE TKGPPYSDTF SNPSEAPVSR 70 80 90 100 110 120 RLNITTEPLT RGHTQHFVNG SEMKVEQLFQ EFGNRRSNTL QSDGISNSEK SSPASQGKSS 130 140 150 160 170 180 ESLSAVKCNL SSRPSKVLPL TPEQALKQYK HHLTAYEKLE IVSYPEIYFV GPNAKKRQGV 190 200 210 220 230 240 IGGPNNGGYD DADGAYIHVP RDHLAYRYEV LKIIGKGSFG QVARVYDHKL RQYVALKMVR 250 260 270 280 290 300 NEKRFHRQAA EEIRILEHLK KQDKTGSMNV IHMLESFTFR NHVCMAFELL SIDLYELIKK 310 320 330 340 350 360 NKFQGFSVQL VRKFAQSILQ SLDALHKNKI IHCDLKPENI LLKHHGRSAT KVIDFGSSCF 370 380 390 400 410 420 EYQKLYTYIQ SRFYRAPEII LGCRYSTPID IWSFGCILAE LLTGQPLFPG EDEGDQLACM 430 440 450 460 470 480 IELLGMPPQK LLEQSKRAKY FINSKGLPRY CSVSTQTDGR VVLLGGRSRR GKKRGPPGSK 490 500 510 520 530 540 DWATALKGCG DYLFIEFLKR CLQWDPSARL TPAQALRHPW ISKSTPKPLT MDKVPGKRVV 550 560 570 580 NPTNAFQGLG SKLPPVVGIA SKLKANLMSE TSGSIPLCSV LPKLIS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary gland.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 49-586. Strain: C57BL/6J. Tissue: Embryo.
[3]	"DYRK3 activation, engagement of protein kinase A/cAMP response element-binding protein, and modulation of progenitor cell survival." Li K., Zhao S., Karur V., Wojchowski D.M. J. Biol. Chem. 277:47052-47060(2002) [PubMed: 12356771] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LYS-237; TYR-366 AND TYR-368.
[4]	"Erythropoietin-dependent erythropoiesis: new insights and questions." Wojchowski D.M., Menon M.P., Sathyanarayana P., Fang J., Karur V., Houde E., Kapelle W., Bogachev O. Blood Cells Mol. Dis. 36:232-238(2006) [PubMed: 16524748] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[5]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC006704 mRNA. Translation: AAH06704.1. AK035114 mRNA. Translation: BAC28949.1.
IPI	IPI00123588.
RefSeq	NP_663483.1.
UniGene	Mm.39299
3D structure databases
HSSP	HSSP built from PDB template 2BAJ based on UniProtKB Q16539.
SMR	Q922Y0. Positions 196-522, 205-555.
ModBase	Search...
Protein-protein interaction databases
STRING	Q922Y0.
PTM databases
PhosphoSite	Q922Y0.
Proteomic databases
PRIDE	Q922Y0.
Genome annotation databases
Ensembl	ENSMUST00000016670; ENSMUSP00000016670; ENSMUSG00000016526; Mus musculus. [Genome view]
GeneID	226419.
KEGG	mmu:226419.
UCSC	uc007cmw.1. mouse.
Organism-specific databases
CTD	226419.
MGI	MGI:1330300. Dyrk3.
Phylogenomic databases
eggNOG	roNOG05902.
HOGENOM	HBG755340.
HOVERGEN	Q922Y0.
InParanoid	Q922Y0.
OMA	SEKCSPT.
OrthoDB	EOG9909W7.
PhylomeDB	Q922Y0.
Enzyme and pathway databases
BRENDA	2.7.12.1. 244.
Gene expression databases
ArrayExpress	Q922Y0.
Bgee	Q922Y0.
Genevestigator	Q922Y0.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	378148.
SOURCE	Search...

Entry information

Entry name

DYRK3_MOUSE

Accession

Primary (citable) accession number: Q922Y0
Secondary accession number(s): Q8BM34

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	December 1, 2001
Last modified:	January 19, 2010
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)