O43781 (DYRK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Regulatory erythroid kinase
Short name=REDK

Gene names

Name:

DYRK3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	588 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.4
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Subcellular location	Nucleus Ref.4.
Tissue specificity	Isoform 1 and isoform 2 are highly expressed in testis and in hematopoietic tissue such as fetal liver, and bone marrow. Isoform 2 is the predominant form in testis. Isoform 1 is the predominant form in fetal liver and bone marrow. Isoform 1 and isoform 2 are present at low levels in heart, pancreas, lymph node, and thymus. Ref.4
Induction	By EPO/erythropoietin. Ref.4
Post-translational modification	Autophosphorylated on tyrosine residues.
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
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Magnesium Metal-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	erythrocyte differentiation Inferred from direct assay Ref.4. Source: UniProtKB
Cellular_component	nucleus Inferred from direct assay Ref.4. Source: UniProtKB
Molecular_function	ATP binding Inferred from direct assay Ref.4. Source: UniProtKB magnesium ion binding Inferred from direct assay Ref.4. Source: UniProtKB protein kinase activity Inferred from direct assay Ref.4. Source: UniProtKB protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine/tyrosine kinase activity Inferred from electronic annotation. Source: EC protein tyrosine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O43781-1)

Also known as: Long;

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.

Isoform 2 (identifier: O43781-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: Missing.
     21-26: PPQQRR → MKWKEK

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 588	588	Dual specificity tyrosine-phosphorylation-regulated kinase 3		PRO_0000085938
Regions
	Domain	209 – 522	314	Protein kinase
	Nucleotide binding	215 – 223	9	ATP By similarity
Sites
	Active site	335	1	Proton acceptor By similarity
	Binding site	238	1	ATP By similarity
Amino acid modifications
	Modified residue	318	1	Phosphoserine By similarity
	Modified residue	369	1	Phosphotyrosine By similarity
Natural variations
	Alternative sequence	1 – 20	20	Missing in isoform 2.		VSP_026178
	Alternative sequence	21 – 26	6	PPQQRR → MKWKEK in isoform 2.		VSP_026179
	Natural variant	239	1	M → L. Ref.10		VAR_040464
Experimental info
	Sequence conflict	313	1	R → H in AAH15501. Ref.9
	Sequence conflict	396	1	G → R in CAA73266. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified June 26, 2007. Version 3. Checksum: 9950F51C39AFED82	FASTA	588	65,714
	10 20 30 40 50 60 MGGTARGPGR KDAGPPGAGL PPQQRRLGDG VYDTFMMIDE TKCPPCSNVL CNPSEPPPPR 70 80 90 100 110 120 RLNMTTEQFT GDHTQHFLDG GEMKVEQLFQ EFGNRKSNTI QSDGISDSEK CSPTVSQGKS 130 140 150 160 170 180 SDCLNTVKSN SSSKAPKVVP LTPEQALKQY KHHLTAYEKL EIINYPEIYF VGPNAKKRHG 190 200 210 220 230 240 VIGGPNNGGY DDADGAYIHV PRDHLAYRYE VLKIIGKGSF GQVARVYDHK LRQYVALKMV 250 260 270 280 290 300 RNEKRFHRQA AEEIRILEHL KKQDKTGSMN VIHMLESFTF RNHVCMAFEL LSIDLYELIK 310 320 330 340 350 360 KNKFQGFSVQ LVRKFAQSIL QSLDALHKNK IIHCDLKPEN ILLKHHGRSS TKVIDFGSSC 370 380 390 400 410 420 FEYQKLYTYI QSRFYRAPEI ILGSRYSTPI DIWSFGCILA ELLTGQPLFP GEDEGDQLAC 430 440 450 460 470 480 MMELLGMPPP KLLEQSKRAK YFINSKGIPR YCSVTTQADG RVVLVGGRSR RGKKRGPPGS 490 500 510 520 530 540 KDWGTALKGC DDYLFIEFLK RCLHWDPSAR LTPAQALRHP WISKSVPRPL TTIDKVSGKR 550 560 570 580 VVNPASAFQG LGSKLPPVVG IANKLKANLM SETNGSIPLC SVLPKLIS
	Isoform 2 (Short) [UniParc]. Checksum: 9B710ECC413873F7	FASTA	568	63,977
	10 20 30 40 50 60 MKWKEKLGDG VYDTFMMIDE TKCPPCSNVL CNPSEPPPPR RLNMTTEQFT GDHTQHFLDG 70 80 90 100 110 120 GEMKVEQLFQ EFGNRKSNTI QSDGISDSEK CSPTVSQGKS SDCLNTVKSN SSSKAPKVVP 130 140 150 160 170 180 LTPEQALKQY KHHLTAYEKL EIINYPEIYF VGPNAKKRHG VIGGPNNGGY DDADGAYIHV 190 200 210 220 230 240 PRDHLAYRYE VLKIIGKGSF GQVARVYDHK LRQYVALKMV RNEKRFHRQA AEEIRILEHL 250 260 270 280 290 300 KKQDKTGSMN VIHMLESFTF RNHVCMAFEL LSIDLYELIK KNKFQGFSVQ LVRKFAQSIL 310 320 330 340 350 360 QSLDALHKNK IIHCDLKPEN ILLKHHGRSS TKVIDFGSSC FEYQKLYTYI QSRFYRAPEI 370 380 390 400 410 420 ILGSRYSTPI DIWSFGCILA ELLTGQPLFP GEDEGDQLAC MMELLGMPPP KLLEQSKRAK 430 440 450 460 470 480 YFINSKGIPR YCSVTTQADG RVVLVGGRSR RGKKRGPPGS KDWGTALKGC DDYLFIEFLK 490 500 510 520 530 540 RCLHWDPSAR LTPAQALRHP WISKSVPRPL TTIDKVSGKR VVNPASAFQG LGSKLPPVVG 550 560 IANKLKANLM SETNGSIPLC SVLPKLIS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence characteristics, subcellular localization, and substrate specificity of DYRK-related kinases, a novel family of dual specificity protein kinases." Becker W., Weber Y., Wetzel K., Eirmbter K., Tejedor F.J., Joost H.-G. J. Biol. Chem. 273:25893-25902(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Fetal brain.
[2]	Becker W. Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO N-TERMINUS.
[3]	"Molecular cloning and characterization of novel protein kinase gene DYRK3." Xia J., Yang X., Ruan Q., Pan Q., Liu C., Xie W., Deng H. Zhonghua Yi Xue Yi Chuan Xue Za Zhi 15:327-332(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"REDK, a novel human regulatory erythroid kinase." Lord K.A., Creasy C.L., King A.G., King C., Burns B.M., Lee J.C., Dillon S.B. Blood 95:2838-2846(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION. Tissue: Skeletal muscle.
[5]	"Cloning of the human testis-specific dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 5 (DYRK5) gene." Zhou Z.M. Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Testis.
[6]	Raya A., de la Luna S. Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[7]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Uterus.
[10]	"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] LEU-239.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y12735 mRNA. Translation: CAA73266.2. AF186773 mRNA. Translation: AAG17028.1. AF186774 mRNA. Translation: AAG17029.1. AF327561 mRNA. Translation: AAK16443.1. AY590695 mRNA. Translation: AAT06103.1. AL591846 Genomic DNA. Translation: CAI13539.1. AL591846 Genomic DNA. Translation: CAI13541.1. CH471100 Genomic DNA. Translation: EAW93533.1. CH471100 Genomic DNA. Translation: EAW93534.1. BC015501 mRNA. Translation: AAH15501.1.
IPI	IPI00465459. IPI00744096.
RefSeq	NP_001004023.1. NM_001004023.1. NP_003573.2. NM_003582.2.
UniGene	Hs.164267.
3D structure databases
ProteinModelPortal	O43781.
ModBase	Search...
Protein-protein interaction databases
IntAct	O43781. 2 interactions.
STRING	9606.ENSP00000356076.
PTM databases
PhosphoSite	O43781.
Proteomic databases
PaxDb	O43781.
PRIDE	O43781.
Protocols and materials databases
DNASU	8444.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000367106; ENSP00000356073; ENSG00000143479. ENST00000367108; ENSP00000356075; ENSG00000143479. ENST00000367109; ENSP00000356076; ENSG00000143479. ENST00000578483; ENSP00000463587; ENSG00000265184. ENST00000581534; ENSP00000462982; ENSG00000265184. ENST00000584909; ENSP00000463633; ENSG00000265184.
GeneID	8444.
KEGG	hsa:8444.
UCSC	uc001hei.3. human. uc001hej.3. human.
Organism-specific databases
CTD	8444.
GeneCards	GC01P206800.
HGNC	HGNC:3094. DYRK3.
MIM	603497. gene.
neXtProt	NX_O43781.
PharmGKB	PA27551.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000220863.
HOVERGEN	HBG051426.
InParanoid	O43781.
KO	K08825.
OMA	LKQYKHH.
OrthoDB	EOG48GW2W.
PhylomeDB	O43781.
Enzyme and pathway databases
BRENDA	2.7.12.1. 2681.
Gene expression databases
ArrayExpress	O43781.
Bgee	O43781.
CleanEx	HS_DYRK3.
Genevestigator	O43781.
GermOnline	ENSG00000143479. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
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
BindingDB	O43781.
ChEMBL	CHEMBL4575.
GenomeRNAi	8444.
NextBio	31590.
SOURCE	Search...

Entry information

Entry name

DYRK3_HUMAN

Accession

Primary (citable) accession number: O43781
Secondary accession number(s): D3DT79 , Q7Z752, Q9HBY6, Q9HBY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	June 26, 2007
Last modified:	May 1, 2013
This is version 127 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.