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Protein

Dual specificity tyrosine-phosphorylation-regulated kinase 3

Gene

DYRK3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

Inhibited by harmine, leucettamine B and leucettine L41.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei238 – 2381ATPPROSITE-ProRule annotation
Active sitei335 – 3351Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi215 – 2239ATPPROSITE-ProRule annotation
Nucleotide bindingi288 – 2914ATPPROSITE-ProRule annotation

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-KW
  • protein tyrosine kinase activity Source: UniProtKB-KW

GO - Biological processi

  • erythrocyte differentiation Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.12.1. 2681.
SignaLinkiO43781.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity tyrosine-phosphorylation-regulated kinase 3 (EC:2.7.12.1)
Alternative name(s):
Regulatory erythroid kinase
Short name:
REDK
Gene namesi
Name:DYRK3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3094. DYRK3.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27551.

Polymorphism and mutation databases

BioMutaiDYRK3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 588588Dual specificity tyrosine-phosphorylation-regulated kinase 3PRO_0000085938Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei369 – 3691PhosphotyrosineBy similarity

Post-translational modificationi

Autophosphorylated on tyrosine residues.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO43781.
PaxDbiO43781.
PRIDEiO43781.

PTM databases

PhosphoSiteiO43781.

Expressioni

Tissue specificityi

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.1 Publication

Inductioni

By EPO/erythropoietin.1 Publication

Gene expression databases

BgeeiO43781.
CleanExiHS_DYRK3.
ExpressionAtlasiO43781. baseline and differential.
GenevestigatoriO43781.

Interactioni

Protein-protein interaction databases

BioGridi114022. 5 interactions.
IntActiO43781. 4 interactions.
STRINGi9606.ENSP00000356076.

Structurei

3D structure databases

ProteinModelPortaliO43781.
SMRiO43781. Positions 137-556.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini209 – 522314Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119032.
HOGENOMiHOG000220863.
HOVERGENiHBG051426.
InParanoidiO43781.
KOiK18669.
OMAiLKQYKHH.
PhylomeDBiO43781.
TreeFamiTF314624.

Family and domain databases

InterProiIPR011009. 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]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O43781-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGGTARGPGR KDAGPPGAGL PPQQRRLGDG VYDTFMMIDE TKCPPCSNVL
60 70 80 90 100
CNPSEPPPPR RLNMTTEQFT GDHTQHFLDG GEMKVEQLFQ EFGNRKSNTI
110 120 130 140 150
QSDGISDSEK CSPTVSQGKS SDCLNTVKSN SSSKAPKVVP LTPEQALKQY
160 170 180 190 200
KHHLTAYEKL EIINYPEIYF VGPNAKKRHG VIGGPNNGGY DDADGAYIHV
210 220 230 240 250
PRDHLAYRYE VLKIIGKGSF GQVARVYDHK LRQYVALKMV RNEKRFHRQA
260 270 280 290 300
AEEIRILEHL KKQDKTGSMN VIHMLESFTF RNHVCMAFEL LSIDLYELIK
310 320 330 340 350
KNKFQGFSVQ LVRKFAQSIL QSLDALHKNK IIHCDLKPEN ILLKHHGRSS
360 370 380 390 400
TKVIDFGSSC FEYQKLYTYI QSRFYRAPEI ILGSRYSTPI DIWSFGCILA
410 420 430 440 450
ELLTGQPLFP GEDEGDQLAC MMELLGMPPP KLLEQSKRAK YFINSKGIPR
460 470 480 490 500
YCSVTTQADG RVVLVGGRSR RGKKRGPPGS KDWGTALKGC DDYLFIEFLK
510 520 530 540 550
RCLHWDPSAR LTPAQALRHP WISKSVPRPL TTIDKVSGKR VVNPASAFQG
560 570 580
LGSKLPPVVG IANKLKANLM SETNGSIPLC SVLPKLIS
Length:588
Mass (Da):65,714
Last modified:June 26, 2007 - v3
Checksum:i9950F51C39AFED82
GO
Isoform 2 (identifier: O43781-2) [UniParc]FASTAAdd to basket

Also known as: Short

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

Show »
Length:568
Mass (Da):63,977
Checksum:i9B710ECC413873F7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti313 – 3131R → H in AAH15501 (PubMed:15489334).Curated
Sequence conflicti396 – 3961G → R in CAA73266 (PubMed:9748265).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti239 – 2391M → L.1 Publication
VAR_040464

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2020Missing in isoform 2. 3 PublicationsVSP_026178Add
BLAST
Alternative sequencei21 – 266PPQQRR → MKWKEK in isoform 2. 3 PublicationsVSP_026179

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS30999.1. [O43781-1]
CCDS31000.1. [O43781-2]
RefSeqiNP_001004023.1. NM_001004023.1. [O43781-2]
NP_003573.2. NM_003582.2. [O43781-1]
XP_005273372.1. XM_005273315.3. [O43781-2]
XP_005273373.1. XM_005273316.2. [O43781-2]
XP_006711639.1. XM_006711576.2. [O43781-2]
UniGeneiHs.164267.

Genome annotation databases

EnsembliENST00000367106; ENSP00000356073; ENSG00000143479. [O43781-2]
ENST00000367108; ENSP00000356075; ENSG00000143479. [O43781-2]
ENST00000367109; ENSP00000356076; ENSG00000143479. [O43781-1]
GeneIDi8444.
KEGGihsa:8444.
UCSCiuc001hei.3. human. [O43781-2]
uc001hej.3. human. [O43781-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS30999.1. [O43781-1]
CCDS31000.1. [O43781-2]
RefSeqiNP_001004023.1. NM_001004023.1. [O43781-2]
NP_003573.2. NM_003582.2. [O43781-1]
XP_005273372.1. XM_005273315.3. [O43781-2]
XP_005273373.1. XM_005273316.2. [O43781-2]
XP_006711639.1. XM_006711576.2. [O43781-2]
UniGeneiHs.164267.

3D structure databases

ProteinModelPortaliO43781.
SMRiO43781. Positions 137-556.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114022. 5 interactions.
IntActiO43781. 4 interactions.
STRINGi9606.ENSP00000356076.

Chemistry

BindingDBiO43781.
ChEMBLiCHEMBL4575.
GuidetoPHARMACOLOGYi2012.

PTM databases

PhosphoSiteiO43781.

Polymorphism and mutation databases

BioMutaiDYRK3.

Proteomic databases

MaxQBiO43781.
PaxDbiO43781.
PRIDEiO43781.

Protocols and materials databases

DNASUi8444.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367106; ENSP00000356073; ENSG00000143479. [O43781-2]
ENST00000367108; ENSP00000356075; ENSG00000143479. [O43781-2]
ENST00000367109; ENSP00000356076; ENSG00000143479. [O43781-1]
GeneIDi8444.
KEGGihsa:8444.
UCSCiuc001hei.3. human. [O43781-2]
uc001hej.3. human. [O43781-1]

Organism-specific databases

CTDi8444.
GeneCardsiGC01P206800.
HGNCiHGNC:3094. DYRK3.
MIMi603497. gene.
neXtProtiNX_O43781.
PharmGKBiPA27551.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119032.
HOGENOMiHOG000220863.
HOVERGENiHBG051426.
InParanoidiO43781.
KOiK18669.
OMAiLKQYKHH.
PhylomeDBiO43781.
TreeFamiTF314624.

Enzyme and pathway databases

BRENDAi2.7.12.1. 2681.
SignaLinkiO43781.

Miscellaneous databases

ChiTaRSiDYRK3. human.
GeneWikiiDYRK3.
GenomeRNAii8444.
NextBioi31590.
PROiO43781.
SOURCEiSearch...

Gene expression databases

BgeeiO43781.
CleanExiHS_DYRK3.
ExpressionAtlasiO43781. baseline and differential.
GenevestigatoriO43781.

Family and domain databases

InterProiIPR011009. 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]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiDYRK3_HUMAN
AccessioniPrimary (citable) accession number: O43781
Secondary accession number(s): D3DT79
, Q7Z752, Q9HBY6, Q9HBY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: June 26, 2007
Last modified: May 27, 2015
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.