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Q4V8A3 (DYRK3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dual specificity tyrosine-phosphorylation-regulated kinase 3

EC=2.7.12.1
Gene names
Name:Dyrk3
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length586 AA.
Sequence statusComplete.
Protein existenceEvidence 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 By similarity. UniProtKB O43781 UniProtKB Q922Y0

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. UniProtKB O43781 UniProtKB Q922Y0

Cofactor

Magnesium By similarity. UniProtKB O43781 UniProtKB Q922Y0

Subcellular location

Nucleus By similarity UniProtKB O43781.

Tissue specificity

Expressed in late pachytene spermatocytes. Ref.2

Post-translational modification

Autophosphorylated on tyrosine residues By similarity. UniProtKB O43781

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 586586Dual specificity tyrosine-phosphorylation-regulated kinase 3
PRO_0000291538

Regions

Domain208 – 521314Protein kinase
Nucleotide binding214 – 2229ATP By similarity UniProtKB P28523

Sites

Active site3341Proton acceptor By similarity UniProtKB P28523
Binding site2371ATP By similarity UniProtKB Q922Y0

Amino acid modifications

Modified residue2081Phosphotyrosine By similarity UniProtKB O43781
Modified residue3171Phosphoserine By similarity
Modified residue3681Phosphotyrosine By similarity UniProtKB Q922Y0

Sequences

Sequence LengthMass (Da)Tools
Q4V8A3 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 9E194D2F960FBE94

FASTA58665,511
        10         20         30         40         50         60 
MGGAARERGR KDAALPGAGL PPQQRRLGDG VYDTFMMIDE TKCPPYTNTL CNPSEAPVSR 

        70         80         90        100        110        120 
RLNITTEPFT RGHTQHFVSG GVMKVEQLFQ EFGSRRTSTL QSDGVSNSEK SSPASQGKSS 

       130        140        150        160        170        180 
DSLGTVKCSL SSRPSKVLPL TPEQALKQYK HHLTAYEKLE IISYPEIYFV 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 
MELLGMPPQK LLEQSKRAKY FINSKGLPRY CSVTTQTDGR VVLLGGRSRR GKKRGPPGSK 

       490        500        510        520        530        540 
DWAAALKGCD DYLFIEFLKR CLQWDPSARL TPAQALRHPW ISKSAPRPLT TDKVSGKRVV 

       550        560        570        580 
NPTNAFQGLG SKLPPVVGIA SKLKANLMSE TSGSIPLCSV LPKLIS 

« Hide

References

« Hide '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].
Tissue: Testis.
[2]"The expression of the testis-specific Dyrk4 kinase is highly restricted to step 8 spermatids but is not required for male fertility in mice."
Sacher F., Moeller C., Bone W., Gottwald U., Fritsch M.
Mol. Cell. Endocrinol. 267:80-88(2007) [PubMed: 17292540] [Abstract]
Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC097474 mRNA. Translation: AAH97474.1.
IPIIPI00371936.
RefSeqNP_001019938.1. NM_001024767.1.
UniGeneRn.162390.

3D structure databases

HSSPHSSP built from PDB template 2BAJ based on UniProtKB Q16539.
ProteinModelPortalQ4V8A3.
ModBaseSearch...

PTM databases

PhosphoSiteQ4V8A3.

Proteomic databases

PRIDEQ4V8A3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID304775.
KEGGrno:304775.

Organism-specific databases

CTD8444.
RGD1310924. Dyrk3.

Phylogenomic databases

eggNOGroNOG05902.
GeneTreeENSGT00570000079111.
HOVERGENHBG051426.
InParanoidQ4V8A3.
OrthoDBEOG48GW2W.
PhylomeDBQ4V8A3.

Gene expression databases

ArrayExpressQ4V8A3.
GenevestigatorQ4V8A3.

Family and domain databases

InterProIPR011009. 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]
KOK08825.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio653596.

Entry information

Entry nameDYRK3_RAT
AccessionPrimary (citable) accession number: Q4V8A3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: July 5, 2005
Last modified: November 16, 2011
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families