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Protein Page:
DYRK2 (human)

Overview
DYRK2 a dual-specificity protein kinase of the DYRK family. Localizes in the cytoplasm. Phosphorylates the translation initiation factor eIF2B at Ser539, priming it for phosphorylation by glycogen synthase kinase-3. Note: This description may include information from UniProtKB.
Protein type: Protein kinase, dual-specificity (non-receptor); Protein kinase, CMGC; Kinase, protein; EC 2.7.12.1; CMGC group; DYRK family; Dyrk2 subfamily
Cellular Component: cytoplasm; nucleolus; ribonucleoprotein complex; nucleus; ubiquitin ligase complex
Molecular Function: protein serine/threonine kinase activity; protein binding; ubiquitin binding; manganese ion binding; protein-tyrosine kinase activity; magnesium ion binding; protein serine/threonine/tyrosine kinase activity; ATP binding
Biological Process: smoothened signaling pathway; peptidyl-tyrosine phosphorylation; positive regulation of glycogen biosynthetic process; negative regulation of NFAT protein import into nucleus; response to DNA damage stimulus; protein amino acid phosphorylation; DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis
Reference #:  Q92630 (UniProtKB)
Alt. Names/Synonyms: Dual specificity tyrosine-phosphorylation-regulated kinase 2; dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 2; DYRK2; FLJ21217; FLJ21365
Gene Symbols: DYRK2
Molecular weight: 66,652 Da
Basal Isoelectric point: 9.7  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

DYRK2

Protein Structure Not Found.

Substrate Sequence Logo
Sequence Logo

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Sites Implicated In
apoptosis, altered: S442‑p
enzymatic activity, induced: S442‑p
intracellular localization: T106‑p
molecular association, regulation: T106‑p
protein stabilization: T106‑p

Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 6 S30-p AVRQLQAsPGLGAGA
0 2 S48-p GVGTGPPsPIALPPL
1 0 T106-p NKRTVLTtQPNGLTT
0 1 S142-p GSSTSLKsMEGMGKV
0 3 Y380-p CYEHQRVytyIQSRF
1 12 T381-p YEHQRVytyIQSRFY
1 1640 Y382-p EHQRVytyIQSRFYR
0 2 Y388 tyIQSRFYRAPEVIL
1 0 S442-p IELLGMPsQKLLDAs
1 0 S449-p sQKLLDAsKRAKNFV
0 1 Y464-p SSKGYPRyCTVTTLS
  mouse

 
S30-p AVRQLQAsPGIGAGA
S48-p GVGTGPPsPIALPPL
T104 NKRTVLTTQPNGLTT
S140 GSSTSLKSMEGMGKV
Y378 CYEHQRVYtyIQSRF
T379-p YEHQRVYtyIQSRFY
Y380-p EHQRVYtyIQSRFYR
Y386 tyIQSRFYRAPEVIL
S440 IELLGMPSQKLLDAS
S447 SQKLLDASKRAKNFV
Y462 SSKGYPRYCTVTTLS
  rat

 
- gap
- gap
T32 NKRTVLTTQPNGLTT
S68 GSSTSLKSMEGMGKV
Y306 CYEHQRVYTyIQSRF
T307 YEHQRVYTyIQSRFy
Y308-p EHQRVYTyIQSRFyR
Y314-p TyIQSRFyRAPEVIL
S368 IELLGMPSQKLLDAS
S375 SQKLLDASKRAKNFV
Y390 SSKGYPRYCTVTTLS
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