Dual specificity phosphatase

spinqualitylabelsall models Human Cdc14B2 core domain (cyan) complex with tripeptide (green) and acetyl (PDB code 1ohe). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Dual specificity phosphatase (DUSP) is a phosphatase which dephosphorylates phosphotyrosine, phosphoserine or phosphothreonine residues. There are several DUSP enzymes in mammals sharing a common catalytic mechanism. The DUSP include: • Slingshot phosphatase • Phosphatase of regenerating liver (PRL) • Cdc14 leads to mitotic exit by dephosphorylation of targets of the protein kinase Cdk1. • Cdc25 activates Cdk1 by its dephosphorylation. • PTEN (Phosphatase and TEnsin homolog) dephosphorylates phosphasitide substrates. For details see PTEN. • Myotubularin dephosphorylates phosphadinylinositol 3-phosphate and phosphadinylinositol (3,5)-bi-phosphate • MAPK phosphatase see MAP kinase phosphatase Relevance Cdc25A and Cdc25B are overexpressed in several types of cancers and their inhibitors are being tested as chemotherapeutic agents. PTEN gene is mutated with high frequency in a variety of human cancers. Phosphatase of regenerating liver is overexpressed in several types of cancers. Disease Myotubularin mutations are responsible for the hereditary motor disease Charcot-Marie-Tooth disease. Structural highlights Tripeptide binding site in human Cdc14B2 (PDB code 1ohe). 3D structures of dual specificity phosphatase Dual specificity phosphatase 3D structures

3D structures of dual specificity phosphatase

Updated on 18-June-2019

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• Dual specificity phosphatase
  • PTEN – hDUSP 7 catalytic domain (mutant) - human
    
  • MAP kinase phosphatase – hDUSP 13A (mutant)
    
  • 1ohe – hDUSP 16 residues 156-301 + MAPK 8
    
  • Dual specificity phosphatase 3D structures – hDUSP 22 (mutant) + nitrophenolphosphate
    
  • 5gtj – hDUSP 26 (mutant)
    
  • 5y15, 5y16 – hDUSP 28 (mutant)
    
• Slingshot phosphatase (SSH)
  • 2nt2 – hSSH-2L catalytic domain - human
    
• Phosphatase of regenerating liver (PRL) or protein tyrosine phosphatase type IVA
  • 1rxd – hPRL-1
    
  • 1xm2 – hPRL-1 (mutant)
    
  • 5bx1 – hPRL-1 + inhibitor
    
  • 1zck, 1x24 – rPRL-1 - rat
    
  • 1zcl – rPRL-1 (mutant)
    
  • 3rz2 – rPRL-1 + peptide
    
  • 5mmz, 5lxq – mPRL-1 + magnesium transporter - mouse
    
  • 5k24 – mPRL-2 + magnesium transporter
    
  • 5k25, 5k23 – hPRL-2 + magnesium transporter
    
  • 5k22 – hPRL-2 (mutant) + magnesium transporter
    
  • 1r6h, 1v3a, 2mbc – hPRL-3 - NMR
    
  • 5tsr – hPRL-3 + magnesium transporter
    
• Cdc14
  • 1ohc, 1ohd – hCdc14B2 core domain
    
  • 1ohe – hCdc14B2 core domain + peptide
    
  • 6g86 – hCdc14 + SIC1 peptide
    
  • 6g85, 6g84 – hCdc14 + CBK1 peptide
    
  • 5xw5 – hCdc14 + SWI6P peptide
    
  • 5xw4 – yCdc14 - yeast
    
  • 4zj7 – yCdc14 C-terminal + importin
    
• Cdc25
  • 1qb0, 1cwr, 1cws, 1cwt, 1ym9, 1ymd, 1ymk, 1yml, 1ys0, 2uzq – hCdc25B catalytic domain
    
  • 2a2k, 2ifd, 2ifv – hCdc25B catalytic domain (mutant)
    
• Phosphoinositide phosphatase PTEN
  • 1d5r, 5bzz, 5bzx, 5bug – hPTEN (mutant)
    
• Phosphoinositide phosphatase Sac1
  • 3lwt – ySac1
    
  • 4tu3 – ySac1 + VPS74
    
• Phosphoinositide phosphatase Sac2
  • 4xuu – hSac2 residues 169-563
    
• Myotubularin-related protein (MTMR)
  • 1zvr – hMTMR2 PH-gram and phosphatase domains (mutant)
    
  • 1zsq - hMTMR2 PH-gram and phosphatase domains (mutant) + phosphatidylinositol 3-phosphate
    
  • 1m7r, 1lw3 - hMTMR2 PH-gram and phosphatase domains (mutant) + phosphate
    
  • 2yf0 – hMTMR6
    

Myotubularin-related protein 15 (MTMR15) or Fanconi-associated nuclease 1

• • 4rid, 4ry3 – hMTMR15 residues 370-1009
    
  • 4rec, 4ri8, 4ri9, 4ria, 4rib, 4ric, 4reb, 4rea – hMTMR15 (mutant) + DNA
    
• MAPK phosphatase see MAP kinase phosphatase

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