Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (Oryctolagus cuniculus)

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Basic Information
Short Name PP-1A, PPP1A, PPP1CA
UNP ID P62136
Organism Oryctolagus cuniculus
Cys Site Cys273
Family/Domain PPP phosphatase family,
PP-1 subfamily
Known Ligand Ligand list
Function Type Phosphatase,
Post-translational Modification

Summary

Protein Function

Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets.
Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. (From Uniprot)

Cys Function & Property

Cys273 is close to the active site and the manganese ions in space.

  • Hydrophobic property:
531-hydro.png
  • SASA：
Cys273: 21.427 A^2

Protein Sequence

MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP
ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS
LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK
TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL
LCDLLWSDPD KDVQGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV
VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAD
KNKGKYGQFS GLNPGGRPIT PPRNSAKAKK

Structural Information

  • Known structures with covalent ligands:
1FJM
  • Protein structure:
531.png

Related Pathway

Experimental Evidence

Cys-directed Mutation, Isotope Labeling

Reference

  1. Pereira S R, Vasconcelos V M, Antunes A. Computational study of the covalent bonding of microcystins to cysteine residues–a reaction involved in the inhibition of the PPP family of protein phosphatases[J]. The FEBS journal, 2013, 280(2): 674-680. 22177231
  2. Goldberg J, Huang H, Kwon Y, et al. Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1[J]. Nature, 1995, 376(6543): 745. 7651533
  3. MacKintosh C, Beattie K A, Klumpp S, et al. Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants[J]. FEBS letters, 1990, 264(2): 187-192. 2162782
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