Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform

From Cysteinome
Jump to: navigation, search
Basic Information
Short Name PP2A-alpha, PPP2CA,
RP-C
UNP ID P67775
Organism Homo sapiens
Cys Site Cys269
Family/Domain PPP phosphatase family,
PP-1 subfamily
Known Ligand Ligand list
Function Type Phosphatase,
Post-translational Modification

Summary

Protein Function

PP2A consists of a dimeric core enzyme composed of the structural A and catalytic C subunits, and a regulatory B subunit. When the PP2A catalytic C subunit associates with the A and B subunits several species of holoenzymes are produced with distinct functions and characteristics. The A subunit, a founding member of the HEAT repeat protein family (huntington-elongation-A subunit-TOR), is the scaffold required for the formation of the heterotrimeric complex. When the A subunit binds it alters the enzymatic activity of the catalytic subunit, even if the B subunit is absent. While C and A subunit sequences show remarkable sequence conservation throughout eukaryotes, regulatory B subunits are more heterogeneous and are believed to play key roles in controlling the localization and specific activity of different holoenzymes. (From Wikipedia)

Cys Function & Property

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

  • Hydrophobic property:
531-hydro.png
  • SASA：
Cys273: 31.279 A^2

Protein Sequence

MDEKVFTKEL DQWIEQLNEC KQLSESQVKS LCEKAKEILT KESNVQEVRC
PVTVCGDVHG QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL
VALKVRYRER ITILRGNHES RQITQVYGFY DECLRKYGNA NVWKYFTDLF
DYLPLTALVD GQIFCLHGGL SPSIDTLDHI RALDRLQEVP HEGPMCDLLW
SDPDDRGGWG ISPRGAGYTF GQDISETFNH ANGLTLVSRA HQLVMEGYNW
CHDRNVVTIF SAPNYCYRCG NQAAIMELDD TLKYSFLQFD PAPRRGEPHV
TRRTPDYFL

Structural Information

  • Known structures with covalent ligands:
2IE3, 4I5N
  • 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. MacKintosh R W, Dalby K N, Campbell D G, et al. The cyanobacterial toxin microcystin binds covalently to cysteine-273 on protein phosphatase 1[J]. Febs Letters, 1995, 371(3): 236-240. 7556599
  3. Hastie C J, Borthwick E B, Morrison L F, et al. Inhibition of several protein phosphatases by a non-covalently interacting microcystin and a novel cyanobacterial peptide, nostocyclin[J]. Biochimica et Biophysica Acta (BBA)-General Subjects, 2005, 1726(2): 187-193. 16046071
Retrieved from "http://173.199.123.204/Cysteinome/index.php?title=Serine/threonine-protein_phosphatase_2A_catalytic_subunit_alpha_isoform&oldid=1595"