This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Protein phosphatase
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
<StructureSection load='' size='350' side='right' scene='54/540142/Cv/1' caption='Human PP2A catalytic (green) and regulatory (cyan) subunits complex with tumor-inducing toxin and sulfate [[3k7v]]'> | <StructureSection load='' size='350' side='right' scene='54/540142/Cv/1' caption='Human PP2A catalytic (green) and regulatory (cyan) subunits complex with tumor-inducing toxin and sulfate [[3k7v]]'> | ||
| + | __TOC__ | ||
| + | |||
== Function == | == Function == | ||
'''Protein phosphatases''' (PP) or '''serine/threonine protein phosphatase''' regulate protein phosphorylation and thus are key in intracellular signal transduction processes.<br /> | '''Protein phosphatases''' (PP) or '''serine/threonine protein phosphatase''' regulate protein phosphorylation and thus are key in intracellular signal transduction processes.<br /> | ||
| Line 15: | Line 17: | ||
*<scene name='54/540142/Cv/6'>Mn+2 ion cofactors coordination site</scene>. | *<scene name='54/540142/Cv/6'>Mn+2 ion cofactors coordination site</scene>. | ||
*<scene name='54/540142/Cv/7'>Whole binding site</scene>. | *<scene name='54/540142/Cv/7'>Whole binding site</scene>. | ||
| + | == 3D Structures of protein phosphatase== | ||
| + | [[Protein phosphatase 3D structures]] | ||
| + | |||
</StructureSection> | </StructureSection> | ||
== 3D Structures of protein phosphatase== | == 3D Structures of protein phosphatase== | ||
| Line 30: | Line 35: | ||
**[[3n5u]] – hPP1A catalytic subunit + retinoblastoma-associated protein<br /> | **[[3n5u]] – hPP1A catalytic subunit + retinoblastoma-associated protein<br /> | ||
**[[4g9j]], [[5ioh]] – hPP1A catalytic subunit + peptide<br /> | **[[4g9j]], [[5ioh]] – hPP1A catalytic subunit + peptide<br /> | ||
| + | **[[6b67]] – hPP1A catalytic subunit (mutant) + peptide<br /> | ||
*Protein phosphatase 1G | *Protein phosphatase 1G | ||
| Line 38: | Line 44: | ||
**[[4da1]] - hPP1K + Mn<br /> | **[[4da1]] - hPP1K + Mn<br /> | ||
| + | **[[6ak7]] – hPP1K (mutant) + Mg<br /> | ||
| - | *Protein phosphatase 2A | + | *Protein phosphatase 2A or serine/threonine-protein phosphatase 2A |
| - | **[[1b3u]], [[2g62]], [[2hv6]] – hPP2A regulatory subunit <br /> | + | **[[1b3u]], [[2g62]], [[2hv6]], [[4mew]], [[4i5k]], [[4i5j]], [[2jak]], [[2ixm]], [[2hv7] – hPP2A regulatory subunit <br /> |
| + | **[[5swf]], [[5k6s]], [[5jja]] – hPP2A regulatory subunit + BUBR1<br /> | ||
| + | **[[5sw9]] – hPP2A regulatory subunit + REPOMAN<br /> | ||
| + | **[[2pkg]], [[2pf4]] – hPP2A regulatory subunit + small T antigen<br /> | ||
**[[2ie3]], [[2ie4]], [[2npp]], [[2nyl]], [[2nym]] – hPP2A catalytic + regulatory subunit + tumor-inducing toxin<br /> | **[[2ie3]], [[2ie4]], [[2npp]], [[2nyl]], [[2nym]] – hPP2A catalytic + regulatory subunit + tumor-inducing toxin<br /> | ||
**[[3c5w]] – hPP2A catalytic + regulatory subunit + PP2A-specific methyltransferase<br /> | **[[3c5w]] – hPP2A catalytic + regulatory subunit + PP2A-specific methyltransferase<br /> | ||
| + | **[[3p71]], [[2iae]] – hPP2A catalytic + regulatory subunit + LCMT-1 <br /> | ||
| + | **[[3dw8]] – hPP2A catalytic + regulatory subunit (mutant) + LCMT-1 <br /> | ||
| + | **[[3fga]] – hPP2A catalytic + regulatory subunit + LCMT-1 + SGO<br /> | ||
| + | **[[4i5n]], [[4i5l]] – hPP2A catalytic + regulatory subunit + MCLR<br /> | ||
| + | **[[3k7w]] – hPP2A catalytic + regulatory subunit + toxin<br /> | ||
| + | **[[4iyp]] – hPP2A catalytic subunit + immunoglobin-binding protein<br /> | ||
| + | **[[6ef4]] – mPP2A (mutant) - mouse<br /> | ||
| + | **[[5w0w]] – mPP2A + TIPRL<br /> | ||
*Protein phosphatase 2B See [[Calcineurin]] | *Protein phosphatase 2B See [[Calcineurin]] | ||
| Line 52: | Line 70: | ||
**[[4raf]], [[4rag]] - hPP2C α (mutant) + Mn<br /> | **[[4raf]], [[4rag]] - hPP2C α (mutant) + Mn<br /> | ||
**[[3d8k]] – PP2C – ''Toxoplasma gondii''<br /> | **[[3d8k]] – PP2C – ''Toxoplasma gondii''<br /> | ||
| - | **[[3jrq]], [[3nmn]] – AtPP2C + Pyl1 + pyrabactin | + | **[[3ujk]] – AtPP2C - ''Arabidopsis thaliana'' <br /> |
| + | **[[4yzg]] – AtPP2C (mutant) <br /> | ||
| + | **[[3jrq]], [[3nmn]] – AtPP2C + Pyl1 + pyrabactin <br /> | ||
**[[3kdj]] - AtPP2C + Pyl1 + abscicic acid<br /> | **[[3kdj]] - AtPP2C + Pyl1 + abscicic acid<br /> | ||
**[[3nmt]], [[3kb3]], [[3nmv]], [[3ujl]] – AtPP2C + Pyl2<br /> | **[[3nmt]], [[3kb3]], [[3nmv]], [[3ujl]] – AtPP2C + Pyl2<br /> | ||
**[[4la7]], [[4lg5]], [[4lga]], [[4lgb]] – AtPP2C + Pyl2 + ligand<br /> | **[[4la7]], [[4lg5]], [[4lga]], [[4lgb]] – AtPP2C + Pyl2 + ligand<br /> | ||
| + | **[[5vr7]], [[5vro]], [[5vs5]], [[5vsq]], [[5vsr]], [[5vt7]] – AtPP2C + Pyl2 + quinolone derivative<br /> | ||
**[[4ds8]], [[5jo1]], [[5jo2]] – AtPP2C + Pyl3 + Mn<br /> | **[[4ds8]], [[5jo1]], [[5jo2]] – AtPP2C + Pyl3 + Mn<br /> | ||
**[[3rt0]] – AtPP2C (mutant) + Pyl10<br /> | **[[3rt0]] – AtPP2C (mutant) + Pyl10<br /> | ||
**[[4n0g]] – AtPP2C + Pyl13<br /> | **[[4n0g]] – AtPP2C + Pyl13<br /> | ||
**[[3qn1]], [[3zvu]], [[4wvo]] – AtPP2C + Pyr1<br /> | **[[3qn1]], [[3zvu]], [[4wvo]] – AtPP2C + Pyr1<br /> | ||
| - | **[[ | + | **[[5or2]], [[5or6]] – AtPP2C + Pyr1 + abscicic acid analog<br /> |
| - | + | ||
**[[4yzh]] – AtPP2C (mutant) + chlorophyll-binding protein peptide<br /> | **[[4yzh]] – AtPP2C (mutant) + chlorophyll-binding protein peptide<br /> | ||
**[[3ujg]] - AtPP2C + SRK2E<br /> | **[[3ujg]] - AtPP2C + SRK2E<br /> | ||
| + | **[[5mn0]] – AtPP2C + ABA receptor <br /> | ||
*Protein phosphatase 4 | *Protein phosphatase 4 | ||
Revision as of 08:36, 2 December 2019
| |||||||||||
3D Structures of protein phosphatase
Updated on 02-December-2019 {{#tree:id=OrganizedByTopic|openlevels=0|
- Protein phosphatase 1
- 2rlt - PP1 regulatory subunit - pig - NMR
- 2rlt - PP1 regulatory subunit - pig - NMR
- Protein phosphatase 1A
- Protein phosphatase 1G
- Protein phosphatase 1K
- Protein phosphatase 2A or serine/threonine-protein phosphatase 2A
- 1b3u, 2g62, 2hv6, 4mew, 4i5k, 4i5j, 2jak, 2ixm, [[2hv7] – hPP2A regulatory subunit
- 5swf, 5k6s, 5jja – hPP2A regulatory subunit + BUBR1
- 5sw9 – hPP2A regulatory subunit + REPOMAN
- 2pkg, 2pf4 – hPP2A regulatory subunit + small T antigen
- 2ie3, 2ie4, 2npp, 2nyl, 2nym – hPP2A catalytic + regulatory subunit + tumor-inducing toxin
- 3c5w – hPP2A catalytic + regulatory subunit + PP2A-specific methyltransferase
- 3p71, 2iae – hPP2A catalytic + regulatory subunit + LCMT-1
- 3dw8 – hPP2A catalytic + regulatory subunit (mutant) + LCMT-1
- 3fga – hPP2A catalytic + regulatory subunit + LCMT-1 + SGO
- 4i5n, 4i5l – hPP2A catalytic + regulatory subunit + MCLR
- 3k7w – hPP2A catalytic + regulatory subunit + toxin
- 4iyp – hPP2A catalytic subunit + immunoglobin-binding protein
- 6ef4 – mPP2A (mutant) - mouse
- 5w0w – mPP2A + TIPRL
- 1b3u, 2g62, 2hv6, 4mew, 4i5k, 4i5j, 2jak, 2ixm, [[2hv7] – hPP2A regulatory subunit
- Protein phosphatase 2B See Calcineurin
- Protein phosphatase 2C
- 2iq1 – hPP2C κ
- 4raf, 4rag - hPP2C α (mutant) + Mn
- 3d8k – PP2C – Toxoplasma gondii
- 3ujk – AtPP2C - Arabidopsis thaliana
- 4yzg – AtPP2C (mutant)
- 3jrq, 3nmn – AtPP2C + Pyl1 + pyrabactin
- 3kdj - AtPP2C + Pyl1 + abscicic acid
- 3nmt, 3kb3, 3nmv, 3ujl – AtPP2C + Pyl2
- 4la7, 4lg5, 4lga, 4lgb – AtPP2C + Pyl2 + ligand
- 5vr7, 5vro, 5vs5, 5vsq, 5vsr, 5vt7 – AtPP2C + Pyl2 + quinolone derivative
- 4ds8, 5jo1, 5jo2 – AtPP2C + Pyl3 + Mn
- 3rt0 – AtPP2C (mutant) + Pyl10
- 4n0g – AtPP2C + Pyl13
- 3qn1, 3zvu, 4wvo – AtPP2C + Pyr1
- 5or2, 5or6 – AtPP2C + Pyr1 + abscicic acid analog
- 4yzh – AtPP2C (mutant) + chlorophyll-binding protein peptide
- 3ujg - AtPP2C + SRK2E
- 5mn0 – AtPP2C + ABA receptor
- 2iq1 – hPP2C κ
- Protein phosphatase 4
- 4wsf – PP4 regulatory subunit + Cenp-C – Drosophila melanogaster
- 4wsf – PP4 regulatory subunit + Cenp-C – Drosophila melanogaster
- Protein phosphatase 5
- 1wao – hPP5 + Mn
- 5muf – hPP5
- 1a17 – hPP5 protein-interacting domain
- 2bug – hPP5 protein-interacting domain (mutant) + Hsp90 peptide - NMR
- 1s95, 3h60 – hPP5 catalytic domain + Mn
- 3h61, 3h62, 3h63, 3h64, 3h66, 3h67, 3h68, 3h69, 4zvz, 4zx2, 4zvz, 4zx2 – hPP5 catalytic domain + inhibitor + Mn
- 5hpe – hPP5 catalytic domain/Hsp90 peptide + Mn
- 4ja7, 4ja9 - rPP5 catalytic domain + inhibitor
- 3icf - yPP5 catalytic domain + Fe - yeast
- 5jjt – AtPP5 + Ni
- 1wao – hPP5 + Mn
- Protein phosphatase
}}
References
- ↑ Ragolia L, Begum N. Protein phosphatase-1 and insulin action. Mol Cell Biochem. 1998 May;182(1-2):49-58. PMID:9609113
- ↑ Resjo S, Goransson O, Harndahl L, Zolnierowicz S, Manganiello V, Degerman E. Protein phosphatase 2A is the main phosphatase involved in the regulation of protein kinase B in rat adipocytes. Cell Signal. 2002 Mar;14(3):231-8. PMID:11812651
- ↑ Lipinszki Z, Lefevre S, Savoian MS, Singleton MR, Glover DM, Przewloka MR. Centromeric binding and activity of Protein Phosphatase 4. Nat Commun. 2015 Jan 6;6:5894. doi: 10.1038/ncomms6894. PMID:25562660 doi:http://dx.doi.org/10.1038/ncomms6894
- ↑ Chinkers M. Protein phosphatase 5 in signal transduction. Trends Endocrinol Metab. 2001 Jan-Feb;12(1):28-32. PMID:11137038
- ↑ Perrotti D, Neviani P. Protein phosphatase 2A: a target for anticancer therapy. Lancet Oncol. 2013 May;14(6):e229-38. doi: 10.1016/S1470-2045(12)70558-2. PMID:23639323 doi:http://dx.doi.org/10.1016/S1470-2045(12)70558-2
- ↑ Rudrabhatla P, Pant HC. Role of protein phosphatase 2A in Alzheimer's disease. Curr Alzheimer Res. 2011 Sep;8(6):623-32. PMID:21605044
- ↑ Huhn J, Jeffrey PD, Larsen K, Rundberget T, Rise F, Cox NR, Arcus V, Shi Y, Miles CO. A structural basis for the reduced toxicity of dinophysistoxin-2. Chem Res Toxicol. 2009 Nov;22(11):1782-6. PMID:19916524 doi:10.1021/tx9001622
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Alexsandra Tifane Santos do Nascimento, Joel L. Sussman

