Difference between revisions of "Phosphatase Subfamily SCP"

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[[Phosphatase classification|Phosphatase Classification]]:  [[Phosphatase_Fold_HAD|Fold HAD]]: [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_FCP|Family FCP]]: [[Phosphatase_Subfamily_SCP|Subfamily SCP]]
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__NOTOC__
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[[Phosphatase classification|Phosphatase Classification]]:  [[Phosphatase_Fold_HAD|Fold HAD]]: [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_FCP|Family FCP]]: [[Phosphatase_Subfamily_SCP|Subfamily SCP]] (Small CTD Phosphatase)
  
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SCP is named after Small CTD (carboxy-terminal domain, RNA polymerase II, polypeptide A) phosphatase.
  
=== Introduction ===
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=== Evolution ===
SCP is named after Small CTD (carboxy-terminal domain, RNA polymerase II, polypeptide A) phosphatase. This subfamily has three members in human, SCP1 (or CTDSP1), SCP2 (or CTDSP2), and SCP3 (or CTDSPL). They are present in neuronal progenitor cells and nonneuronal cells and targets neuronal genes by interacting with the REST/NRSF complext. The SCP1 is a transcriptional corepressor for inhibiting neuronal gene transcription in non-neuronal cells. For its molecular function, the SCP1 prefers to dephosphorylate pSer5 at CTD <cite>Zhang06</cite>.
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SCP is conserved from yeast to human. The SCP subfamily has three members in human, SCP1 (or CTDSP1), SCP2 (or CTDSP2), and SCP3 (or CTDSPL). CTDSPL2 is a member of a different subfamily.
  
=== Substrates and Related Kinases ===
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=== Domain Combination ===
See [[CTD_Phosphorylation|Phosphorylation of RNA polymerase II C-terminal domain]].
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SCP has a single phosphatase domain of HAD fold.
  
=== Evolutionary History ===
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=== Functions ===
SCP is conserved from yeast to human.
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Human SCPs are present in neuronal progenitor cells and nonneuronal cells and targets neuronal genes by interacting with the REST/NRSF complex.  
  
=== Domain Combination ===
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===== SCP1 (CTDSP1) =====
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Human SCP1 prefers to dephosphorylate pSer5 at CTD <cite>Zhang06</cite>. See [[CTD_Phosphorylation|Phosphorylation of RNA polymerase II C-terminal domain]] for other CTD phosphatases.
  
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SCP1 also dephosphorylates c-Myc at Serine-62 which affects its stability in cancer cells <cite>Wang15</cite>.
  
=== Catalytic activity ===
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The SCP1 is a transcriptional corepressor for inhibiting neuronal gene transcription in non-neuronal cells.
  
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===== SCP3 (CTDSPL) =====
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SCP3 dephosphorylates the linker sites of R-Smads to ensure TGFβ-mediated germ layer induction in Xenopus embryos <cite>Sun15</cite>.
  
== References ==
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=== References ===
 
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<biblio>
 
<biblio>
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#Sun15 pmid=26013826
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#Wang15 pmid=25893300
 
#Zhang06 pmid=17157258
 
#Zhang06 pmid=17157258
 
</biblio>
 
</biblio>
  
 
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=== Links ===
== Links ==
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[http://www.ncbi.nlm.nih.gov/gene/58190 Human CTDSP1], [http://www.ncbi.nlm.nih.gov/gene/10106 CTDSP2], and [http://www.ncbi.nlm.nih.gov/gene/10217 CTDSPL] from NCBI Gene
 
[http://www.ncbi.nlm.nih.gov/gene/58190 Human CTDSP1], [http://www.ncbi.nlm.nih.gov/gene/10106 CTDSP2], and [http://www.ncbi.nlm.nih.gov/gene/10217 CTDSPL] from NCBI Gene

Latest revision as of 01:01, 22 March 2017

Phosphatase Classification: Fold HAD: Superfamily HAD: Family FCP: Subfamily SCP (Small CTD Phosphatase)

SCP is named after Small CTD (carboxy-terminal domain, RNA polymerase II, polypeptide A) phosphatase.

Evolution

SCP is conserved from yeast to human. The SCP subfamily has three members in human, SCP1 (or CTDSP1), SCP2 (or CTDSP2), and SCP3 (or CTDSPL). CTDSPL2 is a member of a different subfamily.

Domain Combination

SCP has a single phosphatase domain of HAD fold.

Functions

Human SCPs are present in neuronal progenitor cells and nonneuronal cells and targets neuronal genes by interacting with the REST/NRSF complex.

SCP1 (CTDSP1)

Human SCP1 prefers to dephosphorylate pSer5 at CTD [1]. See Phosphorylation of RNA polymerase II C-terminal domain for other CTD phosphatases.

SCP1 also dephosphorylates c-Myc at Serine-62 which affects its stability in cancer cells [2].

The SCP1 is a transcriptional corepressor for inhibiting neuronal gene transcription in non-neuronal cells.

SCP3 (CTDSPL)

SCP3 dephosphorylates the linker sites of R-Smads to ensure TGFβ-mediated germ layer induction in Xenopus embryos [3].

References

  1. Zhang Y, Kim Y, Genoud N, Gao J, Kelly JW, Pfaff SL, Gill GN, Dixon JE, and Noel JP. Determinants for dephosphorylation of the RNA polymerase II C-terminal domain by Scp1. Mol Cell. 2006 Dec 8;24(5):759-770. DOI:10.1016/j.molcel.2006.10.027 | PubMed ID:17157258 | HubMed [Zhang06]
  2. Wang W, Liao P, Shen M, Chen T, Chen Y, Li Y, Lin X, Ge X, and Wang P. SCP1 regulates c-Myc stability and functions through dephosphorylating c-Myc Ser62. Oncogene. 2016 Jan 28;35(4):491-500. DOI:10.1038/onc.2015.106 | PubMed ID:25893300 | HubMed [Wang15]
  3. Sun G, Hu Z, Min Z, Yan X, Guan Z, Su H, Fu Y, Ma X, Chen YG, Zhang MQ, Tao Q, and Wu W. Small C-terminal Domain Phosphatase 3 Dephosphorylates the Linker Sites of Receptor-regulated Smads (R-Smads) to Ensure Transforming Growth Factor β (TGFβ)-mediated Germ Layer Induction in Xenopus Embryos. J Biol Chem. 2015 Jul 10;290(28):17239-49. DOI:10.1074/jbc.M115.655605 | PubMed ID:26013826 | HubMed [Sun15]
All Medline abstracts: PubMed | HubMed

Links

Human CTDSP1, CTDSP2, and CTDSPL from NCBI Gene