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Gene Review

CTDSP1  -  CTD (carboxy-terminal domain, RNA...

Homo sapiens

Synonyms: Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1, NIF3, NLI-IF, NLI-interacting factor 3, NLIIF, ...
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Disease relevance of CTDSP1


High impact information on CTDSP1

  • Moreover, these results provide a template for the design of specific inhibitors of Scp1 for the study of neuronal stem cell development [3].
  • Fcp1 and Scp1 belong to a family of Mg(2+)-dependent phosphoserine (P.Ser)/phosphothreonine (P.Thr)-specific phosphatases [3].
  • We recently showed that Scp1 is an evolutionarily conserved regulator of neuronal gene silencing [3].
  • Specificity may result from CTD binding to a conserved hydrophobic pocket between the active site and an insertion domain that is unique to Fcp1/Scp1 [4].
  • Depletion of SCP1/2/3 enhanced Smad2/3 linker phosphorylation [5].

Biological context of CTDSP1

  • Accordingly, SCP1 may play a role in the regulation of gene expression, possibly by controlling the transition from initiation/capping to processive transcript elongation [6].
  • SCP1 and related super core promoters (SCPs) with multiple core promoter motifs will be useful for the biophysical analysis of TFIID binding to DNA, the biochemical investigation of the transcription process and the enhancement of gene expression in cells [2].

Anatomical context of CTDSP1

  • In proteins such as the eponymous calponin, IQGAP1, and Scp1, a single CH-domain exists, but there has been some controversy over whether this domain binds to actin filaments [7].

Associations of CTDSP1 with chemical compounds


Enzymatic interactions of CTDSP1

  • The preferred substrate for SCP1 is RNAP II phosphorylated by TFIIH [6].


  1. Differential expression of cancer testis genes in histological subtypes of non-Hodgkin's lymphomas. Xie, X., Wacker, H.H., Huang, S., Regitz, E., Preuss, K.D., Romeike, B., Parwaresch, R., Tiemann, M., Pfreundschuh, M. Clin. Cancer Res. (2003) [Pubmed]
  2. Rational design of a super core promoter that enhances gene expression. Juven-Gershon, T., Cheng, S., Kadonaga, J.T. Nat. Methods (2006) [Pubmed]
  3. Determinants for Dephosphorylation of the RNA Polymerase II C-Terminal Domain by Scp1. Zhang, Y., Kim, Y., Genoud, N., Gao, J., Kelly, J.W., Pfaff, S.L., Gill, G.N., Dixon, J.E., Noel, J.P. Mol. Cell (2006) [Pubmed]
  4. Structure and mechanism of RNA polymerase II CTD phosphatases. Kamenski, T., Heilmeier, S., Meinhart, A., Cramer, P. Mol. Cell (2004) [Pubmed]
  5. Small C-terminal Domain Phosphatases Dephosphorylate the Regulatory Linker Regions of Smad2 and Smad3 to Enhance Transforming Growth Factor-beta Signaling. Wrighton, K.H., Willis, D., Long, J., Liu, F., Lin, X., Feng, X.H. J. Biol. Chem. (2006) [Pubmed]
  6. A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5. Yeo, M., Lin, P.S., Dahmus, M.E., Gill, G.N. J. Biol. Chem. (2003) [Pubmed]
  7. The CH-domain of calponin does not determine the modes of calponin binding to F-actin. Galkin, V.E., Orlova, A., Fattoum, A., Walsh, M.P., Egelman, E.H. J. Mol. Biol. (2006) [Pubmed]
  8. Sterol carrier and lipid transfer proteins. Scallen, T.J., Pastuszyn, A., Noland, B.J., Chanderbhan, R., Kharroubi, A., Vahouny, G.V. Chem. Phys. Lipids (1985) [Pubmed]
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