CTD phosphatase

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CTD phosphatase
CTD phosphatase

Existing structural data : 1J2X , 1ONV , 2K7L

Properties of human protein
Mass / length primary structure 961 amino acids
Secondary to quaternary structure Homodimer
Cofactor TFIIF
Isoforms 3
Identifier
Gene names CTDP1 CCFDN; FCP1
External IDs
Enzyme classification
EC, category 3.1.3.16 ,  phosphatase
Response type Solution of a phosphoric acid ester bond
Substrate Phosphoprotein + H 2 O
Products Protein + phosphate
Occurrence
Parent taxon Eukaryotes
Orthologue
human House mouse
Entrez 9150 67655
Ensemble ENSG00000060069 ENSMUSG00000033323
UniProt Q9Y5B0 Q7TSG2
Refseq (mRNA) NM_001202504 NM_026295
Refseq (protein) NP_001189433 NP_080571
Gene locus Chr 18: 79.68 - 79.76 Mb Chr 18: 80.41 - 80.47 Mb
PubMed search 9150 67655

The CTD phosphatase (FCP1) (more precisely TFIIF-associating CTD phosphatase ) is the enzyme that removes the phosphate residues of serine-2 and serine-5 of polymerase II in eukaryotes during transcription , whereby the polymerase is responsible for elongation (re- ) is activated. So it is a phosphatase . The enzyme can be found in all tissue types in humans. Mutations in the corresponding CTDP1 - gene can be hereditary multiple developmental disorders with cataract, called CCFDN syndrome lead.

In order to maintain its full activity, the CTD phosphatase is itself phosphorylated by casein kinase 2 and requires the RAP74 subunit of TFIIF as a cofactor .

The phosphorylation of FCP1 is inhibited by the proteins Pin1 and Hce1, as well as by the Tat protein of the HI virus. FCP1 is methylated by the arginine methyl transferase PRMT5 and an FCP1-PRMT5 complex methylates histone H4 .

Individual evidence

  1. ↑ InterPro entry
  2. ↑ UniProt Q9Y5B0
  3. ↑ Ao Yang, Karen L. Abbott, Alexandre Desjardins, Paola Di Lello, James G. Omichinski, Pascale Legault: NMR Structure of a Complex Formed by the Carboxyl-Terminal Domain of Human RAP74 and a Phosphorylated Peptide from the Central Domain of the FCP1 Phosphatase . In: Biochemistry . 48, No. 9, March 10, 2009, ISSN  0006-2960 , pp. 1964-1974. doi : 10.1021 / bi801549m . PMID 19215094 .
  4. ↑ Karen L. Abbott, Matthew B. Renfrow, Michael J. Chalmers, Bao D. Nguyen, Alan G. Marshall, Pascale Legault, James G. Omichinski: Enhanced Binding of RNAP II CTD Phosphatase FCP1 to RAP74 Following CK2 Phosphorylation . In: Biochemistry . 44, No. 8, March 1, 2005, ISSN  0006-2960 , pp. 2732-2745. doi : 10.1021 / bi047958h . PMID 15723518 .
  5. ↑ Benoit Palancade, Nicholas F. Marshall, Alexandre Tremeau-Bravard, Olivier Bensaude, Michael E. Dahmus, Marie-Francoise Dubois: Dephosphorylation of RNA Polymerase II by CTD-phosphatase FCP1 is Inhibited by Phospho-CTD Associating Proteins . In: Journal of Molecular Biology . 335, No. 2, January 9, 2004, pp. 415-24. doi : 10.1016 / j.jmb.2003.10.036 . PMID 14672652 .
  6. ↑ Stefano Amente, Giuliana Napolitano, Paolo Licciardo, Maria Monti, Piero Pucci, Luigi Lania, Barbara Majello: Identification of proteins interacting with the RNAPII FCP1 phosphatase: FCP1 forms a complex with arginine methyltransferase PRMT5 and it is a substrate for PRMT5-mediated methylation . In: FEBS Letters . 579, No. 3, January 31, 2005, ISSN  0014-5793 , pp. 683-689. doi : 10.1016 / j.febslet.2004.12.045 . PMID 15670829 .
  7. ↑ Karen L. Abbott, Jacques Archambault, Hua Xiao, Bao D. Nguyen, Robert G. Roeder , Jack Greenblatt, James G. Omichinski, Pascale Legault: Interactions of the HIV-1 Tat and RAP74 Proteins with the RNA Polymerase II CTD Phosphatase FCP1 † . In: Biochemistry . 44, No. 8, March 1, 2005, ISSN  0006-2960 , pp. 2716-2731. doi : 10.1021 / bi047957p . PMID 15723517 .

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