Curated Information

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Curated Information Page

PubMed Id: 12591939

This page summarizes selected information from the article referenced above and curated into PhosphoSitePlus^®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus^®, click here.

Friedl EM, et al. (2003) The C-terminal domain phosphatase and transcription elongation activities of FCP1 are regulated by phosphorylation. Proc Natl Acad Sci U S A 100, 2328-33 12591939

Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.

S575-p - FCP1 (human)

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Orthologous residues

FCP1 (human): S575‑p, FCP1 iso2 (human): S456‑p, FCP1 (mouse): S565‑p, FCP1 (rat): S574‑p

Characterization

Methods used to characterize site in vivo: mass spectrometry (in vitro)

Enzymes shown to modify site in vitro:

Type	Enzyme
KINASE	CK2-A1 (human)

Downstream Regulation

Effect of modification (function): enzymatic activity, induced, molecular association, regulation

Effect of modification (process): transcription, altered

Modification regulates interactions with:

Interacting molecule	Interacting domains	Effect	Consequences (function)	Consequences (process)	Detection assays
GTF2F2 (human)		Induces		transcription, altered	pull-down assay, in vitro

S740-p - FCP1 (human)

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