CTDSP2

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0004722 protein serine/threonine phosphatase activity	IEA GO_REF:0000120	MODIFY	Summary: CTDSP2 has a more specific RNA polymerase II CTD phosphatase activity. Reason: The FCP1 homology domain and catalytic aspartates support phosphatase chemistry, and the curated human record and primary SCP-family study identify the RNA polymerase II CTD substrate. Use the specific CTD heptapeptide phosphatase term rather than a generic phosphatase class. Proposed replacements: RNA polymerase II CTD heptapeptide repeat phosphatase activity Supporting Evidence: file:human/CTDSP2/CTDSP2-uniprot.txt /note="4-aspartylphosphate intermediate"
GO:0005515 protein binding	IPI PMID:16724108 Small carboxyl-terminal domain phosphatase 2 attenuates andr...	KEEP AS NON CORE	Summary: Retain the experimentally curated interaction as a non-core binding observation. Reason: The IPI row from PMID:16724108 records a protein interaction, not a distinct catalytic function. CTDSP2 is a CTD phosphatase; generic protein binding does not identify substrate-directed catalysis or a defined adaptor mechanism. The interaction is retained without inferring that every partner is a phosphatase substrate.
GO:0005515 protein binding	IPI PMID:16882717 Unique players in the BMP pathway: small C-terminal domain p...	KEEP AS NON CORE	Summary: Retain the experimentally curated interaction as a non-core binding observation. Reason: The IPI row from PMID:16882717 records a protein interaction, not a distinct catalytic function. CTDSP2 is a CTD phosphatase; generic protein binding does not identify substrate-directed catalysis or a defined adaptor mechanism. The interaction is retained without inferring that every partner is a phosphatase substrate.
GO:0005515 protein binding	IPI PMID:22458338 Host-pathogen interactome mapping for HTLV-1 and -2 retrovir...	KEEP AS NON CORE	Summary: Retain the experimentally curated interaction as a non-core binding observation. Reason: The IPI row from PMID:22458338 records a protein interaction, not a distinct catalytic function. CTDSP2 is a CTD phosphatase; generic protein binding does not identify substrate-directed catalysis or a defined adaptor mechanism. The interaction is retained without inferring that every partner is a phosphatase substrate.
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	KEEP AS NON CORE	Summary: Retain the experimentally curated interaction as a non-core binding observation. Reason: The IPI row from PMID:25416956 records a protein interaction, not a distinct catalytic function. CTDSP2 is a CTD phosphatase; generic protein binding does not identify substrate-directed catalysis or a defined adaptor mechanism. The interaction is retained without inferring that every partner is a phosphatase substrate.
GO:0005515 protein binding	IPI PMID:27880917 Phenotypic and Interaction Profiling of the Human Phosphatas...	KEEP AS NON CORE	Summary: Retain the experimentally curated interaction as a non-core binding observation. Reason: The IPI row from PMID:27880917 records a protein interaction, not a distinct catalytic function. CTDSP2 is a CTD phosphatase; generic protein binding does not identify substrate-directed catalysis or a defined adaptor mechanism. The interaction is retained without inferring that every partner is a phosphatase substrate.
GO:0005515 protein binding	IPI PMID:28514442 Architecture of the human interactome defines protein commun...	KEEP AS NON CORE	Summary: Retain the experimentally curated interaction as a non-core binding observation. Reason: The IPI row from PMID:28514442 records a protein interaction, not a distinct catalytic function. CTDSP2 is a CTD phosphatase; generic protein binding does not identify substrate-directed catalysis or a defined adaptor mechanism. The interaction is retained without inferring that every partner is a phosphatase substrate.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the experimentally curated interaction as a non-core binding observation. Reason: The IPI row from PMID:32296183 records a protein interaction, not a distinct catalytic function. CTDSP2 is a CTD phosphatase; generic protein binding does not identify substrate-directed catalysis or a defined adaptor mechanism. The interaction is retained without inferring that every partner is a phosphatase substrate.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the experimentally curated interaction as a non-core binding observation. Reason: The IPI row from PMID:32296183 records a protein interaction, not a distinct catalytic function. CTDSP2 is a CTD phosphatase; generic protein binding does not identify substrate-directed catalysis or a defined adaptor mechanism. The interaction is retained without inferring that every partner is a phosphatase substrate.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the experimentally curated interaction as a non-core binding observation. Reason: The IPI row from PMID:32296183 records a protein interaction, not a distinct catalytic function. CTDSP2 is a CTD phosphatase; generic protein binding does not identify substrate-directed catalysis or a defined adaptor mechanism. The interaction is retained without inferring that every partner is a phosphatase substrate.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	KEEP AS NON CORE	Summary: Retain the experimentally curated interaction as a non-core binding observation. Reason: The IPI row from PMID:33961781 records a protein interaction, not a distinct catalytic function. CTDSP2 is a CTD phosphatase; generic protein binding does not identify substrate-directed catalysis or a defined adaptor mechanism. The interaction is retained without inferring that every partner is a phosphatase substrate.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	KEEP AS NON CORE	Summary: Retain the experimentally curated interaction as a non-core binding observation. Reason: The IPI row from PMID:40205054 records a protein interaction, not a distinct catalytic function. CTDSP2 is a CTD phosphatase; generic protein binding does not identify substrate-directed catalysis or a defined adaptor mechanism. The interaction is retained without inferring that every partner is a phosphatase substrate.
GO:0005634 nucleus	IEA GO_REF:0000044	ACCEPT	Summary: Nuclear/nucleoplasmic localization is appropriate for the CTD phosphatase role. Reason: CTDSP2 acts on nuclear RNA polymerase II and is recruited to transcriptional repression machinery. The curated location and Reactome context agree with this substrate-centered role. Supporting Evidence: file:human/CTDSP2/CTDSP2-uniprot.txt SUBCELLULAR LOCATION: Nucleus
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-1791130	ACCEPT	Summary: Nuclear/nucleoplasmic localization is appropriate for the CTD phosphatase role. Reason: CTDSP2 acts on nuclear RNA polymerase II and is recruited to transcriptional repression machinery. The curated location and Reactome context agree with this substrate-centered role. Supporting Evidence: file:human/CTDSP2/CTDSP2-uniprot.txt SUBCELLULAR LOCATION: Nucleus
GO:0006357 regulation of transcription by RNA polymerase II	IEA GO_REF:0000108	ACCEPT	Summary: CTD dephosphorylation contributes directly to regulation of RNA polymerase II transcription. Reason: The CTD phosphorylation cycle controls transcriptional progression, and SCP-family phosphatase perturbation alters transcription. The inferred process is consistent with CTDSP2 catalysis rather than being a generic phenotype-only association. Supporting Evidence: file:human/CTDSP2/CTDSP2-uniprot.txt Negatively regulates RNA CC polymerase II transcription
GO:0006470 protein dephosphorylation	IDA PMID:12721286 A novel RNA polymerase II C-terminal domain phosphatase that...	ACCEPT	Summary: CTDSP2 directly removes phosphate from protein substrates. Reason: Its RNA polymerase II CTD phosphatase activity executes protein dephosphorylation. This broad process is supported by the catalytic mechanism and does not imply kinase activity. Supporting Evidence: file:human/CTDSP2/CTDSP2-uniprot.txt /note="4-aspartylphosphate intermediate"
GO:0008420 RNA polymerase II CTD heptapeptide repeat phosphatase activity	IBA GO_REF:0000033	ACCEPT	Summary: RNA polymerase II CTD heptapeptide phosphatase activity is the defining molecular function. Reason: The human protein has the FCP1-homology catalytic domain, including active-site Asp107 and Asp109, and the curated primary-study annotation assigns the SCP-family CTD phosphatase activity. The cached abstract foregrounds SCP1 but does not exclude experiments on CTDSP2; retain the curated CTDSP2 annotation without asserting that the abstract independently resolves every paralog assay. Supporting Evidence: file:human/CTDSP2/CTDSP2-uniprot.txt /note="4-aspartylphosphate intermediate" file:human/CTDSP2/CTDSP2-uniprot.txt /note="Proton donor"
GO:0008420 RNA polymerase II CTD heptapeptide repeat phosphatase activity	IDA PMID:12721286 A novel RNA polymerase II C-terminal domain phosphatase that...	ACCEPT	Summary: RNA polymerase II CTD heptapeptide phosphatase activity is the defining molecular function. Reason: The human protein has the FCP1-homology catalytic domain, including active-site Asp107 and Asp109, and the curated primary-study annotation assigns the SCP-family CTD phosphatase activity. The cached abstract foregrounds SCP1 but does not exclude experiments on CTDSP2; retain the curated CTDSP2 annotation without asserting that the abstract independently resolves every paralog assay. Supporting Evidence: file:human/CTDSP2/CTDSP2-uniprot.txt /note="4-aspartylphosphate intermediate" file:human/CTDSP2/CTDSP2-uniprot.txt /note="Proton donor"
GO:0008420 RNA polymerase II CTD heptapeptide repeat phosphatase activity	IEA GO_REF:0000120	ACCEPT	Summary: RNA polymerase II CTD heptapeptide phosphatase activity is the defining molecular function. Reason: The human protein has the FCP1-homology catalytic domain, including active-site Asp107 and Asp109, and the curated primary-study annotation assigns the SCP-family CTD phosphatase activity. The cached abstract foregrounds SCP1 but does not exclude experiments on CTDSP2; retain the curated CTDSP2 annotation without asserting that the abstract independently resolves every paralog assay. Supporting Evidence: file:human/CTDSP2/CTDSP2-uniprot.txt /note="4-aspartylphosphate intermediate" file:human/CTDSP2/CTDSP2-uniprot.txt /note="Proton donor"
GO:0016791 phosphatase activity	IEA GO_REF:0000002	MODIFY	Summary: CTDSP2 has a more specific RNA polymerase II CTD phosphatase activity. Reason: The FCP1 homology domain and catalytic aspartates support phosphatase chemistry, and the curated human record and primary SCP-family study identify the RNA polymerase II CTD substrate. Use the specific CTD heptapeptide phosphatase term rather than a generic phosphatase class. Proposed replacements: RNA polymerase II CTD heptapeptide repeat phosphatase activity Supporting Evidence: file:human/CTDSP2/CTDSP2-uniprot.txt /note="4-aspartylphosphate intermediate"