SSU72 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: SSU72
Primary source: FungiDB:YNL222W
Locus tag: YNL222W
See related: SGD:S000005166; AllianceGenome:SGD:S000005166; VEuPathDB:YNL222W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables RNA polymerase II CTD heptapeptide repeat phosphatase activity and protein tyrosine phosphatase activity. Involved in pre-mRNA cleavage required for polyadenylation; regulation of RNA biosynthetic process; and transcription, DNA-templated. Located in nucleus. Part of mRNA cleavage and polyadenylation specificity factor complex. Orthologous to human SSU72 (SSU72 homolog, RNA polymerase II CTD phosphatase). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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Location:: chromosome: XIV

Exon count:: 1

Sequence:: Chromosome: XIV; NC_001146.8 (229094..229714)

Chromosome XIV - NC_001146.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001146.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The Ssu72 phosphatase mediates the RNA polymerase II initiation-elongation transition.
Title: The Ssu72 phosphatase mediates the RNA polymerase II initiation-elongation transition.
analysis of conserved and divergent Ssu72 phosphatases from Saccharomyces cerevisiae and Kluyveromyces lactis
Title: Structurally conserved and functionally divergent yeast Ssu72 phosphatases.
Ssu72 phosphatase-dependent erasure of phospho-Ser7 marks on the RNA polymerase II C-terminal domain is essential for viability and transcription termination.
Title: Ssu72 phosphatase-dependent erasure of phospho-Ser7 marks on the RNA polymerase II C-terminal domain is essential for viability and transcription termination.
the interactions linking Cak1 with the PAF1 complex and with Ssu72 are not direct but mediated via Ctk1 and Bur1
Title: Kinase Cak1 functionally interacts with the PAF1 complex and phosphatase Ssu72 via kinases Ctk1 and Bur1.
Ssu72 catalyzes serine-5-P dephosphorylation subsequent to addition of the 7-methylguanosine cap on pre-mRNA in a manner that facilitates the RNAP II transition into the elongation stage of the transcription cycle.
Title: Role for the Ssu72 C-terminal domain phosphatase in RNA polymerase II transcription elongation.
The mechanisms of reading the CTD code by two classes of protein phosphatases, plant CPLs and yeast Ssu72, that specifically dephosphorylate Ser(5) in vitro are reported.
Title: Different strategies for carboxyl-terminal domain (CTD) recognition by serine 5-specific CTD phosphatases.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables RNA polymerase II CTD heptapeptide repeat phosphatase activity	IBA Inferred from Biological aspect of Ancestor more info
enables RNA polymerase II CTD heptapeptide repeat phosphatase activity	IDA Inferred from Direct Assay more info	PubMed
enables RNA polymerase II CTD heptapeptide repeat phosphatase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables myosin phosphatase activity	IEA Inferred from Electronic Annotation more info
enables phosphoprotein phosphatase activity	IEA Inferred from Electronic Annotation more info
enables phosphoprotein phosphatase activity	IGI Inferred from Genetic Interaction more info	PubMed
enables protein serine/threonine phosphatase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein serine/threonine phosphatase activity	IEA Inferred from Electronic Annotation more info
enables protein serine/threonine phosphatase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables protein tyrosine phosphatase activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in mRNA 3'-end processing	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mRNA processing	IEA Inferred from Electronic Annotation more info
involved_in regulation of transcription by RNA polymerase II	IEA Inferred from Electronic Annotation more info
involved_in sno(s)RNA transcription	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in termination of RNA polymerase II transcription	IBA Inferred from Biological aspect of Ancestor more info
involved_in termination of RNA polymerase II transcription	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in termination of RNA polymerase II transcription, exosome-dependent	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in termination of RNA polymerase II transcription, poly(A)-coupled	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in transcription antitermination	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in transcription elongation by RNA polymerase II	IGI Inferred from Genetic Interaction more info	PubMed
involved_in transcription elongation by RNA polymerase II	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in transcription initiation at RNA polymerase II promoter	IGI Inferred from Genetic Interaction more info	PubMed
involved_in transcription initiation at RNA polymerase II promoter	IPI Inferred from Physical Interaction more info	PubMed
involved_in transcriptional start site selection at RNA polymerase II promoter	IGI Inferred from Genetic Interaction more info	PubMed
involved_in transcriptional start site selection at RNA polymerase II promoter	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of mRNA cleavage and polyadenylation specificity factor complex	IBA Inferred from Biological aspect of Ancestor more info
part_of mRNA cleavage and polyadenylation specificity factor complex	IDA Inferred from Direct Assay more info	PubMed
part_of mRNA cleavage and polyadenylation specificity factor complex	IPI Inferred from Physical Interaction more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info
located_in nucleus	IGI Inferred from Genetic Interaction more info	PubMed
located_in nucleus	IPI Inferred from Physical Interaction more info	PubMed

General protein information

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Preferred Names: RNA polymerase II subunit A C-terminal domain phosphatase

NP_014177.1

EC 3.1.3.16

Phosphatase and transcription/RNA-processing factor; associates with TFIIB and cleavage/polyadenylation factor Pta1p; exhibits phosphatase activity on serine-5 and serine-7 of the RNA polymerase II C-terminal domain; affects start site selection and transcriptional read through in vivo

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001146.8 Reference assembly

Range

229094..229714

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001183060.1 → NP_014177.1 TPA: RNA polymerase II subunit A C-terminal domain phosphatase [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_014177.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6W0W8, P53538, Q6Q569

UniProtKB/TrEMBL

A6ZRL8, B3LP66, B5VQI8, C7GPD5, C8ZG11, G2WLP1, N1P584

Conserved Domains (1) summary

COG5211
Location:3 → 206

SSU72; RNA polymerase II-interacting protein involved in transcription start site selection [Transcription]