PIH1 Pih1p [Saccharomyces cerevisiae S288C] - Gene

Summary

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Gene symbol: PIH1
Gene description: Pih1p
Primary source: FungiDB:YHR034C
Locus tag: YHR034C
See related: SGD:S000001076; AllianceGenome:SGD:S000001076; VEuPathDB:YHR034C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: NOP17
Summary: Involved in box C/D snoRNP assembly; protein folding; and rRNA processing. Located in cytoplasm and nucleus. Part of R2TP complex. Orthologous to human PIH1D1 (PIH1 domain containing 1). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See PIH1 in Genome Data Viewer

Location:: chromosome: VIII

Exon count:: 1

Sequence:: Chromosome: VIII; NC_001140.6 (176965..177999, complement)

Chromosome VIII - NC_001140.6 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001140.6

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Results show that Nop17 interacts with the C-terminal portion of Nop58, affecting its affinity for snoRNA, Nop58 stability, and the localization of the box C/D snoRNP components, indicating a key role played by Nop17 in snoRNP assembly.
Title: Nop17 is a key R2TP factor for the assembly and maturation of box C/D snoRNP complex.
Results show that Nop58 strongly interacts with the R2TP complex through its interaction with Pih1 resulting in Nop58 stabilization.
Title: Nutritional status modulates box C/D snoRNP biogenesis by regulated subcellular relocalization of the R2TP complex.
present a structural and biochemical analysis of Hsp90-Tah1-Pih1, Hsp90-Spagh, and Pih1D1-Tel2 complexes that reveal a domain in Pih1D1 specific for binding CK2 phosphorylation sites
Title: Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1.
The Tah1 C-terminal region is unfolded, and is essential for the recruitment of the Pih1 C-terminal domain and folds upon binding.
Title: High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complex.
The stability of the small nucleolar ribonucleoprotein (snoRNP) assembly protein Pih1 in Saccharomyces cerevisiae is modulated by its C terminus.
Title: The stability of the small nucleolar ribonucleoprotein (snoRNP) assembly protein Pih1 in Saccharomyces cerevisiae is modulated by its C terminus.
a role for the Pih1-Tah1 cochaperone complex in the recruitment of client proteins such as core RNP proteins to Hsp90
Title: The Pih1-Tah1 cochaperone complex inhibits Hsp90 molecular chaperone ATPase activity.
We identify a function for the chaperone in RNA processing and maintenance. This functionality of Hsp90 involves two recently identified interactors of the chaperone: Tah1 and Pih1/Nop17.
Title: Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation.
evidence that Nop17p function is required either for nucleolar retention or for the proper assembly of the box C/D snoRNP
Title: Characterization of Saccharomyces cerevisiae Nop17p, a novel Nop58p-interacting protein that is involved in Pre-rRNA processing.

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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 protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in RNA splicing	IEA Inferred from Electronic Annotation more info
involved_in box C/D snoRNP assembly	IBA Inferred from Biological aspect of Ancestor more info
involved_in box C/D snoRNP assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mRNA processing	IEA Inferred from Electronic Annotation more info
involved_in protein folding	IGI Inferred from Genetic Interaction more info	PubMed
involved_in protein folding	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein folding	IPI Inferred from Physical Interaction more info	PubMed
involved_in rRNA processing	IBA Inferred from Biological aspect of Ancestor more info
involved_in rRNA processing	IGI Inferred from Genetic Interaction more info	PubMed
involved_in rRNA processing	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of cell size	HMP more info	PubMed

Component	Evidence Code	Pubs
part_of R2TP complex	IBA Inferred from Biological aspect of Ancestor more info
part_of R2TP complex	IDA Inferred from Direct Assay more info	PubMed
part_of R2TP complex	IPI Inferred from Physical Interaction more info	PubMed
located_in cytoplasm	HDA more info	PubMed
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in nucleus	HDA more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info
part_of ribonucleoprotein complex	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: Pih1p

NP_011899.1

Component of the conserved R2TP complex (Rvb1-Rvb2-Tah1-Pih1); R2TP complex interacts with Hsp90 (Hsp82p and Hsc82p) to mediate assembly large protein complexes such as box C/D snoRNPs and RNA polymerase II

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_001140.6 Reference assembly

Range

176965..177999 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001179164.1 → NP_011899.1 TPA: Pih1p [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_011899.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D3DKY1, P38768

UniProtKB/TrEMBL

A0A8H4BZP0, G2WFA6, N1P9L9

Conserved Domains (2) summary

pfam18482
Location:265 → 344

Pih1_fungal_CS; Fungal Pih1 CS domain

cl00175
Location:32 → 165

alpha-crystallin-Hsps_p23-like; alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a similar domain found in p23 (a cochaperone for Hsp90) and in other p23-like proteins.