CHP1 ribosome-associated Tef1p biogenesis chaperone CHP1 [Saccharomyces cerevisiae S288C] - Gene

Summary

Official Symbol: CHP1
Official Full Name: ribosome-associated Tef1p biogenesis chaperone CHP1
Primary source: SGD:S000006146
Locus tag: YPL225W
See related: AllianceGenome:SGD:S000006146; FungiDB:YPL225W; VEuPathDB:YPL225W
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 several functions, including misfolded protein binding activity; nascent polypeptide-associated complex binding activity; and translation elongation factor binding activity. Involved in 'de novo' cotranslational protein folding. Located in cytoplasm. Orthologous to human PBDC1 (polysaccharide biosynthesis domain containing 1). [provided by Alliance of Genome Resources, Dec 2024]
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Chromosome XVI - NC_001148.4 Genomic Context describing neighboring genes

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

Function	Evidence Code	Pubs
enables misfolded protein binding	IDA Inferred from Direct Assay more info	PubMed
enables nascent polypeptide-associated complex binding	IDA Inferred from Direct Assay more info	PubMed
enables protein folding chaperone	IDA Inferred from Direct Assay more info	PubMed
enables ribosome binding	IDA Inferred from Direct Assay more info	PubMed
enables translation elongation factor binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in 'de novo' cotranslational protein folding	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info

NP_015099.1

Chaperone for eEF1A; ribosome-associated chaperone dedicated to facilitating high-level expression of eEF1A; transiently binds nascent GTPase domain of eEF1A as soon as it emerges from ribosome tunnel; forms complex with NAC by binding UBA domain of Egd2p; inactivation results in disturbed proteostasis and Hsf1p activation due to abberant eEF1A biogenesis; overlapping phenotypes support notion that Chp1p functions in same eEF1A biogenesis pathway as chaperone Zpr1p-Aim29p

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