Ontology: Biological Process (GO:0006458)

Definition: The process of assisting in the folding of a nascent peptide chain into its correct tertiary structure.

Synonyms: nascent chain protein folding

View Ontology: (graph) | (text)

This table lists the methods used to annotate genes either directly to the term 'de novo' protein folding (6 genes) or to its variants containing one or more qualifiers (0 genes). Note that some genes may have been annotated by more than one method so the numbers in the table below may not add up to the totals given here.

Annotation Method	GO Term	# Yeast Genes Annotated
Manually curated (download data)	'de novo' protein folding	6
High-throughput	none	none
Computational	none	none

Links to Additional Annotations:

• View annotations in multiple organisms using
• Search for S. cerevisiae genes annotated, by the Manually curated or High-throughput methods, to this term or to any terms that are descended from this term, i.e., child terms representing more specific biology than this term.

Annotation details for genes that have been directly annotated to the term 'de novo' protein folding or its variants containing one or more qualifiers (NOT, contributes to, or colocalizes with).

'de novo' protein folding      6 genes directly annotated to this term
Locus	Evidence	Annotation Method	Reference	Assigned By
HSC82/YMR186W	ISS: Inferred from Sequence or structural Similarity with SGD:HSP82 Assigned on 2006-06-13	manually curated	Borkovich KA, et al.  (1989) hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol Cell Biol 9(9):3919-30	SGD
HSP60/YLR259C	IMP: Inferred from Mutant Phenotype Assigned on 2008-07-15	manually curated	Cheng MY, et al.  (1990) The mitochondrial chaperonin hsp60 is required for its own assembly. Nature 348(6300):455-8	SGD
HSP82/YPL240C	IDA: Inferred from Direct Assay Assigned on 2006-06-13	manually curated	Scheibel T, et al.  (1999) Contribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae. Mol Microbiol 34(4):701-13	SGD
	IMP: Inferred from Mutant Phenotype Assigned on 2006-06-13	manually curated	Nathan DF, et al.  (1997) In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. Proc Natl Acad Sci U S A 94(24):12949-56	SGD
MDJ1/YFL016C	IMP: Inferred from Mutant Phenotype Assigned on 2008-06-03	manually curated	Rowley N, et al.  (1994) Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77(2):249-59	SGD
ROT1/YMR200W	IMP: Inferred from Mutant Phenotype, IPI: Inferred from Physical Interaction with SGD:KRE6, SGD:BIG1 Assigned on 2012-04-26	manually curated	Takeuchi M, et al.  (2008) Saccharomyces cerevisiae Rot1 Is an Essential Molecular Chaperone in the Endoplasmic Reticulum. Mol Biol Cell 19(8):3514-25	SGD
YDJ1/YNL064C	IMP: Inferred from Mutant Phenotype Assigned on 2007-02-08	manually curated	Meacham GC, et al.  (1999) Mutations in the yeast Hsp40 chaperone protein Ydj1 cause defects in Axl1 biogenesis and pro-a-factor processing. J Biol Chem 274(48):34396-402	SGD

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