CCT7/YJL111W Summary

CCT7 BASIC INFORMATION

Standard Name	CCT7
Systematic Name	YJL111W
Alias	TCP7
Feature Type	ORF, Verified
Description	Subunit of the cytosolic chaperonin Cct ring complex, related to Tcp1p, required for the assembly of actin and tubulins in vivo (1, 2)
Name Description	Chaperonin Containing TCP-1

GO Annotations	All CCT7 GO evidence and references
	View Computational GO annotations for CCT7
Molecular Function
Manually curated	unfolded protein binding (IDA)
Biological Process
Manually curated	protein folding (IDA)
Cellular Component
Manually curated	chaperonin-containing T-complex (IDA, IPI)
High-throughput	cytoplasm (IDA)

Mutant Phenotype	All CCT7 Phenotype details and references
Large-scale survey
null	competitive fitness: decreased haploinsufficient inviable
overexpression	filamentous growth: decreased invasive growth: absent vegetative growth: decreased

Interactions	CCT7 All interactions details and references
	24 total interaction(s) for 19 unique genes/features.
Physical Interactions	Affinity Capture-MS: 18 Affinity Capture-RNA: 1 Biochemical Activity: 3 Co-purification: 1
Genetic Interactions	Synthetic Growth Defect: 1

Sequence Information

ChrX:207872 to 209524 | |

Last Update

Coordinates: 2009-02-18 | Sequence: 1996-07-31

Subfeature details

	Relative Coordinates	Chromosomal Coordinates	Most Recent Updates
	Relative Coordinates	Chromosomal Coordinates	Coordinates	Sequence
CDS	1..1653	207872..209524	2009-02-18	1996-07-31

External Links	All Associated Seq \| Entrez Gene \| Entrez RefSeq Protein \| MIPS \| UniProtKB

Primary SGDID	S000003647

CCT7 RESOURCES

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SGD ORF map	GBrowse

Click on histogram for expression summary
Expression Summary

ADDITIONAL INFORMATION for CCT7

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for CCT7]

1)	Stoldt V, et al. (1996) Review: the Cct eukaryotic chaperonin subunits of Saccharomyces cerevisiae and other yeasts. Yeast 12(6):523-9
2)	Kim S, et al. (1994) Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains. Trends Biochem Sci 19(12):543-8

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