TCP1/YDR212W Summary Help

TCP1 BASIC INFORMATION

Standard Name TCP1
Systematic Name YDR212W
Alias CCT1
Feature Type ORF, Verified
Description Alpha subunit of chaperonin-containing T-complex, which mediates protein folding in the cytosol; involved in actin cytoskeleton maintenance; overexpression in neurons suppresses formation of pathogenic conformations of huntingtin protein (1, 2, 3, 4, 5)
Name Description Tailless Complex Polypeptide
GO Annotations All TCP1 GO evidence and references
    View Computational GO annotations for TCP1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Mutant Phenotype All TCP1 Phenotype details and references
Classical genetics
null
Large-scale survey
null
Interactions TCP1 All interactions details and references
122 total interaction(s) for 117 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 29
  • Affinity Capture-Western: 1
  • Co-purification: 1
  • Reconstituted Complex: 1
  • Two-hybrid: 4

Genetic Interactions
  • Dosage Rescue: 8
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 76

Sequence Information
ChrIV:887230 to 888909 | ORF Map | GBrowse
Gbrowse
Genetic position: 127 cM
Last Update Coordinates: 2008-06-05 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1680 887230..888909 2008-06-05 1996-07-31
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000002620

TCP1 RESOURCES

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SGD ORF mapGBrowse
SGD ORF map
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  • Functional Analysis

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Expression Summary histogram

NOMENCLATURE CONFLICT NOTE

NameRelevanceDescription
PCT1Nomenclature conflictCCT1 has been used in the literature to refer to both TCP1/YDR212W, which encodes the chaperonin subunit alpha, and PCT1/YGR202C, which encodes a choline-phosphate cytidylyltransferase.

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for TCP1]

1) Ursic D and Culbertson MR  (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11(5):2629-40
2) Ursic D, et al.  (1994) The essential yeast Tcp1 protein affects actin and microtubules. Mol Biol Cell 5(10):1065-80
3) Siegers K, et al.  (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J 18(1):75-84
4) Siegers K, et al.  (2003) TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J 22(19):5230-40
5) Tam S, et al.  (2006) The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 8(10):1155-62