TCP1/YDR212W Summary Help

Standard Name TCP1
Systematic Name YDR212W
Alias CCT1
Feature Type ORF, Verified
Description Alpha subunit of chaperonin-containing T-complex; complex 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
Chromosomal Location
ChrIV:887232 to 888911 | ORF Map | GBrowse
Gbrowse
Genetic position: 127 cM
Gene Ontology 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
Regulators 99 genes
Resources
Classical genetics
null
reduction of function
Large-scale survey
conditional
null
overexpression
reduction of function
Resources
203 total interaction(s) for 169 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 50
  • Affinity Capture-Western: 2
  • Co-fractionation: 1
  • Co-purification: 1
  • Protein-peptide: 3
  • Reconstituted Complex: 1
  • Two-hybrid: 4

Genetic Interactions
  • Dosage Rescue: 9
  • Negative Genetic: 47
  • Positive Genetic: 6
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 77

Resources
Expression Summary
histogram
Resources
Length (a.a.) 559
Molecular Weight (Da) 60,480
Isoelectric Point (pI) 6.45
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrIV:887232 to 888911 | ORF Map | GBrowse
SGD ORF map
Genetic position: 127 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1680 887232..888911 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000002620
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