| Gene |
CCT2
|
| Protein Name |
TCPB_HUMAN |
| Organism |
Homo sapiens (Human) |
| Alternative name(s) |
T-complex protein 1 subunit beta (TCP-1-beta) (CCT-beta) |
| Protein Family |
TCP-1 chaperonin family |
| NCBI Gene ID |
10576
|
| UniProt ID |
P78371
|
| Enzyme Class |
- |
| Molecular Weight |
57488 |
| Protein Length |
535 |
| Protein Domain |
InterPro |
Pfam
|
| 3D Structure |
PDBe |
PDBj |
RCSB PDB |
DrugPort
ModBase |
SwissModel
|
| Gene Expression |
Gene Expression Atlas
|
| Function and Disease |
OMIM |
| Protein-protein Interaction Database |
STRING |
IntAct |
MINT
|
| Kinase Database |
Phospho.ELM
|
PhosphoSite
| NetworKIN
|
| Catalytic Activity (UniProt annotation) |
- |
| Localization |
Cytoplasm |
| Function (UniProt annotation) |
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable). |
| Gene Ontology |
GO:0002199; GO:0005524; GO:0005576; GO:0005829; GO:0005832; GO:0005874; GO:0006457; GO:0007339; GO:0031625; GO:0032212; GO:0035578; GO:0043209; GO:0043312; GO:0044183; GO:0044297; GO:0050821; GO:0051082; GO:0051086; GO:0051131; GO:0051973; GO:0070062; GO:0090666; GO:1901998; GO:1904851; GO:1904871; GO:1904874 |
