Human Gene CCT4 (uc002sbo.4) Description and Page Index
Description: Homo sapiens chaperonin containing TCP1, subunit 4 (delta) (CCT4), transcript variant 1, mRNA. RefSeq Summary (NM_006430): The chaperonin containing TCP1 (MIM 186980) complex (CCT), also called the TCP1 ring complex, consists of 2 back-to-back rings, each containing 8 unique but homologous subunits, such as CCT4. CCT assists the folding of newly translated polypeptide substrates through multiple rounds of ATP-driven release and rebinding of partially folded intermediate forms. Substrates of CCT include the cytoskeletal proteins actin (see MIM 102560) and tubulin (see MIM 191130), as well as alpha-transducin (MIM 139330) (Won et al., 1998 [PubMed 9819444]).[supplied by OMIM, Mar 2008]. Transcript (Including UTRs) Position: hg19 chr2:62,095,262-62,115,806 Size: 20,545 Total Exon Count: 14 Strand: - Coding Region Position: hg19 chr2:62,095,827-62,115,642 Size: 19,816 Coding Exon Count: 14
ID:TCPD_HUMAN DESCRIPTION: RecName: Full=T-complex protein 1 subunit delta; Short=TCP-1-delta; AltName: Full=CCT-delta; AltName: Full=Stimulator of TAR RNA-binding; FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG. Component of the BBS/CCT complex composed at least of MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8. SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Cytoplasm, cytoskeleton, centrosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. SIMILARITY: Belongs to the TCP-1 chaperonin family.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P50991
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0006457 protein folding GO:0006458 'de novo' protein folding GO:0007339 binding of sperm to zona pellucida GO:0032212 positive regulation of telomere maintenance via telomerase GO:0050821 protein stabilization GO:0051973 positive regulation of telomerase activity GO:0061077 chaperone-mediated protein folding GO:0090666 scaRNA localization to Cajal body GO:1901998 toxin transport GO:1904851 positive regulation of establishment of protein localization to telomere GO:1904871 positive regulation of protein localization to Cajal body GO:1904874 positive regulation of telomerase RNA localization to Cajal body
R-HSA-389954 Hydrolysis of ATP and release of tubulin folding intermediate from CCT/TriC R-HSA-389961 ADP is exchanged for ATP in the (ADP:CCT/TriC):tubulin complex R-HSA-389970 Actin/tubulin:prefoldin complex associates with CCT/TriC R-HSA-390470 Association of CCT/TriC with other substrates during biosynthesis (unknown chaperone) R-HSA-391266 Association of CCT/TriC with sphingosine kinase 1 R-HSA-6814119 TRiC/CCT binds unfolded G-protein beta subunit R-HSA-390453 Hydrolysis of ATP and release of folded actin from CCT/TriC R-HSA-8850527 PDCL releases folded G-beta from TRiC/CCT R-HSA-8850539 Release of GNB5:RGS dimers from CCT/TRiC R-HSA-390459 Exchange of ADP for ATP in CCT/TriC:actin complex R-HSA-6814124 ATP binds G-protein beta associated TRiC/CCT R-HSA-8850529 RGS proteins bind GNB5 and CCT/TRiC R-HSA-8850534 PDCL promotes G-protein beta 5 folding R-HSA-6814121 PDCL binds G-protein beta and TRiC/CCT R-HSA-6814120 ATP hydrolysis promotes folding of G-protein beta by TRiC/CCT R-HSA-389960 Formation of tubulin folding intermediates by CCT/TriC R-HSA-389957 Prefoldin mediated transfer of substrate to CCT/TriC R-HSA-390471 Association of TriC/CCT with target proteins during biosynthesis R-HSA-6814122 Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding R-HSA-390450 Folding of actin by CCT/TriC R-HSA-389958 Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding R-HSA-390466 Chaperonin-mediated protein folding R-HSA-391251 Protein folding R-HSA-392499 Metabolism of proteins