6nr9: Difference between revisions

<StructureSection load='6nr9' size='340' side='right'caption='[[6nr9]], [[Resolution|resolution]] 8.50&Aring;' scene=''>

[[http://www.uniprot.org/uniprot/TCPZ_HUMAN TCPZ_HUMAN]] 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). The TRiC complex plays a role in the folding of actin and tubulin (Probable).<ref>PMID:25467444</ref>  [[http://www.uniprot.org/uniprot/PFD3_HUMAN PFD3_HUMAN]] Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.<ref>PMID:9630229</ref>  [[http://www.uniprot.org/uniprot/TCPG_HUMAN TCPG_HUMAN]] 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).<ref>PMID:20080638</ref> <ref>PMID:25467444</ref>  [[http://www.uniprot.org/uniprot/TCPH_HUMAN TCPH_HUMAN]] 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). The TRiC complex plays a role in the folding of actin and tubulin (Probable).<ref>PMID:25467444</ref>  [[http://www.uniprot.org/uniprot/PFD1_HUMAN PFD1_HUMAN]] Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. [[http://www.uniprot.org/uniprot/PFD4_HUMAN PFD4_HUMAN]] Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.<ref>PMID:9630229</ref>  [[http://www.uniprot.org/uniprot/TCPB_HUMAN TCPB_HUMAN]] 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).<ref>PMID:20080638</ref> <ref>PMID:25467444</ref>  [[http://www.uniprot.org/uniprot/PFD6_HUMAN PFD6_HUMAN]] Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.<ref>PMID:9630229</ref>  [[http://www.uniprot.org/uniprot/TCPQ_HUMAN TCPQ_HUMAN]] 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).<ref>PMID:20080638</ref> <ref>PMID:25467444</ref>  [[http://www.uniprot.org/uniprot/TCPA_HUMAN TCPA_HUMAN]] 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).<ref>PMID:20080638</ref> <ref>PMID:25467444</ref>  [[http://www.uniprot.org/uniprot/TCPD_HUMAN TCPD_HUMAN]] 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).<ref>PMID:20080638</ref> <ref>PMID:25467444</ref>  [[http://www.uniprot.org/uniprot/PFD5_HUMAN PFD5_HUMAN]] Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Represses the transcriptional activity of MYC.<ref>PMID:9630229</ref>  [[http://www.uniprot.org/uniprot/PFD2_HUMAN PFD2_HUMAN]] Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.<ref>PMID:9630229</ref>  [[http://www.uniprot.org/uniprot/TCPE_HUMAN TCPE_HUMAN]] 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.<ref>PMID:20080638</ref>   

</StructureSection>