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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: T-complex protein 1 subunit theta

UniprotKB/SwissProt ID: P50990 (P50990)

Gene Name: CCT8

Organism: Homo sapiens (Human)

Function: 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)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, cilium basal body

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR012721 Chap_CCT_theta
IPR017998 Chaperone_TCP-1
IPR002194 Chaperonin_TCP-1_CS
IPR002423 Cpn60/GroEL/TCP-1
IPR027409 GroEL-like_apical_dom_sf
IPR027413 GROEL-like_equatorial_sf
IPR027410 TCP-1-like_intermed_sf

The S-nitrosylation sites of P50990

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 136 SEVIEGYEIA C RKAHEILPNL  CCCCCCCCCC H HHHHHHHHHH  5.87%
2 148 KAHEILPNLV C CSAKNLRDID  CCCCCCCCCC H HHHHHHHHHH  1.38% 22178444
19483679
3 149 AHEILPNLVC C SAKNLRDIDE  CCCCCCCCCC H HHHHHHHHHH  3.27% 22178444
19483679
4 244 VKDAKIAVYS C PFDGMITETK  CCCCCCCCCC H HHHHHHHHHH  1.82%
5 347 TPPVLEEMGH C DSVYLSEVGD  CCCCCCCCCC H HHHHHHHHHH  3.27%
6 36 EEAVYRNIQA C KELAQTTRTA  CCCCCCCCCC H HHHHHHHHHH  1.7%
7 430 AKQITSYGET C PGLEQYAIKK  CCCCCCCCCC H HHHHHHHHHH  1.88% 19483679