Search Results

Overview

Uniprot IDH0V927
Protein NameT-complex protein 1 subunit zeta
Gene NameCCT6A
OrganismCavia porcellus

Kla Sites from experimental identification

Position Flanking peptide
199 EIMEMKHKSETDTSL
251 VNSGFFYKSAEEREK

Function

Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance

Protein Sequence

10 MAAVKTLNPK 20 AEVARAQAAL 30 AVNISAARGL 40 QDVLRTNLGP 50 KGTMKMLVSG 60 AGDIKLTKDG 70 NVLLHEMQIQ 80 HPTASLIAKV 90 ATAQDDITGD 100 GTTSNVLIIG 110 ELLKQADLYI 120 SEGLHPRIIT 130 EGFEAAKEKA 140 LQFLEQVKVT 150 REMDRETLID 160 VARTSLRTKV 170 HAELADVLTE 180 AVVDSILAIR 190 KKDEPIDLFM 200 VEIMEMKHKS 210 ETDTSLIRGL 220 VLDHGARHPD 230 MKKRVENAYI 240 LTCNVSLEYE 250 KTEVNSGFFY 260 KSAEEREKLV 270 KAERKFIEDR 280 VKKIVELKKK 290 VCGDSDRGFV 300 VINQKGIDPF 310 SLDALAKEGI 320 IALRRAKRRN 330 MERLTLACGG 340 VALNSLDELS 350 PDCLGHAGLV 360 YEYTLGEEKF 370 TFIEKCNNPR 380 SVTLLVKGPN 390 KHTLTQIKDA 400 IRDGLRAVKN 410 AIDDGCVVPG 420 AGAVEVAMAE 430 ALMKHKASVK 440 GRAQLGVQAF 450 ADALLIIPKV 460 LAQNSGFDLQ 470 ETLVKIQAEH 480 SESGQLVGVD 490 LNTGEPMVAA 500 EAGVWDNYCV 510 KKQLLHSCTV 520 IATNILLVDE 530 IMRAGMSSLK G

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005832 chaperonin-containing T-complex
Cellular Component GO:0005874 microtubule
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0140662 ATP-dependent protein folding chaperone
Molecular Function GO:0051082 unfolded protein binding
Molecular Function GO:0071987 WD40-repeat domain binding
Biological Process GO:0050821 protein stabilization

Reference

[1] Feng J, Chen X, Li R, Xie Y, Zhang X et al.. Lactylome analysis reveals potential target modified proteins in the retina of form-deprivation myopia.. iScience 27(9):110606. 2024 Sep 20. PMID: 39246443.