Search Results

Overview

Uniprot IDP40227
Protein NameT-complex protein 1 subunit zeta
Gene NameCCT6A
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
10 AVKTLNPKAEVARAQ
127 TEGFEAAKEKALQFL
129 GFEAAKEKALQFLEE
199 EIMEMKHKSETDTSL
251 VNSGFFYKSAEEREK
287 KVCGDSDKGFVVINQ
365 EKFTFIEKCNNPRSV
377 RSVTLLIKGPNKHTL
381 LLIKGPNKHTLTQIK
388 KHTLTQIKDAVRDGL
5 ***MAAVKTLNPKAE
58 AGDIKLTKDGNVLLH

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 (PubMed:25467444, PubMed:36493755, PubMed:35449234, PubMed:37193829). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444)

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 LQFLEEVKVS 150 REMDRETLID 160 VARTSLRTKV 170 HAELADVLTE 180 AVVDSILAIK 190 KQDEPIDLFM 200 IEIMEMKHKS 210 ETDTSLIRGL 220 VLDHGARHPD 230 MKKRVEDAYI 240 LTCNVSLEYE 250 KTEVNSGFFY 260 KSAEEREKLV 270 KAERKFIEDR 280 VKKIIELKRK 290 VCGDSDKGFV 300 VINQKGIDPF 310 SLDALSKEGI 320 VALRRAKRRN 330 MERLTLACGG 340 VALNSFDDLS 350 PDCLGHAGLV 360 YEYTLGEEKF 370 TFIEKCNNPR 380 SVTLLIKGPN 390 KHTLTQIKDA 400 VRDGLRAVKN 410 AIDDGCVVPG 420 AGAVEVAMAE 430 ALIKHKPSVK 440 GRAQLGVQAF 450 ADALLIIPKV 460 LAQNSGFDLQ 470 ETLVKIQAEH 480 SESGQLVGVD 490 LNTGEPMVAA 500 EVGVWDNYCV 510 KKQLLHSCTV 520 IATNILLVDE 530 IMRAGMSSLK G

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005832 chaperonin-containing T-complex
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
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:0044183 protein folding chaperone
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0051082 unfolded protein binding
Molecular Function GO:0071987 WD40-repeat domain binding
Biological Process GO:1904851 positive regulation of establishment of protein localization to telomere
Biological Process GO:1904871 positive regulation of protein localization to Cajal body
Biological Process GO:1904874 positive regulation of telomerase RNA localization to Cajal body
Biological Process GO:0032212 positive regulation of telomere maintenance via telomerase
Biological Process GO:0006457 protein folding
Biological Process GO:0050821 protein stabilization

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[5] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[6] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[7] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.