Search Results

Overview

Uniprot IDP49368
Protein NameT-complex protein 1 subunit gamma
Gene NameCCT3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
128 VVISAYRKALDDMIS
138 DDMISTLKKISIPVD
15 LVLSQNTKRESGRKV
21 TKRESGRKVQSGNIN
248 LDSSLEYKKGESQTD
249 DSSLEYKKGESQTDI
353 GAGLLEIKKIGDEYF
354 AGLLEIKKIGDEYFT
370 ITDCKDPKACTILLR
381 ILLRGASKEILSEVE
527 DDIVSGHKKKGDDQS
528 DIVSGHKKKGDDQSR
78 QVQHPAAKSMIEISR

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). 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)

Protein Sequence

10 MMGHRPVLVL 20 SQNTKRESGR 30 KVQSGNINAA 40 KTIADIIRTC 50 LGPKSMMKML 60 LDPMGGIVMT 70 NDGNAILREI 80 QVQHPAAKSM 90 IEISRTQDEE 100 VGDGTTSVII 110 LAGEMLSVAE 120 HFLEQQMHPT 130 VVISAYRKAL 140 DDMISTLKKI 150 SIPVDISDSD 160 MMLNIINSSI 170 TTKAISRWSS 180 LACNIALDAV 190 KMVQFEENGR 200 KEIDIKKYAR 210 VEKIPGGIIE 220 DSCVLRGVMI 230 NKDVTHPRMR 240 RYIKNPRIVL 250 LDSSLEYKKG 260 ESQTDIEITR 270 EEDFTRILQM 280 EEEYIQQLCE 290 DIIQLKPDVV 300 ITEKGISDLA 310 QHYLMRANIT 320 AIRRVRKTDN 330 NRIARACGAR 340 IVSRPEELRE 350 DDVGTGAGLL 360 EIKKIGDEYF 370 TFITDCKDPK 380 ACTILLRGAS 390 KEILSEVERN 400 LQDAMQVCRN 410 VLLDPQLVPG 420 GGASEMAVAH 430 ALTEKSKAMT 440 GVEQWPYRAV 450 AQALEVIPRT 460 LIQNCGASTI 470 RLLTSLRAKH 480 TQENCETWGV 490 NGETGTLVDM 500 KELGIWEPLA 510 VKLQTYKTAV 520 ETAVLLLRID 530 DIVSGHKKKG 540 DDQSRQGGAP DAGQE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0044297 cell body
Cellular Component GO:0005832 chaperonin-containing T-complex
Cellular Component GO:0005856 cytoskeleton
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005874 microtubule
Cellular Component GO:0002199 zona pellucida receptor complex
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
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] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[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] 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.

[6] 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.