Search Results

Overview

Uniprot IDP48643
Protein NameT-complex protein 1 subunit epsilon
Gene NameCCT5
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
170 EPLIQTAKTTLGSKV
176 AKTTLGSKVVNSCHR
20 GRPFLIIKDQDRKSR
223 GGRLEDTKLIKGVIV
226 LEDTKLIKGVIVDKD
261 PFEPPKPKTKHKLDV
263 EPPKPKTKHKLDVTS
265 PKPKTKHKLDVTSVE
279 EDYKALQKYEKEKFE
370 SFGTTKDKMLVIEQC
496 LGIDCLHKGTNDMKQ
513 VIETLIGKKQQISLA
514 IETLIGKKQQISLAT

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 MASMGTLAFD 20 EYGRPFLIIK 30 DQDRKSRLMG 40 LEALKSHIMA 50 AKAVANTMRT 60 SLGPNGLDKM 70 MVDKDGDVTV 80 TNDGATILSM 90 MDVDHQIAKL 100 MVELSKSQDD 110 EIGDGTTGVV 120 VLAGALLEEA 130 EQLLDRGIHP 140 IRIADGYEQA 150 ARVAIEHLDK 160 ISDSVLVDIK 170 DTEPLIQTAK 180 TTLGSKVVNS 190 CHRQMAEIAV 200 NAVLTVADME 210 RRDVDFELIK 220 VEGKVGGRLE 230 DTKLIKGVIV 240 DKDFSHPQMP 250 KKVEDAKIAI 260 LTCPFEPPKP 270 KTKHKLDVTS 280 VEDYKALQKY 290 EKEKFEEMIQ 300 QIKETGANLA 310 ICQWGFDDEA 320 NHLLLQNNLP 330 AVRWVGGPEI 340 ELIAIATGGR 350 IVPRFSELTA 360 EKLGFAGLVQ 370 EISFGTTKDK 380 MLVIEQCKNS 390 RAVTIFIRGG 400 NKMIIEEAKR 410 SLHDALCVIR 420 NLIRDNRVVY 430 GGGAAEISCA 440 LAVSQEADKC 450 PTLEQYAMRA 460 FADALEVIPM 470 ALSENSGMNP 480 IQTMTEVRAR 490 QVKEMNPALG 500 IDCLHKGTND 510 MKQQHVIETL 520 IGKKQQISLA 530 TQMVRMILKI 540 DDIRKPGESE E

Gene Ontology

Classification GO ID Description
Molecular Function GO:0005524 ATP binding
Cellular Component GO:0044297 cell body
Cellular Component GO:0005813 centrosome
Cellular Component GO:0005832 chaperonin-containing T-complex
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005874 microtubule
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0140662 ATP-dependent protein folding chaperone
Molecular Function GO:0048487 beta-tubulin binding
Molecular Function GO:0031681 G-protein beta-subunit binding
Molecular Function GO:0003730 mRNA 3'-UTR binding
Molecular Function GO:0048027 mRNA 5'-UTR binding
Molecular Function GO:0044183 protein folding chaperone
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
Biological Process GO:0009615 response to virus

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] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[4] 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.

[5] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[6] 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.

[7] 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.

[8] 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.

[9] 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.