Search Results

Overview

Uniprot IDP50990
Protein NameT-complex protein 1 subunit theta
Gene NameCCT8
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
138 GYEIACRKAHEILPN
16 PGFAQMLKEGAKHFS
20 QMLKEGAKHFSGLEE
225 LHGMVFKKETEGDVT
235 EGDVTSVKDAKIAVY
254 DGMITETKGTVLIKT
260 TKGTVLIKTAEELMN
318 MLVRLNSKWDLRRLC
326 WDLRRLCKTVGATAL
37 YRNIQACKELAQTTR
400 DDGVNTFKVLTRDKR
440 LEQYAIKKFAEAFEA
459 LAENSGVKANEVISK
466 KANEVISKLYAVHQE
540 PKPPSGKKDWDDDQN
7 *MALHVPKAPGFAQM

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 MALHVPKAPG 20 FAQMLKEGAK 30 HFSGLEEAVY 40 RNIQACKELA 50 QTTRTAYGPN 60 GMNKMVINHL 70 EKLFVTNDAA 80 TILRELEVQH 90 PAAKMIVMAS 100 HMQEQEVGDG 110 TNFVLVFAGA 120 LLELAEELLR 130 IGLSVSEVIE 140 GYEIACRKAH 150 EILPNLVCCS 160 AKNLRDIDEV 170 SSLLRTSIMS 180 KQYGNEVFLA 190 KLIAQACVSI 200 FPDSGHFNVD 210 NIRVCKILGS 220 GISSSSVLHG 230 MVFKKETEGD 240 VTSVKDAKIA 250 VYSCPFDGMI 260 TETKGTVLIK 270 TAEELMNFSK 280 GEENLMDAQV 290 KAIADTGANV 300 VVTGGKVADM 310 ALHYANKYNI 320 MLVRLNSKWD 330 LRRLCKTVGA 340 TALPRLTPPV 350 LEEMGHCDSV 360 YLSEVGDTQV 370 VVFKHEKEDG 380 AISTIVLRGS 390 TDNLMDDIER 400 AVDDGVNTFK 410 VLTRDKRLVP 420 GGGATEIELA 430 KQITSYGETC 440 PGLEQYAIKK 450 FAEAFEAIPR 460 ALAENSGVKA 470 NEVISKLYAV 480 HQEGNKNVGL 490 DIEAEVPAVK 500 DMLEAGILDT 510 YLGKYWAIKL 520 ATNAAVTVLR 530 VDQIIMAKPA 540 GGPKPPSGKK DWDDDQND

Gene Ontology

Classification GO ID Description
Cellular Component GO:0035578 azurophil granule lumen
Cellular Component GO:0044297 cell body
Cellular Component GO:0005813 centrosome
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:0005576 extracellular region
Cellular Component GO:1904813 ficolin-1-rich granule lumen
Cellular Component GO:0005874 microtubule
Cellular Component GO:0034774 secretory granule lumen
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:0045296 cadherin 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

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] 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] 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] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.

[8] 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.