Search Results

Overview

Uniprot IDQ99832
Protein NameT-complex protein 1 subunit eta
Gene NameCCT7
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
135 ATQLAVNKIKEIAVT
137 QLAVNKIKEIAVTVK
144 KEIAVTVKKADKVEQ
145 EIAVTVKKADKVEQR
157 EQRKLLEKCAMTALS
172 SKLISQQKAFFAKMV
199 LKMIGIKKVQGGALE
218 VAGVAFKKTFSYAGF
250 ELELKAEKDNAEIRV
287 KIHHSGAKVVLSKLP
320 RVPEEDLKRTMMACG
366 NFFTGCPKAKTCTFI
55 LIVDGRGKATISNDG
67 NDGATILKLLDVVHP

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 MMPTPVILLK 20 EGTDSSQGIP 30 QLVSNISACQ 40 VIAEAVRTTL 50 GPRGMDKLIV 60 DGRGKATISN 70 DGATILKLLD 80 VVHPAAKTLV 90 DIAKSQDAEV 100 GDGTTSVTLL 110 AAEFLKQVKP 120 YVEEGLHPQI 130 IIRAFRTATQ 140 LAVNKIKEIA 150 VTVKKADKVE 160 QRKLLEKCAM 170 TALSSKLISQ 180 QKAFFAKMVV 190 DAVMMLDDLL 200 QLKMIGIKKV 210 QGGALEDSQL 220 VAGVAFKKTF 230 SYAGFEMQPK 240 KYHNPKIALL 250 NVELELKAEK 260 DNAEIRVHTV 270 EDYQAIVDAE 280 WNILYDKLEK 290 IHHSGAKVVL 300 SKLPIGDVAT 310 QYFADRDMFC 320 AGRVPEEDLK 330 RTMMACGGSI 340 QTSVNALSAD 350 VLGRCQVFEE 360 TQIGGERYNF 370 FTGCPKAKTC 380 TFILRGGAEQ 390 FMEETERSLH 400 DAIMIVRRAI 410 KNDSVVAGGG 420 AIEMELSKYL 430 RDYSRTIPGK 440 QQLLIGAYAK 450 ALEIIPRQLC 460 DNAGFDATNI 470 LNKLRARHAQ 480 GGTWYGVDIN 490 NEDIADNFEA 500 FVWEPAMVRI 510 NALTAASEAA 520 CLIVSVDETI 530 KNPRSTVDAP 540 TAAGRGRGRG RPH

Gene Ontology

Classification GO ID Description
Cellular Component GO:0044297 cell body
Biological Process GO:0050821 protein stabilization
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:0042802 identical protein 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

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 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.

[4] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[5] 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.