Search Results

Overview

Uniprot IDP78371
Protein NameT-complex protein 1 subunit beta
Gene NameCCT2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
120 AESLIAKKIHPQTII
154 DHGSDEVKFRQDLMN
170 AGTTLSSKLLTHHKD
176 SKLLTHHKDHFTKLA
191 VEAVLRLKGSGNLEA
203 LEAIHIIKKLGGSLA
223 EGFLLDKKIGVNQPK
230 KIGVNQPKRIENAKI
248 NTGMDTDKIKIFGSR
250 GMDTDKIKIFGSRVR
263 VRVDSTAKVAEIEHA
272 AEIEHAEKEKMKEKV
284 EKVERILKHGINCFI
402 CVLAQTVKDSRTVYG
431 LANRTPGKEAVAMES
441 VAMESYAKALRMLPT
522 LRVDNIIKAAPRKRV
527 IIKAAPRKRVPDHHP

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 MASLSLAPVN 20 IFKAGADEER 30 AETARLTSFI 40 GAIAIGDLVK 50 STLGPKGMDK 60 ILLSSGRDAS 70 LMVTNDGATI 80 LKNIGVDNPA 90 AKVLVDMSRV 100 QDDEVGDGTT 110 SVTVLAAELL 120 REAESLIAKK 130 IHPQTIIAGW 140 REATKAAREA 150 LLSSAVDHGS 160 DEVKFRQDLM 170 NIAGTTLSSK 180 LLTHHKDHFT 190 KLAVEAVLRL 200 KGSGNLEAIH 210 IIKKLGGSLA 220 DSYLDEGFLL 230 DKKIGVNQPK 240 RIENAKILIA 250 NTGMDTDKIK 260 IFGSRVRVDS 270 TAKVAEIEHA 280 EKEKMKEKVE 290 RILKHGINCF 300 INRQLIYNYP 310 EQLFGAAGVM 320 AIEHADFAGV 330 ERLALVTGGE 340 IASTFDHPEL 350 VKLGSCKLIE 360 EVMIGEDKLI 370 HFSGVALGEA 380 CTIVLRGATQ 390 QILDEAERSL 400 HDALCVLAQT 410 VKDSRTVYGG 420 GCSEMLMAHA 430 VTQLANRTPG 440 KEAVAMESYA 450 KALRMLPTII 460 ADNAGYDSAD 470 LVAQLRAAHS 480 EGNTTAGLDM 490 REGTIGDMAI 500 LGITESFQVK 510 RQVLLSAAEA 520 AEVILRVDNI 530 IKAAPRKRVP DHHPC

Gene Ontology

Classification GO ID Description
Cellular Component GO:0035578 azurophil granule lumen
Molecular Function GO:0031625 ubiquitin protein ligase binding
Molecular Function GO:0051082 unfolded protein binding
Biological Process GO:0051131 chaperone-mediated protein complex assembly
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:0090666 scaRNA localization to Cajal body
Cellular Component GO:0044297 cell body
Cellular Component GO:0005832 chaperonin-containing T-complex
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
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

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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[5] 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.

[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] 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.

[10] 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.