Search Results

Overview

Uniprot IDP17987
Protein NameT-complex protein 1 subunit alpha
Gene NameTCP1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
111 ADELVKQKIHPTSVI
126 SGYRLACKEAVRYIN
199 VNSVNILKAHGRSQM
243 CLDFSLQKTKMKLGV
400 HDALCVVKRVLESKS
494 GLDLSNGKPRDNKQA
499 NGKPRDNKQAGVFEP
510 VFEPTIVKVKSLKFA
532 LRIDDLIKLHPESKD
84 ELADLQDKEVGDGTT

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 MEGPLSVFGD 20 RSTGETIRSQ 30 NVMAAASIAN 40 IVKSSLGPVG 50 LDKMLVDDIG 60 DVTITNDGAT 70 ILKLLEVEHP 80 AAKVLCELAD 90 LQDKEVGDGT 100 TSVVIIAAEL 110 LKNADELVKQ 120 KIHPTSVISG 130 YRLACKEAVR 140 YINENLIVNT 150 DELGRDCLIN 160 AAKTSMSSKI 170 IGINGDFFAN 180 MVVDAVLAIK 190 YTDIRGQPRY 200 PVNSVNILKA 210 HGRSQMESML 220 ISGYALNCVV 230 GSQGMPKRIV 240 NAKIACLDFS 250 LQKTKMKLGV 260 QVVITDPEKL 270 DQIRQRESDI 280 TKERIQKILA 290 TGANVILTTG 300 GIDDMCLKYF 310 VEAGAMAVRR 320 VLKRDLKRIA 330 KASGATILST 340 LANLEGEETF 350 EAAMLGQAEE 360 VVQERICDDE 370 LILIKNTKAR 380 TSASIILRGA 390 NDFMCDEMER 400 SLHDALCVVK 410 RVLESKSVVP 420 GGGAVEAALS 430 IYLENYATSM 440 GSREQLAIAE 450 FARSLLVIPN 460 TLAVNAAQDS 470 TDLVAKLRAF 480 HNEAQVNPER 490 KNLKWIGLDL 500 SNGKPRDNKQ 510 AGVFEPTIVK 520 VKSLKFATEA 530 AITILRIDDL 540 IKLHPESKDD 550 KHGSYEDAVH SGALND

Gene Ontology

Classification GO ID Description
Cellular Component GO:0001669 acrosomal vesicle
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
Biological Process GO:0007021 tubulin complex assembly
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:0005794 Golgi apparatus
Cellular Component GO:0000792 heterochromatin
Cellular Component GO:0005874 microtubule
Cellular Component GO:0000242 pericentriolar material
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:0031625 ubiquitin protein ligase binding
Molecular Function GO:0051082 unfolded protein binding
Biological Process GO:1904851 positive regulation of establishment of protein localization to telomere
Biological Process GO:1904871 positive regulation of protein localization to Cajal body

Reference

[1] 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.

[2] 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.

[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] 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.

[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.