Search Results

Overview

Uniprot IDQ5XIM9
Protein NameT-complex protein 1 subunit beta
Gene NameCct2
OrganismRattus norvegicus

Kla Sites from experimental identification

Position Flanking peptide
176 SKLLTHHKDHFTKLA
191 VEAVLRLKGSGNLEA
203 LEAIHVIKKLGGSLA
248 NTGMDTDKIKIFGSR
250 GMDTDKIKIFGSRVR
263 VRVDSTAKVAEIEHA
272 AEIEHAEKEKMKEKV
431 LASRTPGKEAVAMES
522 LRVDNIIKAAPRKRV

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. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. 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

Protein Sequence

10 MASLSLAPVN 20 IFKAGADEER 30 AETARLSSFI 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 DEVKFWQDLM 170 NIAGTTLSSK 180 LLTHHKDHFT 190 KLAVEAVLRL 200 KGSGNLEAIH 210 VIKKLGGSLA 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 VKDPRTVYGG 420 GCSEMLMAHA 430 VTMLASRTPG 440 KEAVAMESFA 450 KALRMLPTII 460 ADNAGYDSAD 470 LVAQLRAAHS 480 EGRITAGLDM 490 KEGSIGDMAV 500 LGITESFQVK 510 RQVLLSAAEA 520 AEVILRVDNI 530 IKAAPRKRVP DHHPC

Gene Ontology

Classification GO ID Description
Cellular Component GO:0044297 cell body
Cellular Component GO:0005832 chaperonin-containing T-complex
Cellular Component GO:0005829 cytosol
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:0046872 metal ion binding
Molecular Function GO:0044183 protein folding chaperone
Molecular Function GO:0031625 ubiquitin protein ligase binding
Molecular Function GO:0051082 unfolded protein binding
Biological Process GO:0007339 binding of sperm to zona pellucida
Biological Process GO:0051131 chaperone-mediated protein complex assembly
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

Reference

[1] Yao Y, Bade R, Li G, Zhang A, Zhao H et al.. Global-Scale Profiling of Differential Expressed Lysine-Lactylated Proteins in the Cerebral Endothelium of Cerebral Ischemia-Reperfusion Injury Rats.. Cell Mol Neurobiol 43(5):1989-2004. 2023 Jul. PMID: 36030297.

[2] Sheng L, Xu H, Wang Y, Ni J, Xiang T et al.. Systematic analysis of lysine lactylation in nucleus pulposus cells.. iScience 27(11):111157. 2024 Nov 15. PMID: 39524337.

[3] Chen Y, Sun W, Sun Z, Zhao H, Wu T et al.. Effect of electroacupuncture on hippocampal protein lactylation in a rat model of vascular dementia.. Front Neurol 16:1629474. 2025. PMID: 40963935.