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    TCP1 t-complex 1 [ Homo sapiens (human) ]

    Gene ID: 6950, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    METTL14-mediated N6-methyladenosine modification of TCP1 mRNA promotes acute myeloid leukemia progression.

    METTL14-mediated N6-methyladenosine modification of TCP1 mRNA promotes acute myeloid leukemia progression.
    Zhang M, Xie Z, Tan Y, Wu Y, Wang M, Zhang P, Yuan Y, Li J.

    08/28/2024
    [The Effect of TCP1 Expression on the Proliferation and the Accumulation of Intracellular Drug of HL60/A and HL60 Cell and Its Mechanism].

    [The Effect of TCP1 Expression on the Proliferation and the Accumulation of Intracellular Drug of HL60/A and HL60 Cell and Its Mechanism].
    Chen XF, Chen XL, Chen YZ.

    02/27/2024
    Low expression of TCP1 (T-Complex 1) and PSMC1 (Proteasome 26S subunit, ATPase 1) in heterotopic ossification during ankylosing spondylitis.

    Low expression of TCP1 (T-Complex 1) and PSMC1 (Proteasome 26S subunit, ATPase 1) in heterotopic ossification during ankylosing spondylitis.
    Zhong XL, Qian BP, Huang JC, Zhao SZ, Li Y, Qiu Y., Free PMC Article

    02/26/2022
    TCP1 regulates PI3K/AKT/mTOR signaling pathway to promote proliferation of ovarian cancer cells.

    TCP1 regulates PI3K/AKT/mTOR signaling pathway to promote proliferation of ovarian cancer cells.
    Weng H, Feng X, Lan Y, Zheng Z., Free PMC Article

    12/25/2021
    Native mass spectrometry analyses of chaperonin complex TRiC/CCT reveal subunit N-terminal processing and re-association patterns.

    Native mass spectrometry analyses of chaperonin complex TRiC/CCT reveal subunit N-terminal processing and re-association patterns.
    Collier MP, Moreira KB, Li KH, Chen YC, Itzhak D, Samant R, Leitner A, Burlingame A, Frydman J., Free PMC Article

    11/13/2021
    TCP1 regulates Wnt7b/beta-catenin pathway through P53 to influence the proliferation and migration of hepatocellular carcinoma cells.

    TCP1 regulates Wnt7b/β-catenin pathway through P53 to influence the proliferation and migration of hepatocellular carcinoma cells.
    Tang N, Cai X, Peng L, Liu H, Chen Y., Free PMC Article

    10/9/2021
    Combined use of GM2AP and TCP1-eta urinary levels predicts recovery from intrinsic acute kidney injury.

    Combined use of GM2AP and TCP1-eta urinary levels predicts recovery from intrinsic acute kidney injury.
    Blanco-Gozalo V, Casanova AG, Sancho-Martínez SM, Prieto M, Quiros Y, Morales AI, Martínez-Salgado C, Agüeros-Blanco C, Benito-Hernández A, Ramos-Barron MA, Gómez-Alamillo C, Arias M, López-Hernández FJ., Free PMC Article

    12/12/2020
    TCP1alpha, essential for actin and tubulin folding, was directly bound by the DeltaN-HtrA3L/S but not cleaved.

    HtrA3 is a cellular partner of cytoskeleton proteins and TCP1α chaperonin.
    Wenta T, Zurawa-Janicka D, Rychlowski M, Jarzab M, Glaza P, Lipinska A, Bienkowska-Szewczyk K, Herman-Antosiewicz A, Skorko-Glonek J, Lipinska B.

    07/13/2019
    Chaperonin CCT interferes with fibre assembly by interaction of its CCTzeta and CCTgamma subunits with the A53T central hydrophobic region. This interaction is specific to NAC conformation, as it is produced once soluble alpha-synuclein A53T oligomers form and blocks the reaction before fibres begin to grow.

    The chaperonin CCT inhibits assembly of α-synuclein amyloid fibrils by a specific, conformation-dependent interaction.
    Sot B, Rubio-Muñoz A, Leal-Quintero A, Martínez-Sabando J, Marcilla M, Roodveldt C, Valpuesta JM., Free PMC Article

    10/27/2018
    chaperonin-containing TCP-1 complex required for lysosomal functioning and autophagosome degradation

    CCT complex restricts neuropathogenic protein aggregation via autophagy.
    Pavel M, Imarisio S, Menzies FM, Jimenez-Sanchez M, Siddiqi FH, Wu X, Renna M, O'Kane CJ, Crowther DC, Rubinsztein DC., Free PMC Article

    09/22/2018
    Result suggest the positive correlation between purinergic receptor P2X 7 (P2X7R) and T-complex protein 1 (TCP-1) in lymphoma patients.

    Silencing P2X7 receptor downregulates the expression of TCP-1 involved in lymphoma lymphatic metastasis.
    Jiang X, Mao W, Yang Z, Zeng J, Zhang Y, Song Y, Kong Y, Ren S, Zuo Y., Free PMC Article

    10/1/2016
    Data suggest that biosynthesis and folding of leukemogenic fusion oncoprotein AML1-ETO/RUNX1-RUNX1T1 is facilitated by interaction with the chaperonin TRiC/CCT1/TCP1 and HSP70 (heat shock protein 70).

    Chaperonin TRiC/CCT Modulates the Folding and Activity of Leukemogenic Fusion Oncoprotein AML1-ETO.
    Roh SH, Kasembeli M, Galaz-Montoya JG, Trnka M, Lau WC, Burlingame A, Chiu W, Tweardy DJ., Free PMC Article

    08/6/2016
    Changes for CRMP2, TCP1epsilon, TPM2 and 14-3-3gamma were confirmed in experimental tumors and in a series of 28 human SI-NETs.

    Mechanisms of local invasion in enteroendocrine tumors: identification of novel candidate cytoskeleton-associated proteins in an experimental mouse model by a proteomic approach and validation in human tumors.
    Couderc C, Bollard J, Couté Y, Massoma P, Poncet G, Lepinasse F, Hervieu V, Gadot N, Sanchez JC, Scoazec JY, Diaz JJ, Roche C.

    08/8/2015
    A role for the TRiC subunits TCP1 and CCT2, and potentially the entire TRiC complex, in breast cancer.

    Two members of the TRiC chaperonin complex, CCT2 and TCP1 are essential for survival of breast cancer cells and are linked to driving oncogenes.
    Guest ST, Kratche ZR, Bollig-Fischer A, Haddad R, Ethier SP.

    05/16/2015
    CCT8 might be an oncogene and participate in HCC cell proliferation.

    Chaperonin containing TCP1, subunit 8 (CCT8) is upregulated in hepatocellular carcinoma and promotes HCC proliferation.
    Huang X, Wang X, Cheng C, Cai J, He S, Wang H, Liu F, Zhu C, Ding Z, Huang X, Zhang T, Zhang Y.

    12/20/2014
    identified 6 of the 8 components of the chaperonin-containing TCP-1 (CCT) complex bound to LOX-1 cytoplasmic domain

    Chaperonin-containing TCP-1 complex directly binds to the cytoplasmic domain of the LOX-1 receptor.
    Bakthavatsalam D, Soung RH, Tweardy DJ, Chiu W, Dixon RA, Woodside DG., Free PMC Article

    08/16/2014
    A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration.

    Proteomic analysis identifies dysfunction in cellular transport, energy, and protein metabolism in different brain regions of atypical frontotemporal lobar degeneration.
    Martins-de-Souza D, Guest PC, Mann DM, Roeber S, Rahmoune H, Bauder C, Kretzschmar H, Volk B, Baborie A, Bahn S.

    04/26/2012
    Data suggest that specific molecular mediators involved in glucocerebrosidase maturation and degradation, and abnormal interaction with TCP1 and c-Cbl, could be responsible for phenotypic variation among patients with the same genotypes.

    Decreased glucocerebrosidase activity in Gaucher disease parallels quantitative enzyme loss due to abnormal interaction with TCP1 and c-Cbl.
    Lu J, Chiang J, Iyer RR, Thompson E, Kaneski CR, Xu DS, Yang C, Chen M, Hodes RJ, Lonser RR, Brady RO, Zhuang Z., Free PMC Article

    05/14/2011
    Observational study of gene-disease association, gene-environment interaction, and pharmacogenomic / toxicogenomic. (HuGE Navigator)

    Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.
    Bailey SD, Xie C, Do R, Montpetit A, Diaz R, Mohan V, Keavney B, Yusuf S, Gerstein HC, Engert JC, Anand S, DREAM investigators., Free PMC Article

    09/15/2010
    the membrane binding domain of CTP:phosphocholine cytidylyltransferase has a role in alveolar type II cells

    Functions of membrane binding domain of CTP:phosphocholine cytidylyltransferase in alveolar type II cells.
    Ridsdale R, Tseu I, Wang J, Post M.

    07/19/2010
    Observational study and genome-wide association study of gene-disease association. (HuGE Navigator)

    A genome-wide association study identifies novel and functionally related susceptibility Loci for Kawasaki disease.
    Burgner D, Davila S, Breunis WB, Ng SB, Li Y, Bonnard C, Ling L, Wright VJ, Thalamuthu A, Odam M, Shimizu C, Burns JC, Levin M, Kuijpers TW, Hibberd ML, International Kawasaki Disease Genetics Consortium., Free PMC Article

    02/11/2009
    Observational study of gene-disease association. (HuGE Navigator)See all PubMed (2) articles

    Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.
    Talmud PJ, Drenos F, Shah S, Shah T, Palmen J, Verzilli C, Gaunt TR, Pallas J, Lovering R, Li K, Casas JP, Sofat R, Kumari M, Rodriguez S, Johnson T, Newhouse SJ, Dominiczak A, Samani NJ, Caulfield M, Sever P, Stanton A, Shields DC, Padmanabhan S, Melander O, Hastie C, Delles C, Ebrahim S, Marmot MG, Smith GD, Lawlor DA, Munroe PB, Day IN, Kivimaki M, Whittaker J, Humphries SE, Hingorani AD, ASCOT investigators, NORDIL investigators, BRIGHT Consortium.

    Family-based association studies of the TCP1 gene and schizophrenia in the Chinese Han population.
    Tang W, Shi Y, Feng G, Yan L, Xing Y, Zhu S, Liu J, Zhao X, Tang R, Du J, Zhang J, He G, Liang P, He L.

    03/13/2008
    The specific and directed rearrangement of the beta-actin structure, seen in the natural beta-actin-TRiC system, is vital for guiding beta-actin to the native state.

    Domain-specific chaperone-induced expansion is required for beta-actin folding: a comparison of beta-actin conformations upon interactions with GroEL and tail-less complex polypeptide 1 ring complex (TRiC).
    Villebeck L, Moparthi SB, Lindgren M, Hammarström P, Jonsson BH.

    01/21/2010
    TRiC chaperonin binds to HIF prolyl hydroxylase PHD3

    The HIF prolyl hydroxylase PHD3 is a potential substrate of the TRiC chaperonin.
    Masson N, Appelhoff RJ, Tuckerman JR, Tian YM, Demol H, Puype M, Vandekerckhove J, Ratcliffe PJ, Pugh CW.

    01/21/2010
    Expression patterns of chaperone proteins in cerebral cortex of the fetus with Down syndrome: dysregulation of T-complex protein 1.

    Expression patterns of chaperone proteins in cerebral cortex of the fetus with Down syndrome: dysregulation of T-complex protein 1.
    Yoo BC, Fountoulakis M, Dierssen M, Lubec G.

    01/21/2010
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