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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Cyclin-dependent kinase 14

PFTK1, hPFTAIRE1, PFTAIRE, PFTAIRE protein kinase1
PFTK1 is a member of the CDC2 (MIM 116940)-related protein kinase family (Yang and Chen, 2001 [PubMed 11313143]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: CDC2, PCNA, PCTAIRE-1, Actin, V1a
Papers on PFTK1
PFTK1 regulates cell proliferation, migration and invasion in epithelial ovarian cancer.
Deng et al., Nantong, China. In Int J Biol Macromol, Feb 2016
UNASSIGNED: PFTK1, also named Cyclin-Dependent Kinase 14 (CDK14), is a member of the cell division cycle 2 (CDC2)-related protein kinase family.
A seven-gene expression panel distinguishing clonal expansions of pre-leukemic and chronic lymphocytic leukemia B cells from normal B lymphocytes.
Chiorazzi et al., United States. In Immunol Res, Dec 2015
Therefore, we selected FMOD, CKAP4, PIK3C2B, LEF1, PFTK1, BCL-2, and GPM6a from a set of genes significantly differentially expressed in microarray analyses that compared CLL cells with normal B lymphocytes and used these to determine whether we could discriminate CLL and MBL cells from B cells of healthy controls.
Knockdown of PFTK1 Inhibits the Migration of Glioma Cells.
Tao et al., Nantong, China. In J Mol Neurosci, Oct 2015
PFTK1 is a member of cyclin-dependent kinases (Cdks) family and has been reported to contribute to tumor migration and invasion.
Upregulated PFTK1 promotes tumor cell proliferation, migration, and invasion in breast cancer.
Yang et al., Nantong, China. In Med Oncol, Jul 2015
PFTK1 was a cell division cycle 2-related serine/threonine protein kinase, which was up-regulated in breast cancer tissues and breast cancer lines.
Serine/threonine-protein kinase PFTK1 modulates oligodendrocyte differentiation via PI3K/AKT pathway.
Feng et al., Xinxiang, China. In J Mol Neurosci, Apr 2015
Here, we newly identified a CDK-like protein, PFTK1, to be involved in OPC differentiation.
PFTK1 Promotes Gastric Cancer Progression by Regulating Proliferation, Migration and Invasion.
Wang et al., Nantong, China. In Plos One, 2014
PFTK1, also known as PFTAIRE1, CDK14, is a novel member of Cdc2-related serine/threonine protein kinases.
High Throughput Kinomic Profiling of Human Clear Cell Renal Cell Carcinoma Identifies Kinase Activity Dependent Molecular Subtypes.
Sonpavde et al., Alexandria, Egypt. In Plos One, 2014
Potential driver kinases implicated include PFTAIRE (PFTK1), PKG1, and SRC, which were identified in groups A, B, and C, respectively.
Regulation of protein phosphatase 1I by Cdc25C-associated kinase 1 (C-TAK1) and PFTAIRE protein kinase.
Hemmings et al., New York City, United States. In J Biol Chem, 2014
We studied the effects of two protein kinases identified previously in purified brain PP-1I by mass spectrometry, Cdc25C-associated kinase 1 (C-TAK1) and PFTAIRE (PFTK1) kinase, for their ability to regulate PP-1I.
PFTK1 interacts with cyclin Y to activate non-canonical Wnt signaling in hepatocellular carcinoma.
Wong et al., Hong Kong, Hong Kong. In Biochem Biophys Res Commun, 2014
PFTK1 is a Cdc2-related protein kinase that is frequently upregulated in human hepatocellular carcinoma (HCC) where it correlates with metastatic features and motile phenotypes.
Overexpression of PFTK1 predicts resistance to chemotherapy in patients with oesophageal squamous cell carcinoma.
Doki et al., Suita, Japan. In Br J Cancer, 2012
in patients with oesophageal squamous cell carcinoma 5-year overall survival rate was poorer in patients positive for PFTK1 than those with negative expression; uni- and multivariate analyses identified PFTK1 as an independent marker of prognosis
A novel interplay between oncogenic PFTK1 protein kinase and tumor suppressor TAGLN2 in the control of liver cancer cell motility.
Wong et al., Hong Kong, Hong Kong. In Oncogene, 2011
Taken together, our data propose a novel, oncogene-tumor suppressor interplay, where oncogenic PFTK1 confers HCC cell motility through inactivating the actin-binding motile suppressing function of TAGLN2 via phosphorylation.
Comparative promoter analysis in vivo: identification of a dendritic cell-specific promoter module.
Brocker et al., M√ľnchen, Germany. In Blood, 2011
A promoter database search identified 2 additional genes, Ppef2 and Pftk1, which have a similar promoter organization and are preferentially expressed in murine DCs.
Genome-wide association analysis of incident coronary heart disease (CHD) in African Americans: a short report.
Boerwinkle et al., Houston, United States. In Plos Genet, 2011
PFTK1 encodes a serine/threonine-protein kinase, PFTAIRE-1, that acts as a cyclin-dependent kinase regulating cell cycle progression and cell proliferation.
Phosphorylation of Caldesmon by PFTAIRE1 kinase promotes actin binding and formation of stress fibers.
Wong et al., Hong Kong, Hong Kong. In Mol Cell Biochem, 2011
Novel biological cascade that involved the phosphorylation activation of CaD by PFTK1 kinase in promoting formation of actin stress fibers.
Regulation of Lrp6 phosphorylation.
Shen et al., Heidelberg, Germany. In Cell Mol Life Sci, 2010
Here, we summarize how proline-directed kinases (Gsk3, PKA, Pftk1, Grk5/6) and non-proline-directed kinases (CK1 family) act upon Lrp6, how the phosphorylation is regulated by ligand binding and mitosis, and how Lrp6 phosphorylation leads to beta-catenin stabilization.
Thyrotropin-releasing hormone (TRH) in the cerebellum.
Yamada et al., Maebashi, Japan. In Cerebellum, 2007
Further analysis of TRH-deficient mice revealed that the expression of PFTAIRE protein kinase1 (PFTK1), a cdc2-related kinase, in the cerebellum was induced by TRH through the NO-cGMP pathway.
Functional characterization of human PFTK1 as a cyclin-dependent kinase.
Wu et al., Shanghai, China. In Proc Natl Acad Sci U S A, 2007
PFTK1 acts as a cyclin-dependent kinase that regulates cell cycle progression and cell proliferation
A Cdc2-related protein kinase hPFTAIRE1 from human brain interacting with 14-3-3 proteins.
Chen et al., Shanghai, China. In Cell Res, 2006
Ser119 is crucial for the interaction between hPFTAIRE1 and the 14-3-3 proteins. Binding with the 14-3-3 proteins does not contribute to the subcellular localization of the hPFTAIRE1, although the binding may be involved in its signaling regulation.
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