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Hipk2 promotes PP1c-mediated Dvl (show DVL2 Proteins) dephosphorylation via its C-terminal domain and is essential Dvl (show DVL2 Proteins) stability.
Results indicate that Hipk2 exerts a relevant role in the survival of cerebellar Purkinje cells and that Hipk2 genetic ablation generates cerebellar dysfunction compatible with an ataxic-like phenotype.
Our findings indicate that phosphorylation-dependent restriction of SIRT1 (show SIRT1 Proteins) activity by HIPK2 shapes the p53 (show TP53 Proteins) response
The findings highlight a complex regulation of CREB-binding protein (show CREBBP Proteins) activity by HIPK2, which might be relevant for the control of specific sets of target genes involved in cellular proliferation, differentiation and apoptosis.
MDM4 (show MDM4 Proteins)/HIPK2/p53 (show TP53 Proteins) cytoplasmic assembly uncovers coordinated repression of molecules with anti-apoptotic activity during early DNA damage response.
Results indicate that HIPK2 acts as a caretaker gene, whose inactivation increases tumorigenicity and causes chromosomal instability by cytokinesis failure.
HIPK2 expression tends to be decreased along tumor progression and may be involved with the invasive potential, suggesting a possible tumor suppressor role for HIPK2.
c-Abl (show ABL1 Proteins) was required for endogenous HIPK2 accumulation and phosphorylation of p53 (show TP53 Proteins) at Ser46 in response to DNA damage by gamma- and UV radiation.
Lafora disease proteins laforin (show EPM2A Proteins) and malin (show NHLRC1 Proteins) negatively regulate the HIPK2-p53 (show TP53 Proteins) cell death pathway.
HIPK2/HP1gamma (show CBX3 Proteins) pathway may uncover a new functional aspect of HIPK2 as a tumor suppressor.
Analysis of these mutants revealed that HIPK1 (show HIPK1 Proteins), HIPK2 and HIPK3 (show HIPK3 Proteins) but not HIPK4 (show HIPK4 Proteins) are capable of autophosphorylating on other tyrosines
HIPK2 is ubiquitinated upon heat shock.
Phosphorylation of KLF3 (show KLF3 Proteins) and CtBP2 (show CTBP2 Proteins) by HIPK2 strengthens the interaction between these two factors and increases transcriptional repression by KLF3 (show KLF3 Proteins).
Homeodomain-interacting protein kinase 2, a novel autoimmune regulator (show AIRE Proteins) interaction partner, modulates promiscuous gene expression in medullary thymic epithelial cells.
Hipk2 has an essential role in mouse white fat development
data identify Hipk2 as a novel regulator of C/EBPbeta (show CEBPB Proteins) and implicate different protein kinases in the cooperation of p300 (show NOTCH1 Proteins) with C/EBPbeta (show CEBPB Proteins) and C/EBPalpha (show CEBPA Proteins)
Data indicate a critical kinase HIPK2 function in cytokinesis and in the prevention of tetraploidization.
Hipk2 is a haploinsufficient tumor suppressor gene for mouse lymphoma development.
HIPK2 is an important transcriptional cofactor that regulates bone morphogenetic protein signaling in the maintenance of enteric neurons and glia.
HIPK2-mediated phosphorylation of PDX1 (show PDX1 Proteins) at Ser (show SIGLEC1 Proteins)-269 might be a regulatory mechanism connecting signals generated by changes in extracellular glucose concentration to downstream effectors, thereby influencing islet cell differentiation and function.
This gene encodes a conserved serine/threonine kinase that is a member of the homeodomain-interacting protein kinase family. The encoded protein interacts with homeodomain transcription factors and many other transcription factors such as p53, and can function as both a corepressor and a coactivator depending on the transcription factor and its subcellular localization. Multiple transcript variants encoding different isoforms have been found for this gene.
homeodomain interacting protein kinase 2
, serine/threonine protein kinase
, homeodomain-interacting protein kinase 2-like
, homeodomain-interacting protein kinase 2
, homeodomain-interacting protein kinase-2
, nuclear body-associated kinase 1
, sialophorin tail-associated nuclear serine/threonine-protein kinase
, Mx-interacting protein kinase PKM