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Mice with a liver overexpression of insulin-like growth factor 2 (IGF2 (show IGF2 Proteins)) mRNA-binding protein p62/IMP2 (show IGF2BP2 Proteins)-2/IGF2BP2 (show IGF2BP2 Proteins)-2 show elevated Ccl2 (show CCL2 Proteins) levels, which models all stages of non-alcoholic fatty liver disease.
p62 is up-regulated in mouse proteinopathic hearts and promotes aggresome formation and autophagy activation and protects cardiomyocytes against proteotoxic stress
cdk1 (show CDK1 Proteins) phosphorylates p62 in vitro and in vivo at T269 and S272, which is necessary for the maintenance of appropriate cyclin B1 (show CCNB1 Proteins) levels and the levels of cdk1 (show CDK1 Proteins) activity necessary to allow cells to properly enter and exit mitosis.
p62 is a crucial regulator of ERK1 (show MAPK3 Proteins) in metabolism
p62 normally antagonizes basal ERK (show EPHB2 Proteins) activity and adipocyte differentiation and that its loss leads to the hyperactivation of ERK (show EPHB2 Proteins) that favors adipogenesis and obesity.
These data demonstrate that PKCzeta and its adaptor protein p62 play a key role in the modulation of K(V) channel function in pulmonary arteries.
Data suggest that a common TFIIH subunit (show GTF2H4 Proteins) p62 recruitment mechanism is shared by UV-stimulated scaffold protein A (UVSSA (show KIAA1530 Proteins)) in transcription-coupled repair (TCR) and xeroderma pigmentosum, complementation group C protein (XPC (show XPC Proteins)) in global genome repair (GGR (show GCGR Proteins)).
The N-terminal highly acidic region of TFIIEalpha interacts with the pleckstrin (show PLEK Proteins) homology domain of TFIIH and adopts an extended stringlike structure on the positive groove of the pleckstrin (show PLEK Proteins) homology domain with two hydrophobic amino acids, Phe387 and Val390, inserting into two shallow hydrophobic pockets of the pleckstrin (show PLEK Proteins) homology domain.
Here, the authors show that an acidic region of DP1 (show PTGDR Proteins), whose function has remained elusive, binds to the plekstrin homology (PH) domain of the p62 subunit of TFIIH that contributes to transcriptional activation.
Virulence factor NSs of rift valley fever virus recruits the FBXO3 (show FBXO3 Proteins) to degrade subunit p62 of general transcription factor TFIIH.
These data suggest that the RVFV NSs protein is able to interact with the TFIIH subunit p62 inside infected cells and promotes its degradation, which can occur directly in the nucleus.
p62 subunit of TFIIH interacts with TRbeta (show TXNRD2 Proteins) in a ligand-dependent manner.
The pleckstrin (show PLEK Proteins) homology domain from the 62 kDa subunit Tfb1 (residues 1-108) of TFIIH is sufficient for binding to the activation domain of herpes simplex virus protein VP16.
GTF2H1 polymorphisms/haplotypes may contribute to genetic susceptibility to lung cancer.
Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II.
general transcription factor IIH subunit 1
, TFIIH basal transcription factor complex p62 subunit
, basic transcription factor 2 62 kDa subunit
, general transcription factor IIH, polypeptide 1 (62kD subunit)
, general transcription factor IIH, polypeptide 1, 62kDa
, BTF2 p62
, general transcription factor IIH polypeptide 1
, general transcription factor IIH subunit 1-like