Recombinant human CREBBP protein
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(1 Publication)
Recombinant human CREBBP protein is a Human Fragment protein, in the 1081 to 1197 aa range, expressed in Escherichia coli, with >96%, suitable for SDS-PAGE, FuncS.
View Alternative Names
CBP, CREBBP, CREB-binding protein, Histone lysine acetyltransferase CREBBP, Protein lactyltransferas CREBBP, Protein-lysine acetyltransferase CREBBP
- FuncS
Supplier Data
Functional Studies - Recombinant human CREBBP protein (AB198130)
Activity assay using ab198130.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human CREBBP protein (AB198130)
4-20% SDS-PAGE analysis of ab198130 (2μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
CREBBP plays a pivotal role in regulating gene expression by serving as a coactivator that bridges transcription factors with the basal transcription machinery. CREBBP as part of large multiprotein complexes acetylates histones as well as non-histone proteins influencing chromatin accessibility and transcriptional efficiency. Its HAT activity contributes to the regulation of cell cycle differentiation and DNA repair.
Pathways
CREBBP integrates into both the p53 and Hedgehog signaling pathways modulating various cellular responses. In the p53 pathway CREBBP interacts with the tumor suppressor protein p53 enhancing p53’s ability to initiate expression of genes involved in cell cycle arrest and apoptosis. In the Hedgehog pathway CREBBP regulates transcription factors such as Gli proteins. The interplay between CREBBP and these pathways underlines its importance in maintaining cellular homeostasis and preventing oncogenesis.
Specifications
Form
Liquid
General info
Function
Acetylates histones, giving a specific tag for transcriptional activation (PubMed : 21131905, PubMed : 24616510). Mediates acetylation of histone H3 at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac, respectively) (PubMed : 21131905). Also acetylates non-histone proteins, like DDX21, FBL, IRF2, MAFG, NCOA3, POLR1E/PAF53 and FOXO1 (PubMed : 10490106, PubMed : 11154691, PubMed : 12738767, PubMed : 12929931, PubMed : 24207024, PubMed : 28790157, PubMed : 30540930, PubMed : 35675826, PubMed : 9707565). Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators : NPAS2-BMAL1 and CLOCK-BMAL1 heterodimers (PubMed : 14645221). Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (PubMed : 24939902). Acetylates POLR1E/PAF53, leading to decreased association of RNA polymerase I with the rDNA promoter region and coding region (PubMed : 24207024). Acetylates DDX21, thereby inhibiting DDX21 helicase activity (PubMed : 28790157). Acetylates FBL, preventing methylation of 'Gln-105' of histone H2A (H2AQ104me) (PubMed : 30540930). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as lactoyl-CoA, and is able to mediate protein lactylation (PubMed : 38128537). Catalyzes lactylation of MRE11 in response to DNA damage, thereby promoting DNA double-strand breaks (DSBs) via homologous recombination (HR) (PubMed : 38128537). Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (PubMed : 25514493).
Post-translational modifications
Methylation of the KIX domain by CARM1 blocks association with CREB. This results in the blockade of CREB signaling, and in activation of apoptotic response (By similarity).. Phosphorylated by CHUK/IKKA at Ser-1382 and Ser-1386; these phosphorylations promote cell growth by switching the binding preference of CREBBP from TP53 to NF-kappa-B (PubMed:17434128). Phosphorylated by _ at Ser-124 in response to DNA damage, promoting interaction with MRE11 and lactylation of MRE11 (PubMed:38128537).. Sumoylation negatively regulates transcriptional activity via the recruitment of DAAX.. Autoacetylation is required for binding to protein substrates, such as acetylated histones and acetylated TP53/p53 (PubMed:24616510). Autoacetylation is induced by glucose and fatty acids (PubMed:35675826).
Subcellular localisation
Nucleus
Target data
Publications (1)
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Nucleic acids research 48:9550-9570 PubMed32810208
2020
Applications
Unspecified application
Species
Unspecified reactive species
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