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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: CREB-binding protein

UniprotKB/SwissProt ID: Q92793 (Q92793)

Gene Name: CREBBP

Organism: Homo sapiens (Human)

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)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR001487 Bromodomain
IPR036427 Bromodomain-like_sf
IPR018359 Bromodomain_CS
IPR031162 CBP_P300_HAT
IPR013178 Histone_AcTrfase_Rtt109/CBP
IPR003101 KIX_dom
IPR036529 KIX_dom_sf
IPR009110 Nuc_rcpt_coact
IPR014744 Nuc_rcpt_coact_CREBbp
IPR037073 Nuc_rcpt_coact_CREBbp_sf
IPR056484 PHD_P300
IPR010303 RING_CBP-p300
IPR038547 RING_CBP-p300_sf
IPR035898 TAZ_dom_sf
IPR013083 Znf_RING/FYVE/PHD
IPR000197 Znf_TAZ
IPR000433 Znf_ZZ
IPR043145 Znf_ZZ_sf

The S-nitrosylation sites of Q92793

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 404 HMTHCQAGKA C QVAHCASSRQ