Search Results

Overview

Uniprot IDQ92793
Protein NameCREB-binding protein
Gene NameCREBBP
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
13 LDGPPNPKRAKLSSP
622 TPDPAALKDRRMENL
68 PDAASKHKQLSELLR

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)

Protein Sequence

10 MAENLLDGPP 20 NPKRAKLSSP 30 GFSANDSTDF 40 GSLFDLENDL 50 PDELIPNGGE 60 LGLLNSGNLV 70 PDAASKHKQL 80 SELLRGGSGS 90 SINPGIGNVS 100 ASSPVQQGLG 110 GQAQGQPNSA 120 NMASLSAMGK 130 SPLSQGDSSA 140 PSLPKQAAST 150 SGPTPAASQA 160 LNPQAQKQVG 170 LATSSPATSQ 180 TGPGICMNAN 190 FNQTHPGLLN 200 SNSGHSLINQ 210 ASQGQAQVMN 220 GSLGAAGRGR 230 GAGMPYPTPA 240 MQGASSSVLA 250 ETLTQVSPQM 260 TGHAGLNTAQ 270 AGGMAKMGIT 280 GNTSPFGQPF 290 SQAGGQPMGA 300 TGVNPQLASK 310 QSMVNSLPTF 320 PTDIKNTSVT 330 NVPNMSQMQT 340 SVGIVPTQAI 350 ATGPTADPEK 360 RKLIQQQLVL 370 LLHAHKCQRR 380 EQANGEVRAC 390 SLPHCRTMKN 400 VLNHMTHCQA 410 GKACQVAHCA 420 SSRQIISHWK 430 NCTRHDCPVC 440 LPLKNASDKR 450 NQQTILGSPA 460 SGIQNTIGSV 470 GTGQQNATSL 480 SNPNPIDPSS 490 MQRAYAALGL 500 PYMNQPQTQL 510 QPQVPGQQPA 520 QPQTHQQMRT 530 LNPLGNNPMN 540 IPAGGITTDQ 550 QPPNLISESA 560 LPTSLGATNP 570 LMNDGSNSGN 580 IGTLSTIPTA 590 APPSSTGVRK 600 GWHEHVTQDL 610 RSHLVHKLVQ 620 AIFPTPDPAA 630 LKDRRMENLV 640 AYAKKVEGDM 650 YESANSRDEY 660 YHLLAEKIYK 670 IQKELEEKRR 680 SRLHKQGILG 690 NQPALPAPGA 700 QPPVIPQAQP 710 VRPPNGPLSL 720 PVNRMQVSQG 730 MNSFNPMSLG 740 NVQLPQAPMG 750 PRAASPMNHS 760 VQMNSMGSVP 770 GMAISPSRMP 780 QPPNMMGAHT 790 NNMMAQAPAQ 800 SQFLPQNQFP 810 SSSGAMSVGM 820 GQPPAQTGVS 830 QGQVPGAALP 840 NPLNMLGPQA 850 SQLPCPPVTQ 860 SPLHPTPPPA 870 STAAGMPSLQ 880 HTTPPGMTPP 890 QPAAPTQPST 900 PVSSSGQTPT 910 PTPGSVPSAT 920 QTQSTPTVQA 930 AAQAQVTPQP 940 QTPVQPPSVA 950 TPQSSQQQPT 960 PVHAQPPGTP 970 LSQAAASIDN 980 RVPTPSSVAS 990 AETNSQQPGP 1000 DVPVLEMKTE 1010 TQAEDTEPDP 1020 GESKGEPRSE 1030 MMEEDLQGAS 1040 QVKEETDIAE 1050 QKSEPMEVDE 1060 KKPEVKVEVK 1070 EEEESSSNGT 1080 ASQSTSPSQP 1090 RKKIFKPEEL 1100 RQALMPTLEA 1110 LYRQDPESLP 1120 FRQPVDPQLL 1130 GIPDYFDIVK 1140 NPMDLSTIKR 1150 KLDTGQYQEP 1160 WQYVDDVWLM 1170 FNNAWLYNRK 1180 TSRVYKFCSK 1190 LAEVFEQEID 1200 PVMQSLGYCC 1210 GRKYEFSPQT 1220 LCCYGKQLCT 1230 IPRDAAYYSY 1240 QNRYHFCEKC 1250 FTEIQGENVT 1260 LGDDPSQPQT 1270 TISKDQFEKK 1280 KNDTLDPEPF 1290 VDCKECGRKM 1300 HQICVLHYDI 1310 IWPSGFVCDN 1320 CLKKTGRPRK 1330 ENKFSAKRLQ 1340 TTRLGNHLED 1350 RVNKFLRRQN 1360 HPEAGEVFVR 1370 VVASSDKTVE 1380 VKPGMKSRFV 1390 DSGEMSESFP 1400 YRTKALFAFE 1410 EIDGVDVCFF 1420 GMHVQEYGSD 1430 CPPPNTRRVY 1440 ISYLDSIHFF 1450 RPRCLRTAVY 1460 HEILIGYLEY 1470 VKKLGYVTGH 1480 IWACPPSEGD 1490 DYIFHCHPPD 1500 QKIPKPKRLQ 1510 EWYKKMLDKA 1520 FAERIIHDYK 1530 DIFKQATEDR 1540 LTSAKELPYF 1550 EGDFWPNVLE 1560 ESIKELEQEE 1570 EERKKEESTA 1580 ASETTEGSQG 1590 DSKNAKKKNN 1600 KKTNKNKSSI 1610 SRANKKKPSM 1620 PNVSNDLSQK 1630 LYATMEKHKE 1640 VFFVIHLHAG 1650 PVINTLPPIV 1660 DPDPLLSCDL 1670 MDGRDAFLTL 1680 ARDKHWEFSS 1690 LRRSKWSTLC 1700 MLVELHTQGQ 1710 DRFVYTCNEC 1720 KHHVETRWHC 1730 TVCEDYDLCI 1740 NCYNTKSHAH 1750 KMVKWGLGLD 1760 DEGSSQGEPQ 1770 SKSPQESRRL 1780 SIQRCIQSLV 1790 HACQCRNANC 1800 SLPSCQKMKR 1810 VVQHTKGCKR 1820 KTNGGCPVCK 1830 QLIALCCYHA 1840 KHCQENKCPV 1850 PFCLNIKHKL 1860 RQQQIQHRLQ 1870 QAQLMRRRMA 1880 TMNTRNVPQQ 1890 SLPSPTSAPP 1900 GTPTQQPSTP 1910 QTPQPPAQPQ 1920 PSPVSMSPAG 1930 FPSVARTQPP 1940 TTVSTGKPTS 1950 QVPAPPPPAQ 1960 PPPAAVEAAR 1970 QIEREAQQQQ 1980 HLYRVNINNS 1990 MPPGRTGMGT 2000 PGSQMAPVSL 2010 NVPRPNQVSG 2020 PVMPSMPPGQ 2030 WQQAPLPQQQ 2040 PMPGLPRPVI 2050 SMQAQAAVAG 2060 PRMPSVQPPR 2070 SISPSALQDL 2080 LRTLKSPSSP 2090 QQQQQVLNIL 2100 KSNPQLMAAF 2110 IKQRTAKYVA 2120 NQPGMQPQPG 2130 LQSQPGMQPQ 2140 PGMHQQPSLQ 2150 NLNAMQAGVP 2160 RPGVPPQQQA 2170 MGGLNPQGQA 2180 LNIMNPGHNP 2190 NMASMNPQYR 2200 EMLRRQLLQQ 2210 QQQQQQQQQQ 2220 QQQQQQGSAG 2230 MAGGMAGHGQ 2240 FQQPQGPGGY 2250 PPAMQQQQRM 2260 QQHLPLQGSS 2270 MGQMAAQMGQ 2280 LGQMGQPGLG 2290 ADSTPNIQQA 2300 LQQRILQQQQ 2310 MKQQIGSPGQ 2320 PNPMSPQQHM 2330 LSGQPQASHL 2340 PGQQIATSLS 2350 NQVRSPAPVQ 2360 SPRPQSQPPH 2370 SSPSPRIQPQ 2380 PSPHHVSPQT 2390 GSPHPGLAVT 2400 MASSIDQGHL 2410 GNPEQSAMLP 2420 QLNTPSRSAL 2430 SSELSLVGDT 2440 TGDTLEKFVE GL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Molecular Function GO:0140297 DNA-binding transcription factor binding
Molecular Function GO:0004402 histone acetyltransferase activity
Molecular Function GO:0043993 histone H3K18 acetyltransferase activity
Molecular Function GO:0044017 histone H3K27 acetyltransferase activity
Molecular Function GO:0043426 MRF binding
Molecular Function GO:0002039 p53 binding
Molecular Function GO:0120300 peptide lactyltransferase (CoA-dependent) activity
Molecular Function GO:0061733 protein-lysine-acetyltransferase activity
Molecular Function GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding
Molecular Function GO:0048156 tau protein binding
Molecular Function GO:0003713 transcription coactivator activity
Molecular Function GO:0001223 transcription coactivator binding
Molecular Function GO:0003714 transcription corepressor activity
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0141156 cAMP/PKA signal transduction
Biological Process GO:0007249 canonical NF-kappaB signal transduction
Biological Process GO:0031669 cellular response to nutrient levels
Biological Process GO:0034644 cellular response to UV
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0042733 embryonic digit morphogenesis
Biological Process GO:0016479 negative regulation of transcription by RNA polymerase I
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:1901837 negative regulation of transcription of nucleolar large rRNA by RNA polymerase I
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:1905168 positive regulation of double-strand break repair via homologous recombination
Biological Process GO:1900182 positive regulation of protein localization to nucleus
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0030511 positive regulation of transforming growth factor beta receptor signaling pathway
Biological Process GO:0031648 protein destabilization
Biological Process GO:0065003 protein-containing complex assembly
Biological Process GO:1900034 regulation of cellular response to heat
Biological Process GO:0006355 regulation of DNA-templated transcription
Biological Process GO:2000819 regulation of nucleotide-excision repair
Biological Process GO:0008589 regulation of smoothened signaling pathway
Biological Process GO:0001666 response to hypoxia
Biological Process GO:0048511 rhythmic process
Biological Process GO:0002223 stimulatory C-type lectin receptor signaling pathway
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0000123 histone acetyltransferase complex
Cellular Component GO:0016604 nuclear body
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005667 transcription regulator complex
Molecular Function GO:0016407 acetyltransferase activity
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0031490 chromatin DNA binding
Molecular Function GO:0003684 damaged DNA binding

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[3] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.