P45481

SS
Gene name
Crebbp (Cbp)
Protein name
Histone lysine acetyltransferase CREBBP
Names
EC 2.3.1.48 , Protein lactyltransferas CREBBP , EC 2.3.1.- , Protein-lysine acetyltransferase CREBBP , EC 2.3.1.-
Species
Mus musculus (Mouse)
KEGG Pathway
EC number
2.3.1.48: Transferring groups other than amino-acyl groups
Protein Class

Descriptions

Histone acetyltransferase p300 (EP300, also known as p300) is an enzyme that functions as histone acetyltransferase that regulates transcription of genes. It plays an essential role in regulating cell growth and division, prompting cells to mature and assume specialized functions, and preventing the growth of cancerous tumors. EP300 contains several domains including the CH1, KIX, CH3 (ZZ-TAZ2) and NCBD domains, which enable the interaction with numerous transcription factors and the basal transcription machinery. The activity of EP300 is regulated by its RING domain, or autoinhibitory loop within the HAT domain. The RING domain sterically occludes the HAT active site, and the displacement of the RING domain coupled to autoacetylation in trans results in full catalytic activation. Furthermore, the catalytic activity of EP300 is also regulated through acetylation / deacetylation of the autoinhibitory loop in the HAT domain, which impedes the acetyltransferase activity of EP300 but releases the inhibition upon hyper autoacetylation.

Autoinhibitory domains (AIDs)

1205-1279 (RING domain) SS

Target domain

1322-1702 (HAT domain)

Relief mechanism

PTM

Assay

1557-1619 (Autoinhibitory loop) SS

Target domain

1322-1702 (HAT domain)

Relief mechanism

PTM

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

29 structures for P45481

Entry ID Method Resolution Chain Position Source
1F81 NMR - A 1764-1850 PDB
1JJS NMR - A 2067-2112 PDB
1KBH NMR - B 2059-2117 PDB
1KDX NMR - A 586-666 PDB
1L8C NMR - A 345-439 PDB
1R8U NMR - B 340-439 PDB
1SB0 NMR - A 586-672 PDB
1TOT NMR - A 1700-1751 PDB
1U2N NMR - A 340-439 PDB
2AGH NMR - B 586-672 PDB
2C52 NMR - A 2059-2117 PDB
2KA4 NMR - A 340-439 PDB
2KA6 NMR - A 1764-1855 PDB
2KKJ NMR - A 2059-2117 PDB
2L14 NMR - A 2059-2117 PDB
2LQH NMR - A 586-672 PDB
2LQI NMR - A 586-672 PDB
2LWW NMR - A 340-439 PDB
4I9O X-ray 200 A A 586-672 PDB
5HOU NMR - A 340-439 PDB
5HP0 NMR - A 1764-1857 PDB
5HPD NMR - A 1764-1855 PDB
5U4K NMR - A 586-672 PDB
5U7G X-ray 240 A A/B 1079-1556 PDB
5W0I X-ray 143 A A 1083-1198 PDB
6DMX X-ray 280 A B/D/G/I 586-672 PDB
6DNQ X-ray 235 A B/D 586-672 PDB
7LVS X-ray 202 A B 340-439 PDB
AF-P45481-F1 Predicted AlphaFoldDB

No variants for P45481

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P45481

No associated diseases with P45481

4 regional properties for P45481

Type Name Position InterPro Accession
domain Protein kinase domain 29 - 280 IPR000719
domain SARAH domain 432 - 479 IPR011524
binding_site Protein kinase, ATP binding site 35 - 58 IPR017441
domain Mst1 SARAH domain 432 - 479 IPR024205

Functions

Description
EC Number 2.3.1.48 Transferring groups other than amino-acyl groups
Subcellular Localization
  • Cytoplasm
  • Nucleus
  • Recruited to nuclear bodies by SS18L1/CREST
  • In the presence of ALX1 relocalizes from the cytoplasm to the nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

11 GO annotations of cellular component

Name Definition
chromatin The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
histone acetyltransferase complex A protein complex that possesses histone acetyltransferase activity.
nuclear body Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
outer kinetochore The region of a kinetochore most external to centromeric DNA; this outer region mediates kinetochore-microtubule interactions.
PML body A class of nuclear body; they react against SP100 auto-antibodies (PML, promyelocytic leukemia); cells typically contain 10-30 PML bodies per nucleus; alterations in the localization of PML bodies occurs after viral infection.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
RNA polymerase II transcription regulator complex A transcription factor complex that acts at a regulatory region of a gene transcribed by RNA polymerase II.
transcription regulator complex A protein complex that is capable of associating with DNA by direct binding, or via other DNA-binding proteins or complexes, and regulating transcription.

25 GO annotations of molecular function

Name Definition
acetyltransferase activity Catalysis of the transfer of an acetyl group to an acceptor molecule.
cAMP response element binding protein binding Binding to a cAMP response element binding protein (a CREB protein).
chromatin binding Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.
chromatin DNA binding Binding to DNA that is assembled into chromatin.
damaged DNA binding Binding to damaged DNA.
disordered domain specific binding Binding to a disordered domain of a protein.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA-binding transcription factor binding Binding to a DNA-binding transcription factor, a protein that interacts with a specific DNA sequence (sometimes referred to as a motif) within the regulatory region of a gene to modulate transcription.
histone acetyltransferase activity Catalysis of the reaction
histone H3K18 acetyltransferase activity Catalysis of the reaction
histone H3K27 acetyltransferase activity Catalysis of the reaction
molecular adaptor activity The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.
MRF binding Binding to Myogenic Regulatory Factor (MRF), a member of the basic Helix-Loop-Helix (bHLH) superfamily of transcription factors.
peptide lactyltransferase activity Catalysis of the reaction
peptide-lysine-N-acetyltransferase activity Catalysis of the reaction
peroxisome proliferator activated receptor binding Binding to a peroxisome proliferator activated receptor, alpha, beta or gamma.
protein domain specific binding Binding to a specific domain of a protein.
protein-containing complex binding Binding to a macromolecular complex.
RNA polymerase II transcription regulatory region sequence-specific DNA binding Binding to a specific sequence of DNA that is part of a regulatory region that controls the transcription of a gene or cistron by RNA polymerase II.
RNA polymerase II-specific DNA-binding transcription factor binding Binding to a sequence-specific DNA binding RNA polymerase II transcription factor, any of the factors that interact selectively and non-covalently with a specific DNA sequence in order to modulate transcription.
SMAD binding Binding to a SMAD signaling protein.
TFIIB-class transcription factor binding Binding to a general RNA polymerase II transcription factor of the TFIIB class, one of the factors involved in formation of the preinitiation complex (PIC) by RNA polymerase II.
transcription coactivator activity A transcription coregulator activity that activates or increases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coactivators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. A fourth class of coactivator activity is the bridging of a DNA-binding transcription factor to the general (basal) transcription machinery. The Mediator complex, which bridges sequence-specific DNA binding transcription factors and RNA polymerase, is also a transcription coactivator.
transcription coactivator binding Binding to a transcription coactivator, a protein involved in positive regulation of transcription via protein-protein interactions with transcription factors and other proteins that positively regulate transcription. Transcription coactivators do not bind DNA directly, but rather mediate protein-protein interactions between activating transcription factors and the basal transcription machinery.
zinc ion binding Binding to a zinc ion (Zn).

24 GO annotations of biological process

Name Definition
behavioral response to cocaine Any process that results in a change in the behavior of an organism as a result of a cocaine stimulus.
cellular response to hepatocyte growth factor stimulus Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hepatocyte growth factor stimulus.
cellular response to UV Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers.
cellular response to virus Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a virus.
face morphogenesis The process in which the anatomical structures of the face are generated and organized. The face is the ventral division of the head.
germ-line stem cell population maintenance Any process by which an organism or tissue maintains a population of germ-line stem cells.
long-term memory The memory process that deals with the storage, retrieval and modification of information a long time (typically weeks, months or years) after receiving that information. This type of memory is typically dependent on gene transcription regulated by second messenger activation.
N-terminal peptidyl-lysine acetylation The acetylation of the N-terminal lysine of proteins.
negative regulation of interferon-beta production Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-beta production.
negative regulation of transcription by RNA polymerase I Any process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase I.
negative regulation of viral process Any process that stops, prevents, or reduces the frequency, rate or extent of a multi-organism process in which a virus is a participant.
positive regulation of cell adhesion molecule production Any process that increases the rate, frequency or extent of cell adhesion molecule production. Cell adhesion molecule production is the appearance of a cell adhesion molecule as a result of its biosynthesis or a decrease in its catabolism.
positive regulation of dendritic spine development Any process that increases the rate, frequency, or extent of dendritic spine development, the process whose specific outcome is the progression of the dendritic spine over time, from its formation to the mature structure.
positive regulation of DNA-binding transcription factor activity Any process that activates or increases the frequency, rate or extent of activity of a transcription factor, any factor involved in the initiation or regulation of transcription.
positive regulation of DNA-templated transcription Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription.
positive regulation of double-strand break repair via homologous recombination Any process that activates or increases the frequency, rate or extent of double-strand break repair via homologous recombination.
positive regulation of G1/S transition of mitotic cell cycle Any signalling pathway that increases or activates a cell cycle cyclin-dependent protein kinase to modulate the switch from G1 phase to S phase of the mitotic cell cycle.
positive regulation of gene expression Any process that increases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA).
positive regulation of non-canonical NF-kappaB signal transduction Any process that activates or increases the frequency, rate or extent of NIK/NF-kappaB signaling.
positive regulation of transcription by RNA polymerase II Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter.
protein destabilization Any process that decreases the stability of a protein, making it more vulnerable to degradative processes or aggregation.
protein modification process The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).
regulation of DNA-templated transcription Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
rhythmic process Any process pertinent to the generation and maintenance of rhythms in the physiology of an organism.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q09472 EP300 Histone acetyltransferase p300 Homo sapiens (Human) EV
Q92793 CREBBP CREB-binding protein Homo sapiens (Human) SS
B2RWS6 Ep300 Histone acetyltransferase p300 Mus musculus (Mouse) SS
Q6JHU9 Crebbp Histone lysine acetyltransferase CREBBP Rattus norvegicus (Rat) SS
10 20 30 40 50 60
MAENLLDGPP NPKRAKLSSP GFSANDNTDF GSLFDLENDL PDELIPNGEL SLLNSGNLVP
70 80 90 100 110 120
DAASKHKQLS ELLRGGSGSS INPGIGNVSA SSPVQQGLGG QAQGQPNSTN MASLGAMGKS
130 140 150 160 170 180
PLNQGDSSTP NLPKQAASTS GPTPPASQAL NPQAQKQVGL VTSSPATSQT GPGICMNANF
190 200 210 220 230 240
NQTHPGLLNS NSGHSLMNQA QQGQAQVMNG SLGAAGRGRG AGMPYPAPAM QGATSSVLAE
250 260 270 280 290 300
TLTQVSPQMA GHAGLNTAQA GGMTKMGMTG TTSPFGQPFS QTGGQQMGAT GVNPQLASKQ
310 320 330 340 350 360
SMVNSLPAFP TDIKNTSVTT VPNMSQLQTS VGIVPTQAIA TGPTADPEKR KLIQQQLVLL
370 380 390 400 410 420
LHAHKCQRRE QANGEVRACS LPHCRTMKNV LNHMTHCQAG KACQVAHCAS SRQIISHWKN
430 440 450 460 470 480
CTRHDCPVCL PLKNASDKRN QQTILGSPAS GIQNTIGSVG AGQQNATSLS NPNPIDPSSM
490 500 510 520 530 540
QRAYAALGLP YMNQPQTQLQ PQVPGQQPAQ PPAHQQMRTL NALGNNPMSI PAGGITTDQQ
550 560 570 580 590 600
PPNLISESAL PTSLGATNPL MNDGSNSGNI GSLSTIPTAA PPSSTGVRKG WHEHVTQDLR
610 620 630 640 650 660
SHLVHKLVQA IFPTPDPAAL KDRRMENLVA YAKKVEGDMY ESANSRDEYY HLLAEKIYKI
670 680 690 700 710 720
QKELEEKRRS RLHKQGILGN QPALPASGAQ PPVIPPAQSV RPPNGPLPLP VNRMQVSQGM
730 740 750 760 770 780
NSFNPMSLGN VQLPQAPMGP RAASPMNHSV QMNSMASVPG MAISPSRMPQ PPNMMGTHAN
790 800 810 820 830 840
NIMAQAPTQN QFLPQNQFPS SSGAMSVNSV GMGQPAAQAG VSQGQVPGAA LPNPLNMLAP
850 860 870 880 890 900
QASQLPCPPV TQSPLHPTPP PASTAAGMPS LQHPTAPGMT PPQPAAPTQP STPVSSGQTP
910 920 930 940 950 960
TPTPGSVPSA AQTQSTPTVQ AAAQAQVTPQ PQTPVQPPSV ATPQSSQQQP TPVHTQPPGT
970 980 990 1000 1010 1020
PLSQAAASID NRVPTPSSVT SAETSSQQPG PDVPMLEMKT EVQTDDAEPE PTESKGEPRS
1030 1040 1050 1060 1070 1080
EMMEEDLQGS SQVKEETDTT EQKSEPMEVE EKKPEVKVEA KEEEENSSND TASQSTSPSQ
1090 1100 1110 1120 1130 1140
PRKKIFKPEE LRQALMPTLE ALYRQDPESL PFRQPVDPQL LGIPDYFDIV KNPMDLSTIK
1150 1160 1170 1180 1190 1200
RKLDTGQYQE PWQYVDDVWL MFNNAWLYNR KTSRVYKFCS KLAEVFEQEI DPVMQSLGYC
1210 1220 1230 1240 1250 1260
CGRKYEFSPQ TLCCYGKQLC TIPRDAAYYS YQNRYHFCEK CFTEIQGENV TLGDDPSQPQ
1270 1280 1290 1300 1310 1320
TTISKDQFEK KKNDTLDPEP FVDCKECGRK MHQICVLHYD IIWPSGFVCD NCLKKTGRPR
1330 1340 1350 1360 1370 1380
KENKFSAKRL QTTRLGNHLE DRVNKFLRRQ NHPEAGEVFV RVVASSDKTV EVKPGMKSRF
1390 1400 1410 1420 1430 1440
VDSGEMSESF PYRTKALFAF EEIDGVDVCF FGMHVQNTAL IAPHQIQGRV YISYLDSIHF
1450 1460 1470 1480 1490 1500
FRPRCLRTAV YHEILIGYLE YVKKLGYVTG HIWACPPSEG DDYIFHCHPP DQKIPKPKRL
1510 1520 1530 1540 1550 1560
QEWYKKMLDK AFAERIINDY KDIFKQANED RLTSAKELPY FEGDFWPNVL EESIKELEQE
1570 1580 1590 1600 1610 1620
EEERKKEEST AASETPEGSQ GDSKNAKKKN NKKTNKNKSS ISRANKKKPS MPNVSNDLSQ
1630 1640 1650 1660 1670 1680
KLYATMEKHK EVFFVIHLHA GPVISTQPPI VDPDPLLSCD LMDGRDAFLT LARDKHWEFS
1690 1700 1710 1720 1730 1740
SLRRSKWSTL CMLVELHTQG QDRFVYTCNE CKHHVETRWH CTVCEDYDLC INCYNTKSHT
1750 1760 1770 1780 1790 1800
HKMVKWGLGL DDEGSSQGEP QSKSPQESRR LSIQRCIQSL VHACQCRNAN CSLPSCQKMK
1810 1820 1830 1840 1850 1860
RVVQHTKGCK RKTNGGCPVC KQLIALCCYH AKHCQENKCP VPFCLNIKHK LRQQQIQHRL
1870 1880 1890 1900 1910 1920
QQAQLMRRRM ATMNTRNVPQ QSLPSPTSAP PGTPTQQPST PQTPQPPAQP QPSPVNMSPA
1930 1940 1950 1960 1970 1980
GFPNVARTQP PTIVSAGKPT NQVPAPPPPA QPPPAAVEAA RQIEREAQQQ QHLYRANINN
1990 2000 2010 2020 2030 2040
GMPPGRAGMG TPGSQMTPVG LNVPRPNQVS GPVMSSMPPG QWQQAPIPQQ QPMPGMPRPV
2050 2060 2070 2080 2090 2100
MSMQAQAAVA GPRMPNVQPP RSISPSALQD LLRTLKSPSS PQQQQQVLNI LKSNPQLMAA
2110 2120 2130 2140 2150 2160
FIKQRTAKYV ANQPGMQPQP GLQSQPGMQP QPGMHQQPSL QNLNAMQAGV PRPGVPPPQP
2170 2180 2190 2200 2210 2220
AMGGLNPQGQ ALNIMNPGHN PNMTNMNPQY REMVRRQLLQ HQQQQQQQQQ QQQQQQNSAS
2230 2240 2250 2260 2270 2280
LAGGMAGHSQ FQQPQGPGGY APAMQQQRMQ QHLPIQGSSM GQMAAPMGQL GQMGQPGLGA
2290 2300 2310 2320 2330 2340
DSTPNIQQAL QQRILQQQQM KQQIGSPGQP NPMSPQQHML SGQPQASHLP GQQIATSLSN
2350 2360 2370 2380 2390 2400
QVRSPAPVQS PRPQSQPPHS SPSPRIQPQP SPHHVSPQTG SPHPGLAVTM ASSMDQGHLG
2410 2420 2430 2440
NPEQSAMLPQ LNTPNRSALS SELSLVGDTT GDTLEKFVEG L