Q09472 (EP300_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone acetyltransferase p300
Short name=p300 HAT
EC=2.3.1.48

Alternative name(s):
E1A-associated protein p300

Gene names

Name:	EP300
Synonyms:	P300

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2414 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. Also functions as acetyltransferase for nonhistone targets. Acetylates 'Lys-131' of ALX1 and acts as its coactivator in the presence of CREBBP. Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function. Acetylates HDAC1 leading to its inactivation and modulation of transcription. Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2. Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium. Promotes cardiac myocyte enlargement. Can also mediate transcriptional repression. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Acetylates FOXO1 and enhances its transcriptional activity. Ref.6 Ref.15 Ref.29 Ref.35 Ref.37 Ref.41 Ref.50 Ref.55 Ref.59
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone]. Ref.7
Subunit structure	Interacts with phosphorylated CREB1 By similarity. Interacts with HIF1A; the interaction is stimulated in response to hypoxia and inhibited by CITED2. Interacts (via N-terminus) with TFAP2A (via N-terminus); the interaction requires CITED2. Interacts (via CH1 domain) with CITED2 (via C-terminus). Interacts with CITED1 (unphosphorylated form preferentially and via C-terminus). Interacts with ESR1; the interaction is estrogen-dependent and enhanced by CITED1. Interacts with DTX1, EID1, ELF3, FEN1, LEF1, NCOA1, NCOA6, NR3C1, PCAF, PELP1, PRDM6, SP1, SP3, SPIB, SRY, TCF7L2, TP53, DDX5, DDX17, SATB1, SRCAP, TTC5, JMY and TRERF1. The TAZ-type 1 domain interacts with HIF1A. Probably part of a complex with HIF1A and CREBBP. Part of a complex containing CARM1 and NCOA2/GRIP1. Interacts with ING4 and this interaction may be indirect. Interacts with ING5. Interacts with the C-terminal region of CITED4. Interacts with HTLV-1 Tax and p30II. Interacts with and acetylates HIV-1 Tat. Non-sumoylated EP300 preferentially interacts with SENP3. Interacts with SS18L1/CREST. Interacts with ALX1 (via homeobox domain). Interacts with NEUROD1; the interaction is inhibited by NR0B2. Interacts with TCF3. Interacts (via CREB-binding domain) with MYOCD (via C-terminus) By similarity. Binds to HIPK2 By similarity. Interacts with ROCK2 and PPARG. Forms a complex made of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that stimulates hypertrophy in cardiomyocytes. Interacts with IRF1 and this interaction enhances acetylation of p53/TP53 and stimulation of its activity. Interacts with FOXO1; the interaction acetylates FOXO1 and enhances its transcriptional activity. Interacts with DDIT3/CHOP. Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.46 Ref.47 Ref.50 Ref.51 Ref.52 Ref.53 Ref.56 Ref.57 Ref.58 Ref.63 Ref.66 Ref.70 Ref.72
Subcellular location	Cytoplasm. Nucleus. Note: In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. Co-localizes with ROCK2 in the nucleus. Ref.37 Ref.52
Domain	The CRD1 domain (cell cycle regulatory domain 1) mediates transcriptional repression of a subset of p300 responsive genes; it can be de-repressed by CDKN1A/p21WAF1 at least at some promoters. It conatins sumoylation and acetylation sites and the same lysine residues may be targeted for the respective modifications. It is proposed that deacetylation by SIRT1 allows sumoylation leading to suppressed activity.
Post-translational modification	Acetylated on Lys at up to 17 positions by intermolecular autocatalysis. Deacetylated in the transcriptional repression domain (CRD1) by SIRT1, preferentially at Lys-1020. Citrullinated at Arg-2142 by PADI4, which impairs methylation by CARM1 and promotes interaction with NCOA2/GRIP1. Methylated at Arg-580 and Arg-604 in the KIX domain by CARM1, which blocks association with CREB, inhibits CREB signaling and activates apoptotic response. Also methylated at Arg-2142 by CARM1, which impairs interaction with NCOA2/GRIP1. Ref.6 Ref.51 Sumoylated; sumoylation in the transcriptional repression domain (CRD1) mediates transcriptional repression. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3. Ref.39 Ref.63 Probable target of ubiquitination by FBXO3, leading to rapid proteasome-dependent degradation. Phosphorylated by HIPK2 in a RUNX1-dependent manner. This phosphorylation that activates EP300 happens when RUNX1 is associated with DNA and CBFB. Phosphorylated by ROCK2 and this enhances its activity. Phosphorylation at Ser-89 by AMPK reduces interaction with nuclear receptors, such as PPARG. Ref.22 Ref.34 Ref.52 Ref.60
Involvement in disease	Defects in EP300 may play a role in epithelial cancer. Chromosomal aberrations involving EP300 may be a cause of acute myeloid leukemias. Translocation t(8;22)(p11;q13) with KAT6A. Rubinstein-Taybi syndrome 2 (RSTS2) [MIM:613684]: A disorder characterized by craniofacial abnormalities, postnatal growth deficiency, broad thumbs, broad big toes, mental retardation and a propensity for development of malignancies. Some individuals with RSTS2 have less severe mental impairment, more severe microcephaly, and a greater degree of changes in facial bone structure than RSTS1 patients. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.48
Sequence similarities	Contains 1 bromo domain. Contains 1 KIX domain. Contains 2 TAZ-type zinc fingers. Contains 1 ZZ-type zinc finger.

Ontologies

Keywords
Biological process	Cell cycle Host-virus interaction Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Disease	Disease mutation
Domain	Bromodomain Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Transferase
PTM	Acetylation Citrullination Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	N-terminal peptidyl-lysine acetylation Inferred from direct assay PubMed 12435739. Source: UniProtKB Notch signaling pathway Traceable author statement. Source: Reactome cell cycle Inferred from electronic annotation. Source: UniProtKB-KW heart development Inferred from electronic annotation. Source: Compara histone H4 acetylation Inferred from mutant phenotype PubMed 16325578. Source: UniProtKB innate immune response Traceable author statement. Source: Reactome intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Inferred from direct assay PubMed 17403783. Source: UniProtKB lung development Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.15. Source: UniProtKB nervous system development Traceable author statement PubMed 10205054. Source: ProtInc organ morphogenesis Inferred from electronic annotation. Source: Compara positive regulation by host of viral transcription Inferred from direct assay PubMed 16687403. Source: BHF-UCL positive regulation of protein binding Inferred from electronic annotation. Source: Compara positive regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 10518217. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.35. Source: UniProtKB regulation of androgen receptor signaling pathway Inferred from direct assay PubMed 18487222. Source: BHF-UCL regulation of transcription from RNA polymerase II promoter in response to hypoxia Traceable author statement. Source: Reactome response to estrogen stimulus Inferred from direct assay Ref.21. Source: UniProtKB skeletal muscle tissue development Inferred from electronic annotation. Source: Compara somitogenesis Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA histone acetyltransferase complex Inferred from electronic annotation. Source: Compara nucleoplasm Traceable author statement. Source: Reactome transcription factor complex Inferred from electronic annotation. Source: Compara
Molecular_function	chromatin DNA binding Inferred from electronic annotation. Source: Compara chromatin binding Inferred from mutant phenotype PubMed 17641689. Source: UniProtKB core promoter binding Inferred from direct assay PubMed 17641689. Source: UniProtKB histone acetyltransferase activity Inferred from direct assay PubMed 12040021. Source: UniProtKB lysine N-acetyltransferase activity Inferred from direct assay PubMed 20019387. Source: UniProtKB transcription coactivator activity Inferred from direct assay PubMed 12435739Ref.35. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APEX1	P27695	6	EBI-447295,EBI-1048805
BRD7	Q9NPI1	3	EBI-447295,EBI-711221
CITED2	Q99967	3	EBI-447295,EBI-937732
DDX5	P17844	4	EBI-447295,EBI-351962
HIF1A	Q16665	5	EBI-447295,EBI-447269
Hif1a	Q61221	2	EBI-447295,EBI-298954	From a different organism.
Jmy	Q9QXM1	16	EBI-447295,EBI-866001	From a different organism.
KAT2B	Q92831	2	EBI-447295,EBI-477430
NAP1L1	P55209	3	EBI-447295,EBI-356392
POU3F2	P20265	3	EBI-447295,EBI-1167176
SIRT1	Q96EB6	2	EBI-447295,EBI-1802965
SKP2	Q13309	3	EBI-447295,EBI-456291
TFAP2A	P05549	7	EBI-447295,EBI-347351
TP53	P04637	7	EBI-447295,EBI-366083
YBX1	P67809	2	EBI-447295,EBI-354065

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 2414

2413

Histone acetyltransferase p300

PRO_0000211193

Regions

Domain

566 – 645

80

KIX

Domain

1067 – 1139

73

Bromo

Zinc finger

331 – 417

87

TAZ-type 1

Zinc finger

1664 – 1707

44

ZZ-type

Zinc finger

1728 – 1809

82

TAZ-type 2

Region

2 – 139

138

Interaction with ALX1

Region

1017 – 1029

13

CRD1; mediates transcriptional repression

Region

1572 – 1818

247

Binding region for E1A adenovirus

Region

2003 – 2212

210

Interaction with HTLV-1 Tax

Region

2041 – 2240

200

Interaction with NCOA2

Motif

11 – 17

7

Nuclear localization signal Potential

Compositional bias

797 – 800

4

Poly-Ser

Compositional bias

1519 – 1526

8

Poly-Glu

Compositional bias

2066 – 2069

4

Poly-Gln

Compositional bias

2190 – 2195

6

Poly-Gln

Sites

Metal binding

347

1

Zinc 1

Metal binding

351

1

Zinc 1

Metal binding

364

1

Zinc 1

Metal binding

369

1

Zinc 1

Metal binding

378

1

Zinc 2

Metal binding

382

1

Zinc 2

Metal binding

388

1

Zinc 2

Metal binding

393

1

Zinc 2

Metal binding

402

1

Zinc 3

Metal binding

406

1

Zinc 3

Metal binding

411

1

Zinc 3

Metal binding

414

1

Zinc 3

Site

31 – 32

2

Breakpoint for translocation to form KAT6A-EP300 and EP300-KAT6A

Site

2088

1

Interaction with NCOA2

Site

2142

1

Interaction with NCOA2

Amino acid modifications

Modified residue

2

1

N-acetylalanine

Modified residue

89

1

Phosphoserine; by AMPK Ref.22 Ref.52

Modified residue

285

1

Phosphoserine

Modified residue

580

1

Omega-N-methylated arginine; by CARM1 Ref.6

Modified residue

604

1

Omega-N-methylated arginine; by CARM1 Ref.6

Modified residue

636

1

N6-acetyllysine Ref.65

Modified residue

885

1

Phosphothreonine

Modified residue

887

1

Phosphothreonine

Modified residue

977

1

N6-acetyllysine Ref.65

Modified residue

981

1

N6-acetyllysine

Modified residue

1020

1

N6-acetyllysine; alternate Ref.49

Modified residue

1024

1

N6-acetyllysine; alternate Ref.49

Modified residue

1038

1

Phosphoserine Ref.68

Modified residue

1103

1

N6-acetyllysine

Modified residue

1336

1

N6-acetyllysine Ref.54

Modified residue

1473

1

N6-acetyllysine Ref.54

Modified residue

1499

1

N6-acetyllysine; by autocatalysis Ref.45

Modified residue

1542

1

N6-acetyllysine Ref.65

Modified residue

1546

1

N6-acetyllysine Ref.65

Modified residue

1549

1

N6-acetyllysine; by autocatalysis Ref.45

Modified residue

1554

1

N6-acetyllysine; by autocatalysis Ref.45 Ref.65

Modified residue

1555

1

N6-acetyllysine Ref.65

Modified residue

1558

1

N6-acetyllysine Ref.45 Ref.65

Modified residue

1560

1

N6-acetyllysine; by autocatalysis Ref.45 Ref.65

Modified residue

1583

1

N6-acetyllysine Ref.65

Modified residue

1590

1

N6-acetyllysine

Modified residue

1674

1

N6-acetyllysine

Modified residue

1734

1

Phosphoserine

Modified residue

1857

1

Phosphothreonine

Modified residue

1859

1

Phosphothreonine

Modified residue

2142

1

Asymmetric dimethylarginine; by CARM1; alternate Ref.51

Modified residue

2142

1

Citrulline; by PADI4; alternate

Cross-link

1020

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.39

Cross-link

1024

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.39

Natural variations

Natural variant

289

1

M → V.
Corresponds to variant rs2230111 [ dbSNP | Ensembl ].

VAR_055554

Natural variant

827

1

L → P in a breast cancer sample. Ref.73

VAR_014428

Natural variant

997

1

I → V.
Corresponds to variant rs20551 [ dbSNP | Ensembl ].

VAR_020425

Natural variant

1013

1

E → G in a breast cancer sample. Ref.73

VAR_014429

Natural variant

1650

1

S → Y in a pancreatic cancer sample. Ref.73

VAR_014430

Natural variant

2174

1

T → S.
Corresponds to variant rs5758252 [ dbSNP | Ensembl ].

VAR_038376

Natural variant

2221

1

P → Q in a colorectal cancer sample. Ref.73
Corresponds to variant rs28937578 [ dbSNP | Ensembl ].

VAR_014431

Natural variant

2223

1

Q → P. Ref.1
Corresponds to variant rs1046088 [ dbSNP | Ensembl ].

VAR_038377

Experimental info

Mutagenesis

89

1

S → A: Abolishes AMPK-mediated phosphorylation. Ref.22

Mutagenesis

89

1

S → D: Phosphomimetic mutant that leads to descreased interaction with nuclear receptors. Ref.22

Mutagenesis

344

1

L → A: Inhibits interaction with HIF1A and transcription activation; when associated with A-345. Ref.70

Mutagenesis

345

1

L → A: Inhibits interaction with HIF1A and transcription activation; when associated with A-344. Ref.70

Mutagenesis

371 – 376

6

TMKNVL → NAAIRS: Inhibits interaction with HIF1A. Reduces interaction with CITED2. Ref.13

Mutagenesis

413 – 418

6

VCLPLK → NAAIRS: Inhibits interaction with HIF1A. Does not inhibit interaction with CITED2. Ref.13

Mutagenesis

1020

1

K → A: Abolishes sumoylation and transcriptional repression when associated with A-1024. Ref.39 Ref.49

Mutagenesis

1020

1

K → R: Abolishes sumoylation and transcriptional repression; when associated with R-1024. Ref.39 Ref.49

Mutagenesis

1024

1

K → A: Abolishes sumoylation and transcriptional repression; when associated with A-1020. Ref.39 Ref.49

Mutagenesis

1024

1

K → R: Abolishes sumoylation and transcriptional repression; when associated with R-1020. Ref.39 Ref.49

Mutagenesis

1357

1

T → L: 40% decrease in activity. Ref.71

Mutagenesis

1357

1

T → R: 40% decrease in activity. 90% decrease in activity; when associated with R-1505; R-1625 and R-1628. Ref.71

Mutagenesis

1396

1

S → R: Loss of activity; when associated with R-1397. Ref.71

Mutagenesis

1396

1

S → W: Loss of activity; when associated with W-1396. Ref.71

Mutagenesis

1397

1

Y → R: Loss of activity; when associated with R-1396. Ref.71

Mutagenesis

1397

1

Y → W: Loss of activity; when associated with W-1397. Ref.71

Mutagenesis

1399

1

D → Y: Does not interact with TFAP2A and inhibits transcriptional coactivation of TFAP2A by CITED2. Does not inhibit interaction with CITED2, DNA-binding of TFAP2A or nuclear localization of TFAP2A or CITED2. No enhancement of FOXO1-mediated transcriptional activity. No inhibition of insulin-mediated translocation to the cytoplasm. Ref.35 Ref.50

Mutagenesis

1505

1

E → R: 90% decrease in activity; when associated with R-1625 and R-1628. 90% decrease in activity; when associated with R-1357; R-1625 and R-1628. Ref.71

Mutagenesis

1625

1

D → R: 70% decrease in activity; when associated with R-1628. 90% decrease in activity; when associated with R-1505 and R-1628. 90% decrease in activity; when associated with R-1357; R-1505 and R-1628. Ref.71

Mutagenesis

1628

1

D → R: 70% decrease in activity; when associated with R-1625. 90% decrease in activity; when associated with E-1505 and R-1625. 90% decrease in activity; when associated with R-1357; R-1505 and R-1625. Ref.71

Mutagenesis

2056

1

R → K: No effect on interaction with NCOA2. Ref.51

Mutagenesis

2088

1

R → K: Abolishes interaction with NCOA2. Ref.51

Mutagenesis

2142

1

R → K: Strongly reduces interaction with NCOA2. Ref.51

Sequence conflict

169

1

M → T in AAA18639. Ref.1

Sequence conflict

204

1

N → D in AAA18639. Ref.1

Sequence conflict

928

1

T → N in AAA18639. Ref.1

Sequence conflict

1924

1

A → T in AAA18639. Ref.1

Secondary structure

1

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2414

Helix Strand Turn

Details...

Helix

332 – 334

3

Helix

335 – 355

21

Turn

356 – 358

3

Helix

367 – 379

13

Beta strand

386 – 389

4

Helix

391 – 405

15

Beta strand

408 – 410

3

Helix

414 – 418

5

Helix

1051 – 1066

16

Turn

1069 – 1072

4

Helix

1073 – 1075

3

Helix

1081 – 1084

4

Helix

1089 – 1092

4

Helix

1099 – 1107

9

Helix

1114 – 1131

18

Helix

1137 – 1159

23

Helix

1297 – 1313

17

Beta strand

1321 – 1334

14

Helix

1339 – 1342

4

Turn

1343 – 1347

5

Beta strand

1351 – 1366

16

Beta strand

1369 – 1381

13

Beta strand

1392 – 1400

9

Helix

1407 – 1409

3

Helix

1410 – 1428

19

Beta strand

1432 – 1436

5

Beta strand

1446 – 1450

5

Helix

1460 – 1476

17

Beta strand

1482 – 1485

4

Helix

1486 – 1493

8

Helix

1498 – 1500

3

Helix

1508 – 1517

10

Helix

1582 – 1590

9

Helix

1592 – 1594

3

Beta strand

1595 – 1601

7

Helix

1603 – 1606

4

Helix

1622 – 1624

3

Beta strand

1625 – 1627

3

Helix

1628 – 1636

9

Helix

1644 – 1662

19

Helix

1730 – 1747

18

Helix

1756 – 1770

15

Turn

1774 – 1778

5

Helix

1780 – 1793

14

Helix

1806 – 1818

13

Sequences

	Sequence		Length	Mass (Da)
	Q09472 [UniParc]. Last modified February 10, 2009. Version 2. Checksum: 8E869E1F174A6FEB	FASTA	2,414	264,161
	10 20 30 40 50 60 MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS TELGLTNGGD 70 80 90 100 110 120 INQLQTSLGM VQDAASKHKQ LSELLRSGSS PNLNMGVGGP GQVMASQAQQ SSPGLGLINS 130 140 150 160 170 180 MVKSPMTQAG LTSPNMGMGT SGPNQGPTQS TGMMNSPVNQ PAMGMNTGMN AGMNPGMLAA 190 200 210 220 230 240 GNGQGIMPNQ VMNGSIGAGR GRQNMQYPNP GMGSAGNLLT EPLQQGSPQM GGQTGLRGPQ 250 260 270 280 290 300 PLKMGMMNNP NPYGSPYTQN PGQQIGASGL GLQIQTKTVL SNNLSPFAMD KKAVPGGGMP 310 320 330 340 350 360 NMGQQPAPQV QQPGLVTPVA QGMGSGAHTA DPEKRKLIQQ QLVLLLHAHK CQRREQANGE 370 380 390 400 410 420 VRQCNLPHCR TMKNVLNHMT HCQSGKSCQV AHCASSRQII SHWKNCTRHD CPVCLPLKNA 430 440 450 460 470 480 GDKRNQQPIL TGAPVGLGNP SSLGVGQQSA PNLSTVSQID PSSIERAYAA LGLPYQVNQM 490 500 510 520 530 540 PTQPQVQAKN QQNQQPGQSP QGMRPMSNMS ASPMGVNGGV GVQTPSLLSD SMLHSAINSQ 550 560 570 580 590 600 NPMMSENASV PSLGPMPTAA QPSTTGIRKQ WHEDITQDLR NHLVHKLVQA IFPTPDPAAL 610 620 630 640 650 660 KDRRMENLVA YARKVEGDMY ESANNRAEYY HLLAEKIYKI QKELEEKRRT RLQKQNMLPN 670 680 690 700 710 720 AAGMVPVSMN PGPNMGQPQP GMTSNGPLPD PSMIRGSVPN QMMPRITPQS GLNQFGQMSM 730 740 750 760 770 780 AQPPIVPRQT PPLQHHGQLA QPGALNPPMG YGPRMQQPSN QGQFLPQTQF PSQGMNVTNI 790 800 810 820 830 840 PLAPSSGQAP VSQAQMSSSS CPVNSPIMPP GSQGSHIHCP QLPQPALHQN SPSPVPSRTP 850 860 870 880 890 900 TPHHTPPSIG AQQPPATTIP APVPTPPAMP PGPQSQALHP PPRQTPTPPT TQLPQQVQPS 910 920 930 940 950 960 LPAAPSADQP QQQPRSQQST AASVPTPTAP LLPPQPATPL SQPAVSIEGQ VSNPPSTSST 970 980 990 1000 1010 1020 EVNSQAIAEK QPSQEVKMEA KMEVDQPEPA DTQPEDISES KVEDCKMEST ETEERSTELK 1030 1040 1050 1060 1070 1080 TEIKEEEDQP STSATQSSPA PGQSKKKIFK PEELRQALMP TLEALYRQDP ESLPFRQPVD 1090 1100 1110 1120 1130 1140 PQLLGIPDYF DIVKSPMDLS TIKRKLDTGQ YQEPWQYVDD IWLMFNNAWL YNRKTSRVYK 1150 1160 1170 1180 1190 1200 YCSKLSEVFE QEIDPVMQSL GYCCGRKLEF SPQTLCCYGK QLCTIPRDAT YYSYQNRYHF 1210 1220 1230 1240 1250 1260 CEKCFNEIQG ESVSLGDDPS QPQTTINKEQ FSKRKNDTLD PELFVECTEC GRKMHQICVL 1270 1280 1290 1300 1310 1320 HHEIIWPAGF VCDGCLKKSA RTRKENKFSA KRLPSTRLGT FLENRVNDFL RRQNHPESGE 1330 1340 1350 1360 1370 1380 VTVRVVHASD KTVEVKPGMK ARFVDSGEMA ESFPYRTKAL FAFEEIDGVD LCFFGMHVQE 1390 1400 1410 1420 1430 1440 YGSDCPPPNQ RRVYISYLDS VHFFRPKCLR TAVYHEILIG YLEYVKKLGY TTGHIWACPP 1450 1460 1470 1480 1490 1500 SEGDDYIFHC HPPDQKIPKP KRLQEWYKKM LDKAVSERIV HDYKDIFKQA TEDRLTSAKE 1510 1520 1530 1540 1550 1560 LPYFEGDFWP NVLEESIKEL EQEEEERKRE ENTSNESTDV TKGDSKNAKK KNNKKTSKNK 1570 1580 1590 1600 1610 1620 SSLSRGNKKK PGMPNVSNDL SQKLYATMEK HKEVFFVIRL IAGPAANSLP PIVDPDPLIP 1630 1640 1650 1660 1670 1680 CDLMDGRDAF LTLARDKHLE FSSLRRAQWS TMCMLVELHT QSQDRFVYTC NECKHHVETR 1690 1700 1710 1720 1730 1740 WHCTVCEDYD LCITCYNTKN HDHKMEKLGL GLDDESNNQQ AAATQSPGDS RRLSIQRCIQ 1750 1760 1770 1780 1790 1800 SLVHACQCRN ANCSLPSCQK MKRVVQHTKG CKRKTNGGCP ICKQLIALCC YHAKHCQENK 1810 1820 1830 1840 1850 1860 CPVPFCLNIK QKLRQQQLQH RLQQAQMLRR RMASMQRTGV VGQQQGLPSP TPATPTTPTG 1870 1880 1890 1900 1910 1920 QQPTTPQTPQ PTSQPQPTPP NSMPPYLPRT QAAGPVSQGK AAGQVTPPTP PQTAQPPLPG 1930 1940 1950 1960 1970 1980 PPPAAVEMAM QIQRAAETQR QMAHVQIFQR PIQHQMPPMT PMAPMGMNPP PMTRGPSGHL 1990 2000 2010 2020 2030 2040 EPGMGPTGMQ QQPPWSQGGL PQPQQLQSGM PRPAMMSVAQ HGQPLNMAPQ PGLGQVGISP 2050 2060 2070 2080 2090 2100 LKPGTVSQQA LQNLLRTLRS PSSPLQQQQV LSILHANPQL LAAFIKQRAA KYANSNPQPI 2110 2120 2130 2140 2150 2160 PGQPGMPQGQ PGLQPPTMPG QQGVHSNPAM QNMNPMQAGV QRAGLPQQQP QQQLQPPMGG 2170 2180 2190 2200 2210 2220 MSPQAQQMNM NHNTMPSQFR DILRRQQMMQ QQQQQGAGPG IGPGMANHNQ FQQPQGVGYP 2230 2240 2250 2260 2270 2280 PQQQQRMQHH MQQMQQGNMG QIGQLPQALG AEAGASLQAY QQRLLQQQMG SPVQPNPMSP 2290 2300 2310 2320 2330 2340 QQHMLPNQAQ SPHLQGQQIP NSLSNQVRSP QPVPSPRPQS QPPHSSPSPR MQPQPSPHHV 2350 2360 2370 2380 2390 2400 SPQTSSPHPG LVAAQANPME QGHFASPDQN SMLSQLASNP GMANLHGASA TDLGLSTDNS 2410 DLNSNLSQST LDIH

References

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[2]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"MOZ is fused to p300 in an acute monocytic leukemia with t(8;22)." Chaffanet M., Gressin L., Preudhomme C., Soenen-Cornu V., Birnbaum D., Pebusque M.-J. Genes Chromosomes Cancer 28:138-144(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-42, CHROMOSOMAL TRANSLOCATION WITH KAT6A.
[5]	"Adenoviral E1A-associated protein p300 as a functional homologue of the transcriptional co-activator CBP." Lundblad J.R., Kwok R.P.S., Laurance M.E., Harter M.L., Goodman R.H. Nature 374:85-88(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 552-660.
[6]	"A transcriptional switch mediated by cofactor methylation." Xu W., Chen H., Du K., Asahara H., Tini M., Emerson B.M., Montminy M., Evans R.M. Science 294:2507-2511(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, INTERACTION WITH CARM1, METHYLATION AT ARG-580 AND ARG-604, FUNCTION.
[7]	"The transcriptional coactivators p300 and CBP are histone acetyltransferases." Ogryzko V.V., Schiltz R.L., Russanova V., Howard B.H., Nakatani Y. Cell 87:953-959(1996) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME ACTIVITY.
[8]	"A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A." Yang X.-J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y. Nature 382:319-324(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PCAF.
[9]	"An essential role for p300/CBP in the cellular response to hypoxia." Arany Z., Huang L.E., Eckner R., Bhattacharya S., Jiang C., Goldberg M.A., Bunn H.F., Livingston D.M. Proc. Natl. Acad. Sci. U.S.A. 93:12969-12973(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIF1A AND CREBBP.
[10]	"Differential transcriptional activation by human T-cell leukemia virus type 1 Tax mutants is mediated by distinct interactions with CREB binding protein and p300." Bex F., Yin M.-J., Burny A., Gaynor R.B. Mol. Cell. Biol. 18:2392-2405(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HTLV-1 TAX.
[11]	"Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex." Fryer C.J., Archer T.K. Nature 393:88-91(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NR3C1.
[12]	"HIV-1 tat transcriptional activity is regulated by acetylation." Kiernan R.E., Vanhulle C., Schiltz L., Adam E., Xiao H., Maudoux F., Calomme C., Burny A., Nakatani Y., Jeang K.-T., Benkirane M., Van Lint C. EMBO J. 18:6106-6118(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[13]	"Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1." Bhattacharya S., Michels C.M., Leung M.K., Arany Z.P., Kung A.L., Livingston D.M. Genes Dev. 13:64-75(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CITED2 AND HIF1A, MUTAGENESIS OF 371-THR--LEU-376 AND 413-VAL--LYS-418.
[14]	"The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors." Yahata T., de Caestecker M.P., Lechleider R.J., Andriole S., Roberts A.B., Isselbacher K.J., Shioda T. J. Biol. Chem. 275:8825-8834(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CITED1.
[15]	"A novel transcriptional repression domain mediates p21(WAF1/CIP1) induction of p300 transactivation." Snowden A.W., Anderson L.A., Webster G.A., Perkins N.D. Mol. Cell. Biol. 20:2676-2686(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TRANSCRIPTIONAL REPRESSION.
[16]	Erratum Snowden A.W., Anderson L.A., Webster G.A., Perkins N.D. Mol. Cell. Biol. 20:5360-5360(2000)
[17]	"Cells degrade a novel inhibitor of differentiation with E1A-like properties upon exiting the cell cycle." Miyake S., Sellers W.R., Safran M., Li X., Zhao W., Grossman S.R., Gan J., DeCaprio J.A., Adams P.D., Kaelin W.G. Jr. Mol. Cell. Biol. 20:8889-8902(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EID1.
[18]	"A novel Rb- and p300-binding protein inhibits transactivation by MyoD." MacLellan W.R., Xiao G., Abdellatif M., Schneider M.D. Mol. Cell. Biol. 20:8903-8915(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EID1.
[19]	"Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator." Ko L., Cardona G.R., Chin W.W. Proc. Natl. Acad. Sci. U.S.A. 97:6212-6217(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NCOA6.
[20]	"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones." Deng L., de la Fuente C., Fu P., Wang L., Donnelly R., Wade J.D., Lambert P., Li H., Lee C.-G., Kashanchi F. Virology 277:278-295(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[21]	"Selective coactivation of estrogen-dependent transcription by CITED1 CBP/p300-binding protein." Yahata T., Shao W., Endoh H., Hur J., Coser K.R., Sun H., Ueda Y., Kato S., Isselbacher K.J., Brown M., Shioda T. Genes Dev. 15:2598-2612(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ESR1.
[22]	"Regulation of transcription by AMP-activated protein kinase: phosphorylation of p300 blocks its interaction with nuclear receptors." Yang W., Hong Y.H., Shen X.Q., Frankowski C., Camp H.S., Leff T. J. Biol. Chem. 276:38341-38344(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-89, MUTAGENESIS OF SER-89, INTERACTION WITH PPARG.
[23]	"Adenovirus DNA binding protein interacts with the SNF2-related CBP activator protein (SrCap) and inhibits SrCap-mediated transcription." Xu X., Chackalaparampil I., Monroy M.A., Cannella M.T., Pesek E., Chrivia J., Yaciuk P. J. Virol. 75:10033-10040(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SRCAP.
[24]	"The oncoprotein Tax binds the SRC-1-interacting domain of CBP/p300 to mediate transcriptional activation." Scoggin K.E.S., Ulloa A., Nyborg J.K. Mol. Cell. Biol. 21:5520-5530(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HTLV-1 TAX.
[25]	"Human T-lymphotropic virus type 1 p30(II) regulates gene transcription by binding CREB binding protein/p300." Zhang W., Nisbet J.W., Albrecht B., Ding W., Kashanchi F., Bartoe J.T., Lairmore M.D. J. Virol. 75:9885-9895(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P30II.
[26]	"A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression." Gizard F., Lavallee B., DeWitte F., Hum D.W. J. Biol. Chem. 276:33881-33892(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRERF1.
[27]	"Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha." Vadlamudi R.K., Wang R.-A., Mazumdar A., Kim Y.-S., Shin J., Sahin A., Kumar R. J. Biol. Chem. 276:38272-38279(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PELP1.
[28]	"Role of Deltex-1 as a transcriptional regulator downstream of the Notch receptor." Yamamoto N., Yamamoto S., Inagaki F., Kawaichi M., Fukamizu A., Kishi N., Matsuno K., Nakamura K., Weinmaster G., Okano H., Nakafuku M. J. Biol. Chem. 276:45031-45040(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DTX1.
[29]	"Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300." Hasan S., Stucki M., Hassa P.O., Imhof R., Gehrig P., Hunziker P., Hubscher U., Hottiger M.O. Mol. Cell 7:1221-1231(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH FEN1.
[30]	"Interaction between the hematopoietic Ets transcription factor Spi-B and the coactivator CREB-binding protein associated with negative cross-talk with c-Myb." Yamamoto H., Kihara-Negishi F., Yamada T., Suzuki M., Nakano T., Oikawa T. Cell Growth Differ. 13:69-75(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SPIB.
[31]	"Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2." Braganca J., Swingler T., Marques F.I.R., Jones T., Eloranta J.J., Hurst H.C., Shioda T., Bhattacharya S. J. Biol. Chem. 277:8559-8565(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CITED4.
[32]	"Synergy among nuclear receptor coactivators: selective requirement for protein methyltransferase and acetyltransferase activities." Lee Y.-H., Koh S.S., Zhang X., Cheng X., Stallcup M.R. Mol. Cell. Biol. 22:3621-3632(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH CARM1 AND NCOA2.
[33]	"p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity." Shiseki M., Nagashima M., Pedeux R.M., Kitahama-Shiseki M., Miura K., Okamura S., Onogi H., Higashimoto Y., Appella E., Yokota J., Harris C.C. Cancer Res. 63:2373-2378(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ING4 AND ING5.
[34]	"Identification of a promoter-specific transcriptional activation domain at the C-terminus of the Wnt effector protein T-cell factor 4." Hecht A., Stemmler M.P. J. Biol. Chem. 278:3776-3785(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH TCF7L2 AND LEF1.
[35]	"Physical and functional interactions among AP-2 transcription factors, p300/CREB-binding protein, and CITED2." Braganca J., Eloranta J.J., Bamforth S.D., Ibbitt J.C., Hurst H.C., Bhattacharya S. J. Biol. Chem. 278:16021-16029(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CITED2 AND TFAP2A, MUTAGENESIS OF ASP-1399.
[36]	"Acetylated SP3 is a transcriptional activator." Ammanamanchi S., Freeman J.W., Brattain M.G. J. Biol. Chem. 278:35775-35780(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SP3.
[37]	"P300/CBP acts as a coactivator to cartilage homeoprotein-1 (Cart1), paired-like homeoprotein, through acetylation of the conserved lysine residue adjacent to the homeodomain." Iioka T., Furukawa K., Yamaguchi A., Shindo H., Yamashita S., Tsukazaki T. J. Bone Miner. Res. 18:1419-1429(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ALX1.
[38]	"SATB1 makes a complex with p300 and represses gp91(phox) promoter activity." Fujii Y., Kumatori A., Nakamura M. Microbiol. Immunol. 47:803-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SATB1.
[39]	"P300 transcriptional repression is mediated by SUMO modification." Girdwood D., Bumpass D., Vaughan O.A., Thain A., Anderson L.A., Snowden A.W., Garcia-Wilson E., Perkins N.D., Hay R.T. Mol. Cell 11:1043-1054(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-1020 AND LYS-1024, MUTAGENESIS OF LYS-1020 AND LYS-1024.
[40]	"Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300." Rossow K.L., Janknecht R. Oncogene 22:151-156(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DDX5.
[41]	"Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53." An W., Kim J., Roeder R.G. Cell 117:735-748(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TP53, FUNCTION.
[42]	"Regulation of human SRY subcellular distribution by its acetylation/deacetylation." Thevenet L., Mejean C., Moniot B., Bonneaud N., Galeotti N., Aldrian-Herrada G., Poulat F., Berta P., Benkirane M., Boizet-Bonhoure B. EMBO J. 23:3336-3345(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SRY.
[43]	"Positive and negative modulation of the transcriptional activity of the ETS factor ESE-1 through interaction with p300, CREB-binding protein, and Ku 70/86." Wang H., Fang R., Cho J.-Y., Libermann T.A., Oettgen P. J. Biol. Chem. 279:25241-25250(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ELF3.
[44]	"Interferon regulatory factor 1 binding to p300 stimulates DNA-dependent acetylation of p53." Dornan D., Eckert M., Wallace M., Shimizu H., Ramsay E., Hupp T.R., Ball K.L. Mol. Cell. Biol. 24:10083-10098(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IRF1.
[45]	"Regulation of the p300 HAT domain via a novel activation loop." Thompson P.R., Wang D., Wang L., Fulco M., Pediconi N., Zhang D., An W., Ge Q., Roeder R.G., Wong J., Levrero M., Sartorelli V., Cotter R.J., Cole P.A. Nat. Struct. Mol. Biol. 11:308-315(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-1499; LYS-1549; LYS-1554; LYS-1558 AND LYS-1560.
[46]	"Orphan nuclear receptor small heterodimer partner, a novel corepressor for a basic helix-loop-helix transcription factor BETA2/neuroD." Kim J.Y., Chu K., Kim H.J., Seong H.A., Park K.C., Sanyal S., Takeda J., Ha H., Shong M., Tsai M.J., Choi H.S. Mol. Endocrinol. 18:776-790(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NEUROD1 AND TCF3.
[47]	"Dendrite development regulated by CREST, a calcium-regulated transcriptional activator." Aizawa H., Hu S.-C., Bobb K., Balakrishnan K., Ince G., Gurevich I., Cowan M., Ghosh A. Science 303:197-202(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SS18L1/CREST.
[48]	"Genetic heterogeneity in Rubinstein-Taybi syndrome: mutations in both the CBP and EP300 genes cause disease." Roelfsema J.H., White S.J., Ariyuerek Y., Bartholdi D., Niedrist D., Papadia F., Bacino C.A., den Dunnen J.T., van Ommen G.-J.B., Breuning M.H., Hennekam R.C., Peters D.J.M. Am. J. Hum. Genet. 76:572-580(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN RSTS2.
[49]	"SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1." Bouras T., Fu M., Sauve A.A., Wang F., Quong A.A., Perkins N.D., Hay R.T., Gu W., Pestell R.G. J. Biol. Chem. 280:10264-10276(2005) [PubMed] [Europe PMC] [Abstract] Cited for: DEACETYLATION BY SIRT1, ACETYLATION AT LYS-1020 AND LYS-1024, MUTAGENESIS OF LYS-1020 AND LYS-1024.
[50]	"The coactivator p300 directly acetylates the forkhead transcription factor Foxo1 and stimulates Foxo1-induced transcription." Perrot V., Rechler M.M. Mol. Endocrinol. 19:2283-2298(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FOXO1, FUNCTION, MUTAGENESIS OF ASP-1399.
[51]	"Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination." Lee Y.-H., Coonrod S.A., Kraus W.L., Jelinek M.A., Stallcup M.R. Proc. Natl. Acad. Sci. U.S.A. 102:3611-3616(2005) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT ARG-2142, CITRULLINATION AT ARG-2142, INTERACTION WITH NCOA2, MUTAGENESIS OF ARG-2056; ARG-2088 AND ARG-2142.
[52]	"Nuclear Rho kinase, ROCK2, targets p300 acetyltransferase." Tanaka T., Nishimura D., Wu R.C., Amano M., Iso T., Kedes L., Nishida H., Kaibuchi K., Hamamori Y. J. Biol. Chem. 281:15320-15329(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ROCK2, PHOSPHORYLATION AT SER-89.
[53]	"The transcriptional activity of CITED1 is regulated by phosphorylation in a cell cycle-dependent manner." Shi G., Boyle S.C., Sparrow D.B., Dunwoodie S.L., Shioda T., de Caestecker M.P. J. Biol. Chem. 281:27426-27435(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CITED1.
[54]	"Kinetic and mass spectrometric analysis of p300 histone acetyltransferase domain autoacetylation." Karanam B., Jiang L., Wang L., Kelleher N.L., Cole P.A. J. Biol. Chem. 281:40292-40301(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-1336 AND LYS-1473, MASS SPECTROMETRY.
[55]	"HDAC1 acetylation is linked to progressive modulation of steroid receptor-induced gene transcription." Qiu Y., Zhao Y., Becker M., John S., Parekh B.S., Huang S., Hendarwanto A., Martinez E.D., Chen Y., Lu H., Adkins N.L., Stavreva D.A., Wiench M., Georgel P.T., Schiltz R.L., Hager G.L. Mol. Cell 22:669-679(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ACETYLATION OF HDAC1.
[56]	"Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription." Hung J.J., Wang Y.T., Chang W.C. Mol. Cell. Biol. 26:1770-1785(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SP1.
[57]	"Critical and functional regulation of CHOP (C/EBP homologous protein) through the N-terminal portion." Ohoka N., Hattori T., Kitagawa M., Onozaki K., Hayashi H. J. Biol. Chem. 282:35687-35694(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DDIT3.
[58]	"Concerted activation of the Mdm2 promoter by p72 RNA helicase and the coactivators p300 and P/CAF." Shin S., Janknecht R. J. Cell. Biochem. 101:1252-1265(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DDX17.
[59]	"Acetylation of Sirt2 by p300 attenuates its deacetylase activity." Han Y., Jin Y.H., Kim Y.J., Kang B.Y., Choi H.J., Kim D.W., Yeo C.Y., Lee K.Y. Biochem. Biophys. Res. Commun. 375:576-580(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ACETYLATION OF SIRT2.
[60]	"PEBP2-beta/CBF-beta-dependent phosphorylation of RUNX1 and p300 by HIPK2: implications for leukemogenesis." Wee H.-J., Voon D.C.-C., Bae S.-C., Ito Y. Blood 112:3777-3787(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY HIPK2.
[61]	"PML activates transcription by protecting HIPK2 and p300 from SCFFbx3-mediated degradation." Shima Y., Shima T., Chiba T., Irimura T., Pandolfi P.P., Kitabayashi I. Mol. Cell. Biol. 28:7126-7138(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FBXO3-MEDIATED DEGRADATION.
[62]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[63]	"SENP3 is responsible for HIF-1 transactivation under mild oxidative stress via p300 de-SUMOylation." Huang C., Han Y., Wang Y., Sun X., Yan S., Yeh E.T.H., Chen Y., Cang H., Li H., Shi G., Cheng J., Tang X., Yi J. EMBO J. 28:2748-2762(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SENP3, SUMOYLATION.
[64]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[65]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-636; LYS-977; LYS-1542; LYS-1546; LYS-1554; LYS-1555; LYS-1558; LYS-1560 AND LYS-1583, MASS SPECTROMETRY.
[66]	"Cyclin-dependent kinase-9 is a component of the p300/GATA4 complex required for phenylephrine-induced hypertrophy in cardiomyocytes." Sunagawa Y., Morimoto T., Takaya T., Kaichi S., Wada H., Kawamura T., Fujita M., Shimatsu A., Kita T., Hasegawa K. J. Biol. Chem. 285:9556-9568(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN COMPLEX WITH CCNT1; CDK9 AND GATA4.
[67]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[68]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1038, MASS SPECTROMETRY.
[69]	"Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha." Freedman S.J., Sun Z.-Y.J., Poy F., Kung A.L., Livingston D.M., Wagner G., Eck M.J. Proc. Natl. Acad. Sci. U.S.A. 99:5367-5372(2002) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 302-418 IN COMPLEX WITH 786-826 OF HIF1A.
[70]	"Structural basis for negative regulation of hypoxia-inducible factor-1alpha by CITED2." Freedman S.J., Sun Z.Y., Kung A.L., France D.S., Wagner G., Eck M.J. Nat. Struct. Biol. 10:504-512(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 323-423 IN COMPLEX WITH 216-259 OF CITED2 AND ZINC IONS, INTERACTION WITH CITED2, MUTAGENESIS OF LEU-344 AND LEU-345.
[71]	"The structural basis of protein acetylation by the p300/CBP transcriptional coactivator." Liu X., Wang L., Zhao K., Thompson P.R., Hwang Y., Marmorstein R., Cole P.A. Nature 451:846-850(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1287-1666 IN COMPLEX WITH LYS-COA, MUTAGENESIS OF THR-1357; SER-1396; TYR-1397; GLU-1505; ASP-1625 AND ASP-1628.
[72]	"Structural basis for p300 Taz2-p53 TAD1 binding and modulation by phosphorylation." Feng H., Jenkins L.M.M., Durell S.R., Hayashi R., Mazur S.J., Cherry S., Tropea J.E., Miller M., Wlodawer A., Appella E., Bai Y. Structure 17:202-210(2009) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1723-1812, INTERACTION WITH TP53.
[73]	"Mutations truncating the EP300 acetylase in human cancers." Gayther S.A., Batley S.J., Linger L., Bannister A., Thorpe K., Chin S.-F., Daigo Y., Russell P., Wilson A., Sowter H.M., Delhanty J.D.A., Ponder B.A.J., Kouzarides T., Caldas C. Nat. Genet. 24:300-303(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PRO-827; GLY-1013; TYR-1650 AND GLN-2221, POSSIBLE INVOLVEMENT IN CANCER.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Wikipedia

P300/CBP entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U01877 mRNA. Translation: AAA18639.1.
AL080243, AL035658, AL096765 Genomic DNA. Translation: CAH70384.1.
AL096765, AL035658, AL080243 Genomic DNA. Translation: CAH73688.1.
AL035658, AL080243, AL096765 Genomic DNA. Translation: CAI23037.1.
CH471095 Genomic DNA. Translation: EAW60408.1.

IPI

IPI00020985.

PIR

A54277.

RefSeq

NP_001420.2. NM_001429.3.

UniGene

Hs.517517.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L3E	NMR	-	B	323-423	[»]
1P4Q	NMR	-	B	323-423	[»]
2K8F	NMR	-	A	1723-1812	[»]
3BIY	X-ray	1.70	A	1287-1666	[»]
3I3J	X-ray	2.33	A/B/C/D/E/F/G/H/I/J/K/L	1040-1161	[»]
3IO2	X-ray	2.50	A	1723-1836	[»]
3P57	X-ray	2.19	P	1726-1835	[»]
3T92	X-ray	1.50	A	1723-1818	[»]

ProteinModelPortal

Q09472.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-257N.

IntAct

Q09472. 121 interactions.

MINT

MINT-104535.

STRING

9606.ENSP00000263253.

PTM databases

PhosphoSite

Q09472.

Polymorphism databases

DMDM

223590203.

Proteomic databases

PaxDb

Q09472.

PRIDE

Q09472.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263253; ENSP00000263253; ENSG00000100393.

GeneID

2033.

KEGG

hsa:2033.

UCSC

uc003azl.4. human.

Organism-specific databases

CTD

2033.

GeneCards

GC22P041487.

H-InvDB

HIX0203186.

HGNC

HGNC:3373. EP300.

HPA

CAB000146.
HPA003128.
HPA004112.

MIM

602700. gene.
613684. phenotype.

neXtProt

NX_Q09472.

Orphanet

783. Rubinstein-Taybi syndrome.

PharmGKB

PA27807.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5076.

HOGENOM

HOG000111353.

HOVERGEN

HBG000185.

InParanoid

Q09472.

KO

K04498.

OMA

KMEAKME.

OrthoDB

EOG4Z0B4S.

PhylomeDB

Q09472.

Enzyme and pathway databases

Pathway_Interaction_DB

pi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
hnf3apathway. FOXA1 transcription factor network.
foxm1pathway. FOXM1 transcription factor network.
foxopathway. FoxO family signaling.
hif1_tfpathway. HIF-1-alpha transcription factor network.
ifngpathway. IFN-gamma pathway.
ar_tf_pathway. Regulation of Androgen receptor activity.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
retinoic_acid_pathway. Retinoic acid receptors-mediated signaling.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.
hdac_classiii_pathway. Signaling events mediated by HDAC Class III.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_120956. Cellular responses to stress.
REACT_24941. Circadian Clock.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q09472.

Bgee

Q09472.

CleanEx

HS_EP300.

Genevestigator

Q09472.

GermOnline

ENSG00000100393. Homo sapiens.

Family and domain databases

Gene3D

1.10.1630.10. 1 hit.
1.10.246.20. 1 hit.
1.20.1020.10. 2 hits.
1.20.920.10. 1 hit.

InterPro

IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR010303. DUF902_CREBbp.
IPR013178. Histone_H3-K56_AcTrfase_RTT109.
IPR003101. KIX_dom.
IPR009110. Nuc_rcpt_coact.
IPR014744. Nuc_rcpt_coact_CREBbp.
IPR000197. Znf_TAZ.
IPR000433. Znf_ZZ.
[Graphical view]

Pfam

PF00439. Bromodomain. 1 hit.
PF09030. Creb_binding. 1 hit.
PF06001. DUF902. 1 hit.
PF08214. KAT11. 1 hit.
PF02172. KIX. 1 hit.
PF02135. zf-TAZ. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view]

PRINTS

PR00503. BROMODOMAIN.

SMART

SM00297. BROMO. 1 hit.
SM00551. ZnF_TAZ. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]

SUPFAM

SSF47370. Bromodomain. 1 hit.
SSF47040. KIX. 1 hit.
SSF69125. Nuc_recept_coact. 1 hit.
SSF57933. TAZ_finger. 2 hits.

PROSITE

PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS50952. KIX. 1 hit.
PS50134. ZF_TAZ. 2 hits.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q09472.

ChEMBL

CHEMBL3784.

ChiTaRS

EP300. human.

EvolutionaryTrace

Q09472.

GenomeRNAi

2033.

NextBio

8251.

SOURCE

Search...

Entry information

Entry name

EP300_HUMAN

Accession

Primary (citable) accession number: Q09472
Secondary accession number(s): B1AKC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	February 10, 2009
Last modified:	May 1, 2013
This is version 174 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.