Histone acetyltransferase p300 - Mus musculus (Mouse)

Contribute

Send feedback

Read comments (?) or add your own

B2RWS6 (EP300_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 50. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	2415 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. Acetylates FOXO1 and enhances its transcriptional activity By similarity. Ref.2
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subunit structure	Interacts with phosphorylated CREB1. 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 HIPK2, 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. 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 with PPARG By similarity. Forms a complex made of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that stimulates hypertrophy in cardiomyocytes By similarity. Interacts with CITED1 and CITED2. Interacts with ROCK2 By similarity. Interacts with NEUROD1. Interacts (via CREB-binding domain) with MYOCD (via C-terminus). 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 By similarity. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Note: In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. Co-localizes with ROCK2 in the nucleus By similarity.
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 By similarity.
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-1019 By similarity. Citrullinated at Arg-2143 by PADI4, which impairs methylation by CARM1 and promotes interaction with NCOA2/GRIP1 By similarity. Methylated at Arg-581 and Arg-605 in the KIX domain by CARM1, which blocks association with CREB, inhibits CREB signaling and activates apoptotic response. Also methylated at Arg-2143 by CARM1, which impairs interaction with NCOA2/GRIP1 By similarity. Sumoylated; sumoylation in the transcriptional repression domain (CRD1) mediates transcriptional repression. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3 By similarity. Probable target of ubiquitination by FBXO3, leading to rapid proteasome-dependent degradation By similarity. Phosphorylation at Ser-89 by AMPK reduces interaction with nuclear receptors, such as PPARG By similarity. 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 By similarity. Ref.6
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 Differentiation Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	Bromodomain Coiled coil Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Transferase
PTM	Acetylation Citrullination Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	N-terminal peptidyl-lysine acetylation Inferred from sequence or structural similarity PubMed 12435739. Source: UniProtKB apoptotic process Inferred from sequence or structural similarity PubMed 9194565. Source: UniProtKB cartilage development Non-traceable author statement PubMed 19828133. Source: UniProtKB cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW heart development Inferred from mutant phenotype PubMed 14517255. Source: MGI histone H4 acetylation Inferred from sequence or structural similarity PubMed 16325578. Source: UniProtKB lung development Inferred from mutant phenotype PubMed 14517255. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB organ morphogenesis Inferred from mutant phenotype PubMed 14517255. Source: MGI positive regulation of protein binding Inferred from direct assay PubMed 16619037. Source: MGI positive regulation of sequence-specific DNA binding transcription factor activity Inferred from sequence or structural similarity PubMed 10518217. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.2. Source: UniProtKB response to estrogen stimulus Inferred from sequence or structural similarity. Source: UniProtKB response to hypoxia Inferred from sequence or structural similarity PubMed 15261140. Source: UniProtKB skeletal muscle tissue development Inferred from mutant phenotype PubMed 14517256. Source: MGI somitogenesis Inferred from genetic interaction PubMed 15937931. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell histone acetyltransferase complex Inferred from direct assay PubMed 9742083. Source: MGI transcription factor complex Inferred from direct assay PubMed 19828133. Source: UniProtKB
Molecular_function	chromatin DNA binding Inferred from direct assay PubMed 18458156. Source: MGI histone acetyltransferase activity Inferred from sequence or structural similarity PubMed 12040021. Source: UniProtKB lysine N-acetyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB transcription coactivator activity Inferred from mutant phenotype PubMed 17641689. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 2415

2414

Histone acetyltransferase p300

PRO_0000409386

Regions

Domain

567 – 646

KIX

Domain

1066 – 1138

Bromo

Zinc finger

332 – 418

TAZ-type 1

Zinc finger

1663 – 1706

ZZ-type

Zinc finger

1727 – 1808

TAZ-type 2

Region

2 – 139

138

Interaction with ALX1 By similarity

Region

1016 – 1028

CRD1; mediates transcriptional repression By similarity

Region

2042 – 2240

199

Interaction with NCOA2 By similarity

Coiled coil

1510 – 1539

Potential

Motif

11 – 17

Nuclear localization signal Potential

Compositional bias

660 – 942

283

Pro-rich

Compositional bias

798 – 801

Poly-Ser

Compositional bias

1518 – 1525

Poly-Glu

Sites

Metal binding

348

Zinc 1 By similarity

Metal binding

352

Zinc 1 By similarity

Metal binding

365

Zinc 1 By similarity

Metal binding

370

Zinc 1 By similarity

Metal binding

379

Zinc 2 By similarity

Metal binding

383

Zinc 2 By similarity

Metal binding

389

Zinc 2 By similarity

Metal binding

394

Zinc 2 By similarity

Metal binding

403

Zinc 3 By similarity

Metal binding

407

Zinc 3 By similarity

Metal binding

412

Zinc 3 By similarity

Metal binding

415

Zinc 3 By similarity

Site

2089

Interaction with NCOA2 By similarity

Site

2143

Interaction with NCOA2 By similarity

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

Phosphoserine; by AMPK By similarity

Modified residue

286

Phosphoserine By similarity

Modified residue

581

Omega-N-methylated arginine; by CARM1 By similarity

Modified residue

605

Omega-N-methylated arginine; by CARM1 By similarity

Modified residue

637

N6-acetyllysine By similarity

Modified residue

885

Phosphothreonine By similarity

Modified residue

887

Phosphothreonine By similarity

Modified residue

976

N6-acetyllysine By similarity

Modified residue

980

N6-acetyllysine By similarity

Modified residue

1019

N6-acetyllysine; alternate By similarity

Modified residue

1023

N6-acetyllysine; alternate By similarity

Modified residue

1037

Phosphoserine By similarity

Modified residue

1102

N6-acetyllysine By similarity

Modified residue

1335

N6-acetyllysine By similarity

Modified residue

1472

N6-acetyllysine By similarity

Modified residue

1498

N6-acetyllysine; by autocatalysis By similarity

Modified residue

1541

N6-acetyllysine By similarity

Modified residue

1545

N6-acetyllysine By similarity

Modified residue

1548

N6-acetyllysine; by autocatalysis By similarity

Modified residue

1553

N6-acetyllysine; by autocatalysis By similarity

Modified residue

1554

N6-acetyllysine By similarity

Modified residue

1557

N6-acetyllysine By similarity

Modified residue

1559

N6-acetyllysine; by autocatalysis By similarity

Modified residue

1582

N6-acetyllysine By similarity

Modified residue

1589

N6-acetyllysine By similarity

Modified residue

1673

N6-acetyllysine By similarity

Modified residue

1733

Phosphoserine By similarity

Modified residue

1856

Phosphothreonine By similarity

Modified residue

1858

Phosphothreonine By similarity

Modified residue

2143

Asymmetric dimethylarginine; by CARM1; alternate By similarity

Modified residue

2143

Citrulline; by PADI4; alternate By similarity

Cross-link

1019

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity

Cross-link

1023

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

B2RWS6 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: FBCF19B91EE70A1C
Show »

FASTA

2,415

263,762

        10         20         30         40         50         60 
MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS TELGLTNGGD 

        70         80         90        100        110        120 
ISQLQTSLGI VQDAASKHKQ LSELLRSGSS PNLNMGVGGP GQAMASQAQQ NSPGLSLINS 

       130        140        150        160        170        180 
MVKSPMAQTG LTSPNMGIGS SGPNQGPTQS PAGMMNSPVN QPAMGMNTGM NAGMNPGMLA 

       190        200        210        220        230        240 
AGNGQGIMPN QVMNGSIGAG RGRPNMQYPN AGMGNAGSLL TEPLQQGSPQ MGGQPGLRGP 

       250        260        270        280        290        300 
QPLKMGMMNN PSPYGSPYTQ NSGQQIGASG LGLQIQTKTV LPNNLSPFAM DKKAVPGGGM 

       310        320        330        340        350        360 
PSMGQQPTPS VQQPGLVTPV AAGMGSGAHT ADPEKRKLIQ QQLVLLLHAH KCQRREQANG 

       370        380        390        400        410        420 
EVRQCNLPHC RTMKNVLNHM THCQSGKSCQ VAHCASSRQI ISHWKNCTRH DCPVCLPLKN 

       430        440        450        460        470        480 
AGDKRNQQSI LTGAPVGLGN PSSLGVGQQS TPSLSTVSQI DPSSIERAYA ALGLPYQVNQ 

       490        500        510        520        530        540 
IPPQPQVQAK NQQSQPSGQS PQGMRSVNNM SASPMGVNGG VGVQTPNLLS DSMLHSTINS 

       550        560        570        580        590        600 
QNPMMSENAG VASLGPLPTA AQPSSTGIRK QWHEDITQDL RNHLVHKLVQ AIFPTPDPAA 

       610        620        630        640        650        660 
LKDRRMENLV AYARKVEGDM YESANNRAEY YHLLAEKIYK IQKELEEKRR TRLQKQNMLP 

       670        680        690        700        710        720 
NAPGMGPVPM NTGSNMEQQP TGMTTNGPVP DPSMIRGSVP NHMMPRMTPQ PGLNQFGQMN 

       730        740        750        760        770        780 
MPQPPIGPRQ PSPLQHHGQL AQSGSLNPPM GYGPRMQQAS GQNQFLSQTQ FTSQGMNVTN 

       790        800        810        820        830        840 
MPLAPSSGQA PVSQAQMSSS SCPVNSPIMP PGSQGSHIHC PTLPQQAHQN SPSPVPSRTP 

       850        860        870        880        890        900 
TPHHTPPSIG NQPPPATAIP TPVPTPPAIP PGPQPPSLHP SSRQTPTPPT HLPPQVQPSL 

       910        920        930        940        950        960 
PAAPSADQSQ QQPRSQQSTA VSVPTPTAPL LPPQPSTPLS QPAVSIEGQV SNPPSTSSTE 

       970        980        990       1000       1010       1020 
VNSQTIPEKQ PSQEVKMESK MEVDKPEPAD AQPEDTKEAK GEDVKVEPTE MEERGPELKT 

      1030       1040       1050       1060       1070       1080 
DGKEEEEQPS TSATQSSPAP GQSKKKIFKP EELRQALMPT LEALYRQDPE SLPFRQPVDP 

      1090       1100       1110       1120       1130       1140 
QLLGIPDYFD IVKSPMDLST IKRKLDTGQY QEPWQYIDDI WLMFNNAWLY NRKTSRVYKY 

      1150       1160       1170       1180       1190       1200 
CSKLSEVFEQ EIDPVMQSLG YCCGRKLEFS PQTLCCYGKQ LCTIPRDATY YSYQNRYHFC 

      1210       1220       1230       1240       1250       1260 
EKCFNEIQGE SVSLGDDPSQ PQTTINKEQF SKRKNDTLDP ELFVECTECG RKMHQICVLH 

      1270       1280       1290       1300       1310       1320 
HEIIWPSGFV CDGCLKKTAR TRKENKLSAK RLPSTRLGTF LENRVNDFLR RQNHPESGEV 

      1330       1340       1350       1360       1370       1380 
TVRVVHASDK TVEVKPGMKA RFVDSGEMAE SFPYRTKALF AFEEIDGVDL CFFGMHVQEY 

      1390       1400       1410       1420       1430       1440 
GSDCPPPNQR RVYISYLDSV HFFRPKCLRT AVYHEILIGY LEYVKKLGYT TGHIWACPPS 

      1450       1460       1470       1480       1490       1500 
EGDDYIFHCH PPDQKIPKPK RLQEWYKKML DKAVSERIVH DYKDILKQAT EDRLTSAKEL 

      1510       1520       1530       1540       1550       1560 
PYFEGDFWPN VLEESIKELE QEEEERKREE NTSNESTDVT KGDSKNAKKK NNKKTSKNKS 

      1570       1580       1590       1600       1610       1620 
SLSRGNKKKP GMPNVSNDLS QKLYATMEKH KEVFFVIRLI ACPAPNSLPP IVDPDPLIPC 

      1630       1640       1650       1660       1670       1680 
DLMDGRDAFL TLARDKHLEF SSLRRAQWST MCMLVELHTQ SQDRFVYTCN ECKHHVETRW 

      1690       1700       1710       1720       1730       1740 
HCTVCEDYDL CITCYNTKNH DHKMEKLGLG LDDESNNQQA AATQSPGDSR RLSIQRCIQS 

      1750       1760       1770       1780       1790       1800 
LVHACQCRNA NCSLPSCQKM KRVVQHTKGC KRKTNGGCPI CKQLIALCCY HAKHCQENKC 

      1810       1820       1830       1840       1850       1860 
PVPFCLNIKQ KLRQQQLQHR LQQAQMLRRR MASMQRTGVA GQQQGLPSPT PATPTTPTGQ 

      1870       1880       1890       1900       1910       1920 
QPATPQTPQP QPTSQPQPTP PNNMTPYLPR TQTTGPVSQG KAPGQVTPPT PPQTAQAPLP 

      1930       1940       1950       1960       1970       1980 
GPPPAAVEMA MQIQRAAETQ RQMAHVQIFQ RPIQHQMPQM SPMAPMGMNP PPMARGPGGH 

      1990       2000       2010       2020       2030       2040 
LDPGIGPAGM QQQPPWAQGG MPQPQQMQSG MPRPAMMSVA QHGQPLNMAP QPGLGQVGVS 

      2050       2060       2070       2080       2090       2100 
PLKPGTVSQQ ALQNLLRTLR SPSSPLQQQQ VLSILHANPQ LLAAFIKQRA AKYANPNPQP 

      2110       2120       2130       2140       2150       2160 
LPGQPGMTQG QPGLQPPTMP GQQGVHSNPA LQNMNPLQAG VQRAGLPQQQ PQQQLQPPMG 

      2170       2180       2190       2200       2210       2220 
AMSPQAQQMN MNHNTMPSQF RDILRRQMMQ QQGAGPGIGP GMANQFQQPQ GIGYPPQQQQ 

      2230       2240       2250       2260       2270       2280 
QQQQQRMQHH MQQMQQGNMG QMGQLPQALG AEAGASLQAY QQRLLQQQMG SPAQPNPMSP 

      2290       2300       2310       2320       2330       2340 
QQHMLPNQAQ SPHLQGQQIP NSLSNQVRSP QPVPSPRPQS QPPHSSPSPR MQPQPSPHHV 

      2350       2360       2370       2380       2390       2400 
SPQTSSPHPG LVAAQAANPM EQGHFASPDQ NSMLSQLASN PGMANLHGAS ATDLGLSSDN 

      2410 
ADLNSNLSQS TLDIH

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[2]	"The basic helix-loop-helix protein BETA2 interacts with p300 to coordinate differentiation of secretin-expressing enteroendocrine cells." Mutoh H., Naya F.J., Tsai M.J., Leiter A.B. Genes Dev. 12:820-830(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH NEUROD1.
[3]	"MRG1 binds to the LIM domain of Lhx2 and may function as a coactivator to stimulate glycoprotein hormone alpha-subunit gene expression." Glenn D.J., Maurer R.A. J. Biol. Chem. 274:36159-36167(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CITED2.
[4]	"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.
[5]	"Modulation of smooth muscle gene expression by association of histone acetyltransferases and deacetylases with myocardin." Cao D., Wang Z., Zhang C.L., Oh J., Xing W., Li S., Richardson J.A., Wang D.Z., Olson E.N. Mol. Cell. Biol. 25:364-376(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MYOCD.
[6]	"Roles of HIPK1 and HIPK2 in AML1- and p300-dependent transcription, hematopoiesis and blood vessel formation." Aikawa Y., Nguyen L.A., Isono K., Takakura N., Tagata Y., Schmitz M.L., Koseki H., Kitabayashi I. EMBO J. 25:3955-3965(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIPK2, PHOSPHORYLATION BY HIPK2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC144976 mRNA. Translation: AAI44977.1. BC150681 mRNA. Translation: AAI50682.1.
IPI	IPI00461822.
UniGene	Mm.258397.
3D structure databases
ProteinModelPortal	B2RWS6.
SMR	B2RWS6. Positions 324-424, 567-653, 1046-1160, 1286-1712, 1725-1833, 2051-2093.
ModBase	Search...
Protein-protein interaction databases
IntAct	B2RWS6. 3 interactions.
STRING	10090.ENSMUSP00000066789.
Proteomic databases
PaxDb	B2RWS6.
PRIDE	B2RWS6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
UCSC	uc007wws.1. mouse.
Organism-specific databases
MGI	MGI:1276116. Ep300.
Phylogenomic databases
eggNOG	COG5076.
HOGENOM	HOG000111353.
HOVERGEN	HBG000185.
InParanoid	B2RWS6.
OrthoDB	EOG4Z0B4S.
Enzyme and pathway databases
Reactome	REACT_109335. Circadian Clock. REACT_127416. Developmental Biology. REACT_24972. Circadian Clock (mouse). REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
Gene expression databases
Genevestigator	B2RWS6.
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
ChiTaRS	EP300. mouse.
SOURCE	Search...

Entry information

Entry name

EP300_MOUSE

Accession

Primary (citable) accession number: B2RWS6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 31, 2011
Last sequence update:	July 1, 2008
Last modified:	May 1, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents