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B2RWS6 (EP300_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2412 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Mediates acetylation of histone H3 at 'Lys-122' (H3K122ac), a modification that localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability. Mediates acetylation of histone H3 at 'Lys-27' (H3K27ac). 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. Acetylates BCL6 wich disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity. Ref.3

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. Forms a complex made of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that stimulates hypertrophy in cardiomyocytes. Interacts with CITED1 and CITED2. Interacts with ROCK2. 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 ALKBH4 and DDIT3/CHOP. Interacts with KLF15. Interacts with CEBPB and RORA. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Subcellular location

Cytoplasm By similarity. Nucleus. Note: In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. Colocalizes with ROCK2 in the nucleus By similarity. Ref.8

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.7

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 processCell cycle
Differentiation
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DomainBromodomain
Coiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionTransferase
   PTMAcetylation
Citrullination
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-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 H2B acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

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.3. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 19828133. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from sequence or structural similarity PubMed 15261140. Source: UniProtKB

response to estrogen

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-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

histone acetyltransferase complex

Inferred from direct assay PubMed 9742083. Source: MGI

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence or structural similarity PubMed 9194565. Source: UniProtKB

transcription factor complex

Inferred from direct assay PubMed 19828133. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from sequence or structural similarity PubMed 9194565. Source: UniProtKB

RNA polymerase II activating transcription factor binding

Inferred from physical interaction PubMed 18605988. Source: MGI

RNA polymerase II transcription factor binding

Inferred from physical interaction PubMed 18605988. Source: MGI

acetyltransferase activity

Inferred from sequence or structural similarity PubMed 12435739. Source: UniProtKB

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

p53 binding

Inferred from physical interaction PubMed 17591690. Source: MGI

transcription coactivator activity

Inferred from mutant phenotype PubMed 17641689. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 17641689. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 24122411Histone acetyltransferase p300
PRO_0000409386

Regions

Domain567 – 64680KIX
Domain1066 – 113873Bromo
Zinc finger332 – 41887TAZ-type 1
Zinc finger1663 – 170644ZZ-type
Zinc finger1727 – 180882TAZ-type 2
Region2 – 149148Interaction with RORA
Region2 – 139138Interaction with ALX1 By similarity
Region1016 – 102813CRD1; mediates transcriptional repression By similarity
Region2042 – 2237196Interaction with NCOA2 By similarity
Coiled coil1510 – 153930 Potential
Motif11 – 177Nuclear localization signal Potential
Compositional bias660 – 942283Pro-rich
Compositional bias798 – 8014Poly-Ser
Compositional bias1518 – 15258Poly-Glu

Sites

Metal binding3481Zinc 1 By similarity
Metal binding3521Zinc 1 By similarity
Metal binding3651Zinc 1 By similarity
Metal binding3701Zinc 1 By similarity
Metal binding3791Zinc 2 By similarity
Metal binding3831Zinc 2 By similarity
Metal binding3891Zinc 2 By similarity
Metal binding3941Zinc 2 By similarity
Metal binding4031Zinc 3 By similarity
Metal binding4071Zinc 3 By similarity
Metal binding4121Zinc 3 By similarity
Metal binding4151Zinc 3 By similarity
Site20891Interaction with NCOA2 By similarity
Site21431Interaction with NCOA2 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue891Phosphoserine; by AMPK By similarity
Modified residue2861Phosphoserine By similarity
Modified residue5811Omega-N-methylated arginine; by CARM1 By similarity
Modified residue6051Omega-N-methylated arginine; by CARM1 By similarity
Modified residue6371N6-acetyllysine By similarity
Modified residue8851Phosphothreonine By similarity
Modified residue8871Phosphothreonine By similarity
Modified residue9761N6-acetyllysine By similarity
Modified residue9801N6-acetyllysine By similarity
Modified residue10191N6-acetyllysine; alternate By similarity
Modified residue10231N6-acetyllysine; alternate By similarity
Modified residue10371Phosphoserine By similarity
Modified residue11021N6-acetyllysine By similarity
Modified residue11791N6-acetyllysine Ref.9
Modified residue13351N6-acetyllysine By similarity
Modified residue14721N6-acetyllysine By similarity
Modified residue14981N6-acetyllysine; by autocatalysis By similarity
Modified residue15411N6-acetyllysine By similarity
Modified residue15451N6-acetyllysine By similarity
Modified residue15481N6-acetyllysine; by autocatalysis By similarity
Modified residue15531N6-acetyllysine; by autocatalysis By similarity
Modified residue15541N6-acetyllysine By similarity
Modified residue15571N6-acetyllysine Ref.9
Modified residue15591N6-acetyllysine; alternate Ref.9
Modified residue15591N6-acetyllysine; by autocatalysis; alternate By similarity
Modified residue15821N6-acetyllysine By similarity
Modified residue15891N6-acetyllysine By similarity
Modified residue16731N6-acetyllysine By similarity
Modified residue17331Phosphoserine By similarity
Modified residue18561Phosphothreonine By similarity
Modified residue18581Phosphothreonine By similarity
Modified residue21431Asymmetric dimethylarginine; by CARM1; alternate By similarity
Modified residue21431Citrulline; by PADI4; alternate By similarity
Cross-link1019Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Cross-link1023Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity

Experimental info

Sequence conflict6771G → E in AAI44977. Ref.2
Sequence conflict6771G → E in AAI50682. Ref.2
Sequence conflict22171Q → QQQQ in AAI44977. Ref.2
Sequence conflict22171Q → QQQQ in AAI50682. Ref.2

Sequences

Sequence LengthMass (Da)Tools
B2RWS6 [UniParc].

Last modified April 16, 2014. Version 2.
Checksum: 0E9B2D9508237671

FASTA2,412263,305
        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 NTGSNMGQQP 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 
QQRMQHHMQQ MQQGNMGQMG QLPQALGAEA GASLQAYQQR LLQQQMGSPA QPNPMSPQQH 

      2290       2300       2310       2320       2330       2340 
MLPNQAQSPH LQGQQIPNSL SNQVRSPQPV PSPRPQSQPP HSSPSPRMQP QPSPHHVSPQ 

      2350       2360       2370       2380       2390       2400 
TSSPHPGLVA AQAANPMEQG HFASPDQNSM LSQLASNPGM ANLHGASATD LGLSSDNADL 

      2410 
NSNLSQSTLD IH 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"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.
[3]"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.
[4]"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.
[5]"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.
[6]"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.
[7]"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.
[8]"The orphan nuclear receptor RORalpha restrains adipocyte differentiation through a reduction of C/EBPbeta activity and perilipin gene expression."
Ohoka N., Kato S., Takahashi Y., Hayashi H., Sato R.
Mol. Endocrinol. 23:759-771(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CEBPB, SUBCELLULAR LOCATION.
[9]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1179; LYS-1557 AND LYS-1559, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC102262 Genomic DNA. No translation available.
AC160528 Genomic DNA. No translation available.
BC144976 mRNA. Translation: AAI44977.1.
BC150681 mRNA. Translation: AAI50682.1.
UniGeneMm.258397.

3D structure databases

ProteinModelPortalB2RWS6.
SMRB2RWS6. Positions 324-424, 567-647, 1045-1712, 1725-1833, 2051-2093.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-60610N.
IntActB2RWS6. 3 interactions.
STRING10090.ENSMUSP00000066789.

Proteomic databases

PaxDbB2RWS6.
PRIDEB2RWS6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:1276116. Ep300.

Phylogenomic databases

eggNOGCOG5076.
HOGENOMHOG000111353.
HOVERGENHBG000185.
InParanoidB2RWS6.

Enzyme and pathway databases

ReactomeREACT_109335. Circadian Clock.
REACT_188257. Signal Transduction.
REACT_188576. Developmental Biology.
REACT_189085. Disease.
REACT_24972. Circadian Clock.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Gene expression databases

GenevestigatorB2RWS6.

Family and domain databases

Gene3D1.10.1630.10. 1 hit.
1.10.246.20. 1 hit.
1.20.1020.10. 2 hits.
1.20.920.10. 1 hit.
InterProIPR001487. 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]
PfamPF00439. 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]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 1 hit.
SM00551. ZnF_TAZ. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMSSF47040. SSF47040. 1 hit.
SSF47370. SSF47370. 1 hit.
SSF57933. SSF57933. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEPS00633. 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]
ProtoNetSearch...

Other

ChiTaRSEP300. mouse.
PROB2RWS6.
SOURCESearch...

Entry information

Entry nameEP300_MOUSE
AccessionPrimary (citable) accession number: B2RWS6
Secondary accession number(s): E9PYJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: April 16, 2014
Last modified: April 16, 2014
This is version 60 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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