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B2RWS6

- EP300_MOUSE

UniProt

B2RWS6 - EP300_MOUSE

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Protein

Histone acetyltransferase p300

Gene
Ep300, P300
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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. Participates in CLOCK or NPAS2-regulated rhythmic gene transcription; exhibits a circadian association with CLOCK or NPAS2, correlating with increase in PER1/2 mRNA and histone H3 acetylation on the PER1/2 promoter.2 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi348 – 3481Zinc 1 By similarity
Metal bindingi352 – 3521Zinc 1 By similarity
Metal bindingi365 – 3651Zinc 1 By similarity
Metal bindingi370 – 3701Zinc 1 By similarity
Metal bindingi379 – 3791Zinc 2 By similarity
Metal bindingi383 – 3831Zinc 2 By similarity
Metal bindingi389 – 3891Zinc 2 By similarity
Metal bindingi394 – 3941Zinc 2 By similarity
Metal bindingi403 – 4031Zinc 3 By similarity
Metal bindingi407 – 4071Zinc 3 By similarity
Metal bindingi412 – 4121Zinc 3 By similarity
Metal bindingi415 – 4151Zinc 3 By similarity
Sitei2089 – 20891Interaction with NCOA2 By similarity
Sitei2143 – 21431Interaction with NCOA2 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri332 – 41887TAZ-type 1Add
BLAST
Zinc fingeri1663 – 170644ZZ-typeAdd
BLAST
Zinc fingeri1727 – 180882TAZ-type 2Add
BLAST

GO - Molecular functioni

  1. acetyltransferase activity Source: UniProtKB
  2. chromatin DNA binding Source: MGI
  3. DNA binding Source: UniProtKB
  4. histone acetyltransferase activity Source: UniProtKB
  5. lysine N-acetyltransferase activity Source: UniProtKB
  6. p53 binding Source: MGI
  7. pre-mRNA intronic binding Source: MGI
  8. protein binding Source: UniProtKB
  9. RNA polymerase II activating transcription factor binding Source: MGI
  10. RNA polymerase II core promoter sequence-specific DNA binding Source: MGI
  11. RNA polymerase II transcription factor binding Source: MGI
  12. transcription coactivator activity Source: UniProtKB
  13. transcription factor binding Source: UniProtKB
  14. zinc ion binding Source: InterPro

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. cartilage development Source: UniProtKB
  3. cell cycle Source: UniProtKB-KW
  4. cell differentiation Source: UniProtKB-KW
  5. circadian rhythm Source: UniProtKB
  6. heart development Source: MGI
  7. histone H2B acetylation Source: UniProtKB
  8. histone H4 acetylation Source: UniProtKB
  9. internal protein amino acid acetylation Source: UniProtKB
  10. lung development Source: MGI
  11. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  12. N-terminal peptidyl-lysine acetylation Source: UniProtKB
  13. organ morphogenesis Source: MGI
  14. positive regulation of protein binding Source: MGI
  15. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  16. positive regulation of transcription, DNA-templated Source: UniProtKB
  17. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  18. regulation of transcription, DNA-templated Source: UniProtKB
  19. regulation of tubulin deacetylation Source: UniProtKB
  20. response to estrogen Source: UniProtKB
  21. response to hypoxia Source: UniProtKB
  22. skeletal muscle tissue development Source: MGI
  23. somitogenesis Source: MGI
  24. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Biological rhythms, Cell cycle, Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118837. Rora activates circadian gene expression.
REACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196520. Pre-NOTCH Transcription and Translation.
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_196593. NOTCH2 intracellular domain regulates transcription.
REACT_198351. RORA activates circadian gene expression.
REACT_198352. REV-ERBA represses gene expression.
REACT_198521. TRAF6 mediated IRF7 activation.
REACT_198602. PPARA activates gene expression.
REACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_199107. Regulation of gene expression by Hypoxia-inducible Factor.
REACT_216539. formation of the beta-catenin:TCF transactivating complex.
REACT_223626. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_223784. Attenuation phase.
REACT_24972. Circadian Clock.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase p300 (EC:2.3.1.48)
Short name:
p300 HAT
Alternative name(s):
E1A-associated protein p300
Gene namesi
Name:Ep300
Synonyms:P300
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1276116. Ep300.

Subcellular locationi

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.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. histone acetyltransferase complex Source: MGI
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. transcription factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 24122411Histone acetyltransferase p300PRO_0000409386Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei89 – 891Phosphoserine; by AMPK By similarity
Modified residuei286 – 2861Phosphoserine By similarity
Modified residuei419 – 4191N6-acetyllysine By similarity
Modified residuei424 – 4241N6-acetyllysine By similarity
Modified residuei581 – 5811Omega-N-methylated arginine; by CARM1 By similarity
Modified residuei605 – 6051Omega-N-methylated arginine; by CARM1 By similarity
Modified residuei637 – 6371N6-acetyllysine By similarity
Modified residuei885 – 8851Phosphothreonine By similarity
Modified residuei887 – 8871Phosphothreonine By similarity
Modified residuei976 – 9761N6-acetyllysine By similarity
Modified residuei1019 – 10191N6-acetyllysine; alternate By similarity
Cross-linki1019 – 1019Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Modified residuei1023 – 10231N6-acetyllysine; alternate By similarity
Cross-linki1023 – 1023Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Modified residuei1037 – 10371Phosphoserine By similarity
Modified residuei1179 – 11791N6-acetyllysine1 Publication
Modified residuei1335 – 13351N6-acetyllysine By similarity
Modified residuei1472 – 14721N6-acetyllysine By similarity
Modified residuei1498 – 14981N6-acetyllysine; by autocatalysis By similarity
Modified residuei1541 – 15411N6-acetyllysine By similarity
Modified residuei1545 – 15451N6-acetyllysine By similarity
Modified residuei1548 – 15481N6-acetyllysine; by autocatalysis By similarity
Modified residuei1553 – 15531N6-acetyllysine; by autocatalysis By similarity
Modified residuei1554 – 15541N6-acetyllysine By similarity
Modified residuei1557 – 15571N6-acetyllysine1 Publication
Modified residuei1559 – 15591N6-acetyllysine; alternate1 Publication
Modified residuei1559 – 15591N6-acetyllysine; by autocatalysis; alternate By similarity
Modified residuei1582 – 15821N6-acetyllysine By similarity
Modified residuei1698 – 16981N6-acetyllysine By similarity
Modified residuei1703 – 17031N6-acetyllysine By similarity
Modified residuei1706 – 17061N6-acetyllysine By similarity
Modified residuei1733 – 17331Phosphoserine By similarity
Modified residuei1856 – 18561Phosphothreonine By similarity
Modified residuei1858 – 18581Phosphothreonine By similarity
Modified residuei2143 – 21431Asymmetric dimethylarginine; by CARM1; alternate By similarity
Modified residuei2143 – 21431Citrulline; by PADI4; alternate By similarity

Post-translational modificationi

Acetylated on Lys at up to 17 positions by intermolecular autocatalysis. Deacetylated in the transcriptional repression domain (CRD1) by SIRT1, preferentially at Lys-1019. Deacetylated by SIRT2, preferentially at Lys-419, Lys-424, Lys-1541, Lys-1545, Lys-1548, Lys-1698, Lys-1703 and Lys-1706 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.1 Publication

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiB2RWS6.
PRIDEiB2RWS6.

Expressioni

Gene expression databases

GenevestigatoriB2RWS6.

Interactioni

Subunit structurei

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. Interacts with ARNTL/BMAL1 and CLOCK By similarity. Interacts with SIRT2 By similarity. Interacts with NPAS2.7 Publications

Protein-protein interaction databases

DIPiDIP-60610N.
IntActiB2RWS6. 3 interactions.
STRINGi10090.ENSMUSP00000066789.

Structurei

3D structure databases

ProteinModelPortaliB2RWS6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini567 – 64680KIXAdd
BLAST
Domaini1066 – 113873BromoAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 149148Interaction with RORAAdd
BLAST
Regioni2 – 139138Interaction with ALX1 By similarityAdd
BLAST
Regioni1016 – 102813CRD1; mediates transcriptional repression By similarityAdd
BLAST
Regioni2042 – 2237196Interaction with NCOA2 By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1510 – 153930 Reviewed predictionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi11 – 177Nuclear localization signal Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi660 – 942283Pro-richAdd
BLAST
Compositional biasi798 – 8014Poly-Ser
Compositional biasi1518 – 15258Poly-Glu

Domaini

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.

Sequence similaritiesi

Contains 1 bromo domain.
Contains 1 KIX domain.

Keywords - Domaini

Bromodomain, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5076.
GeneTreeiENSGT00730000110623.
HOGENOMiHOG000111353.
HOVERGENiHBG000185.
InParanoidiB2RWS6.
KOiK04498.
OMAiPTMIRGS.
PhylomeDBiB2RWS6.

Family and domain databases

Gene3Di1.10.1630.10. 1 hit.
1.10.246.20. 1 hit.
1.20.1020.10. 2 hits.
1.20.920.10. 1 hit.
InterProiIPR001487. 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]
PfamiPF00439. 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]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
SM00551. ZnF_TAZ. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF47040. SSF47040. 1 hit.
SSF47370. SSF47370. 1 hit.
SSF57933. SSF57933. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEiPS00633. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

B2RWS6-1 [UniParc]FASTAAdd to Basket

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MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS     50
TELGLTNGGD ISQLQTSLGI VQDAASKHKQ LSELLRSGSS PNLNMGVGGP 100
GQAMASQAQQ NSPGLSLINS MVKSPMAQTG LTSPNMGIGS SGPNQGPTQS 150
PAGMMNSPVN QPAMGMNTGM NAGMNPGMLA AGNGQGIMPN QVMNGSIGAG 200
RGRPNMQYPN AGMGNAGSLL TEPLQQGSPQ MGGQPGLRGP QPLKMGMMNN 250
PSPYGSPYTQ NSGQQIGASG LGLQIQTKTV LPNNLSPFAM DKKAVPGGGM 300
PSMGQQPTPS VQQPGLVTPV AAGMGSGAHT ADPEKRKLIQ QQLVLLLHAH 350
KCQRREQANG EVRQCNLPHC RTMKNVLNHM THCQSGKSCQ VAHCASSRQI 400
ISHWKNCTRH DCPVCLPLKN AGDKRNQQSI LTGAPVGLGN PSSLGVGQQS 450
TPSLSTVSQI DPSSIERAYA ALGLPYQVNQ IPPQPQVQAK NQQSQPSGQS 500
PQGMRSVNNM SASPMGVNGG VGVQTPNLLS DSMLHSTINS QNPMMSENAG 550
VASLGPLPTA AQPSSTGIRK QWHEDITQDL RNHLVHKLVQ AIFPTPDPAA 600
LKDRRMENLV AYARKVEGDM YESANNRAEY YHLLAEKIYK IQKELEEKRR 650
TRLQKQNMLP NAPGMGPVPM NTGSNMGQQP TGMTTNGPVP DPSMIRGSVP 700
NHMMPRMTPQ PGLNQFGQMN MPQPPIGPRQ PSPLQHHGQL AQSGSLNPPM 750
GYGPRMQQAS GQNQFLSQTQ FTSQGMNVTN MPLAPSSGQA PVSQAQMSSS 800
SCPVNSPIMP PGSQGSHIHC PTLPQQAHQN SPSPVPSRTP TPHHTPPSIG 850
NQPPPATAIP TPVPTPPAIP PGPQPPSLHP SSRQTPTPPT HLPPQVQPSL 900
PAAPSADQSQ QQPRSQQSTA VSVPTPTAPL LPPQPSTPLS QPAVSIEGQV 950
SNPPSTSSTE VNSQTIPEKQ PSQEVKMESK MEVDKPEPAD AQPEDTKEAK 1000
GEDVKVEPTE MEERGPELKT DGKEEEEQPS TSATQSSPAP GQSKKKIFKP 1050
EELRQALMPT LEALYRQDPE SLPFRQPVDP QLLGIPDYFD IVKSPMDLST 1100
IKRKLDTGQY QEPWQYIDDI WLMFNNAWLY NRKTSRVYKY CSKLSEVFEQ 1150
EIDPVMQSLG YCCGRKLEFS PQTLCCYGKQ LCTIPRDATY YSYQNRYHFC 1200
EKCFNEIQGE SVSLGDDPSQ PQTTINKEQF SKRKNDTLDP ELFVECTECG 1250
RKMHQICVLH HEIIWPSGFV CDGCLKKTAR TRKENKLSAK RLPSTRLGTF 1300
LENRVNDFLR RQNHPESGEV TVRVVHASDK TVEVKPGMKA RFVDSGEMAE 1350
SFPYRTKALF AFEEIDGVDL CFFGMHVQEY GSDCPPPNQR RVYISYLDSV 1400
HFFRPKCLRT AVYHEILIGY LEYVKKLGYT TGHIWACPPS EGDDYIFHCH 1450
PPDQKIPKPK RLQEWYKKML DKAVSERIVH DYKDILKQAT EDRLTSAKEL 1500
PYFEGDFWPN VLEESIKELE QEEEERKREE NTSNESTDVT KGDSKNAKKK 1550
NNKKTSKNKS SLSRGNKKKP GMPNVSNDLS QKLYATMEKH KEVFFVIRLI 1600
ACPAPNSLPP IVDPDPLIPC DLMDGRDAFL TLARDKHLEF SSLRRAQWST 1650
MCMLVELHTQ SQDRFVYTCN ECKHHVETRW HCTVCEDYDL CITCYNTKNH 1700
DHKMEKLGLG LDDESNNQQA AATQSPGDSR RLSIQRCIQS LVHACQCRNA 1750
NCSLPSCQKM KRVVQHTKGC KRKTNGGCPI CKQLIALCCY HAKHCQENKC 1800
PVPFCLNIKQ KLRQQQLQHR LQQAQMLRRR MASMQRTGVA GQQQGLPSPT 1850
PATPTTPTGQ QPATPQTPQP QPTSQPQPTP PNNMTPYLPR TQTTGPVSQG 1900
KAPGQVTPPT PPQTAQAPLP GPPPAAVEMA MQIQRAAETQ RQMAHVQIFQ 1950
RPIQHQMPQM SPMAPMGMNP PPMARGPGGH LDPGIGPAGM QQQPPWAQGG 2000
MPQPQQMQSG MPRPAMMSVA QHGQPLNMAP QPGLGQVGVS PLKPGTVSQQ 2050
ALQNLLRTLR SPSSPLQQQQ VLSILHANPQ LLAAFIKQRA AKYANPNPQP 2100
LPGQPGMTQG QPGLQPPTMP GQQGVHSNPA LQNMNPLQAG VQRAGLPQQQ 2150
PQQQLQPPMG AMSPQAQQMN MNHNTMPSQF RDILRRQMMQ QQGAGPGIGP 2200
GMANQFQQPQ GIGYPPQQQQ QQRMQHHMQQ MQQGNMGQMG QLPQALGAEA 2250
GASLQAYQQR LLQQQMGSPA QPNPMSPQQH MLPNQAQSPH LQGQQIPNSL 2300
SNQVRSPQPV PSPRPQSQPP HSSPSPRMQP QPSPHHVSPQ TSSPHPGLVA 2350
AQAANPMEQG HFASPDQNSM LSQLASNPGM ANLHGASATD LGLSSDNADL 2400
NSNLSQSTLD IH 2412
Length:2,412
Mass (Da):263,305
Last modified:April 16, 2014 - v2
Checksum:i0E9B2D9508237671
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti677 – 6771G → E in AAI44977. 1 Publication
Sequence conflicti677 – 6771G → E in AAI50682. 1 Publication
Sequence conflicti2217 – 22171Q → QQQQ in AAI44977. 1 Publication
Sequence conflicti2217 – 22171Q → QQQQ in AAI50682. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC102262 Genomic DNA. No translation available.
AC160528 Genomic DNA. No translation available.
BC144976 mRNA. Translation: AAI44977.1.
BC150681 mRNA. Translation: AAI50682.1.
CCDSiCCDS37149.1.
RefSeqiNP_808489.4. NM_177821.6.
UniGeneiMm.258397.

Genome annotation databases

EnsembliENSMUST00000068387; ENSMUSP00000066789; ENSMUSG00000055024.
GeneIDi328572.
KEGGimmu:328572.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC102262 Genomic DNA. No translation available.
AC160528 Genomic DNA. No translation available.
BC144976 mRNA. Translation: AAI44977.1 .
BC150681 mRNA. Translation: AAI50682.1 .
CCDSi CCDS37149.1.
RefSeqi NP_808489.4. NM_177821.6.
UniGenei Mm.258397.

3D structure databases

ProteinModelPortali B2RWS6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-60610N.
IntActi B2RWS6. 3 interactions.
STRINGi 10090.ENSMUSP00000066789.

Proteomic databases

PaxDbi B2RWS6.
PRIDEi B2RWS6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000068387 ; ENSMUSP00000066789 ; ENSMUSG00000055024 .
GeneIDi 328572.
KEGGi mmu:328572.

Organism-specific databases

CTDi 2033.
MGIi MGI:1276116. Ep300.

Phylogenomic databases

eggNOGi COG5076.
GeneTreei ENSGT00730000110623.
HOGENOMi HOG000111353.
HOVERGENi HBG000185.
InParanoidi B2RWS6.
KOi K04498.
OMAi PTMIRGS.
PhylomeDBi B2RWS6.

Enzyme and pathway databases

Reactomei REACT_118837. Rora activates circadian gene expression.
REACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196520. Pre-NOTCH Transcription and Translation.
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_196593. NOTCH2 intracellular domain regulates transcription.
REACT_198351. RORA activates circadian gene expression.
REACT_198352. REV-ERBA represses gene expression.
REACT_198521. TRAF6 mediated IRF7 activation.
REACT_198602. PPARA activates gene expression.
REACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_199107. Regulation of gene expression by Hypoxia-inducible Factor.
REACT_216539. formation of the beta-catenin:TCF transactivating complex.
REACT_223626. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_223784. Attenuation phase.
REACT_24972. Circadian Clock.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Miscellaneous databases

ChiTaRSi EP300. mouse.
NextBioi 398354.
PROi B2RWS6.
SOURCEi Search...

Gene expression databases

Genevestigatori B2RWS6.

Family and domain databases

Gene3Di 1.10.1630.10. 1 hit.
1.10.246.20. 1 hit.
1.20.1020.10. 2 hits.
1.20.920.10. 1 hit.
InterProi 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 ]
Pfami 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 ]
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00297. BROMO. 1 hit.
SM00551. ZnF_TAZ. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view ]
SUPFAMi SSF47040. SSF47040. 1 hit.
SSF47370. SSF47370. 1 hit.
SSF57933. SSF57933. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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. "Histone acetyltransferase-dependent chromatin remodeling and the vascular clock."
    Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M., Chakravarti D., FitzGerald G.A., McNamara P.
    J. Biol. Chem. 279:7091-7097(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NPAS2.
  7. "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.
  8. "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.
  9. "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.
  10. "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.

Entry informationi

Entry nameiEP300_MOUSE
AccessioniPrimary (citable) accession number: B2RWS6
Secondary accession number(s): E9PYJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: April 16, 2014
Last modified: September 3, 2014
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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