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B2RWS6

- EP300_MOUSE

UniProt

B2RWS6 - EP300_MOUSE

Protein

Histone acetyltransferase p300

Gene

Ep300

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 2 (16 Apr 2014)
      Previous versions | rss
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    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. Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity.2 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi348 – 3481Zinc 1By similarity
    Metal bindingi352 – 3521Zinc 1By similarity
    Metal bindingi365 – 3651Zinc 1By similarity
    Metal bindingi370 – 3701Zinc 1By similarity
    Metal bindingi379 – 3791Zinc 2By similarity
    Metal bindingi383 – 3831Zinc 2By similarity
    Metal bindingi389 – 3891Zinc 2By similarity
    Metal bindingi394 – 3941Zinc 2By similarity
    Metal bindingi403 – 4031Zinc 3By similarity
    Metal bindingi407 – 4071Zinc 3By similarity
    Metal bindingi412 – 4121Zinc 3By similarity
    Metal bindingi415 – 4151Zinc 3By similarity
    Sitei2089 – 20891Interaction with NCOA2By similarity
    Sitei2143 – 21431Interaction with NCOA2By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri332 – 41887TAZ-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1663 – 170644ZZ-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1727 – 180882TAZ-type 2PROSITE-ProRule annotationAdd
    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, acting on acetyl phosphate as donor 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

    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 1 PublicationPROSITE-ProRule annotation
    Note: In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. Colocalizes with ROCK2 in the nucleus By similarity.By similarity

    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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei89 – 891Phosphoserine; by AMPKBy similarity
    Modified residuei286 – 2861PhosphoserineBy similarity
    Modified residuei419 – 4191N6-acetyllysineBy similarity
    Modified residuei424 – 4241N6-acetyllysineBy similarity
    Modified residuei581 – 5811Omega-N-methylated arginine; by CARM1By similarity
    Modified residuei605 – 6051Omega-N-methylated arginine; by CARM1By similarity
    Modified residuei637 – 6371N6-acetyllysineBy similarity
    Modified residuei885 – 8851PhosphothreonineBy similarity
    Modified residuei887 – 8871PhosphothreonineBy similarity
    Modified residuei976 – 9761N6-acetyllysineBy similarity
    Modified residuei1019 – 10191N6-acetyllysine; alternateBy similarity
    Cross-linki1019 – 1019Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
    Modified residuei1023 – 10231N6-acetyllysine; alternateBy similarity
    Cross-linki1023 – 1023Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
    Modified residuei1037 – 10371PhosphoserineBy similarity
    Modified residuei1179 – 11791N6-acetyllysine1 Publication
    Modified residuei1335 – 13351N6-acetyllysineBy similarity
    Modified residuei1472 – 14721N6-acetyllysineBy similarity
    Modified residuei1498 – 14981N6-acetyllysine; by autocatalysisBy similarity
    Modified residuei1541 – 15411N6-acetyllysineBy similarity
    Modified residuei1545 – 15451N6-acetyllysineBy similarity
    Modified residuei1548 – 15481N6-acetyllysine; by autocatalysisBy similarity
    Modified residuei1553 – 15531N6-acetyllysine; by autocatalysisBy similarity
    Modified residuei1554 – 15541N6-acetyllysineBy similarity
    Modified residuei1557 – 15571N6-acetyllysine1 Publication
    Modified residuei1559 – 15591N6-acetyllysine; alternate1 Publication
    Modified residuei1559 – 15591N6-acetyllysine; by autocatalysis; alternateBy similarity
    Modified residuei1582 – 15821N6-acetyllysineBy similarity
    Modified residuei1698 – 16981N6-acetyllysineBy similarity
    Modified residuei1703 – 17031N6-acetyllysineBy similarity
    Modified residuei1706 – 17061N6-acetyllysineBy similarity
    Modified residuei1733 – 17331PhosphoserineBy similarity
    Modified residuei1856 – 18561PhosphothreonineBy similarity
    Modified residuei1858 – 18581PhosphothreonineBy similarity
    Modified residuei2143 – 21431Asymmetric dimethylarginine; by CARM1; alternateBy similarity
    Modified residuei2143 – 21431Citrulline; by PADI4; alternateBy 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.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.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.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.By similarity

    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. Interacts with MTA1. Interacts with HDAC4 and HDAC5 in the presence of TFAP2C By similarity. Interacts with NPAS2.By similarity7 Publications

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

    ProteinModelPortaliB2RWS6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini567 – 64680KIXPROSITE-ProRule annotationAdd
    BLAST
    Domaini1066 – 113873BromoPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 149148Interaction with RORAAdd
    BLAST
    Regioni2 – 139138Interaction with ALX1By similarityAdd
    BLAST
    Regioni1016 – 102813CRD1; mediates transcriptional repressionBy similarityAdd
    BLAST
    Regioni2042 – 2237196Interaction with NCOA2By similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1510 – 153930Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi11 – 177Nuclear localization signalSequence Analysis

    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.By similarity

    Sequence similaritiesi

    Contains 1 bromo domain.PROSITE-ProRule annotation
    Contains 1 KIX domain.PROSITE-ProRule annotation
    Contains 2 TAZ-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri332 – 41887TAZ-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1663 – 170644ZZ-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1727 – 180882TAZ-type 2PROSITE-ProRule annotationAdd
    BLAST

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti677 – 6771G → E in AAI44977. (PubMed:15489334)Curated
    Sequence conflicti677 – 6771G → E in AAI50682. (PubMed:15489334)Curated
    Sequence conflicti2217 – 22171Q → QQQQ in AAI44977. (PubMed:15489334)Curated
    Sequence conflicti2217 – 22171Q → QQQQ in AAI50682. (PubMed:15489334)Curated

    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

    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: October 1, 2014
    This is version 65 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