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Protein

Histone acetyltransferase p300

Gene

Ep300

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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. Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity (PubMed:14645221, PubMed:9512516). Acetylates XBP1 isoform 2; acetylation increases protein stability of XBP1 isoform 2 and enhances its transcriptional activity (PubMed:20955178).By similarity3 Publications

Catalytic activityi

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

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
Binding sitei1456 – 14561Acetyl-CoA; via carbonyl oxygenBy similarity
Binding sitei1461 – 14611Acetyl-CoABy similarity
Binding sitei1465 – 14651Acetyl-CoABy 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. activating transcription factor binding Source: MGI
  3. androgen receptor binding Source: MGI
  4. antigen binding Source: Ensembl
  5. beta-catenin binding Source: MGI
  6. chromatin binding Source: MGI
  7. chromatin DNA binding Source: MGI
  8. core promoter binding Source: MGI
  9. DNA binding Source: UniProtKB
  10. histone acetyltransferase activity Source: UniProtKB
  11. lysine N-acetyltransferase activity, acting on acetyl phosphate as donor Source: UniProtKB
  12. nuclear hormone receptor binding Source: MGI
  13. p53 binding Source: MGI
  14. pre-mRNA intronic binding Source: MGI
  15. protein C-terminus binding Source: MGI
  16. RNA polymerase II activating transcription factor binding Source: MGI
  17. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  18. RNA polymerase II core promoter sequence-specific DNA binding Source: MGI
  19. RNA polymerase II transcription factor binding Source: MGI
  20. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
  21. transcription coactivator activity Source: UniProtKB
  22. transcription factor binding Source: UniProtKB
  23. transferase activity, transferring acyl groups Source: MGI
  24. 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. cellular response to cAMP Source: Ensembl
  5. cellular response to dexamethasone stimulus Source: Ensembl
  6. cellular response to drug Source: Ensembl
  7. cellular response to glucose stimulus Source: Ensembl
  8. cellular response to hydrogen peroxide Source: Ensembl
  9. cellular response to mineralocorticoid stimulus Source: Ensembl
  10. cellular response to nerve growth factor stimulus Source: Ensembl
  11. cellular response to retinoic acid Source: Ensembl
  12. cellular response to trichostatin A Source: Ensembl
  13. circadian rhythm Source: UniProtKB
  14. digestive tract development Source: Ensembl
  15. heart development Source: MGI
  16. histone H2B acetylation Source: UniProtKB
  17. histone H3 acetylation Source: Ensembl
  18. histone H4 acetylation Source: UniProtKB
  19. internal peptidyl-lysine acetylation Source: MGI
  20. internal protein amino acid acetylation Source: UniProtKB
  21. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: MGI
  22. liver development Source: Ensembl
  23. lung development Source: MGI
  24. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  25. negative regulation of miRNA metabolic process Source: Ensembl
  26. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  27. N-terminal peptidyl-lysine acetylation Source: UniProtKB
  28. organ morphogenesis Source: MGI
  29. positive regulation by host of viral transcription Source: MGI
  30. positive regulation of axon extension Source: Ensembl
  31. positive regulation of cell death Source: Ensembl
  32. positive regulation of cell size Source: Ensembl
  33. positive regulation of collagen biosynthetic process Source: Ensembl
  34. positive regulation of DNA binding Source: Ensembl
  35. positive regulation of glycoprotein biosynthetic process Source: Ensembl
  36. positive regulation of muscle atrophy Source: Ensembl
  37. positive regulation of protein acetylation Source: Ensembl
  38. positive regulation of protein binding Source: MGI
  39. positive regulation of protein import into nucleus, translocation Source: Ensembl
  40. positive regulation of protein phosphorylation Source: Ensembl
  41. positive regulation of protein secretion Source: Ensembl
  42. positive regulation of proteolysis Source: Ensembl
  43. positive regulation of sarcomere organization Source: Ensembl
  44. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  45. positive regulation of transcription, DNA-templated Source: UniProtKB
  46. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  47. positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response Source: UniProtKB
  48. positive regulation of translation Source: Ensembl
  49. protein acetylation Source: UniProtKB
  50. protein-DNA complex assembly Source: Ensembl
  51. protein kinase B signaling Source: Ensembl
  52. protein stabilization Source: UniProtKB
  53. regulation of androgen receptor signaling pathway Source: MGI
  54. regulation of angiotensin metabolic process Source: Ensembl
  55. regulation of transcription, DNA-templated Source: UniProtKB
  56. regulation of tubulin deacetylation Source: UniProtKB
  57. response to calcium ion Source: Ensembl
  58. response to cobalt ion Source: Ensembl
  59. response to estrogen Source: UniProtKB
  60. response to ethanol Source: Ensembl
  61. response to fatty acid Source: Ensembl
  62. response to hypoxia Source: UniProtKB
  63. response to tumor necrosis factor Source: Ensembl
  64. skeletal muscle tissue development Source: MGI
  65. somitogenesis Source: MGI
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_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_231481. TRAF3-dependent IRF activation pathway.
REACT_241925. Circadian Clock.
REACT_24972. Circadian Clock.
REACT_252217. Transcriptional regulation of white adipocyte differentiation.
REACT_268602. Pre-NOTCH Transcription and Translation.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase p300 (EC:2.3.1.48By similarity)
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: Chromosome 15

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

GO - Cellular componenti

  1. chromatin Source: Ensembl
  2. cytoplasm Source: MGI
  3. histone acetyltransferase complex Source: MGI
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
  6. protein-DNA complex Source: Ensembl
  7. 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 – 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
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 TRIP4 (By similarity). Interacts with NPAS2.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Tp53P023402EBI-3953360,EBI-474016

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliB2RWS6.
SMRiB2RWS6. Positions 324-424, 567-647, 1045-1712, 1725-1833, 2051-2093.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini567 – 64680KIXPROSITE-ProRule annotationAdd
BLAST
Domaini1066 – 113873BromoPROSITE-ProRule annotationAdd
BLAST
Domaini1286 – 1662377CBP/p300-type HATPROSITE-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
Regioni1396 – 13983Interaction with histoneBy similarity
Regioni1397 – 13993Acetyl-CoA bindingBy similarity
Regioni1409 – 14102Acetyl-CoA bindingBy similarity
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 CBP/p300-type HAT (histone acetyltransferase) 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.
GeneTreeiENSGT00760000119206.
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.
PS51727. CBP_P300_HAT. 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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        10         20         30         40         50
MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS
60 70 80 90 100
TELGLTNGGD ISQLQTSLGI VQDAASKHKQ LSELLRSGSS PNLNMGVGGP
110 120 130 140 150
GQAMASQAQQ NSPGLSLINS MVKSPMAQTG LTSPNMGIGS SGPNQGPTQS
160 170 180 190 200
PAGMMNSPVN QPAMGMNTGM NAGMNPGMLA AGNGQGIMPN QVMNGSIGAG
210 220 230 240 250
RGRPNMQYPN AGMGNAGSLL TEPLQQGSPQ MGGQPGLRGP QPLKMGMMNN
260 270 280 290 300
PSPYGSPYTQ NSGQQIGASG LGLQIQTKTV LPNNLSPFAM DKKAVPGGGM
310 320 330 340 350
PSMGQQPTPS VQQPGLVTPV AAGMGSGAHT ADPEKRKLIQ QQLVLLLHAH
360 370 380 390 400
KCQRREQANG EVRQCNLPHC RTMKNVLNHM THCQSGKSCQ VAHCASSRQI
410 420 430 440 450
ISHWKNCTRH DCPVCLPLKN AGDKRNQQSI LTGAPVGLGN PSSLGVGQQS
460 470 480 490 500
TPSLSTVSQI DPSSIERAYA ALGLPYQVNQ IPPQPQVQAK NQQSQPSGQS
510 520 530 540 550
PQGMRSVNNM SASPMGVNGG VGVQTPNLLS DSMLHSTINS QNPMMSENAG
560 570 580 590 600
VASLGPLPTA AQPSSTGIRK QWHEDITQDL RNHLVHKLVQ AIFPTPDPAA
610 620 630 640 650
LKDRRMENLV AYARKVEGDM YESANNRAEY YHLLAEKIYK IQKELEEKRR
660 670 680 690 700
TRLQKQNMLP NAPGMGPVPM NTGSNMGQQP TGMTTNGPVP DPSMIRGSVP
710 720 730 740 750
NHMMPRMTPQ PGLNQFGQMN MPQPPIGPRQ PSPLQHHGQL AQSGSLNPPM
760 770 780 790 800
GYGPRMQQAS GQNQFLSQTQ FTSQGMNVTN MPLAPSSGQA PVSQAQMSSS
810 820 830 840 850
SCPVNSPIMP PGSQGSHIHC PTLPQQAHQN SPSPVPSRTP TPHHTPPSIG
860 870 880 890 900
NQPPPATAIP TPVPTPPAIP PGPQPPSLHP SSRQTPTPPT HLPPQVQPSL
910 920 930 940 950
PAAPSADQSQ QQPRSQQSTA VSVPTPTAPL LPPQPSTPLS QPAVSIEGQV
960 970 980 990 1000
SNPPSTSSTE VNSQTIPEKQ PSQEVKMESK MEVDKPEPAD AQPEDTKEAK
1010 1020 1030 1040 1050
GEDVKVEPTE MEERGPELKT DGKEEEEQPS TSATQSSPAP GQSKKKIFKP
1060 1070 1080 1090 1100
EELRQALMPT LEALYRQDPE SLPFRQPVDP QLLGIPDYFD IVKSPMDLST
1110 1120 1130 1140 1150
IKRKLDTGQY QEPWQYIDDI WLMFNNAWLY NRKTSRVYKY CSKLSEVFEQ
1160 1170 1180 1190 1200
EIDPVMQSLG YCCGRKLEFS PQTLCCYGKQ LCTIPRDATY YSYQNRYHFC
1210 1220 1230 1240 1250
EKCFNEIQGE SVSLGDDPSQ PQTTINKEQF SKRKNDTLDP ELFVECTECG
1260 1270 1280 1290 1300
RKMHQICVLH HEIIWPSGFV CDGCLKKTAR TRKENKLSAK RLPSTRLGTF
1310 1320 1330 1340 1350
LENRVNDFLR RQNHPESGEV TVRVVHASDK TVEVKPGMKA RFVDSGEMAE
1360 1370 1380 1390 1400
SFPYRTKALF AFEEIDGVDL CFFGMHVQEY GSDCPPPNQR RVYISYLDSV
1410 1420 1430 1440 1450
HFFRPKCLRT AVYHEILIGY LEYVKKLGYT TGHIWACPPS EGDDYIFHCH
1460 1470 1480 1490 1500
PPDQKIPKPK RLQEWYKKML DKAVSERIVH DYKDILKQAT EDRLTSAKEL
1510 1520 1530 1540 1550
PYFEGDFWPN VLEESIKELE QEEEERKREE NTSNESTDVT KGDSKNAKKK
1560 1570 1580 1590 1600
NNKKTSKNKS SLSRGNKKKP GMPNVSNDLS QKLYATMEKH KEVFFVIRLI
1610 1620 1630 1640 1650
ACPAPNSLPP IVDPDPLIPC DLMDGRDAFL TLARDKHLEF SSLRRAQWST
1660 1670 1680 1690 1700
MCMLVELHTQ SQDRFVYTCN ECKHHVETRW HCTVCEDYDL CITCYNTKNH
1710 1720 1730 1740 1750
DHKMEKLGLG LDDESNNQQA AATQSPGDSR RLSIQRCIQS LVHACQCRNA
1760 1770 1780 1790 1800
NCSLPSCQKM KRVVQHTKGC KRKTNGGCPI CKQLIALCCY HAKHCQENKC
1810 1820 1830 1840 1850
PVPFCLNIKQ KLRQQQLQHR LQQAQMLRRR MASMQRTGVA GQQQGLPSPT
1860 1870 1880 1890 1900
PATPTTPTGQ QPATPQTPQP QPTSQPQPTP PNNMTPYLPR TQTTGPVSQG
1910 1920 1930 1940 1950
KAPGQVTPPT PPQTAQAPLP GPPPAAVEMA MQIQRAAETQ RQMAHVQIFQ
1960 1970 1980 1990 2000
RPIQHQMPQM SPMAPMGMNP PPMARGPGGH LDPGIGPAGM QQQPPWAQGG
2010 2020 2030 2040 2050
MPQPQQMQSG MPRPAMMSVA QHGQPLNMAP QPGLGQVGVS PLKPGTVSQQ
2060 2070 2080 2090 2100
ALQNLLRTLR SPSSPLQQQQ VLSILHANPQ LLAAFIKQRA AKYANPNPQP
2110 2120 2130 2140 2150
LPGQPGMTQG QPGLQPPTMP GQQGVHSNPA LQNMNPLQAG VQRAGLPQQQ
2160 2170 2180 2190 2200
PQQQLQPPMG AMSPQAQQMN MNHNTMPSQF RDILRRQMMQ QQGAGPGIGP
2210 2220 2230 2240 2250
GMANQFQQPQ GIGYPPQQQQ QQRMQHHMQQ MQQGNMGQMG QLPQALGAEA
2260 2270 2280 2290 2300
GASLQAYQQR LLQQQMGSPA QPNPMSPQQH MLPNQAQSPH LQGQQIPNSL
2310 2320 2330 2340 2350
SNQVRSPQPV PSPRPQSQPP HSSPSPRMQP QPSPHHVSPQ TSSPHPGLVA
2360 2370 2380 2390 2400
AQAANPMEQG HFASPDQNSM LSQLASNPGM ANLHGASATD LGLSSDNADL
2410
NSNLSQSTLD IH
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliB2RWS6.
SMRiB2RWS6. Positions 324-424, 567-647, 1045-1712, 1725-1833, 2051-2093.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiB2RWS6.
PRIDEiB2RWS6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2033.
MGIiMGI:1276116. Ep300.

Phylogenomic databases

eggNOGiCOG5076.
GeneTreeiENSGT00760000119206.
HOGENOMiHOG000111353.
HOVERGENiHBG000185.
InParanoidiB2RWS6.
KOiK04498.
OMAiPTMIRGS.
PhylomeDBiB2RWS6.

Enzyme and pathway databases

ReactomeiREACT_118837. Rora activates circadian gene expression.
REACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
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_231481. TRAF3-dependent IRF activation pathway.
REACT_241925. Circadian Clock.
REACT_24972. Circadian Clock.
REACT_252217. Transcriptional regulation of white adipocyte differentiation.
REACT_268602. Pre-NOTCH Transcription and Translation.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Miscellaneous databases

ChiTaRSiEp300. mouse.
NextBioi398354.
PROiB2RWS6.
SOURCEiSearch...

Gene expression databases

GenevestigatoriB2RWS6.

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.
PS51727. CBP_P300_HAT. 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]
ProtoNetiSearch...

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. "Regulation of unfolded protein response modulator XBP1s by acetylation and deacetylation."
    Wang F.M., Chen Y.J., Ouyang H.J.
    Biochem. J. 433:245-252(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACETYLATION OF XBP1.
  11. "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: February 4, 2015
This is version 69 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.