Product: KAT3B/p300 Antibody
Catalog: AF5360
Description: Rabbit polyclonal antibody to KAT3B/p300
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Bovine, Horse, Sheep, Rabbit, Chicken, Xenopus
Mol.Wt.: 300 kDa; 264kD(Calculated).
Uniprot: Q09472
RRID: AB_2837845

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 100ul $280 In stock
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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Prediction:
Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Chicken(100%), Xenopus(82%)
Clonality:
Polyclonal
Specificity:
KAT3B / p300 Antibody detects endogenous levels of total KAT3B/p300.
RRID:
AB_2837845
Cite Format: Affinity Biosciences Cat# AF5360, RRID:AB_2837845.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

E1A associated protein p300; E1A binding protein p300; E1A-associated protein p300; EP300; EP300: E1A binding protein p300; EP300_HUMAN; Histone acetyltransferase p300; KAT3B; p300 HAT; RSTS2;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Description:
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.
Sequence:
MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGDINQLQTSLGMVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQSSPGLGLINSMVKSPMTQAGLTSPNMGMGTSGPNQGPTQSTGMMNSPVNQPAMGMNTGMNAGMNPGMLAAGNGQGIMPNQVMNGSIGAGRGRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTGLRGPQPLKMGMMNNPNPYGSPYTQNPGQQIGASGLGLQIQTKTVLSNNLSPFAMDKKAVPGGGMPNMGQQPAPQVQQPGLVTPVAQGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNAGDKRNQQPILTGAPVGLGNPSSLGVGQQSAPNLSTVSQIDPSSIERAYAALGLPYQVNQMPTQPQVQAKNQQNQQPGQSPQGMRPMSNMSASPMGVNGGVGVQTPSLLSDSMLHSAINSQNPMMSENASVPSLGPMPTAAQPSTTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPNAAGMVPVSMNPGPNMGQPQPGMTSNGPLPDPSMIRGSVPNQMMPRITPQSGLNQFGQMSMAQPPIVPRQTPPLQHHGQLAQPGALNPPMGYGPRMQQPSNQGQFLPQTQFPSQGMNVTNIPLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPQLPQPALHQNSPSPVPSRTPTPHHTPPSIGAQQPPATTIPAPVPTPPAMPPGPQSQALHPPPRQTPTPPTTQLPQQVQPSLPAAPSADQPQQQPRSQQSTAASVPTPTAPLLPPQPATPLSQPAVSIEGQVSNPPSTSSTEVNSQAIAEKQPSQEVKMEAKMEVDQPEPADTQPEDISESKVEDCKMESTETEERSTELKTEIKEEEDQPSTSATQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHFCEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEIIWPAGFVCDGCLKKSARTRKENKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENKCPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVVGQQQGLPSPTPATPTTPTGQQPTTPQTPQPTSQPQPTPPNSMPPYLPRTQAAGPVSQGKAAGQVTPPTPPQTAQPPLPGPPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPPMTPMAPMGMNPPPMTRGPSGHLEPGMGPTGMQQQPPWSQGGLPQPQQLQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGISPLKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPIPGQPGMPQGQPGLQPPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQFRDILRRQQMMQQQQQQGAGPGIGPGMANHNQFQQPQGVGYPPQQQQRMQHHMQQMQQGNMGQIGQLPQALGAEAGASLQAYQQRLLQQQMGSPVQPNPMSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSPQTSSPHPGLVAAQANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSTDNSDLNSNLSQSTLDIH

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Horse
100
Bovine
100
Sheep
100
Chicken
100
Rabbit
100
Xenopus
82
Pig
31
Dog
0
Zebrafish
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - Q09472 As Substrate

Site PTM Type Enzyme
A2 Acetylation
S12 Phosphorylation
K14 Acetylation
S19 Phosphorylation
S24 Phosphorylation
K77 Acetylation
K79 Acetylation
S89 Phosphorylation Q05655 (PRKCD) , P17252 (PRKCA) , Q13131 (PRKAA1)
S106 Phosphorylation Q13315 (ATM)
S133 Phosphorylation
R237 Methylation
K243 Methylation
S285 Phosphorylation
K291 Acetylation
K292 Acetylation
T317 Phosphorylation P28482 (MAPK1)
K336 Acetylation
K350 Acetylation
K373 Acetylation
K373 Ubiquitination
S384 Phosphorylation Q04759 (PRKCQ)
K386 Acetylation
K404 Acetylation
K418 Acetylation
K423 Acetylation
K489 Acetylation
S499 Phosphorylation
K569 Acetylation
K569 Ubiquitination
R580 Methylation
K601 Acetylation
R604 Methylation
Y611 Phosphorylation
K614 Acetylation
K614 Ubiquitination
Y620 Phosphorylation
Y629 Phosphorylation
Y630 Phosphorylation
K636 Acetylation
K636 Ubiquitination
R705 Methylation
R728 Methylation
S831 Phosphorylation
S833 Phosphorylation
T839 Phosphorylation
T841 Phosphorylation
T845 Phosphorylation
T885 Phosphorylation
T887 Phosphorylation
T891 Phosphorylation
T938 Phosphorylation P28482 (MAPK1)
K970 Acetylation
K977 Acetylation
K981 Acetylation
K1001 Acetylation
K1006 Acetylation
K1020 Acetylation
K1020 Sumoylation
K1024 Acetylation
K1024 Sumoylation
S1037 Phosphorylation
S1038 Phosphorylation P06493 (CDK1) , P27361 (MAPK3) , P28482 (MAPK1)
S1044 Phosphorylation
K1045 Acetylation
K1046 Acetylation
K1047 Acetylation
Y1089 Phosphorylation
K1094 Acetylation
K1103 Acetylation
K1105 Acetylation
T1135 Phosphorylation
K1144 Acetylation
K1167 Acetylation
K1167 Ubiquitination
K1180 Acetylation
K1203 Acetylation
K1228 Acetylation
S1295 Phosphorylation
T1296 Phosphorylation
K1331 Acetylation
K1336 Acetylation
K1340 Acetylation
K1340 Ubiquitination
Y1355 Phosphorylation
K1427 Acetylation
Y1446 Phosphorylation
K1473 Acetylation
K1488 Ubiquitination
K1499 Acetylation Q09472 (EP300)
K1499 Ubiquitination
K1518 Acetylation
K1528 Acetylation
T1533 Phosphorylation
S1534 Phosphorylation
K1542 Acetylation
K1546 Acetylation
K1549 Acetylation Q09472 (EP300)
K1550 Acetylation
K1551 Acetylation
K1554 Acetylation Q09472 (EP300)
K1555 Acetylation
K1558 Acetylation
K1560 Acetylation Q09472 (EP300)
K1568 Acetylation
K1569 Acetylation
K1570 Acetylation
S1577 Phosphorylation
S1581 Phosphorylation
K1583 Acetylation
K1583 Ubiquitination
K1590 Acetylation
K1590 Ubiquitination
T1632 Phosphorylation
K1637 Acetylation
K1637 Ubiquitination
K1674 Acetylation
K1699 Acetylation
K1704 Acetylation
K1707 Acetylation
S1726 Phosphorylation
S1754 Phosphorylation
K1760 Acetylation
K1762 Acetylation
K1769 Acetylation
K1772 Acetylation
K1774 Acetylation
K1783 Acetylation
K1794 Acetylation
K1800 Acetylation
K1810 Acetylation
K1812 Acetylation
S1834 Phosphorylation P31751 (AKT2) , P31749 (AKT1) , O00141 (SGK1)
T1857 Phosphorylation
T1859 Phosphorylation
K1900 Acetylation
T1906 Phosphorylation
T1909 Phosphorylation
T1960 Phosphorylation P28482 (MAPK1)
S2039 Phosphorylation P28482 (MAPK1) , P27361 (MAPK3) , P06493 (CDK1)
R2059 Methylation
K2086 Acetylation
K2091 Acetylation
R2142 Methylation
Y2219 Phosphorylation
R2226 Methylation
S2279 Phosphorylation P28482 (MAPK1)
S2309 Phosphorylation
S2315 Phosphorylation P28482 (MAPK1)
R2317 Methylation
S2320 Phosphorylation
S2325 Phosphorylation
S2326 Phosphorylation
S2328 Phosphorylation
R2330 Methylation
S2366 Phosphorylation P28482 (MAPK1)

PTMs - Q09472 As Enzyme

Substrate Site Source
Q09472 (EP300) K1499 Uniprot
Q09472 (EP300) K1549 Uniprot
Q09472 (EP300) K1554 Uniprot
Q09472 (EP300) K1560 Uniprot

Research Backgrounds

Function:

Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. Mediates acetylation of histone H3 at 'Lys-122' (H3K122ac), a modification that localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability. Mediates acetylation of histone H3 at 'Lys-27' (H3K27ac). Also functions as acetyltransferase for non-histone targets, such as ALX1, HDAC1, PRMT1 or SIRT2. Acetylates 'Lys-131' of ALX1 and acts as its coactivator. Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function. Acetylates HDAC1 leading to its inactivation and modulation of transcription. Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2. Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium. Promotes cardiac myocyte enlargement. Can also mediate transcriptional repression. Acetylates FOXO1 and enhances its transcriptional activity. 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. Acetylates XBP1 isoform 2; acetylation increases protein stability of XBP1 isoform 2 and enhances its transcriptional activity. Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER). Acetylates MEF2D. Acetylates and stabilizes ZBTB7B protein by antagonizing ubiquitin conjugation and degragation, this mechanism may be involved in CD4/CD8 lineage differentiation. Acetylates GABPB1, impairing GABPB1 heterotetramerization and activity (By similarity). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA), butanoyl-CoA (butyryl-CoA), 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA) or propanoyl-CoA (propionyl-CoA), and is able to mediate protein crotonylation, butyrylation, 2-hydroxyisobutyrylation or propionylation, respectively. Acts as a histone crotonyltransferase; crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. Histone crotonyltransferase activity is dependent on the concentration of (2E)-butenoyl-CoA (crotonyl-CoA) substrate and such activity is weak when (2E)-butenoyl-CoA (crotonyl-CoA) concentration is low. Also acts as a histone butyryltransferase; butyrylation marks active promoters. Acts as a protein-lysine 2-hydroxyisobutyryltransferase; regulates glycolysis by mediating 2-hydroxyisobutyrylation of glycolytic enzymes. Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway. Acetylates PCK1 and promotes PCK1 anaplerotic activity. Acetylates RXRA and RXRG.

(Microbial infection) 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. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein.

PTMs:

Acetylated on Lys at up to 17 positions by intermolecular autocatalysis. Deacetylated in the transcriptional repression domain (CRD1) by SIRT1, preferentially at Lys-1020. Deacetylated by SIRT2, preferentially at Lys-418, Lys-423, Lys-1542, Lys-1546, Lys-1549, Lys-1699, Lys-1704 and Lys-1707.

Citrullinated at Arg-2142 by PADI4, which impairs methylation by CARM1 and promotes interaction with NCOA2/GRIP1.

Methylated at Arg-580 and Arg-604 in the KIX domain by CARM1, which blocks association with CREB, inhibits CREB signaling and activates apoptotic response. Also methylated at Arg-2142 by CARM1, which impairs interaction with NCOA2/GRIP1.

Sumoylated; sumoylation in the transcriptional repression domain (CRD1) mediates transcriptional repression. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3.

Probable target of ubiquitination by FBXO3, leading to rapid proteasome-dependent degradation.

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. Phosphorylation at Ser-89 by AMPK reduces interaction with nuclear receptors, such as PPARG.

Subcellular Location:

Cytoplasm. Nucleus. Chromosome.
Note: Localizes to active chromatin: Colocalizes with histone H3 acetylated and/or crotonylated at 'Lys-18' (H3K18ac and H3K18cr, respectively) (PubMed:25818647). In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. Colocalizes with ROCK2 in the nucleus (PubMed:12929931).

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Interacts with phosphorylated CREB1. Interacts with HIF1A; the interaction is stimulated in response to hypoxia and inhibited by CITED2. Interacts (via N-terminus) with TFAP2A (via N-terminus); the interaction requires CITED2. Interacts (via CH1 domain) with CITED2 (via C-terminus). Interacts with CITED1 (unphosphorylated form preferentially and via C-terminus). Interacts with ESR1; the interaction is estrogen-dependent and enhanced by CITED1. Interacts with 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 (via CREB-binding domain) with MYOCD (via C-terminus). Binds to HIPK2. Interacts with ROCK2 and PPARG. Forms a complex made of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that stimulates hypertrophy in cardiomyocytes. 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 p30II. Interacts with NPAS2, ARNTL/BMAL1 and CLOCK. Interacts with SIRT2 isoform 1, isoform 2 and isoform 5. Interacts with MTA1. Interacts with HDAC4 and HDAC5 in the presence of TFAP2C. Interacts with TRIP4. Directly interacts with ZBTB49; this interaction leads to synergistic transactivation of CDKN1A. Interacts with NR4A3 (By similarity). Interacts with ZNF451. Interacts with ATF5; EP300 is required for ATF5 and CEBPB interaction and DNA binding (By similarity). Interacts with HSF1. Interacts with ZBTB48/TZAP. Interacts with STAT1; the interaction is enhanced upon IFN-gamma stimulation. Interacts with HNRNPU (via C-terminus); this interaction enhances DNA-binding of HNRNPU to nuclear scaffold/matrix attachment region (S/MAR) elements. Interacts with BCL11B. Interacts with SMAD4; negatively regulated by ZBTB7A. Interacts with DUX4 (via C-terminus). Interacts with NUPR1; this interaction enhances the effect of EP300 on PAX2 transcription factor activity. Interacts with RXRA; the interaction is decreased by 9-cis retinoic acid. NR4A1 competes with EP300 for interaction with RXRA and thereby attenuates EP300 mediated acetylation of RXRA. Interacts with RB1 (By similarity). Interacts with DDX3X; this interaction may facilitate HNF4A acetylation.

(Microbial infection) Interacts with human adenovirus 5 E1A protein; this interaction stimulates the acetylation of RB1 by recruiting EP300 and RB1 into a multimeric-protein complex.

(Microbial infection) Interacts with and acetylates HIV-1 Tat.

(Microbial infection) Interacts with HTLV-1 proteins Tax, p30II and HBZ.

Family&Domains:

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.

Research Fields

· Cellular Processes > Cell growth and death > Cell cycle.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Adherens junction.   (View pathway)

· Environmental Information Processing > Signal transduction > cAMP signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > HIF-1 signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > FoxO signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Wnt signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Notch signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > TGF-beta signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Jak-STAT signaling pathway.   (View pathway)

· Human Diseases > Neurodegenerative diseases > Huntington's disease.

· Human Diseases > Infectious diseases: Bacterial > Tuberculosis.

· Human Diseases > Infectious diseases: Viral > Hepatitis B.

· Human Diseases > Infectious diseases: Viral > Influenza A.

· Human Diseases > Infectious diseases: Viral > Human papillomavirus infection.

· Human Diseases > Infectious diseases: Viral > HTLV-I infection.

· Human Diseases > Infectious diseases: Viral > Herpes simplex infection.

· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.

· Human Diseases > Cancers: Overview > Pathways in cancer.   (View pathway)

· Human Diseases > Cancers: Overview > Viral carcinogenesis.

· Human Diseases > Cancers: Overview > MicroRNAs in cancer.

· Human Diseases > Cancers: Specific types > Renal cell carcinoma.   (View pathway)

· Human Diseases > Cancers: Specific types > Prostate cancer.   (View pathway)

· Organismal Systems > Nervous system > Long-term potentiation.

· Organismal Systems > Endocrine system > Melanogenesis.

· Organismal Systems > Endocrine system > Thyroid hormone signaling pathway.   (View pathway)

· Organismal Systems > Endocrine system > Glucagon signaling pathway.

References

1). Han J et al. YY1 complex promotes Quaking expression via super-enhancer binding during EMT of hepatocellular carcinoma. CANCER RESEARCH 2019 Feb 13 (PubMed: 30760518) [IF=11.2]

Application: WB    Species: human    Sample: PLC-PRF-5 cells

Fig. 7 |Hyperoside inhibits the EMT and metastasis of HCC by targeting YY1 complex.(a) Detailed binding mode of YY1, p65, and p300. (b) Prediction score of docking between small-molecule drugs and YY1 complex. (c) The structure of hyperoside (left). Predicted binding modes of hyperoside (green) and YY1/p65/p300 complex (right). (d) Co-IP of endogenous YY1, p65, and p300 was performed in PLC-PRF-5 cells treated with 120 µM hyperoside.

2). Jin Z et al. The mechanism of SP1/p300 complex promotes proliferation of multiple myeloma cells through regulating IQGAP1 transcription. BIOMEDICINE & PHARMACOTHERAPY 2019 Sep 16;119:109434 (PubMed: 31536933) [IF=7.5]

Application: WB    Species: human    Sample: myeloma cell

Fig. 2.| A. The mRNA expression level of IQGAP1 in myeloma cell lines among different group (Sp1-siRNA: p<0.0001; p300-siRNA: p = 0.0003;pcDNA3.1-Sp1: p<0.0001; pcDNA3.1- p300: p<0.0001). B. The mRNA expression level of Sp1 in myeloma cell lines among different group (Sp1-siRNA: p = 0.0014; pcDNA3.1-Sp1:p = 0.0001; pcDNA3.1- p300: p = 0.0006). C. The mRNA expression level of p300 in myeloma cell lines among different group (p300-siRNA: p = 0.0012; pcDNA3.1-Sp1: p = 0.0003; pcDNA3.1- p300: p = 0.0002). D. The protein level of Sp1, p300, IQGAP1, ERK1/2 and p-ERK1/2 in myeloma cell lines among different group.

3). Li JF et al. Regulation of P300 and HDAC1 on endoplasmic reticulum stress in isoniazid-induced HL-7702 hepatocyte injury. JOURNAL OF CELLULAR PHYSIOLOGY 2019 Feb 20 (PubMed: 30786008) [IF=5.6]

Application: WB    Species: human    Sample: ADLI cell

FIGURE 5| Altered P300 and HDAC1 affect ERS in cells in ADLI. (a) The mRNA content of P300, HDAC1, GRP78, and CHOP in different groups after treatment with C646 and MS‐275 for 6 hr. (b) Western blot analysis and (c) gray value detection of P300, HDAC1, GRP78, and CHOP in different groups. Means ± SEM were calculated from six independent experiments. A one‐way ANOVA with SNK‐q test was performed.*p < 0.05 compared with the levels in the control group.

4). Wu J et al. β-Patchoulene Ameliorates Water Transport and the Mucus Barrier in 5-Fluorouracil-Induced Intestinal Mucositis Rats via the cAMP/PKA/CREB Signaling Pathway. Frontiers in Pharmacology 2021 Aug 25;12:689491. (PubMed: 34512326) [IF=5.6]

Application: WB    Species: Rat    Sample:

FIGURE 5 Effects of β-PAE on AQP3 expression and cAMP/PKA/CREB signaling pathway-related proteins. (A,B) AQP3 expression; (C,D) VIP, VIPR2, cAMP and PKA expression; (E,F) MEK1/2, p-MEK1/2, ERK, p-ERK, p-p38, p38, MSK1, p-MSK1, CREB, p-CREB, and P300/CBP expression. Data are shown as mean ± SD (n = 3). # p < 0.05, ## p < 0.01 versus control group; * p < 0.05, ** p < 0.01 versus 5-FU group.

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