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  • Product Name
    Phospho-p53 (Ser366) Antibody
  • Catalog No.
    AF3078
  • RRID
    AB_2834515
  • Source
    Rabbit
  • Application
    WB,IHC,IF/ICC,ELISA
  • Reactivity
    Human, Mouse
  • Prediction
    Pig(83%), Bovine(92%), Sheep(92%), Rabbit(85%), Dog(92%)
  • UniProt
  • Mol.Wt
    (Observed)48kD; (Calculated)44kDa
  • Concentration
    1mg/ml
  • Browse similar products>>

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Product Information

Alternative Names:Expand▼

Antigen NY-CO-13; BCC7; Cellular tumor antigen p53; FLJ92943; LFS1; Mutant tumor protein 53; p53; p53 tumor suppressor; P53_HUMAN; Phosphoprotein p53; Tp53; Transformation related protein 53; TRP53; Tumor protein 53; Tumor protein p53; Tumor suppressor p53;

Applications:

WB 1:500-1:2000, IHC 1:50-1:1000, IF/ICC 1:100-1:500, ELISA(peptide) 1:20000-1:40000

Reactivity:

Human, Mouse

Predicted Reactivity:

Pig(83%), Bovine(92%), Sheep(92%), Rabbit(85%), Dog(92%)

Source:

Rabbit

Clonality:

Polyclonal

Purification:

The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.

Specificity:

Phospho-p53 (Ser366) Antibody detects endogenous levels of p53 only when phosphorylated at Serine 366.

RRID:

AB_2834515
Please cite this product as: Affinity Biosciences Cat# AF3078, RRID:AB_2834515.

Format:

Liquid

Concentration:

1mg/ml

Storage Condition and Buffer:

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.

Immunogen Information

Immunogen:

A synthesized peptide derived from human p53 around the phosphorylation site of Ser366.

Uniprot:



>>Visit The Human Protein Atlas

Gene ID:

Gene Name:

TP53

Molecular Weight:

Observed Mol.Wt.: (Observed)48kD.
Predicted Mol.Wt.: (Calculated)44kDa.

Subcellular Location:

Cytoplasm; Cytoplasm. Nucleus. Nucleus > PML body. Endoplasmic reticulum. Interaction with BANP promotes nuclear localization. Recruited into PML bodies together with CHEK2; Nucleus. Cytoplasm. Localized in both nucleus and cytoplasm in most cells. In some cells, forms foci in the nucleus that are different from nucleoli; Nucleus. Cytoplasm. Localized in the nucleus in most cells but found in the cytoplasm in some cells; Nucleus. Cytoplasm. Localized mainly in the nucleus with minor staining in the cytoplasm; Nucleus. Cytoplasm. Predominantly nuclear but localizes to the cytoplasm when expressed with isoform 4 and Nucleus. Cytoplasm. Predominantly nuclear but translocates to the cytoplasm following cell stress.

Tissue Specificity:

P04637 P53_HUMAN:
Ubiquitous. Isoforms are expressed in a wide range of normal tissues but in a tissue-dependent manner. Isoform 2 is expressed in most normal tissues but is not detected in brain, lung, prostate, muscle, fetal brain, spinal cord and fetal liver. Isoform 3 is expressed in most normal tissues but is not detected in lung, spleen, testis, fetal brain, spinal cord and fetal liver. Isoform 7 is expressed in most normal tissues but is not detected in prostate, uterus, skeletal muscle and breast. Isoform 8 is detected only in colon, bone marrow, testis, fetal brain and intestine. Isoform 9 is expressed in most normal tissues but is not detected in brain, heart, lung, fetal liver, salivary gland, breast or intestine.

Description:

Tumor protein p53, a nuclear protein, plays an essential role in the regulation of cell cycle, specifically in the transition from G0 to G1. It is found in very low levels in normal cells, however, in a variety of transformed cell lines, it is expressed in high amounts, and believed to contribute to transformation and malignancy.

Sequence:
MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD

Research Background

Function:

Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (PubMed:12524540). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (PubMed:12524540). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Implicated in Notch signaling cross-over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis. Regulates the circadian clock by repressing CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER2 (PubMed:24051492).

Post-translational Modifications:

Acetylated. Acetylation of Lys-382 by CREBBP enhances transcriptional activity. Deacetylation of Lys-382 by SIRT1 impairs its ability to induce proapoptotic program and modulate cell senescence. Deacetylation by SIRT2 impairs its ability to induce transcription activation in a AKT-dependent manner.

Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylated by HIPK1 (By similarity). Phosphorylation at Ser-9 by HIPK4 increases repression activity on BIRC5 promoter. Phosphorylated on Thr-18 by VRK1. Phosphorylated on Ser-20 by CHEK2 in response to DNA damage, which prevents ubiquitination by MDM2. Phosphorylated on Ser-20 by PLK3 in response to reactive oxygen species (ROS), promoting p53/TP53-mediated apoptosis. Phosphorylated on Thr-55 by TAF1, which promotes MDM2-mediated degradation. Phosphorylated on Ser-33 by CDK7 in a CAK complex in response to DNA damage. Phosphorylated on Ser-46 by HIPK2 upon UV irradiation. Phosphorylation on Ser-46 is required for acetylation by CREBBP. Phosphorylated on Ser-392 following UV but not gamma irradiation. Phosphorylated on Ser-15 upon ultraviolet irradiation; which is enhanced by interaction with BANP. Phosphorylated by NUAK1 at Ser-15 and Ser-392; was initially thought to be mediated by STK11/LKB1 but it was later shown that it is indirect and that STK11/LKB1-dependent phosphorylation is probably mediated by downstream NUAK1 (PubMed:21317932). It is unclear whether AMP directly mediates phosphorylation at Ser-15. Phosphorylated on Thr-18 by isoform 1 and isoform 2 of VRK2. Phosphorylation on Thr-18 by isoform 2 of VRK2 results in a reduction in ubiquitination by MDM2 and an increase in acetylation by EP300. Stabilized by CDK5-mediated phosphorylation in response to genotoxic and oxidative stresses at Ser-15, Ser-33 and Ser-46, leading to accumulation of p53/TP53, particularly in the nucleus, thus inducing the transactivation of p53/TP53 target genes. Phosphorylated by DYRK2 at Ser-46 in response to genotoxic stress. Phosphorylated at Ser-315 and Ser-392 by CDK2 in response to DNA-damage. Phosphorylation at Ser-15 is required for interaction with DDX3X and gamma-tubulin (PubMed:28842590).

Dephosphorylated by PP2A-PPP2R5C holoenzyme at Thr-55. SV40 small T antigen inhibits the dephosphorylation by the AC form of PP2A.

May be O-glycosylated in the C-terminal basic region. Studied in EB-1 cell line.

Ubiquitinated by MDM2 and SYVN1, which leads to proteasomal degradation (PubMed:10722742, PubMed:12810724, PubMed:15340061, PubMed:17170702, PubMed:19880522). Ubiquitinated by RFWD3, which works in cooperation with MDM2 and may catalyze the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome (PubMed:10722742, PubMed:12810724, PubMed:20173098). Ubiquitinated by MKRN1 at Lys-291 and Lys-292, which leads to proteasomal degradation (PubMed:19536131). Deubiquitinated by USP10, leading to its stabilization (PubMed:20096447). Ubiquitinated by TRIM24, RFFL, RNF34 and RNF125, which leads to proteasomal degradation (PubMed:19556538). Ubiquitination by TOPORS induces degradation (PubMed:19473992). Deubiquitination by USP7, leading to stabilization (PubMed:15053880). Isoform 4 is monoubiquitinated in an MDM2-independent manner (PubMed:15340061). Ubiquitinated by COP1, which leads to proteasomal degradation (PubMed:19837670). Ubiquitination and subsequent proteasomal degradation is negatively regulated by CCAR2 (PubMed:25732823). Polyubiquitinated by C10orf90/FATS, polyubiquitination is 'Lys-48'-linkage independent and non-proteolytic, leading to TP53 stabilization (By similarity).

Monomethylated at Lys-372 by SETD7, leading to stabilization and increased transcriptional activation (PubMed:15525938, PubMed:16415881). Monomethylated at Lys-370 by SMYD2, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity (PubMed:17108971). Lys-372 monomethylation prevents interaction with SMYD2 and subsequent monomethylation at Lys-370 (PubMed:17108971). Dimethylated at Lys-373 by EHMT1 and EHMT2 (PubMed:20118233). Monomethylated at Lys-382 by KMT5A, promoting interaction with L3MBTL1 and leading to repress transcriptional activity (PubMed:17707234). Dimethylation at Lys-370 and Lys-382 diminishes p53 ubiquitination, through stabilizing association with the methyl reader PHF20 (PubMed:22864287). Demethylation of dimethylated Lys-370 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation (PubMed:17805299). Monomethylated at Arg-333 and dimethylated at Arg-335 and Arg-337 by PRMT5; methylation is increased after DNA damage and might possibly affect TP53 target gene specificity (PubMed:19011621).

Sumoylated with SUMO1. Sumoylated at Lys-386 by UBC9.

Subcellular Location:

Cytoplasm. Nucleus. Nucleus>PML body. Endoplasmic reticulum. Mitochondrion matrix. Cytoplasm>Cytoskeleton>Microtubule organizing center>Centrosome.
Note: Interaction with BANP promotes nuclear localization (PubMed:15701641). Recruited into PML bodies together with CHEK2 (PubMed:12810724). Translocates to mitochondria upon oxidative stress (PubMed:22726440). Translocates to mitochondria in response to mitomycin C treatment (PubMed:27323408).

Nucleus. Cytoplasm.
Note: Predominantly nuclear but localizes to the cytoplasm when expressed with isoform 4.

Nucleus. Cytoplasm.
Note: Localized mainly in the nucleus with minor staining in the cytoplasm.

Nucleus. Cytoplasm.
Note: Localized in the nucleus in most cells but found in the cytoplasm in some cells.

Nucleus. Cytoplasm.
Note: Predominantly nuclear but translocates to the cytoplasm following cell stress.

Nucleus. Cytoplasm.
Note: Localized mainly in the nucleus with minor staining in the cytoplasm.

Nucleus. Cytoplasm.
Note: Localized in both nucleus and cytoplasm in most cells. In some cells, forms foci in the nucleus that are different from nucleoli.

Cytoplasm.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte

Tissue Specificity:

Ubiquitous. Isoforms are expressed in a wide range of normal tissues but in a tissue-dependent manner. Isoform 2 is expressed in most normal tissues but is not detected in brain, lung, prostate, muscle, fetal brain, spinal cord and fetal liver. Isoform 3 is expressed in most normal tissues but is not detected in lung, spleen, testis, fetal brain, spinal cord and fetal liver. Isoform 7 is expressed in most normal tissues but is not detected in prostate, uterus, skeletal muscle and breast. Isoform 8 is detected only in colon, bone marrow, testis, fetal brain and intestine. Isoform 9 is expressed in most normal tissues but is not detected in brain, heart, lung, fetal liver, salivary gland, breast or intestine.

Subunit Structure:

Forms homodimers and homotetramers (PubMed:19011621). Binds DNA as a homotetramer. Interacts with AXIN1. Probably part of a complex consisting of TP53, HIPK2 and AXIN1 (By similarity). Interacts with histone acetyltransferases EP300 and methyltransferases HRMT1L2 and CARM1, and recruits them to promoters. Interacts (via C-terminus) with TAF1; when TAF1 is part of the TFIID complex. Interacts with ING4; this interaction may be indirect. Found in a complex with CABLES1 and TP73. Interacts with HIPK1, HIPK2, and TP53INP1. Interacts with WWOX. May interact with HCV core protein. Interacts with USP7 and SYVN1. Interacts with HSP90AB1. Interacts with CHD8; leading to recruit histone H1 and prevent transactivation activity (By similarity). Interacts with ARMC10, BANP, CDKN2AIP, NUAK1, STK11/LKB1, UHRF2 and E4F1. Interacts with YWHAZ; the interaction enhances TP53 transcriptional activity. Phosphorylation of YWHAZ on 'Ser-58' inhibits this interaction. Interacts (via DNA-binding domain) with MAML1 (via N-terminus). Interacts with MKRN1. Interacts with PML (via C-terminus). Interacts with MDM2; leading to ubiquitination and proteasomal degradation of TP53. Directly interacts with FBXO42; leading to ubiquitination and degradation of TP53. Interacts (phosphorylated at Ser-15 by ATM) with the phosphatase PP2A-PPP2R5C holoenzyme; regulates stress-induced TP53-dependent inhibition of cell proliferation. Interacts with PPP2R2A. Interacts with AURKA, DAXX, BRD7 and TRIM24. Interacts (when monomethylated at Lys-382) with L3MBTL1. Isoform 1 interacts with isoform 2 and with isoform 4. Interacts with GRK5. Binds to the CAK complex (CDK7, cyclin H and MAT1) in response to DNA damage. Interacts with CDK5 in neurons. Interacts with AURKB, SETD2, UHRF2 and NOC2L. Interacts (via N-terminus) with PTK2/FAK1; this promotes ubiquitination by MDM2. Interacts with PTK2B/PYK2; this promotes ubiquitination by MDM2. Interacts with PRKCG. Interacts with PPIF; the association implicates preferentially tetrameric TP53, is induced by oxidative stress and is impaired by cyclosporin A (CsA). Interacts with SNAI1; the interaction induces SNAI1 degradation via MDM2-mediated ubiquitination and inhibits SNAI1-induced cell invasion. Interacts with KAT6A. Interacts with UBC9. Interacts with ZNF385B; the interaction is direct. Interacts (via DNA-binding domain) with ZNF385A; the interaction is direct and enhances p53/TP53 transactivation functions on cell-cycle arrest target genes, resulting in growth arrest. Interacts with ANKRD2. Interacts with RFFL and RNF34; involved in p53/TP53 ubiquitination. Interacts with MTA1 and COP1. Interacts with CCAR2 (via N-terminus). Interacts with MORC3 (PubMed:17332504). Interacts (via C-terminus) with POU4F2 isoform 1 (via C-terminus) (PubMed:17145718). Interacts (via oligomerization region) with NOP53; the interaction is direct and may prevent the MDM2-mediated proteasomal degradation of TP53 (PubMed:22522597). Interacts with AFG1L; mediates mitochondrial translocation of TP53 (PubMed:27323408). Interacts with UBD (PubMed:25422469). Interacts with TAF6 isoform 1 and isoform 4 (PubMed:20096117). Interacts with C10orf90/FATS; the interaction inhibits binding of TP53 and MDM2 (By similarity). Interacts with NUPR1; interaction is stress-dependent (PubMed:18690848). Forms a complex with EP300 and NUPR1; this complex binds CDKN1A promoter leading to transcriptional induction of CDKN1A (PubMed:18690848). Interacts with PRMT5 in response to DNA damage; the interaction is STRAP dependent (PubMed:19011621). Interacts with PPP1R13L (via SH3 domain and ANK repeats); the interaction inhibits pro-apoptotic activity of p53/TP53 (PubMed:12524540). Interacts with PPP1R13B/ASPP1 and TP53BP2/ASPP2; the interactions promotes pro-apototic activity (PubMed:12524540). When phosphorylated at Ser-15, interacts with DDX3X and gamma-tubulin (PubMed:28842590).

(Microbial infection) Interacts with cancer-associated/HPV E6 viral proteins leading to ubiquitination and degradation of TP53 giving a possible model for cell growth regulation. This complex formation requires an additional factor, E6-AP, which stably associates with TP53 in the presence of E6.

(Microbial infection) Interacts with human cytomegalovirus/HHV-5 protein UL123.

(Microbial infection) Interacts (via N-terminus) with human adenovirus 5 E1B-55K protein; this interaction leads to the inhibition of TP53 function and/or its degradation.

Similarity:

The nuclear export signal acts as a transcriptional repression domain. The TADI and TADII motifs (residues 17 to 25 and 48 to 56) correspond both to 9aaTAD motifs which are transactivation domains present in a large number of yeast and animal transcription factors.

Belongs to the p53 family.

Research Fields

Research Fields:

· Cellular Processes > Cell growth and death > Cell cycle.(View pathway)
· Cellular Processes > Cell growth and death > Ferroptosis.(View pathway)
· Cellular Processes > Cell growth and death > p53 signaling pathway.(View pathway)
· Cellular Processes > Cell growth and death > Apoptosis.(View pathway)
· Cellular Processes > Cell growth and death > Cellular senescence.(View pathway)
· Environmental Information Processing > Signal transduction > MAPK signaling pathway.(View pathway)
· Environmental Information Processing > Signal transduction > Wnt signaling pathway.(View pathway)
· Environmental Information Processing > Signal transduction > Sphingolipid signaling pathway.(View pathway)
· Environmental Information Processing > Signal transduction > PI3K-Akt signaling pathway.(View pathway)
· Human Diseases > Cancers: Specific types > Pancreatic cancer.(View pathway)
· Human Diseases > Cancers: Specific types > Basal cell carcinoma.(View pathway)
· Human Diseases > Cancers: Specific types > Thyroid cancer.(View pathway)
· Human Diseases > Cancers: Specific types > Bladder cancer.(View pathway)
· Human Diseases > Cancers: Overview > Pathways in cancer.(View pathway)
· Human Diseases > Cancers: Specific types > Gastric cancer.(View pathway)
· Human Diseases > Cancers: Specific types > Non-small cell lung cancer.(View pathway)
· Human Diseases > Cancers: Specific types > Glioma.(View pathway)
· Human Diseases > Cancers: Specific types > Colorectal cancer.(View pathway)
· Human Diseases > Cancers: Overview > Proteoglycans in cancer.
· Human Diseases > Cancers: Specific types > Hepatocellular carcinoma.(View pathway)
· Human Diseases > Cancers: Overview > MicroRNAs in cancer.
· Human Diseases > Cancers: Specific types > Endometrial cancer.(View pathway)
· Human Diseases > Cancers: Specific types > Breast cancer.(View pathway)
· Human Diseases > Cancers: Specific types > Chronic myeloid leukemia.(View pathway)
· Human Diseases > Cancers: Specific types > Small cell lung cancer.(View pathway)
· Human Diseases > Neurodegenerative diseases > Amyotrophic lateral sclerosis (ALS).
· Human Diseases > Cancers: Overview > Central carbon metabolism in cancer.(View pathway)
· Human Diseases > Infectious diseases: Viral > Herpes simplex infection.
· Human Diseases > Infectious diseases: Viral > Hepatitis C.
· Human Diseases > Cancers: Overview > Viral carcinogenesis.
· Human Diseases > Infectious diseases: Viral > Measles.
· Human Diseases > Infectious diseases: Viral > Hepatitis B.
· Human Diseases > Cancers: Specific types > Melanoma.(View pathway)
· Human Diseases > Infectious diseases: Viral > Human papillomavirus infection.
· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.
· Human Diseases > Drug resistance: Antineoplastic > Platinum drug resistance.
· Human Diseases > Neurodegenerative diseases > Huntington's disease.
· Human Diseases > Infectious diseases: Viral > HTLV-I infection.
· Human Diseases > Cancers: Overview > Transcriptional misregulation in cancer.
· Human Diseases > Drug resistance: Antineoplastic > Endocrine resistance.
· Human Diseases > Cancers: Specific types > Prostate cancer.(View pathway)
· Organismal Systems > Endocrine system > Thyroid hormone signaling pathway.(View pathway)
· Organismal Systems > Nervous system > Neurotrophin signaling pathway.(View pathway)
· Organismal Systems > Aging > Longevity regulating pathway.(View pathway)

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Catalog Number :

AF3078-BP
(Blocking peptide available as AF3078-BP)

Price/Size :

$350/1mg.
Tips: For phospho antibody, we provide phospho peptide(0.5mg) and non-phospho peptide(0.5mg).

Function :

Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. This mechanism is useful when non-specific binding is an issue, for example, in Western blotting (immunoblot) and immunohistochemistry (IHC). By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific; Specific binding will be absent from the western blot or immunostaining performed with the neutralized antibody.

Format and storage :

Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 10 mg/ml.The purity is >90%,tested by HPLC and MS.Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.

Precautions :

This product is for research use only. Not for use in diagnostic or therapeutic procedures.

Sheep
92%
Bovine
92%
Dog
92%
Rabbit
85%
Pig
83%
Xenopus
55%
Horse
0%
Chicken
0%
Zebrafish
0%
High similarity Medium similarity Low similarity No similarity
P04637 as Substrate
Site PTM Type Enzyme
Ubiquitination
S6 Phosphorylation P45984 (MAPK9)
S9 Phosphorylation P78527 (PRKDC) , Q13315 (ATM) , P48730 (CSNK1D)
S15 Phosphorylation Q16539 (MAPK14) , O60285 (NUAK1) , Q15831 (STK11) , Q13315 (ATM) , P78527 (PRKDC) , Q05655 (PRKCD) , Q13464 (ROCK1) , P57059 (SIK1) , Q96Q15 (SMG1) , P27361 (MAPK3) , P28482 (MAPK1) , Q14680 (MELK) , O14757 (CHEK1) , O96017 (CHEK2) , Q96S44 (TP53RK) , Q13535 (ATR) , Q00535 (CDK5) , Q13131 (PRKAA1) , P51812 (RPS6KA3) , Q13627 (DYRK1A)
T18 Phosphorylation P53355 (DAPK1) , P48730 (CSNK1D) , Q99986 (VRK1) , O96017 (CHEK2) , Q86Y07-2 (VRK2) , P33981 (TTK) , P78527 (PRKDC) , P48729 (CSNK1A1) , Q13131 (PRKAA1) , O14757 (CHEK1)
S20 Phosphorylation P78527 (PRKDC) , Q13131 (PRKAA1) , Q13315 (ATM) , O96017 (CHEK2) , Q9H4B4 (PLK3) , Q9UEE5 (STK17A) , P45983 (MAPK8) , P48729 (CSNK1A1) , P49137 (MAPKAPK2) , Q00535 (CDK5) , O14757 (CHEK1) , O43293 (DAPK3) , P53355 (DAPK1) , P48730 (CSNK1D) , Q683Z8 (CHK2) , P45984 (MAPK9)
K24 Ubiquitination
S33 Phosphorylation P50750 (CDK9) , O15264 (MAPK13) , Q00535 (CDK5) , P50613 (CDK7) , Q16539 (MAPK14) , P49841 (GSK3B) , P45985 (MAP2K4)
S37 Phosphorylation O96017 (CHEK2) , Q8IW41 (MAPKAPK5) , O14757 (CHEK1) , P78527 (PRKDC) , Q13535 (ATR) , P53779 (MAPK10) , P45984 (MAPK9) , P45983 (MAPK8)
S46 Phosphorylation Q92630 (DYRK2) , Q00535 (CDK5) , Q13315 (ATM) , Q05655 (PRKCD) , Q16539 (MAPK14) , P78527 (PRKDC) , Q9H2X6 (HIPK2) , O15264 (MAPK13)
T55 Phosphorylation P28482 (MAPK1) , P21675 (TAF1) , P34947 (GRK5)
T81 Phosphorylation P45984 (MAPK9) , P45983 (MAPK8)
S99 Phosphorylation
K101 Ubiquitination
S106 Phosphorylation O14965 (AURKA)
R110 Methylation
H115 Methylation
K120 Acetylation
K120 Ubiquitination
C124 S-Nitrosylation
Y126 Phosphorylation
K132 Ubiquitination
K139 Ubiquitination
C141 S-Nitrosylation
S149 O-Glycosylation
S149 Phosphorylation P68400 (CSNK2A1)
T150 Phosphorylation P68400 (CSNK2A1)
T155 Phosphorylation P68400 (CSNK2A1)
K164 Acetylation
K164 Ubiquitination
S166 Phosphorylation
C182 S-Nitrosylation
S183 Phosphorylation Q96GD4 (AURKB)
R209 Methylation
T211 Phosphorylation Q96GD4 (AURKB)
R213 Methylation
S215 Phosphorylation O14965 (AURKA) , Q96GD4 (AURKB) , O96013 (PAK4)
Y220 Phosphorylation
R249 Phosphorylation
S260 Phosphorylation
S269 Phosphorylation P53355 (DAPK1) , Q96GD4 (AURKB)
T284 Phosphorylation Q96GD4 (AURKB)
R290 Methylation
K291 Ubiquitination
K292 Acetylation
K292 Ubiquitination
T304 Phosphorylation Q5S007 (LRRK2)
K305 Acetylation
K305 Ubiquitination
T312 Phosphorylation
S313 Phosphorylation P24941 (CDK2)
S314 Phosphorylation P24941 (CDK2)
S315 Phosphorylation P24941 (CDK2) , P06493 (CDK1) , O14965 (AURKA) , P50750 (CDK9)
K319 Acetylation
K319 Ubiquitination
K320 Acetylation
K320 Ubiquitination
K321 Ubiquitination
Y327 Phosphorylation
R333 Methylation
R335 Methylation
R337 Methylation
K351 Ubiquitination
K357 Ubiquitination
S362 Phosphorylation O14920 (IKBKB)
S366 Phosphorylation O14757 (CHEK1) , O14920 (IKBKB) , O96017 (CHEK2)
K370 Acetylation
K370 Methylation
K370 Ubiquitination
S371 Phosphorylation P17252 (PRKCA) , P50613 (CDK7)
K372 Acetylation
K372 Methylation
K372 Ubiquitination
K373 Acetylation
K373 Methylation
K373 Ubiquitination
S376 Phosphorylation P50613 (CDK7) , P17252 (PRKCA) , P49841 (GSK3B)
T377 Phosphorylation P17252 (PRKCA) , Q5S007 (LRRK2)
S378 Phosphorylation O96017 (CHEK2) , P50613 (CDK7) , P17612 (PRKACA) , P17252 (PRKCA) , O14757 (CHEK1)
K381 Acetylation
K381 Ubiquitination
K382 Acetylation
K382 Methylation
K382 Ubiquitination
K386 Acetylation
K386 Methylation
K386 Sumoylation
K386 Ubiquitination
T387 Phosphorylation O14757 (CHEK1)
S392 Phosphorylation P19525 (EIF2AK2) , O60285 (NUAK1) , P23443 (RPS6KB1) , Q15831 (STK11) , P50750 (CDK9) , P27361 (MAPK3) , P50613 (CDK7) , P68400 (CSNK2A1)
IMPORTANT: For western blots, incubate membrane with diluted antibody in 5% w/v milk , 1X TBS, 0.1% Tween®20 at 4°C with gentle shaking, overnight.

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