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Protein Page:
p53 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
p53 a transcription factor and major tumor suppressor that plays a major role in regulating cellular responses to DNA damage and other genomic aberrations. Activation of p53 can lead to either cell cycle arrest and DNA repair or apoptosis. More than 50 percent of human tumors contain a mutation or deletion of the TP53 gene. p53 is modified post-translationally at multiple sites. DNA damage induces phosphorylation of p53 at S15, S20 and S37, reducing its interaction with the oncoprotein MDM2. MDM2 inhibits p53 accumulation by targeting it for ubiquitination and proteasomal degradation. Phosphorylated by many kinases including Chk2 and Chk1 at S20, enhancing its tetramerization, stability and activity. The phosphorylation by CAK at S392 is increased in human tumors and has been reported to influence the growth suppressor function, DNA binding and transcriptional activation of p53. Phosphorylation of p53 at S46 regulates the ability of p53 to induce apoptosis. The acetylation of p53 appears to play a positive role in the accumulation of p53 during the stress response. Following DNA damage, p53 becomes acetylated at K382, enhancing its binding to DNA. Deacetylation of p53 can occur through interaction with SIRT1, a deacetylase that may be involved in cellular aging and the DNA damage response. p53 regulates the transcription of a set of genes encoding endosomal proteins that regulate endosomal functions. These include STEAP3 and CHMP4C, which enhance exosome production, and CAV1 and CHMP4C, which produce a more rapid endosomal clearance of the EGFR from the plasma membrane. DNA damage regulates a p53-mediated secretory pathway, increasing the secretion of some proteins such as Hsp90, SERPINE1, SERPINB5, NKEF-A, and CyPA, and inhibiting the secretion of others including CTSL and IGFBP-2. Two alternatively spliced human isoforms have been reported. Isoform 2 is expressed in quiescent lymphocytes. Seems to be non-functional. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Note: This description may include information from UniProtKB.
Protein type: Transcription factor; Motility/polarity/chemotaxis; DNA-binding; Tumor suppressor; Nuclear receptor co-regulator; Activator
Chromosomal Location of Human Ortholog: 17p13.1
Cellular Component: cytoplasm; cytosol; endoplasmic reticulum; mitochondrial matrix; mitochondrion; nuclear body; nuclear chromatin; nuclear matrix; nucleolus; nucleoplasm; nucleus; PML body; protein complex; replication fork; transcription factor TFIID complex
Molecular Function: ATP binding; chaperone binding; chromatin binding; copper ion binding; damaged DNA binding; DNA binding; double-stranded DNA binding; enzyme binding; histone acetyltransferase binding; identical protein binding; p53 binding; protease binding; protein binding; protein heterodimerization activity; protein kinase binding; protein N-terminus binding; protein phosphatase 2A binding; protein phosphatase binding; protein self-association; receptor tyrosine kinase binding; sequence-specific DNA binding; transcription factor activity; transcription factor binding; ubiquitin protein ligase binding; zinc ion binding
Biological Process: base-excision repair; cell aging; cell cycle arrest; cell differentiation; cell proliferation; cellular response to glucose starvation; chromatin assembly; circadian behavior; determination of adult life span; DNA damage response, signal transduction by p53 class mediator; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis; DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; DNA strand renaturation; entrainment of circadian clock by photoperiod; ER overload response; G1 DNA damage checkpoint; multicellular organismal development; negative regulation of apoptosis; negative regulation of cell growth; negative regulation of cell proliferation; negative regulation of fibroblast proliferation; negative regulation of helicase activity; negative regulation of telomerase activity; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; nucleotide-excision repair; positive regulation of apoptosis; positive regulation of histone deacetylation; positive regulation of neuron apoptosis; positive regulation of peptidyl-tyrosine phosphorylation; positive regulation of protein export from nucleus; positive regulation of protein oligomerization; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription, DNA-dependent; proteasomal ubiquitin-dependent protein catabolic process; protein complex assembly; protein localization; protein sumoylation; protein tetramerization; Ras protein signal transduction; regulation of apoptosis; regulation of mitochondrial membrane permeability; regulation of transcription, DNA-dependent; response to antibiotic; response to DNA damage stimulus; response to gamma radiation; response to X-ray; transcription from RNA polymerase II promoter; viral reproduction
Disease: Adrenocortical Carcinoma, Hereditary; Basal Cell Carcinoma, Susceptibility To, 7; Breast Cancer; Colorectal Cancer; Glioma Susceptibility 1; Hepatocellular Carcinoma; Li-fraumeni Syndrome 1; Nasopharyngeal Carcinoma; Osteogenic Sarcoma; Pancreatic Cancer; Papilloma Of Choroid Plexus
Reference #:  P04637 (UniProtKB)
Gene Symbols: TP53
Molecular weight: 43,653 Da
Basal Isoelectric point: 6.33  Predict pI for various phosphorylation states
CST Pathways:  AMPK Signaling  |  Apoptosis Regulation  |  ErbB/HER Signaling  |  G1/S Checkpoint  |  G2/M DNA Damage Checkpoint  |  Mitochondrial Control of Apoptosis  |  PI3K/Akt Signaling  |  Protein Acetylation  |  Regulation of P38 MAPKs  |  SAPK/JNK Signaling Cascades  |  Warburg Effect
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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p53

Protein Structure Not Found.
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Sites Implicated In
apoptosis, altered: S6‑p, S9‑p, S15‑p, T18‑p, S20‑p, S37‑p, S46‑p, T55‑p, S269‑p, T284‑p, S315‑p, S392‑p
apoptosis, induced: S6‑p, S9‑p, S15‑p, S20‑p, S33‑p, S37‑p, S46‑p, T81‑p, K120‑ac, K164‑ac, T304‑p, K370‑ac, K372‑ac, K373‑ac, T377‑p, K381‑ac, K382‑ac, K386‑sm, K386‑ac, S392‑p
apoptosis, inhibited: S183‑p, T211‑p, S215‑p, S315‑p, S376‑p
carcinogenesis, induced: S183‑p, T211‑p, S215‑p
cell cycle regulation: S9‑p, S15‑p, S20‑p, T55‑p, S183‑p, T211‑p, S215‑p, S315‑p, S376‑p, S378‑p, S392‑p
cell growth, altered: S15‑p, S20‑p, S33‑p, S46‑p, S215‑p, S269‑p, S315‑p
cell growth, induced: K372‑ac, K373‑ac, K381‑ac, K382‑ac
cell growth, inhibited: S15‑p, S392‑p
cell motility, altered: S315‑p
chromatin organization, altered: S15‑p, S376‑p, S378‑p
DNA repair, induced: S37‑p, S46‑p
transcription, altered: S6‑p, S9‑p, S15‑p, T18‑p, S20‑p, S33‑p, S37‑p, S46‑p, T55‑p, T81‑p, K120‑ac, K164‑ac, S215‑p, S269‑p, S315‑p, S366‑p, K370‑ac, K372‑ac, K373‑ac, K381‑ac, K382‑ac, K386‑sm, K386‑ac, T387‑p, S392‑p
transcription, induced: S6‑p, S15‑p, S37‑p, S46‑p, T81‑p, K120‑ac, S215‑p, T304‑p, S315‑p, K373‑ac, S376‑p, T377‑p, S378‑p, K382‑ac, K386‑ub
transcription, inhibited: S15‑p, S37‑p, T55‑p, S183‑p, T211‑p, S215‑p, S269‑p, T284‑p, K370‑ub, K372‑ub, K373‑ub, K381‑ub, K382‑ub, K386‑ub
acetylation: S6‑p, S9‑p, S15‑p, T18‑p, S46‑p
activity, induced: S6‑p, S15‑p, S20‑p, S33‑p, S37‑p, S46‑p, T55‑p, S315‑p, S366‑p, S371‑p, S376‑p, S378‑p, K386‑sm, T387‑p, S392‑p
activity, inhibited: S215‑p, S269‑p, S315‑p, S376‑p
intracellular localization: S15‑p, S20‑p, T55‑p, K101‑ub, K120‑ub, K132‑ub, K139‑ub, K164‑ub, S269‑p, T304‑p, S315‑p, K370‑ub, K372‑ub, K373‑ub, S376‑p, T377‑p, S378‑p, K381‑ub, K382‑ub, K386‑ub, S392‑p
molecular association, regulation: S15‑p, T18‑p, S20‑p, S33‑p, S37‑p, S46‑p, T55‑p, T81‑p, S315‑p, S366‑p, S371‑p, K373‑ac, S376‑p, S378‑p, K382‑m2, K382‑ac, T387‑p, S392‑p
phosphorylation: S6‑p, S9‑p, S15‑p, S20‑p, S33‑p, S149‑gl
protein conformation: S15‑p, T18‑p, S20‑p, S37‑p, S215‑p, S269‑p, S315‑p, S392‑p
protein degradation: S15‑p, S20‑p, T55‑p, K101‑ub, K120‑ub, K132‑ub, K139‑ub, T155‑p, K164‑ub, S183‑p, T211‑p, S215‑p, S315‑p, K370‑ub, K372‑ub, K372‑ac, K373‑ac, K373‑ub, S376‑p, K381‑ub, K381‑ac, K382‑ac, K382‑ub, K386‑ub, S392‑p
protein stabilization: S15‑p, T18‑p, S20‑p, S37‑p, T81‑p, S106‑p, S149‑gl, S215‑p, S269‑p, K382‑m2, K382‑ac, S392‑p
ubiquitination: S15‑p, S149‑gl, S183‑p, T211‑p, S215‑p, S269‑p, S315‑p, K372‑ac, K373‑ac, K381‑ac, K382‑ac, S392‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
6 0 P4 ____MEEPQsDPsVE
31 4 S6‑p __MEEPQsDPsVEPP
34 3 S9‑p EEPQsDPsVEPPLsQ
380 4 S15‑p PsVEPPLsQEtFsDL
31 0 T18‑p EPPLsQEtFsDLWKL
115 1 S20‑p PLsQEtFsDLWKLLP
30 3 S33‑p LPENNVLsPLPsQAM
67 3 S37‑p NVLsPLPsQAMDDLM
95 3 S46‑p AMDDLMLsPDDIEQW
18 0 T55‑p DDIEQWFtEDPGPDE
2 0 D61 FtEDPGPDEAPRMPE
8 2 T81‑p APAPAAPtPAAPAPA
0 2 S99‑p PLSSSVPsQkTYQGs
1 2 K101‑ub SSSVPsQkTYQGsYG
1 0 S106‑p sQkTYQGsYGFrLGF
0 1 R110‑m1 YQGsYGFrLGFLhSG
0 1 H115‑m1 GFrLGFLhSGTAkSV
28 1 K120‑ac FLhSGTAkSVTCTyS
1 19 K120‑ub FLhSGTAkSVTCTyS
1 0 Y126‑p AkSVTCTySPALNkM
1 1 K132‑ub TySPALNkMFCQLAk
1 0 K139‑ub kMFCQLAkTCPVQLW
3 1 S149‑p PVQLWVDstPPPGtR
1 1 S149‑gl PVQLWVDstPPPGtR
4 8 T150‑p VQLWVDstPPPGtRV
4 1 T155‑p DstPPPGtRVRAMAI
5 1 K164‑ac VRAMAIYkQSQHMTE
1 1 K164‑ub VRAMAIYkQSQHMTE
2 0 S183‑p CPHHERCsDSDGLAP
0 1 R209‑m1 RVEYLDDrNtFrHsV
1 0 T211‑p EYLDDrNtFrHsVVV
0 1 R213‑m1 LDDrNtFrHsVVVPy
5 0 S215‑p DrNtFrHsVVVPyEP
1 0 Y220‑p rHsVVVPyEPPEVGS
0 1 C229 PPEVGSDCTTIHYNY
0 1 Y234 SDCTTIHYNYMCNSS
3 0 S269‑p GNLLGRNsFEVRVCA
1 0 T284‑p CPGRDRRtEEENLRk
1 0 K291‑ub tEEENLRkkGEPHHE
1 3 K292‑ac EEENLRkkGEPHHEL
1 6 K292‑ub EEENLRkkGEPHHEL
1 0 T304‑p HELPPGStkRALPNN
2 15 K305‑ac ELPPGStkRALPNNt
1 20 K305‑ub ELPPGStkRALPNNt
0 1 T312‑p kRALPNNtsssPQPk
1 5 S313‑p RALPNNtsssPQPkk
1 7 S314‑p ALPNNtsssPQPkkk
40 30 S315‑p LPNNtsssPQPkkkP
0 4 K319‑ac tsssPQPkkkPLDGE
1 0 K319‑ub tsssPQPkkkPLDGE
39 0 K320‑ac sssPQPkkkPLDGEy
2 17 K320‑ub sssPQPkkkPLDGEy
1 0 K320‑ne sssPQPkkkPLDGEy
2 10 K321‑ub ssPQPkkkPLDGEyF
1 0 K321‑ne ssPQPkkkPLDGEyF
0 15 Y327‑p kkPLDGEyFTLQIrG
1 0 R333‑me EyFTLQIrGrErFEM
1 0 R335‑m2 FTLQIrGrErFEMFR
1 0 R337‑m2 LQIrGrErFEMFREL
0 2 K351‑ub LNEALELkDAQAGkE
0 1 K357 LkDAQAGKEPGGsRA
0 3 K357‑ub LkDAQAGkEPGGsRA
0 1 S362‑p AGkEPGGsRAHsSHL
5 0 S366‑p PGGsRAHsSHLkskk
15 3 K370‑ac RAHsSHLkskkGQst
1 0 K370‑me RAHsSHLkskkGQst
4 0 K370‑m1 RAHsSHLkskkGQst
2 1 K370‑m2 RAHsSHLkskkGQst
2 0 K370‑m3 RAHsSHLkskkGQst
9 0 K370‑ub RAHsSHLkskkGQst
1 0 K370‑ne RAHsSHLkskkGQst
4 0 S371‑p AHsSHLkskkGQsts
18 3 K372‑ac HsSHLkskkGQstsR
3 0 K372‑me HsSHLkskkGQstsR
3 0 K372‑m1 HsSHLkskkGQstsR
9 0 K372‑ub HsSHLkskkGQstsR
1 0 K372‑ne HsSHLkskkGQstsR
67 3 K373‑ac sSHLkskkGQstsRH
1 0 K373‑m1 sSHLkskkGQstsRH
1 0 K373‑m2 sSHLkskkGQstsRH
9 0 K373‑ub sSHLkskkGQstsRH
1 0 K373‑ne sSHLkskkGQstsRH
12 0 S376‑p LkskkGQstsRHkkL
4 0 T377‑p kskkGQstsRHkkLM
15 1 S378‑p skkGQstsRHkkLMF
24 4 K381‑ac GQstsRHkkLMFktE
9 0 K381‑ub GQstsRHkkLMFktE
128 4 K382‑ac QstsRHkkLMFktEG
1 0 K382‑m1 QstsRHkkLMFktEG
2 1 K382‑m2 QstsRHkkLMFktEG
9 0 K382‑ub QstsRHkkLMFktEG
6 3 K386‑ac RHkkLMFktEGPDsD
0 1 K386‑m1 RHkkLMFktEGPDsD
0 1 K386‑m2 RHkkLMFktEGPDsD
9 1 K386‑ub RHkkLMFktEGPDsD
12 0 K386‑sm RHkkLMFktEGPDsD
4 0 T387‑p HkkLMFktEGPDsD_
2 0 T387 HkkLMFkTEGPDsD_
0 1 - gap
93 11 S392‑p FktEGPDsD______
9285 : Phospho-p53 (Ser6) Antibody
9288 : Phospho-p53 (Ser9) Antibody
4030 : Phospho-p53 (Ser15) (16G8) Mouse mAb (Biotinylated)
8514 : Phospho-p53 (Ser15) (16G8) Mouse mAb (PE Conjugate)
8695 : Phospho-p53 (Ser15) (16G8) Mouse mAb (Alexa Fluor(R) 647 Conjugate)
9235 : Phospho-p53 (Ser15) (16G8) Mouse mAb (Alexa Fluor(R) 488 Conjugate)
9284 : Phospho-p53 (Ser15) Antibody
9286 : Phospho-p53 (Ser15) (16G8) Mouse mAb
9481 : Phospho-p53 (Ser15) (16G8) Mouse mAb (Alexa Fluor(R) 555 Conjugate)
2529 : Phospho-p53 (Thr18) Antibody
9287 : Phospho-p53 (Ser20) Antibody
2526 : Phospho-p53 (Ser33) Antibody
9289 : Phospho-p53 (Ser37) Antibody
2521 : Phospho-p53 (Ser46) Antibody
2676 : Phospho-p53 (Thr81) Antibody
2528 : Phospho-p53 (Ser315) Antibody
2525 : Acetyl-p53 (Lys382) Antibody
2570 : Acetyl-p53 (Lys379) Antibody
9281 : Phospho-p53 (Ser392) Antibody
  p53 iso4  
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
S7‑p _MDDLMLsPDDIEQW
T16 DDIEQWFTEDPGPDE
D22 FTEDPGPDEAPRMPE
T42 APAPAAPTPAAPAPA
S60 PLSSSVPSQKTYQGS
K62 SSSVPSQKTYQGSYG
S67 SQKTYQGSYGFRLGF
R71 YQGSYGFRLGFLHSG
H76 GFRLGFLHSGTAKSV
K81 FLHSGTAKSVTCTYS
K81 FLHSGTAKSVTCTYS
Y87 AKSVTCTYSPALNKM
K93 TYSPALNKMFCQLAK
K100 KMFCQLAKTCPVQLW
S110 PVQLWVDSTPPPGTR
S110 PVQLWVDSTPPPGTR
T111 VQLWVDSTPPPGTRV
T116 DSTPPPGTRVRAMAI
K125 VRAMAIYKQSQHMTE
K125 VRAMAIYKQSQHMTE
S144 CPHHERCSDSDGLAP
R170 RVEYLDDRNTFRHSV
T172 EYLDDRNTFRHSVVV
R174 LDDRNTFRHSVVVPY
S176 DRNTFRHSVVVPYEP
Y181 RHSVVVPYEPPEVGS
C190 PPEVGSDCTTIHYNY
Y195 SDCTTIHYNYMCNSS
S230 GNLLGRNSFEVRVCA
T245 CPGRDRRTEEENLRK
K252 TEEENLRKKGEPHHE
K253 EEENLRKKGEPHHEL
K253 EEENLRKKGEPHHEL
T265 HELPPGSTKRALPNN
K266 ELPPGSTKRALPNNT
K266 ELPPGSTKRALPNNT
T273 KRALPNNTSSSPQPK
S274 RALPNNTSSSPQPKK
S275 ALPNNTSSSPQPKKK
S276 LPNNTSSSPQPKKKP
K280 TSSSPQPKKKPLDGE
K280 TSSSPQPKKKPLDGE
K281 SSSPQPKKKPLDGEY
K281 SSSPQPKKKPLDGEY
K281 SSSPQPKKKPLDGEY
K282 SSPQPKKKPLDGEYF
K282 SSPQPKKKPLDGEYF
Y288 KKPLDGEYFTLQIRG
R294 EYFTLQIRGRERFEM
R296 FTLQIRGRERFEMFR
R298 LQIRGRERFEMFREL
K312 LNEALELKDAQAGKE
K318 LKDAQAGKEPGGSRA
K318 LKDAQAGKEPGGSRA
S323 AGKEPGGSRAHSSHL
S327 PGGSRAHSSHLKSKk
K331 RAHSSHLKSKkGQST
K331 RAHSSHLKSKkGQST
K331 RAHSSHLKSKkGQST
K331 RAHSSHLKSKkGQST
K331 RAHSSHLKSKkGQST
K331 RAHSSHLKSKkGQST
K331 RAHSSHLKSKkGQST
S332 AHSSHLKSKkGQSTS
K333 HSSHLKSKkGQSTSR
K333 HSSHLKSKkGQSTSR
K333 HSSHLKSKkGQSTSR
K333 HSSHLKSKkGQSTSR
K333 HSSHLKSKkGQSTSR
K334‑ac SSHLKSKkGQSTSRH
K334 SSHLKSKKGQSTSRH
K334 SSHLKSKKGQSTSRH
K334 SSHLKSKKGQSTSRH
K334 SSHLKSKKGQSTSRH
S337 LKSKkGQSTSRHKkL
T338 KSKkGQSTSRHKkLM
S339 SKkGQSTSRHKkLMF
K342 GQSTSRHKkLMFKTE
K342 GQSTSRHKkLMFKTE
K343‑ac QSTSRHKkLMFKTEG
K343 QSTSRHKKLMFKTEG
K343 QSTSRHKKLMFKTEG
K343 QSTSRHKKLMFKTEG
K347 RHKkLMFKTEGPDSD
K347 RHKkLMFKTEGPDSD
K347 RHKkLMFKTEGPDSD
K347 RHKkLMFKTEGPDSD
K347 RHKkLMFKTEGPDSD
T348 HKkLMFKTEGPDSD_
T348 HKkLMFKTEGPDSD_
- gap
S353 FKTEGPDSD______
  mouse

► Hide Isoforms
 
S4‑p ____MEEsQsDIsLE
S6‑p __MEEsQsDIsLELP
S9‑p EEsQsDIsLELPLsQ
S15‑p IsLELPLsQEtFsGL
T18‑p ELPLsQEtFsGLWKL
S20‑p PLsQEtFsGLWKLLP
P33 LPPEDILPsPHCMDD
S34‑p PPEDILPsPHCMDDL
L43 HCMDDLLLPQDVEEF
- gap
S55‑p EEFFEGPsEALRVSG
G75 DPVTETPGPVAPAPA
S93 PLSSFVPSQKTYQGN
K95 SSFVPSQKTYQGNYG
N100 SQKTYQGNYGFHLGF
H104 YQGNYGFHLGFLQSG
Q109 GFHLGFLQSGTAkSV
K114‑ac FLQSGTAkSVMCTYS
K114 FLQSGTAKSVMCTYS
Y120 AkSVMCTYSPPLNKL
K126 TYSPPLNKLFCQLAK
K133 KLFCQLAKTCPVQLW
A143 PVQLWVSATPPAGsR
A143 PVQLWVSATPPAGsR
T144 VQLWVSATPPAGsRV
S149‑p SATPPAGsRVRAMAI
K158 VRAMAIYKKSQHMTE
K158 VRAMAIYKKSQHMTE
S177 CPHHERCSDGDGLAP
R203 YPEYLEDRQTFRHSV
T205 EYLEDRQTFRHSVVV
R207 LEDRQTFRHSVVVPY
S209 DRQTFRHSVVVPYEP
Y214 RHSVVVPYEPPEAGS
Y223‑p PPEAGSEyTTIHyKY
Y228‑p SEyTTIHyKYMCNSS
S263 GNLLGRDSFEVRVCA
T278 CPGRDRRTEEENFRK
K285 TEEENFRKkEVLCPE
K286 EEENFRKKEVLCPEL
K286‑ub EEENFRKkEVLCPEL
A298 PELPPGSAkRALPTC
K299‑ac ELPPGSAkRALPTCT
K299‑ub ELPPGSAkRALPTCT
T306 kRALPTCTsAsPPQk
S307‑p RALPTCTsAsPPQkk
A308 ALPTCTsAsPPQkkk
S309‑p LPTCTsAsPPQkkkP
K313‑ac TsAsPPQkkkPLDGE
K313 TsAsPPQKkkPLDGE
K314‑ac sAsPPQkkkPLDGEy
K314‑ub sAsPPQkkkPLDGEy
K314 sAsPPQkKkPLDGEy
K315‑ub AsPPQkkkPLDGEyF
K315 AsPPQkkKPLDGEyF
Y321‑p kkPLDGEyFTLKIRG
R327 EyFTLKIRGRKRFEM
R329 FTLKIRGRKRFEMFR
R331 LKIRGRKRFEMFREL
K345 LNEALELKDAHATEE
E351 LKDAHATEESGDSRA
E351 LKDAHATEESGDSRA
S356 ATEESGDSRAHSSYL
S360 SGDSRAHSSYLkTkk
K364 RAHSSYLKTkkGQsT
K364 RAHSSYLKTkkGQsT
K364 RAHSSYLKTkkGQsT
K364 RAHSSYLKTkkGQsT
K364 RAHSSYLKTkkGQsT
K364‑ub RAHSSYLkTkkGQsT
K364 RAHSSYLKTkkGQsT
T365 AHSSYLkTkkGQsTs
K366 HSSYLkTKkGQsTsR
K366‑me HSSYLkTkkGQsTsR
K366 HSSYLkTKkGQsTsR
K366‑ub HSSYLkTkkGQsTsR
K366 HSSYLkTKkGQsTsR
K367‑ac SSYLkTkkGQsTsRH
K367 SSYLkTkKGQsTsRH
K367 SSYLkTkKGQsTsRH
K367‑ub SSYLkTkkGQsTsRH
K367 SSYLkTkKGQsTsRH
S370‑p LkTkkGQsTsRHkkT
T371 kTkkGQsTsRHkkTM
S372‑p TkkGQsTsRHkkTMV
K375 GQsTsRHKkTMVkkV
K375‑ub GQsTsRHkkTMVkkV
K376‑ac QsTsRHkkTMVkkVG
K376 QsTsRHkKTMVkkVG
K376 QsTsRHkKTMVkkVG
K376‑ub QsTsRHkkTMVkkVG
K380‑ac RHkkTMVkkVGPDsD
K380 RHkkTMVKkVGPDsD
K380 RHkkTMVKkVGPDsD
K380‑ub RHkkTMVkkVGPDsD
K380 RHkkTMVKkVGPDsD
K381 HkkTMVkKVGPDsD_
K381‑ub HkkTMVkkVGPDsD_
- gap
S386‑p VkkVGPDsD______
9285 : Phospho-p53 (Ser6) Antibody
9284 : Phospho-p53 (Ser15) Antibody
9286 : Phospho-p53 (Ser15) (16G8) Mouse mAb
12571 : Phospho-p53 (Ser15) (D4S1H) XP(R) Rabbit mAb (Mouse Specific)
14789 : Phospho-p53 (Ser15) (D4S1H) XP(R) Rabbit mAb (Rodent Specific) (PE Conjugate)
9287 : Phospho-p53 (Ser20) Antibody
2570 : Acetyl-p53 (Lys379) Antibody
9281 : Phospho-p53 (Ser392) Antibody
  p53 iso2  
S7 _MTAMEESQSDISLE
S9 TAMEESQSDISLELP
S12 EESQSDISLELPLsQ
S18‑p ISLELPLsQETFSGL
T21 ELPLsQETFSGLWKL
S23 PLsQETFSGLWKLLP
P36 LPPEDILPSPHCMDD
S37 PPEDILPSPHCMDDL
L46 HCMDDLLLPQDVEEF
- gap
S58 EEFFEGPSEALRVSG
G78 DPVTETPGPVAPAPA
S96 PLSSFVPSQKTYQGN
K98 SSFVPSQKTYQGNYG
N103 SQKTYQGNYGFHLGF
H107 YQGNYGFHLGFLQSG
Q112 GFHLGFLQSGTAkSV
K117‑ac FLQSGTAkSVMCTYS
K117 FLQSGTAKSVMCTYS
Y123 AkSVMCTYSPPLNKL
K129 TYSPPLNKLFCQLAK
K136 KLFCQLAKTCPVQLW
A146 PVQLWVSATPPAGSR
A146 PVQLWVSATPPAGSR
T147 VQLWVSATPPAGSRV
S152 SATPPAGSRVRAMAI
K161 VRAMAIYKKSQHMTE
K161 VRAMAIYKKSQHMTE
S180 CPHHERCSDGDGLAP
R206 YPEYLEDRQTFRHSV
T208 EYLEDRQTFRHSVVV
R210 LEDRQTFRHSVVVPY
S212 DRQTFRHSVVVPYEP
Y217 RHSVVVPYEPPEAGS
Y226 PPEAGSEYTTIHYKY
Y231 SEYTTIHYKYMCNSS
S266 GNLLGRDSFEVRVCA
T281 CPGRDRRTEEENFRK
K288 TEEENFRKKEVLCPE
K289 EEENFRKKEVLCPEL
K289 EEENFRKKEVLCPEL
A301 PELPPGSAKRALPTC
K302 ELPPGSAKRALPTCT
K302 ELPPGSAKRALPTCT
T309 KRALPTCTSASPPQK
S310 RALPTCTSASPPQKk
A311 ALPTCTSASPPQKkK
S312 LPTCTSASPPQKkKP
K316 TSASPPQKkKPLDGE
K316 TSASPPQKkKPLDGE
K317‑ac SASPPQKkKPLDGEY
K317 SASPPQKKKPLDGEY
K317 SASPPQKKKPLDGEY
K318 ASPPQKkKPLDGEYF
K318 ASPPQKkKPLDGEYF
Y324 kKPLDGEYFTLKIRG
R330 EYFTLKIRGRKRFEM
R332 FTLKIRGRKRFEMFR
R334 LKIRGRKRFEMFREL
K348 LNEALELKDAHATEE
E354 LKDAHATEESGDSRA
E354 LKDAHATEESGDSRA
S359 ATEESGDSRAHSSLQ
S363 SGDSRAHSSLQPRAF
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
K375‑sm RAFQALIkEEsPNC_
- gap
- gap
S378‑p QALIkEEsPNC____
- gap
14789 : Phospho-p53 (Ser15) (D4S1H) XP(R) Rabbit mAb (Rodent Specific) (PE Conjugate)
  rat