UniProt ID | P53_HUMAN | |
---|---|---|
UniProt AC | P04637 | |
Protein Name | Cellular tumor antigen p53 | |
Gene Name | TP53 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 393 | |
Subcellular Localization | Cytoplasm. Nucleus. Nucleus, PML body. Endoplasmic reticulum. Mitochondrion matrix. Interaction with BANP promotes nuclear localization. Recruited into PML bodies together with CHEK2. Translocates to mitochondria upon oxidative stress. Translocates t | |
Protein Description | 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. 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 seem to have to 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] | |
Protein Sequence | MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
6 | Phosphorylation | --MEEPQSDPSVEPP --CCCCCCCCCCCCC | 63.30 | 15792956 | |
7 (in isoform 4) | Phosphorylation | - | 33.96 | - | |
7 (in isoform 5) | Phosphorylation | - | 33.96 | - | |
7 (in isoform 6) | Phosphorylation | - | 33.96 | - | |
9 | Phosphorylation | EEPQSDPSVEPPLSQ CCCCCCCCCCCCCCH | 44.07 | 9765199 | |
15 | Phosphorylation | PSVEPPLSQETFSDL CCCCCCCCHHHHHHH | 31.57 | 20123963 | |
18 | Phosphorylation | EPPLSQETFSDLWKL CCCCCHHHHHHHHHH | 22.32 | 10606744 | |
20 | Phosphorylation | PLSQETFSDLWKLLP CCCHHHHHHHHHHCC | 38.93 | 11258706 | |
24 | Ubiquitination | ETFSDLWKLLPENNV HHHHHHHHHCCCCCC | 47.66 | - | |
32 | Ubiquitination | LLPENNVLSPLPSQA HCCCCCCCCCCCHHH | 4.79 | 21890473 | |
32 | Ubiquitination | LLPENNVLSPLPSQA HCCCCCCCCCCCHHH | 4.79 | 21890473 | |
33 | Phosphorylation | LPENNVLSPLPSQAM CCCCCCCCCCCHHHH | 21.80 | 17906639 | |
37 | Phosphorylation | NVLSPLPSQAMDDLM CCCCCCCHHHHHHHC | 37.95 | ||
46 | Phosphorylation | AMDDLMLSPDDIEQW HHHHHCCCHHHHHHH | 16.59 | 16793543 | |
55 | Phosphorylation | DDIEQWFTEDPGPDE HHHHHHHHCCCCCCC | 36.20 | 16793543 | |
81 | Phosphorylation | APAPAAPTPAAPAPA CCCCCCCCCCCCCCC | 22.34 | 12531896 | |
99 | Phosphorylation | PLSSSVPSQKTYQGS CCCCCCCCCCEEECC | 42.00 | 17525332 | |
101 | Ubiquitination | SSSVPSQKTYQGSYG CCCCCCCCEEECCCE | 54.24 | 21890473 | |
101 (in isoform 1) | Ubiquitination | - | 54.24 | 21890473 | |
101 (in isoform 2) | Ubiquitination | - | 54.24 | 21890473 | |
101 | Ubiquitination | SSSVPSQKTYQGSYG CCCCCCCCEEECCCE | 54.24 | 21890473 | |
101 | Ubiquitination | SSSVPSQKTYQGSYG CCCCCCCCEEECCCE | 54.24 | 21890473 | |
101 | Ubiquitination | SSSVPSQKTYQGSYG CCCCCCCCEEECCCE | 54.24 | 21890473 | |
103 | Nitration | SVPSQKTYQGSYGFR CCCCCCEEECCCEEE | 20.22 | - | |
103 | Phosphorylation | SVPSQKTYQGSYGFR CCCCCCEEECCCEEE | 20.22 | 29496907 | |
106 | Phosphorylation | SQKTYQGSYGFRLGF CCCEEECCCEEEEEE | 13.42 | - | |
107 | Nitration | QKTYQGSYGFRLGFL CCEEECCCEEEEEEE | 27.40 | - | |
110 | Methylation | YQGSYGFRLGFLHSG EECCCEEEEEEECCC | 29.55 | 5168515 | |
115 | Methylation | GFRLGFLHSGTAKSV EEEEEEECCCCCCEE | 23.17 | 5168519 | |
120 | Acetylation | FLHSGTAKSVTCTYS EECCCCCCEEEEECC | 45.34 | 23431171 | |
120 | Ubiquitination | FLHSGTAKSVTCTYS EECCCCCCEEEEECC | 45.34 | 19536131 | |
120 (in isoform 1) | Ubiquitination | - | 45.34 | 21890473 | |
120 (in isoform 2) | Ubiquitination | - | 45.34 | 21890473 | |
122 | Ubiquitination | HSGTAKSVTCTYSPA CCCCCCEEEEECCHH | 5.13 | 21890473 | |
124 | Glutathionylation | GTAKSVTCTYSPALN CCCCEEEEECCHHHH | 2.93 | 22833525 | |
124 | S-nitrosylation | GTAKSVTCTYSPALN CCCCEEEEECCHHHH | 2.93 | 23796488 | |
125 | Phosphorylation | TAKSVTCTYSPALNK CCCEEEEECCHHHHH | 20.05 | 26471730 | |
126 | Nitration | AKSVTCTYSPALNKM CCEEEEECCHHHHHH | 18.14 | - | |
126 | Phosphorylation | AKSVTCTYSPALNKM CCEEEEECCHHHHHH | 18.14 | 30377224 | |
127 | Phosphorylation | KSVTCTYSPALNKMF CEEEEECCHHHHHHH | 5.88 | 30377224 | |
132 | Ubiquitination | TYSPALNKMFCQLAK ECCHHHHHHHHHHHC | 33.92 | 21890473 | |
132 (in isoform 1) | Ubiquitination | - | 33.92 | 21890473 | |
132 (in isoform 2) | Ubiquitination | - | 33.92 | 21890473 | |
132 | Ubiquitination | TYSPALNKMFCQLAK ECCHHHHHHHHHHHC | 33.92 | 21890473 | |
132 | Ubiquitination | TYSPALNKMFCQLAK ECCHHHHHHHHHHHC | 33.92 | 21890473 | |
132 | Ubiquitination | TYSPALNKMFCQLAK ECCHHHHHHHHHHHC | 33.92 | 21890473 | |
139 | Ubiquitination | KMFCQLAKTCPVQLW HHHHHHHCCCCEEEE | 60.29 | 17371868 | |
141 | Glutathionylation | FCQLAKTCPVQLWVD HHHHHCCCCEEEEEC | 2.83 | 22833525 | |
141 | S-nitrosylation | FCQLAKTCPVQLWVD HHHHHCCCCEEEEEC | 2.83 | 23796488 | |
149 | O-linked_Glycosylation | PVQLWVDSTPPPGTR CEEEEECCCCCCCCE | 32.94 | 25619971 | |
149 | Phosphorylation | PVQLWVDSTPPPGTR CEEEEECCCCCCCCE | 32.94 | 28450419 | |
150 | Phosphorylation | VQLWVDSTPPPGTRV EEEEECCCCCCCCEE | 35.04 | 17906639 | |
154 | Ubiquitination | VDSTPPPGTRVRAMA ECCCCCCCCEEEEEE | 31.74 | 21890473 | |
155 | Phosphorylation | DSTPPPGTRVRAMAI CCCCCCCCEEEEEEE | 31.59 | 28450419 | |
160 | Acetylation | PGTRVRAMAIYKQSQ CCCEEEEEEEEEHHH | 1.31 | 19608861 | |
160 | Ubiquitination | PGTRVRAMAIYKQSQ CCCEEEEEEEEEHHH | 1.31 | 19608861 | |
160 | Ubiquitination | PGTRVRAMAIYKQSQ CCCEEEEEEEEEHHH | 1.31 | 21890473 | |
160 | Ubiquitination | PGTRVRAMAIYKQSQ CCCEEEEEEEEEHHH | 1.31 | 21890473 | |
163 | Nitration | RVRAMAIYKQSQHMT EEEEEEEEEHHHHHH | 8.08 | - | |
164 | Acetylation | VRAMAIYKQSQHMTE EEEEEEEEHHHHHHH | 37.04 | 18485870 | |
164 | Ubiquitination | VRAMAIYKQSQHMTE EEEEEEEEHHHHHHH | 37.04 | 21890473 | |
164 (in isoform 1) | Ubiquitination | - | 37.04 | 21890473 | |
164 (in isoform 2) | Ubiquitination | - | 37.04 | 21890473 | |
164 | Ubiquitination | VRAMAIYKQSQHMTE EEEEEEEEHHHHHHH | 37.04 | 21890473 | |
164 | Ubiquitination | VRAMAIYKQSQHMTE EEEEEEEEHHHHHHH | 37.04 | 21890473 | |
164 | Ubiquitination | VRAMAIYKQSQHMTE EEEEEEEEHHHHHHH | 37.04 | 21890473 | |
173 | Acetylation | SQHMTEVVRRCPHHE HHHHHHHHHHCCCCC | 2.32 | 19608861 | |
173 | Ubiquitination | SQHMTEVVRRCPHHE HHHHHHHHHHCCCCC | 2.32 | 19608861 | |
173 | Ubiquitination | SQHMTEVVRRCPHHE HHHHHHHHHHCCCCC | 2.32 | 21890473 | |
173 | Ubiquitination | SQHMTEVVRRCPHHE HHHHHHHHHHCCCCC | 2.32 | 21890473 | |
182 | Glutathionylation | RCPHHERCSDSDGLA HCCCCCCCCCCCCCC | 4.89 | 22833525 | |
182 | S-nitrosylation | RCPHHERCSDSDGLA HCCCCCCCCCCCCCC | 4.89 | 23796488 | |
183 | Phosphorylation | CPHHERCSDSDGLAP CCCCCCCCCCCCCCC | 46.50 | 22611192 | |
187 | Acetylation | ERCSDSDGLAPPQHL CCCCCCCCCCCCHHE | 27.91 | 17110336 | |
187 | Ubiquitination | ERCSDSDGLAPPQHL CCCCCCCCCCCCHHE | 27.91 | 17110336 | |
188 | Acetylation | RCSDSDGLAPPQHLI CCCCCCCCCCCHHEE | 8.52 | 9891054 | |
188 | Ubiquitination | RCSDSDGLAPPQHLI CCCCCCCCCCCHHEE | 8.52 | 9891054 | |
189 | Acetylation | CSDSDGLAPPQHLIR CCCCCCCCCCHHEEE | 21.18 | 17110336 | |
189 | Ubiquitination | CSDSDGLAPPQHLIR CCCCCCCCCCHHEEE | 21.18 | 17110336 | |
205 | Nitration | EGNLRVEYLDDRNTF ECCEEEEEECCCCCE | 16.75 | - | |
205 | Phosphorylation | EGNLRVEYLDDRNTF ECCEEEEEECCCCCE | 16.75 | 25690035 | |
209 | Methylation | RVEYLDDRNTFRHSV EEEEECCCCCEEEEE | 43.70 | 5168513 | |
211 | Phosphorylation | EYLDDRNTFRHSVVV EEECCCCCEEEEEEE | 23.96 | 22611192 | |
213 | Methylation | LDDRNTFRHSVVVPY ECCCCCEEEEEEECC | 21.09 | 5168517 | |
215 | Phosphorylation | DRNTFRHSVVVPYEP CCCCEEEEEEECCCC | 16.61 | 22611192 | |
219 | Ubiquitination | FRHSVVVPYEPPEVG EEEEEEECCCCCCCC | 19.03 | 11046142 | |
220 | Nitration | RHSVVVPYEPPEVGS EEEEEECCCCCCCCC | 29.47 | - | |
220 | Phosphorylation | RHSVVVPYEPPEVGS EEEEEECCCCCCCCC | 29.47 | - | |
225 | Ubiquitination | VPYEPPEVGSDCTTI ECCCCCCCCCCCEEE | 12.56 | 11046142 | |
234 | Nitration | SDCTTIHYNYMCNSS CCCEEEECEECCCCC | 12.25 | - | |
236 | Nitration | CTTIHYNYMCNSSCM CEEEECEECCCCCCC | 8.90 | - | |
238 | Acetylation | TIHYNYMCNSSCMGG EEECEECCCCCCCCC | 2.93 | 17110336 | |
238 | Methylation | TIHYNYMCNSSCMGG EEECEECCCCCCCCC | 2.93 | 17110336 | |
238 | Ubiquitination | TIHYNYMCNSSCMGG EEECEECCCCCCCCC | 2.93 | 17110336 | |
240 | Acetylation | HYNYMCNSSCMGGMN ECEECCCCCCCCCCC | 21.71 | 9288740 | |
240 | Methylation | HYNYMCNSSCMGGMN ECEECCCCCCCCCCC | 21.71 | 9288740 | |
240 | Ubiquitination | HYNYMCNSSCMGGMN ECEECCCCCCCCCCC | 21.71 | 9288740 | |
241 | Acetylation | YNYMCNSSCMGGMNR CEECCCCCCCCCCCC | 8.30 | 17110336 | |
241 | Methylation | YNYMCNSSCMGGMNR CEECCCCCCCCCCCC | 8.30 | 17110336 | |
241 | Ubiquitination | YNYMCNSSCMGGMNR CEECCCCCCCCCCCC | 8.30 | 17110336 | |
249 | Acetylation | CMGGMNRRPILTIIT CCCCCCCCCEEEEEE | 20.01 | 17110336 | |
249 | Phosphorylation | CMGGMNRRPILTIIT CCCCCCCCCEEEEEE | 20.01 | - | |
249 | Ubiquitination | CMGGMNRRPILTIIT CCCCCCCCCEEEEEE | 20.01 | 17110336 | |
250 | Acetylation | MGGMNRRPILTIITL CCCCCCCCEEEEEEE | 23.78 | 19608861 | |
250 | Methylation | MGGMNRRPILTIITL CCCCCCCCEEEEEEE | 23.78 | 19608861 | |
250 | Ubiquitination | MGGMNRRPILTIITL CCCCCCCCEEEEEEE | 23.78 | 19608861 | |
253 | Acetylation | MNRRPILTIITLEDS CCCCCEEEEEEEECC | 15.85 | 19608861 | |
253 | Ubiquitination | MNRRPILTIITLEDS CCCCCEEEEEEEECC | 15.85 | 19608861 | |
254 | Acetylation | NRRPILTIITLEDSS CCCCEEEEEEEECCC | 1.71 | 17110336 | |
254 | Methylation | NRRPILTIITLEDSS CCCCEEEEEEEECCC | 1.71 | 17110336 | |
254 | Ubiquitination | NRRPILTIITLEDSS CCCCEEEEEEEECCC | 1.71 | 17110336 | |
266 | Acetylation | DSSGNLLGRNSFEVR CCCCCCCCCCCEEEE | 29.86 | 19608861 | |
266 | Ubiquitination | DSSGNLLGRNSFEVR CCCCCCCCCCCEEEE | 29.86 | 19608861 | |
269 | Phosphorylation | GNLLGRNSFEVRVCA CCCCCCCCEEEEEEE | 22.79 | 22817900 | |
280 | Acetylation | RVCACPGRDRRTEEE EEEECCCCCCCCHHH | 21.29 | 17110336 | |
280 | Ubiquitination | RVCACPGRDRRTEEE EEEECCCCCCCCHHH | 21.29 | 17110336 | |
281 | Acetylation | VCACPGRDRRTEEEN EEECCCCCCCCHHHH | 50.78 | 9891054 | |
281 | Ubiquitination | VCACPGRDRRTEEEN EEECCCCCCCCHHHH | 50.78 | 9891054 | |
282 | Acetylation | CACPGRDRRTEEENL EECCCCCCCCHHHHH | 46.16 | 17110336 | |
282 | Ubiquitination | CACPGRDRRTEEENL EECCCCCCCCHHHHH | 46.16 | 17110336 | |
282 | Ubiquitination | CACPGRDRRTEEENL EECCCCCCCCHHHHH | 46.16 | 21890473 | |
284 | Phosphorylation | CPGRDRRTEEENLRK CCCCCCCCHHHHHHH | 48.95 | 20959462 | |
290 | Methylation | RTEEENLRKKGEPHH CCHHHHHHHCCCCCC | 50.66 | 115486213 | |
291 | Ubiquitination | TEEENLRKKGEPHHE CHHHHHHHCCCCCCC | 69.19 | 19536131 | |
292 | Acetylation | EEENLRKKGEPHHEL HHHHHHHCCCCCCCC | 63.17 | 19608861 | |
292 | Propionylation | EEENLRKKGEPHHEL HHHHHHHCCCCCCCC | 63.17 | - | |
292 | Ubiquitination | EEENLRKKGEPHHEL HHHHHHHCCCCCCCC | 63.17 | 19536131 | |
292 (in isoform 1) | Ubiquitination | - | 63.17 | 21890473 | |
292 (in isoform 2) | Ubiquitination | - | 63.17 | 21890473 | |
292 | Ubiquitination | EEENLRKKGEPHHEL HHHHHHHCCCCCCCC | 63.17 | 21890473 | |
292 | Ubiquitination | EEENLRKKGEPHHEL HHHHHHHCCCCCCCC | 63.17 | 21890473 | |
292 | Ubiquitination | EEENLRKKGEPHHEL HHHHHHHCCCCCCCC | 63.17 | 21890473 | |
295 | Ubiquitination | NLRKKGEPHHELPPG HHHHCCCCCCCCCCC | 42.68 | 21890473 | |
304 | Phosphorylation | HELPPGSTKRALPNN CCCCCCCCCCCCCCC | 30.39 | - | |
305 | Acetylation | ELPPGSTKRALPNNT CCCCCCCCCCCCCCC | 37.05 | 19608861 | |
305 | Ubiquitination | ELPPGSTKRALPNNT CCCCCCCCCCCCCCC | 37.05 | 19608861 | |
305 (in isoform 1) | Ubiquitination | - | 37.05 | 21890473 | |
305 (in isoform 2) | Ubiquitination | - | 37.05 | 21890473 | |
305 | Ubiquitination | ELPPGSTKRALPNNT CCCCCCCCCCCCCCC | 37.05 | 21890473 | |
305 | Ubiquitination | ELPPGSTKRALPNNT CCCCCCCCCCCCCCC | 37.05 | 21890473 | |
305 | Ubiquitination | ELPPGSTKRALPNNT CCCCCCCCCCCCCCC | 37.05 | 21890473 | |
310 | Ubiquitination | STKRALPNNTSSSPQ CCCCCCCCCCCCCCC | 66.32 | 21890473 | |
311 | Ubiquitination | TKRALPNNTSSSPQP CCCCCCCCCCCCCCC | 39.12 | 21890473 | |
312 | Phosphorylation | KRALPNNTSSSPQPK CCCCCCCCCCCCCCC | 36.30 | 30266825 | |
313 | Phosphorylation | RALPNNTSSSPQPKK CCCCCCCCCCCCCCC | 30.83 | 30266825 | |
314 | Phosphorylation | ALPNNTSSSPQPKKK CCCCCCCCCCCCCCC | 43.96 | 29255136 | |
315 | Phosphorylation | LPNNTSSSPQPKKKP CCCCCCCCCCCCCCC | 27.59 | 29255136 | |
318 (in isoform 4) | Ubiquitination | - | 54.54 | - | |
319 | Acetylation | TSSSPQPKKKPLDGE CCCCCCCCCCCCCCC | 69.08 | 17267393 | |
319 | Butyrylation | TSSSPQPKKKPLDGE CCCCCCCCCCCCCCC | 69.08 | - | |
319 | Propionylation | TSSSPQPKKKPLDGE CCCCCCCCCCCCCCC | 69.08 | - | |
319 | Ubiquitination | TSSSPQPKKKPLDGE CCCCCCCCCCCCCCC | 69.08 | 19927155 | |
320 | Acetylation | SSSPQPKKKPLDGEY CCCCCCCCCCCCCCC | 67.32 | 9891054 | |
320 | Butyrylation | SSSPQPKKKPLDGEY CCCCCCCCCCCCCCC | 67.32 | - | |
320 | Neddylation | SSSPQPKKKPLDGEY CCCCCCCCCCCCCCC | 67.32 | - | |
320 | Propionylation | SSSPQPKKKPLDGEY CCCCCCCCCCCCCCC | 67.32 | - | |
320 | Ubiquitination | SSSPQPKKKPLDGEY CCCCCCCCCCCCCCC | 67.32 | 9891054 | |
320 (in isoform 1) | Ubiquitination | - | 67.32 | 21890473 | |
320 | Ubiquitination | SSSPQPKKKPLDGEY CCCCCCCCCCCCCCC | 67.32 | 21890473 | |
321 | Acetylation | SSPQPKKKPLDGEYF CCCCCCCCCCCCCCE | 57.87 | 19608861 | |
321 | Neddylation | SSPQPKKKPLDGEYF CCCCCCCCCCCCCCE | 57.87 | - | |
321 | Ubiquitination | SSPQPKKKPLDGEYF CCCCCCCCCCCCCCE | 57.87 | 19608861 | |
321 (in isoform 1) | Ubiquitination | - | 57.87 | 21890473 | |
321 | Ubiquitination | SSPQPKKKPLDGEYF CCCCCCCCCCCCCCE | 57.87 | 21890473 | |
327 | Nitration | KKPLDGEYFTLQIRG CCCCCCCCEEEEEEC | 13.85 | - | |
327 | Phosphorylation | KKPLDGEYFTLQIRG CCCCCCCCEEEEEEC | 13.85 | 27642862 | |
333 | Methylation | EYFTLQIRGRERFEM CCEEEEEECHHHHHH | 25.75 | 19011621 | |
334 (in isoform 4) | Acetylation | - | 37.11 | - | |
335 | Dimethylation | FTLQIRGRERFEMFR EEEEEECHHHHHHHH | 23.28 | - | |
335 | Methylation | FTLQIRGRERFEMFR EEEEEECHHHHHHHH | 23.28 | 19011621 | |
337 | Dimethylation | LQIRGRERFEMFREL EEEECHHHHHHHHHH | 31.31 | - | |
337 | Methylation | LQIRGRERFEMFREL EEEECHHHHHHHHHH | 31.31 | 19011621 | |
340 | Sulfoxidation | RGRERFEMFRELNEA ECHHHHHHHHHHHHH | 3.36 | 18781628 | |
343 (in isoform 4) | Acetylation | - | 44.69 | - | |
347 (in isoform 4) | Ubiquitination | - | 12.79 | - | |
351 | Ubiquitination | LNEALELKDAQAGKE HHHHHHHHHHHCCCC | 41.46 | 11046142 | |
357 | Acetylation | LKDAQAGKEPGGSRA HHHHHCCCCCCCCCC | 64.85 | 19155208 | |
357 | Ubiquitination | LKDAQAGKEPGGSRA HHHHHCCCCCCCCCC | 64.85 | 19536131 | |
357 (in isoform 1) | Ubiquitination | - | 64.85 | 21890473 | |
362 | Phosphorylation | AGKEPGGSRAHSSHL CCCCCCCCCCCHHHH | 32.01 | 29954749 | |
366 | Phosphorylation | PGGSRAHSSHLKSKK CCCCCCCHHHHCCCC | 20.61 | 19933256 | |
367 | Phosphorylation | GGSRAHSSHLKSKKG CCCCCCHHHHCCCCC | 23.99 | 30387612 | |
370 | "N6,N6-dimethyllysine" | RAHSSHLKSKKGQST CCCHHHHCCCCCCCC | 55.60 | - | |
370 | Acetylation | RAHSSHLKSKKGQST CCCHHHHCCCCCCCC | 55.60 | 21057544 | |
370 | Methylation | RAHSSHLKSKKGQST CCCHHHHCCCCCCCC | 55.60 | 9288740 | |
370 | Neddylation | RAHSSHLKSKKGQST CCCHHHHCCCCCCCC | 55.60 | - | |
370 | Ubiquitination | RAHSSHLKSKKGQST CCCHHHHCCCCCCCC | 55.60 | 19536131 | |
370 (in isoform 1) | Ubiquitination | - | 55.60 | 21890473 | |
371 | Phosphorylation | AHSSHLKSKKGQSTS CCHHHHCCCCCCCCC | 46.06 | 30387612 | |
372 | Acetylation | HSSHLKSKKGQSTSR CHHHHCCCCCCCCCH | 60.37 | 18485870 | |
372 | Butyrylation | HSSHLKSKKGQSTSR CHHHHCCCCCCCCCH | 60.37 | - | |
372 | Methylation | HSSHLKSKKGQSTSR CHHHHCCCCCCCCCH | 60.37 | 9288740 | |
372 | Neddylation | HSSHLKSKKGQSTSR CHHHHCCCCCCCCCH | 60.37 | - | |
372 | Ubiquitination | HSSHLKSKKGQSTSR CHHHHCCCCCCCCCH | 60.37 | 9288740 | |
373 | "N6,N6-dimethyllysine" | SSHLKSKKGQSTSRH HHHHCCCCCCCCCHH | 70.08 | - | |
373 | Acetylation | SSHLKSKKGQSTSRH HHHHCCCCCCCCCHH | 70.08 | 9288740 | |
373 | Butyrylation | SSHLKSKKGQSTSRH HHHHCCCCCCCCCHH | 70.08 | - | |
373 | Methylation | SSHLKSKKGQSTSRH HHHHCCCCCCCCCHH | 70.08 | 20118233 | |
373 | Neddylation | SSHLKSKKGQSTSRH HHHHCCCCCCCCCHH | 70.08 | - | |
373 | Ubiquitination | SSHLKSKKGQSTSRH HHHHCCCCCCCCCHH | 70.08 | 9288740 | |
376 | Phosphorylation | LKSKKGQSTSRHKKL HCCCCCCCCCHHHEE | 36.70 | 9571186 | |
377 | Phosphorylation | KSKKGQSTSRHKKLM CCCCCCCCCHHHEEE | 23.15 | 22817900 | |
378 | Phosphorylation | SKKGQSTSRHKKLMF CCCCCCCCHHHEEEE | 37.32 | 1454855 | |
381 | Acetylation | GQSTSRHKKLMFKTE CCCCCHHHEEEEECC | 46.63 | 19608861 | |
381 | Ubiquitination | GQSTSRHKKLMFKTE CCCCCHHHEEEEECC | 46.63 | 19608861 | |
382 | "N6,N6-dimethyllysine" | QSTSRHKKLMFKTEG CCCCHHHEEEEECCC | 38.77 | - | |
382 | Acetylation | QSTSRHKKLMFKTEG CCCCHHHEEEEECCC | 38.77 | 17707234 | |
382 | Butyrylation | QSTSRHKKLMFKTEG CCCCHHHEEEEECCC | 38.77 | - | |
382 | Methylation | QSTSRHKKLMFKTEG CCCCHHHEEEEECCC | 38.77 | 17707234 | |
382 | Ubiquitination | QSTSRHKKLMFKTEG CCCCHHHEEEEECCC | 38.77 | 17707234 | |
386 | "N6,N6-dimethyllysine" | RHKKLMFKTEGPDSD HHHEEEEECCCCCCC | 31.53 | - | |
386 | Acetylation | RHKKLMFKTEGPDSD HHHEEEEECCCCCCC | 31.53 | 18485870 | |
386 | Methylation | RHKKLMFKTEGPDSD HHHEEEEECCCCCCC | 31.53 | - | |
386 | Sumoylation | RHKKLMFKTEGPDSD HHHEEEEECCCCCCC | 31.53 | 22214662 | |
386 | Ubiquitination | RHKKLMFKTEGPDSD HHHEEEEECCCCCCC | 31.53 | 10562557 | |
387 | Phosphorylation | HKKLMFKTEGPDSD- HHEEEEECCCCCCC- | 34.60 | 23927012 | |
392 | Phosphorylation | FKTEGPDSD------ EECCCCCCC------ | 48.64 | 23927012 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
9 | S | Phosphorylation | Kinase | HIPK4 | Q8NE63 | Uniprot |
9 | S | Phosphorylation | Kinase | CSNK1D | P48730 | GPS |
9 | S | Phosphorylation | Kinase | PRKDC | P78527 | GPS |
15 | S | Phosphorylation | Kinase | AMPK | Q9Y478 | Uniprot |
15 | S | Phosphorylation | Kinase | ATM | Q13315 | Uniprot |
15 | S | Phosphorylation | Kinase | ATM | Q62388 | PSP |
15 | S | Phosphorylation | Kinase | ATR | Q13535 | PSP |
15 | S | Phosphorylation | Kinase | BTK | Q06187 | PSP |
15 | S | Phosphorylation | Kinase | CDK5 | Q00535 | Uniprot |
15 | S | Phosphorylation | Kinase | CHEK1 | O14757 | GPS |
15 | S | Phosphorylation | Kinase | CHEK2 | O96017 | GPS |
15 | S | Phosphorylation | Kinase | DYRK1A | Q13627 | PSP |
15 | S | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
15 | S | Phosphorylation | Kinase | ERK2 | P63085 | PSP |
15 | S | Phosphorylation | Kinase | MAPK3 | P27361 | GPS |
15 | S | Phosphorylation | Kinase | MAPK14 | Q16539 | GPS |
15 | S | Phosphorylation | Kinase | NUAK1 | O60285 | Uniprot |
15 | S | Phosphorylation | Kinase | PRKDC | P78527 | PhosphoELM |
15 | S | Phosphorylation | Kinase | TP53RK | Q96S44 | GPS |
15 | S | Phosphorylation | Kinase | SMG1 | Q96Q15 | PSP |
15 | S | Phosphorylation | Kinase | STK11 | Q15831 | GPS |
15 | S | Phosphorylation | Kinase | P38-SUBFAMILY | - | GPS |
18 | T | Phosphorylation | Kinase | PRKAA1 | Q13131 | GPS |
18 | T | Phosphorylation | Kinase | CHEK1 | O14757 | GPS |
18 | T | Phosphorylation | Kinase | CHEK2 | O96017 | GPS |
18 | T | Phosphorylation | Kinase | DAPK1 | P53355 | PSP |
18 | T | Phosphorylation | Kinase | CSNK1A1 | P48729 | GPS |
18 | T | Phosphorylation | Kinase | CSNK1D | P48730 | GPS |
18 | T | Phosphorylation | Kinase | PRKDC | P78527 | GPS |
18 | T | Phosphorylation | Kinase | TTK | P33981 | PhosphoELM |
18 | T | Phosphorylation | Kinase | VRK1 | Q99986 | Uniprot |
18 | T | Phosphorylation | Kinase | VRK2 | Q86Y07 | Uniprot |
18 | T | Phosphorylation | Kinase | CK1-FAMILY | - | GPS |
18 | T | Phosphorylation | Kinase | CK1 | - | Uniprot |
18 | T | Phosphorylation | Kinase | CK1_GROUP | - | PhosphoELM |
20 | S | Phosphorylation | Kinase | PRKAA1 | Q13131 | GPS |
20 | S | Phosphorylation | Kinase | ATM | Q13315 | PSP |
20 | S | Phosphorylation | Kinase | CDK5 | Q00535 | PSP |
20 | S | Phosphorylation | Kinase | CHEK1 | O14757 | GPS |
20 | S | Phosphorylation | Kinase | CHK2 | O96017 | PSP |
20 | S | Phosphorylation | Kinase | DAPK1 | P53355 | PSP |
20 | S | Phosphorylation | Kinase | DAPK3 | O43293 | PSP |
20 | S | Phosphorylation | Kinase | CSNK1A1 | P48729 | GPS |
20 | S | Phosphorylation | Kinase | CSNK1D | P48730 | GPS |
20 | S | Phosphorylation | Kinase | MAPKAPK2 | P49137 | PSP |
20 | S | Phosphorylation | Kinase | MAPK8 | P45983 | GPS |
20 | S | Phosphorylation | Kinase | MAPK9 | P45984 | GPS |
20 | S | Phosphorylation | Kinase | PLK3 | Q9H4B4 | Uniprot |
20 | S | Phosphorylation | Kinase | PRKDC | P78527 | GPS |
20 | S | Phosphorylation | Kinase | STK17A | Q9UEE5 | GPS |
20 | S | Phosphorylation | Kinase | CK1 | - | Uniprot |
33 | S | Phosphorylation | Kinase | CDK5 | Q00535 | Uniprot |
33 | S | Phosphorylation | Kinase | CDK7 | P50613 | Uniprot |
33 | S | Phosphorylation | Kinase | CDK9 | P50750 | PSP |
33 | S | Phosphorylation | Kinase | P38G | P53778 | PSP |
33 | S | Phosphorylation | Kinase | MAPK14 | Q16539 | GPS |
33 | S | Phosphorylation | Kinase | CDK-FAMILY | - | GPS |
33 | S | Phosphorylation | Kinase | GSK-FAMILY | - | GPS |
33 | S | Phosphorylation | Kinase | CDK_GROUP | - | PhosphoELM |
33 | S | Phosphorylation | Kinase | GSK-3_GROUP | - | PhosphoELM |
37 | S | Phosphorylation | Kinase | ATR | Q13535 | PSP |
37 | S | Phosphorylation | Kinase | CHEK1 | O14757 | GPS |
37 | S | Phosphorylation | Kinase | CHEK2 | O96017 | GPS |
37 | S | Phosphorylation | Kinase | CK1A | P48729 | PSP |
37 | S | Phosphorylation | Kinase | MAPK5 | Q8IW41 | PhosphoELM |
37 | S | Phosphorylation | Kinase | PRKDC | P78527 | PhosphoELM |
46 | S | Phosphorylation | Kinase | ATM | Q13315 | PSP |
46 | S | Phosphorylation | Kinase | CDK5 | Q00535 | Uniprot |
46 | S | Phosphorylation | Kinase | DYRK2 | Q92630 | Uniprot |
46 | S | Phosphorylation | Kinase | HIPK2 | Q9H2X6 | Uniprot |
46 | S | Phosphorylation | Kinase | PRKCD | Q05655 | GPS |
46 | S | Phosphorylation | Kinase | PRKCG | P05129 | Uniprot |
46 | S | Phosphorylation | Kinase | JNK2 | P45984 | PSP |
46 | S | Phosphorylation | Kinase | MAPK14 | Q16539 | GPS |
46 | S | Phosphorylation | Kinase | PRKDC | P78527 | GPS |
55 | T | Phosphorylation | Kinase | GRK5 | P34947 | Uniprot |
55 | T | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
55 | T | Phosphorylation | Kinase | TAF1 | P21675 | Uniprot |
55 | T | Phosphorylation | Kinase | MAPK-FAMILY | - | GPS |
55 | T | Phosphorylation | Kinase | MAPK_GROUP | - | PhosphoELM |
81 | T | Phosphorylation | Kinase | MAPK8 | P45983 | GPS |
106 | S | Phosphorylation | Kinase | AURKA | O14965 | GPS |
126 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
149 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
150 | T | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
155 | T | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
183 | S | Phosphorylation | Kinase | AURB | Q96GD4 | PSP |
211 | T | Phosphorylation | Kinase | AURKB | Q96GD4 | GPS |
215 | S | Phosphorylation | Kinase | AURKA | O14965 | PhosphoELM |
215 | S | Phosphorylation | Kinase | AURKB | Q96GD4 | GPS |
215 | S | Phosphorylation | Kinase | PAK4 | O96013 | PSP |
220 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
269 | S | Phosphorylation | Kinase | AURB | Q96GD4 | PSP |
269 | S | Phosphorylation | Kinase | DAPK1 | P53355 | PSP |
284 | T | Phosphorylation | Kinase | AURB | Q96GD4 | PSP |
304 | T | Phosphorylation | Kinase | LRRK2 | Q5S007 | PSP |
315 | S | Phosphorylation | Kinase | AURA | O14965 | PSP |
315 | S | Phosphorylation | Kinase | CDK1 | P06493 | Uniprot |
315 | S | Phosphorylation | Kinase | CDK2 | P24941 | Uniprot |
315 | S | Phosphorylation | Kinase | CDK9 | P50750 | PSP |
315 | S | Phosphorylation | Kinase | NEK2 | P51955 | PSP |
366 | S | Phosphorylation | Kinase | CHEK2 | O96017 | GPS |
371 | S | Phosphorylation | Kinase | CDK7 | P50613 | PSP |
371 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
376 | S | Phosphorylation | Kinase | CDK7 | P50613 | PSP |
376 | S | Phosphorylation | Kinase | GSK3B | P49841 | PSP |
376 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
377 | T | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
377 | T | Phosphorylation | Kinase | LRRK2 | Q5S007 | PSP |
378 | S | Phosphorylation | Kinase | CDK7 | P50613 | PSP |
378 | S | Phosphorylation | Kinase | CHEK1 | O14757 | GPS |
378 | S | Phosphorylation | Kinase | CHEK2 | O96017 | GPS |
378 | S | Phosphorylation | Kinase | PRKACA | P17612 | GPS |
378 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
387 | T | Phosphorylation | Kinase | CHEK1 | O14757 | GPS |
392 | S | Phosphorylation | Kinase | CDK2 | P24941 | Uniprot |
392 | S | Phosphorylation | Kinase | CDK7 | P50613 | PSP |
392 | S | Phosphorylation | Kinase | CDK9 | P50750 | PSP |
392 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
392 | S | Phosphorylation | Kinase | CK2B | P67870 | PSP |
392 | S | Phosphorylation | Kinase | EIF2AK2 | P19525 | GPS |
392 | S | Phosphorylation | Kinase | MAPK3 | P27361 | GPS |
392 | S | Phosphorylation | Kinase | NUAK1 | O60285 | Uniprot |
392 | S | Phosphorylation | Kinase | STK11 | Q15831 | GPS |
392 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
- | K | Ubiquitination | E3 ubiquitin ligase | MDM2 | Q00987 | PMID:10207051 |
- | K | Ubiquitination | E3 ubiquitin ligase | MDM4 | O15151 | PMID:12393902 |
- | K | Ubiquitination | E3 ubiquitin ligase | FBXO42 | Q6P3S6 | PMID:19509332 |
- | K | Ubiquitination | E3 ubiquitin ligase | MUL1 | Q969V5 | PMID:31235254 |
- | K | Ubiquitination | E3 ubiquitin ligase | TRIM39 | Q9HCM9 | PMID:23213260 |
- | K | Ubiquitination | E3 ubiquitin ligase | RNF38 | Q9H0F5 | PMID:23973461 |
- | K | Ubiquitination | E3 ubiquitin ligase | UHRF1 | Q96T88 | PMID:26102039 |
- | K | Ubiquitination | E3 ubiquitin ligase | BTRC | Q9Y297 | PMID:24658274 |
- | K | Ubiquitination | E3 ubiquitin ligase | C10orf90 | Q96M02 | PMID:24240685 |
- | K | Ubiquitination | E3 ubiquitin ligase | STUB1 | Q9UNE7 | PMID:20618441 |
- | K | Ubiquitination | E3 ubiquitin ligase | HUWE1 | Q7Z6Z7 | PMID:17580310 |
- | K | Ubiquitination | E3 ubiquitin ligase | TRIM28 | Q13263 | PMID:20864041 |
- | K | Ubiquitination | E3 ubiquitin ligase | DTL | Q9NZJ0 | PMID:22199232 |
- | K | Ubiquitination | E3 ubiquitin ligase | RCHY1 | Q96PM5 | PMID:17721809 |
- | K | Ubiquitination | E3 ubiquitin ligase | TOPORS | Q9NS56 | PMID:19895323 |
- | K | Ubiquitination | E3 ubiquitin ligase | UBE3A | Q05086 | PMID:10726657 |
- | K | Ubiquitination | E3 ubiquitin ligase | SYVN1 | Q86TM6 | PMID:17828301 |
- | K | Ubiquitination | E3 ubiquitin ligase | FBXO11 | Q86XK2 | PMID:22199232 |
- | K | Ubiquitination | E3 ubiquitin ligase | MSL2 | Q9HCI7 | PMID:19033443 |
- | K | Ubiquitination | E3 ubiquitin ligase | DET1 | Q7L5Y6 | PMID:17968316 |
- | K | Ubiquitination | E3 ubiquitin ligase | E4F1 | Q66K89 | PMID:17110336 |
- | K | Ubiquitination | E3 ubiquitin ligase | RFWD3 | Q6PCD5 | PMID:20173098 |
- | K | Ubiquitination | E3 ubiquitin ligase | RNF34 | Q969K3 | PMID:17121812 |
- | K | Ubiquitination | E3 ubiquitin ligase | RFFL | Q8WZ73 | PMID:32296023 |
- | K | Ubiquitination | E3 ubiquitin ligase | WWP1 | Q9H0M0 | PMID:16924229 |
- | K | Ubiquitination | E3 ubiquitin ligase | MKRN1 | Q9UHC7 | PMID:19536131 |
- | K | Ubiquitination | E3 ubiquitin ligase | TRIM24 | O15164 | PMID:19844164 |
- | K | Ubiquitination | E3 ubiquitin ligase | SIAH2 | O43255 | PMID:22199232 |
- | K | Ubiquitination | E3 ubiquitin ligase | RNF125 | Q96EQ8 | PMID:22199232 |
- | K | Ubiquitination | E3 ubiquitin ligase | EP300 | Q09472 | PMID:12690203 |
- | K | Ubiquitination | E3 ubiquitin ligase | SKP2 | Q13309 | PMID:21127074 |
- | K | Ubiquitination | E3 ubiquitin ligase | UBE4B | O95155 | PMID:21317885 |
- | K | Ubiquitination | E3 ubiquitin ligase | TRAF7 | Q6Q0C0 | PMID:23128672 |
- | K | Ubiquitination | E3 ubiquitin ligase | DET1#COP1 | Q7L5Y6#Q8NHY2 | PMID:22199232 |
- | K | Ubiquitination | E3 ubiquitin ligase | FBXW7 | Q969H0 | PMID:25860929:31346036 |
- | K | Ubiquitination | E3 ubiquitin ligase | CCAR1 | Q8IX12 | PMID:32296023 |
- | K | Ubiquitination | E3 ubiquitin ligase | CUL1 | Q13616 | PMID:32296023 |
- | K | Ubiquitination | E3 ubiquitin ligase | CUL5 | Q93034 | PMID:32296023 |
- | K | Ubiquitination | E3 ubiquitin ligase | CUL7 | Q14999 | PMID:32296023 |
- | K | Ubiquitination | E3 ubiquitin ligase | COP1 | Q8NHY2 | PMID:15103385 |
- | K | Ubiquitination | E3 ubiquitin ligase | FBXO22 | Q8NEZ5 | PMID:26868148 |
- | K | Ubiquitination | E3 ubiquitin ligase | E6 | P03126 | PMID:22199232 |
- | K | Ubiquitination | E3 ubiquitin ligase | ICP0 | P08393 | PMID:22199232 |
- | K | Ubiquitination | E3 ubiquitin ligase | N/A#E4 | P03243#Q6VGT3 | PMID:22199232 |
- | K | Ubiquitination | E3 ubiquitin ligase | ASAP1#TP53BP1 | Q9ULH1#Q12888 | PMID:32296023 |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
9 | S | Phosphorylation |
| 20959462 |
15 | S | Oxidation |
| 20959462 |
15 | S | Phosphorylation |
| 20959462 |
15 | S | Phosphorylation |
| 28842590 |
15 | S | Phosphorylation |
| 20959462 |
15 | S | Phosphorylation |
| 21317932 |
15 | S | Phosphorylation |
| 20959462 |
18 | T | ubiquitylation |
| 20959462 |
18 | T | Phosphorylation |
| 20959462 |
18 | T | Phosphorylation |
| 20959462 |
18 | T | Phosphorylation |
| 20959462 |
18 | T | Acetylation |
| 20959462 |
20 | S | Phosphorylation |
| 20959462 |
20 | S | ubiquitylation |
| 20959462 |
20 | S | Phosphorylation |
| 20959462 |
24 | K | ubiquitylation |
| 21597459 |
33 | S | Phosphorylation |
| 20959462 |
33 | S | Phosphorylation |
| 20959462 |
33 | S | Oxidation |
| 20959462 |
46 | S | Oxidation |
| 20959462 |
46 | S | Acetylation |
| 20959462 |
46 | S | Phosphorylation |
| 20959462 |
46 | S | Phosphorylation |
| 20959462 |
46 | S | Phosphorylation |
| 20959462 |
46 | S | Phosphorylation |
| 20959462 |
55 | T | Phosphorylation |
| 20959462 |
55 | T | Phosphorylation |
| - |
291 | K | ubiquitylation |
| 19536131 |
292 | K | ubiquitylation |
| 19536131 |
315 | S | Phosphorylation |
| 20959462 |
333 | R | Methylation |
| 19011621 |
335 | R | Methylation |
| 19011621 |
337 | R | Methylation |
| 19011621 |
370 | K | Methylation |
| 17805299 |
370 | K | Methylation |
| 22864287 |
370 | K | Methylation |
| 17108971 |
370 | K | Methylation |
| 17108971 |
370 | K | ubiquitylation |
| 22864287 |
372 | K | Methylation |
| 15525938 |
372 | K | Methylation |
| 17108971 |
373 | K | Methylation |
| 20118233 |
382 | K | Acetylation |
| 20228809 |
382 | K | Acetylation |
| 20228809 |
382 | K | Methylation |
| 22864287 |
382 | K | Methylation |
| 17707234 |
382 | K | ubiquitylation |
| 22864287 |
386 | K | Sumoylation |
| 22214662 |
392 | S | Phosphorylation |
| 20959462 |
392 | S | Phosphorylation |
| 21317932 |
392 | S | Phosphorylation |
| 20959462 |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of P53_HUMAN !! |
Kegg Disease | |
---|---|
There are no disease associations of PTM sites. | |
OMIM Disease | |
Note=TP53 is found in increased amounts in a wide variety of transformed cells. TP53 is frequently mutated or inactivated in about 60% of cancers. TP53 defects are found in Barrett metaplasia a condition in which the normally stratified squamous epithelium of the lower esophagus is replaced by a metaplastic columnar epithelium. The condition develops as a complication in approximately 10% of patients with chronic gastroesophageal reflux disease and predisposes to the development of esophageal adenocarcinoma. | |
133239 | |
151623 | Li-Fraumeni syndrome (LFS) |
275355 | Squamous cell carcinoma of the head and neck (HNSCC) |
211980 | Lung cancer (LNCR) |
260500 | Papilloma of choroid plexus (CPP) |
202300 | Adrenocortical carcinoma (ADCC) |
614740 | Basal cell carcinoma 7 (BCC7) |
Kegg Drug | |
There are no disease associations of PTM sites. | |
DrugBank | |
DB00945 | Acetylsalicylic acid |
loading...
Acetylation | |
Reference | PubMed |
"BRD7 is a candidate tumour suppressor gene required for p53function."; Drost J., Mantovani F., Tocco F., Elkon R., Comel A., Holstege H.,Kerkhoven R., Jonkers J., Voorhoeve P.M., Agami R., Del Sal G.; Nat. Cell Biol. 12:380-389(2010). Cited for: INTERACTION WITH BRD7, AND ACETYLATION AT LYS-382. | |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-292; LYS-305; LYS-381 ANDLYS-382, AND MASS SPECTROMETRY. | |
"Identification and characterization of a novel p300-mediated p53acetylation site, lysine 305."; Wang Y.H., Tsay Y.G., Tan B.C., Lo W.Y., Lee S.C.; J. Biol. Chem. 278:25568-25576(2003). Cited for: ACETYLATION AT LYS-305. | |
"hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase."; Vaziri H., Dessain S.K., Ng Eaton E., Imai S., Frye R.A.,Pandita T.K., Guarente L., Weinberg R.A.; Cell 107:149-159(2001). Cited for: DEACETYLATION AT LYS-382 BY SIRT1. | |
"Post-translational modification of p53 protein in response toionizing radiation analyzed by mass spectrometry."; Abraham J., Kelly J., Thibault P., Benchimol S.; J. Mol. Biol. 295:853-864(2000). Cited for: ACETYLATION AT LYS-373 AND LYS-382. | |
Methylation | |
Reference | PubMed |
"G9a and Glp methylate lysine 373 in the tumor suppressor p53."; Huang J., Dorsey J., Chuikov S., Perez-Burgos L., Zhang X.,Jenuwein T., Reinberg D., Berger S.L.; J. Biol. Chem. 285:9636-9641(2010). Cited for: METHYLATION AT LYS-373, AND MUTAGENESIS OF LYS-373. | |
"Repression of p53 activity by Smyd2-mediated methylation."; Huang J., Perez-Burgos L., Placek B.J., Sengupta R., Richter M.,Dorsey J.A., Kubicek S., Opravil S., Jenuwein T., Berger S.L.; Nature 444:629-632(2006). Cited for: METHYLATION AT LYS-370, AND MUTAGENESIS OF LYS-370. | |
"The MBT repeats of L3MBTL1 link SET8-mediated p53 methylation atlysine 382 to target gene repression."; West L.E., Roy S., Lachmi-Weiner K., Hayashi R., Shi X., Appella E.,Kutateladze T.G., Gozani O.; J. Biol. Chem. 285:37725-37732(2010). Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 377-386, METHYLATION ATLYS-382, MUTAGENESIS OF LYS-382, AND INTERACTION WITH L3MBTL1. | |
"Modulation of p53 function by SET8-mediated methylation at lysine382."; Shi X., Kachirskaia I., Yamaguchi H., West L.E., Wen H., Wang E.W.,Dutta S., Appella E., Gozani O.; Mol. Cell 27:636-646(2007). Cited for: METHYLATION AT LYS-382, AND MUTAGENESIS OF LYS-382. | |
"Structural basis for the methylation site specificity of SET7/9."; Couture J.-F., Collazo E., Hauk G., Trievel R.C.; Nat. Struct. Mol. Biol. 13:140-146(2006). Cited for: MOTIF, AND METHYLATION AT LYS-372. | |
"Regulation of p53 activity through lysine methylation."; Chuikov S., Kurash J.K., Wilson J.R., Xiao B., Justin N., Ivanov G.S.,McKinney K., Tempst P., Prives C., Gamblin S.J., Barlev N.A.,Reinberg D.; Nature 432:353-360(2004). Cited for: METHYLATION AT LYS-372, AND MUTAGENESIS OF LYS-372. | |
Phosphorylation | |
Reference | PubMed |
"A new role of NUAK1: directly phosphorylating p53 and regulating cellproliferation."; Hou X., Liu J.E., Liu W., Liu C.Y., Liu Z.Y., Sun Z.Y.; Oncogene 30:2933-2942(2011). Cited for: INTERACTION WITH NUAK1, AND PHOSPHORYLATION AT SER-15 AND SER-392. | |
"Aurora B interacts with NIR-p53, leading to p53 phosphorylation inits DNA-binding domain and subsequent functional suppression."; Wu L., Ma C.A., Zhao Y., Jain A.; J. Biol. Chem. 286:2236-2244(2011). Cited for: FUNCTION, INTERACTION WITH AURKB AND NOC2L, PHOSPHORYLATION ATSER-183; SER-269 AND THR-284, CHARACTERIZATION OF VARIANT ALA-284,MUTAGENESIS OF SER-183 AND SER-269, AND MASS SPECTROMETRY. | |
"Isoform specific phosphorylation of p53 by protein kinase CK1."; Venerando A., Marin O., Cozza G., Bustos V.H., Sarno S., Pinna L.A.; Cell. Mol. Life Sci. 67:1105-1118(2010). Cited for: PHOSPHORYLATION AT SER-20 BY CSNK1D/CK1. | |
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313; SER-314 ANDSER-392, AND MASS SPECTROMETRY. | |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-315 ANDSER-392, AND MASS SPECTROMETRY. | |
"Serine 15 phosphorylation of p53 directs its interaction withB56gamma and the tumor suppressor activity of B56gamma-specificprotein phosphatase 2A."; Shouse G.P., Cai X., Liu X.; Mol. Cell. Biol. 28:448-456(2008). Cited for: INTERACTION WITH PPP2CA; PPP2R1A AND PPP2R5C, PHOSPHORYLATION ATSER-15 BY ATM, AND MUTAGENESIS OF SER-15. | |
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND MASSSPECTROMETRY. | |
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND MASSSPECTROMETRY. | |
"Stabilization and activation of p53 induced by Cdk5 contributes toneuronal cell death."; Lee J.-H., Kim H.-S., Lee S.-J., Kim K.-T.; J. Cell Sci. 120:2259-2271(2007). Cited for: PHOSPHORYLATION AT SER-15; SER-33 AND SER-46, INTERACTION WITH CDK5,AND SUBCELLULAR LOCATION. | |
"Novel homeodomain-interacting protein kinase family member, HIPK4,phosphorylates human p53 at serine 9."; Arai S., Matsushita A., Du K., Yagi K., Okazaki Y., Kurokawa R.; FEBS Lett. 581:5649-5657(2007). Cited for: PHOSPHORYLATION AT SER-9. | |
"PRAK is essential for ras-induced senescence and tumor suppression."; Sun P., Yoshizuka N., New L., Moser B.A., Li Y., Liao R., Xie C.,Chen J., Deng Q., Yamout M., Dong M.Q., Frangou C.G., Yates J.R. III,Wright P.E., Han J.; Cell 128:295-308(2007). Cited for: PHOSPHORYLATION AT SER-37, AND MUTAGENESIS OF SER-37. | |
"Protein kinase C delta regulates Ser46 phosphorylation of p53 tumorsuppressor in the apoptotic response to DNA damage."; Yoshida K., Liu H., Miki Y.; J. Biol. Chem. 281:5734-5740(2006). Cited for: PHOSPHORYLATION AT SER-46, AND INTERACTION WITH PRKCG. | |
"LKB1 is recruited to the p21/WAF1 promoter by p53 to mediatetranscriptional activation."; Zeng P.Y., Berger S.L.; Cancer Res. 66:10701-10708(2006). Cited for: INTERACTION WITH STK11/LKB1, AND PHOSPHORYLATION AT SER-15 ANDSER-392. | |
"AMP-activated protein kinase induces a p53-dependent metaboliccheckpoint."; Jones R.G., Plas D.R., Kubek S., Buzzai M., Mu J., Xu Y.,Birnbaum M.J., Thompson C.B.; Mol. Cell 18:283-293(2005). Cited for: PHOSPHORYLATION AT SER-15. | |
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, AND MASSSPECTROMETRY. | |
"Tumor suppressor SMAR1 activates and stabilizes p53 through itsarginine-serine-rich motif."; Jalota-Badhwar A., Singh K., Pavithra L., Kaul-Ghanekar R., Jameel S.,Chattopadhyay S.; J. Biol. Chem. 280:16019-16029(2005). Cited for: INTERACTION WITH BANP, SUBCELLULAR LOCATION, AND PHOSPHORYLATION ATSER-15. | |
"Phosphorylation by aurora kinase A induces Mdm2-mediateddestabilization and inhibition of p53."; Katayama H., Sasai K., Kawai H., Yuan Z.M., Bondaruk J., Suzuki F.,Fujii S., Arlinghaus R.B., Czerniak B.A., Sen S.; Nat. Genet. 36:55-62(2004). Cited for: INTERACTION WITH AURKA, AND PHOSPHORYLATION AT SER-315. | |
"The promyelocytic leukemia protein protects p53 from Mdm2-mediatedinhibition and degradation."; Louria-Hayon I., Grossman T., Sionov R.V., Alsheich O., Pandolfi P.P.,Haupt Y.; J. Biol. Chem. 278:33134-33141(2003). Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHEK2 AND PML,UBIQUITINATION BY MDM2, AND PHOSPHORYLATION AT SER-20. | |
"Homeodomain-interacting protein kinase-2 phosphorylates p53 at Ser 46and mediates apoptosis."; D'Orazi G., Cecchinelli B., Bruno T., Manni I., Higashimoto Y.,Saito S., Gostissa M., Coen S., Marchetti A., Del Sal G., Piaggio G.,Fanciulli M., Appella E., Soddu S.; Nat. Cell Biol. 4:11-19(2002). Cited for: INTERACTION WITH HIPK2, AND PHOSPHORYLATION AT SER-46. | |
"Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2."; Hofmann T.G., Moeller A., Sirma H., Zentgraf H., Taya Y., Droege W.,Will H., Schmitz M.L.; Nat. Cell Biol. 4:1-10(2002). Cited for: INTERACTION WITH HIPK2, PHOSPHORYLATION AT SER-46, AND MUTAGENESIS OFSER-46 AND LYS-382. | |
"A DNA damage-induced p53 serine 392 kinase complex contains CK2,hSpt16, and SSRP1."; Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H.,Goodman R., Lozano G., Zhao Y., Lu H.; Mol. Cell 7:283-292(2001). Cited for: PHOSPHORYLATION AT SER-392. | |
"Plk3 functionally links DNA damage to cell cycle arrest and apoptosisat least in part via the p53 pathway."; Xie S., Wu H., Wang Q., Cogswell J.P., Husain I., Conn C.,Stambrook P., Jhanwar-Uniyal M., Dai W.; J. Biol. Chem. 276:43305-43312(2001). Cited for: PHOSPHORYLATION AT SER-20 BY PLK3. | |
"Reactive oxygen species-induced phosphorylation of p53 on serine 20is mediated in part by polo-like kinase-3."; Xie S., Wang Q., Wu H., Cogswell J., Lu L., Jhanwar-Uniyal M., Dai W.; J. Biol. Chem. 276:36194-36199(2001). Cited for: PHOSPHORYLATION AT SER-20 BY PLK3. | |
"Cell cycle regulation via p53 phosphorylation by a 5'-AMP activatedprotein kinase activator, 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside, in a human hepatocellular carcinoma cell line."; Imamura K., Ogura T., Kishimoto A., Kaminishi M., Esumi H.; Biochem. Biophys. Res. Commun. 287:562-567(2001). Cited for: PHOSPHORYLATION AT SER-15. | |
"The C-terminal regulatory domain of p53 contains a functional dockingsite for cyclin A."; Luciani M.G., Hutchins J.R.A., Zheleva D., Hupp T.R.; J. Mol. Biol. 300:503-518(2000). Cited for: PHOSPHORYLATION AT SER-315 AND SER-392 BY CDK2, AND MUTAGENESIS OFLYS-382; LEU-383 AND PHE-385. | |
"Phosphorylation of Ser-20 mediates stabilization of human p53 inresponse to DNA damage."; Chehab N.H., Malikzay A., Stavridi E.S., Halazonetis T.D.; Proc. Natl. Acad. Sci. U.S.A. 96:13777-13782(1999). Cited for: PHOSPHORYLATION AT SER-15 AND SER-20, INDUCTION BY DNA DAMAGE,CHARACTERIZATION OF LFS VARIANT HIS-273, MUTAGENESIS OF THR-18; SER-20AND 22-LEU-TRP-23, SUBCELLULAR LOCATION, AND INTERACTION WITH PML ANDMDM2. | |
"p53 is phosphorylated by CDK7-cyclin H in a p36MAT1-dependentmanner."; Ko L.J., Shieh S.-Y., Chen X., Jayaraman L., Tamai K., Taya Y.,Prives C., Pan Z.-Q.; Mol. Cell. Biol. 17:7220-7229(1997). Cited for: PHOSPHORYLATION AT SER-33. | |
"G-protein-coupled receptor kinase 5 phosphorylates p53 and inhibitsDNA damage-induced apoptosis."; Chen X., Zhu H., Yuan M., Fu J., Zhou Y., Ma L.; J. Biol. Chem. 285:12823-12830(2010). Cited for: PHOSPHORYLATION AT THR-55, AND INTERACTION WITH GRK5. | |
"The subcellular localization of vaccinia-related kinase-2 (VRK2)isoforms determines their different effect on p53 stability in tumourcell lines."; Blanco S., Klimcakova L., Vega F.M., Lazo P.A.; FEBS J. 273:2487-2504(2006). Cited for: PHOSPHORYLATION AT THR-18. | |
"Phosphorylation on Thr-55 by TAF1 mediates degradation of p53: a rolefor TAF1 in cell G1 progression."; Li H.-H., Li A.G., Sheppard H.M., Liu X.; Mol. Cell 13:867-878(2004). Cited for: PHOSPHORYLATION AT THR-55, MUTAGENESIS OF THR-55, AND INTERACTION WITHTAF1. | |
"The human vaccinia-related kinase 1 (VRK1) phosphorylates threonine-18 within the mdm-2 binding site of the p53 tumour suppressorprotein."; Lopez-Borges S., Lazo P.A.; Oncogene 19:3656-3664(2000). Cited for: PHOSPHORYLATION AT THR-18. | |
"Protein kinase CK1 is a p53-threonine 18 kinase which requires priorphosphorylation of serine 15."; Dumaz N., Milne D.M., Meek D.W.; FEBS Lett. 463:312-316(1999). Cited for: PHOSPHORYLATION AT THR-18 BY CSNK1D/CK1. | |
Sumoylation | |
Reference | PubMed |
"SUMO-1 conjugation in vivo requires both a consensus modificationmotif and nuclear targeting."; Rodriguez M.S., Dargemont C., Hay R.T.; J. Biol. Chem. 276:12654-12659(2001). Cited for: SUMOYLATION AT LYS-386, SUBCELLULAR LOCATION, AND MUTAGENESIS OFPHE-385; LYS-386; THR-387 AND GLU-388. | |
Ubiquitylation | |
Reference | PubMed |
"Differential regulation of p53 and p21 by MKRN1 E3 ligase controlscell cycle arrest and apoptosis."; Lee E.-W., Lee M.-S., Camus S., Ghim J., Yang M.-R., Oh W., Ha N.-C.,Lane D.P., Song J.; EMBO J. 28:2100-2113(2009). Cited for: INTERACTION WITH MKRN1, MUTAGENESIS OF 291-LYS-LYS-292, ANDUBIQUITINATION AT LYS-291 AND LYS-292 BY MKRN1. |