logo CaMPDB: Calpain for Modulatory Proteolysis Database

SB0053 : p53

[ CaMP Format ]

* Basic Information

OrganismHomo sapiens (human)
Protein Namescellular tumor antigen p53 isoform a [Homo sapiens]; cellular tumor antigen p53 isoform a; tumor protein 53; mutant tumor protein 53; cellular tumor antigen p53; phosphoprotein p53; transformation-related protein 53; p53 tumor suppressor; antigen NY-CO-13; Cellular tumor antigen p53; Antigen NY-CO-13; Phosphoprotein p53; Tumor suppressor p53
Gene NamesTP53; P53; tumor protein p53
Gene Locus17p13.1; chromosome 17
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
NP_000537 NM_000546 7157 P04637 191170 HGNC:11998 N/A hsa:7157

* Information From OMIM

Description: The transcription factor p53 responds to diverse cellular stresses to regulate target genes that induce cell cycle arrest, apoptosis, senescence, DNA repair, or changes in metabolism. In addition, p53 appears to induce apoptosis through nontranscriptional cytoplasmic processes. In unstressed cells, p53 is kept inactive essentially through the actions of the ubiquitin ligase MDM2 (OMIM:164785), which inhibits p53 transcriptional activity and ubiquitinates p53 to promote its degradation. Numerous posttranslational modifications modulate p53 activity, most notably phosphorylation and acetylation. Several less abundant p53 isoforms also modulate p53 activity. Activity of p53 is ubiquitously lost in human cancer either by mutation of the p53 gene itself or by loss of cell signaling upstream or downstream of p53 (Toledo and Wahl, 2006; Bourdon, 2007; Vousden and Lane, 2007).

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* Structure Information

1. Primary Information

Length: 393 aa

Average Mass: 43.653 kDa

Monoisotopic Mass: 43.625 kDa

2. Domain Information

Annotated Domains: interpro / pfam / smart / prosite

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
P53 transactivation motif 1. 5291.05.3
--- cleavage 25 (inside P53 transactivation motif 5..29) ---
DEC-1 protein, N-terminal region 1. 6695121.06.4
P53 tetramerisation motif 1. 3193571.01.6

3. Sequence Information

Fasta Sequence: SB0053.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Known Structures in PDB: 1A1U (NMR; -; A/C=324-358), 1AIE (X-ray; 150 A; A=326-356), 1C26 (X-ray; 170 A; A=325-356), 1DT7 (NMR; -; X/Y=367-388), 1GZH (X-ray; 260 A; A/C=95-292), 1H26 (X-ray; 224 A; E=376-386), 1HS5 (NMR; -; A/B=324-357), 1JSP (NMR; -; A=367-386), 1KZY (X-ray; 250 A; A/B=95-289), 1MA3 (X-ray; 200 A; B=372-389), 1OLG (NMR; -; A/B/C/D=319-360), 1OLH (NMR; -; A/B/C/D=319-360), 1PES (NMR; -; A/B/C/D=325-355), 1PET (NMR; -; A/B/C/D=325-355), 1SAE (NMR; -; A/B/C/D=319-360), 1SAF (NMR; -; A/B/C/D=319-360), 1SAK (NMR; -; A/B/C/D=319-360), 1SAL (NMR; -; A/B/C/D=319-360), 1TSR (X-ray; 220 A; A/B/C=94-312), 1TUP (X-ray; 220 A; A/B/C=94-312), 1UOL (X-ray; 190 A; A/B=94-312), 1XQH (X-ray; 175 A; B/F=369-377), 1YC5 (X-ray; 140 A; B=372-389), 1YCQ (X-ray; 230 A; B=13-29), 1YCR (X-ray; 260 A; B=15-29), 1YCS (X-ray; 220 A; A=94-292), 2AC0 (X-ray; 180 A; A/B/C/D=94-293), 2ADY (X-ray; 250 A; A/B=94-293), 2AHI (X-ray; 185 A; A/B/C/D=94-293), 2ATA (X-ray; 220 A; A/B/C/D=94-293), 2B3G (X-ray; 160 A; B=33-60), 2BIM (X-ray; 198 A; A/B=94-312), 2BIN (X-ray; 190 A; A=94-312), 2BIO (X-ray; 190 A; A=94-312), 2BIP (X-ray; 180 A; A=94-312), 2BIQ (X-ray; 180 A; A=94-312), 2F1X (X-ray; 230 A; A/B=359-368), 2FEJ (NMR; -; A=94-297), 2FOJ (X-ray; 160 A; B=361-367), 2FOO (X-ray; 220 A; B=358-363), 2GS0 (NMR; -; B=20-73), 2H1L (X-ray; 316 A; M/N/O/P/Q/R/S/T/U/V/W/X=92-292), 2H2D (X-ray; 170 A; B=372-389), 2H2F (X-ray; 220 A; B=372-389), 2H4F (X-ray; 200 A; D=372-389), 2H4H (X-ray; 199 A; B=372-389), 2H4J (X-ray; 210 A; D=372-389), 2H59 (X-ray; 190 A; D/E=372-389), 2J0Z (NMR; -; A/B/C/D=326-356), 2J10 (NMR; -; A/B/C/D=326-356), 2J11 (NMR; -; A/B/C/D=326-356), 2J1W (X-ray; 180 A; A/B=94-312), 2J1X (X-ray; 165 A; A/B=94-312), 2J1Y (X-ray; 169 A; A/B/C/D=94-293), 2J1Z (X-ray; 180 A; A/B=94-312), 2J20 (X-ray; 180 A; A/B=94-312), 2J21 (X-ray; 160 A; A/B=94-312), 2K8F (NMR; -; B=1-39), 2L14 (NMR; -; B=13-61), 2LY4 (NMR; -; B=1-93), 2MEJ (NMR; -; B=96-312), 2MWO (NMR; -; B=363-377), 2MWP (NMR; -; B=376-387), 2MZD (NMR; -; B=35-59), 2OCJ (X-ray; 205 A; A/B/C/D=94-312), 2PCX (X-ray; 154 A; A=94-292), 2RUK (NMR; -; A=41-62), 2VUK (X-ray; 150 A; A/B=94-312), 2WGX (X-ray; 175 A; A/B=94-312), 2X0U (X-ray; 160 A; A/B=94-312), 2X0V (X-ray; 180 A; A/B=94-312), 2X0W (X-ray; 210 A; A/B=94-312), 2XWR (X-ray; 168 A; A/B=89-293), 2YBG (X-ray; 190 A; A/B/C/D=94-293), 2YDR (X-ray; 275 A; P=144-154), 2Z5S (X-ray; 230 A; P/Q/R=15-29), 2Z5T (X-ray; 230 A; P/Q/R=15-29), 3D05 (X-ray; 170 A; A=94-293), 3D06 (X-ray; 120 A; A=94-293), 3D07 (X-ray; 220 A; A/B=94-293), 3D08 (X-ray; 140 A; A=94-293), 3D09 (X-ray; 190 A; A=94-293), 3D0A (X-ray; 180 A; A/B/C/D=94-293), 3DAB (X-ray; 190 A; B/D/F/H=15-29), 3DAC (X-ray; 180 A; B/P=17-37), 3IGK (X-ray; 170 A; A=94-293), 3IGL (X-ray; 180 A; A=94-293), 3KMD (X-ray; 215 A; A/B/C/D=92-291), 3KZ8 (X-ray; 191 A; A/B=94-293), 3LW1 (X-ray; 128 A; P=385-393), 3OQ5 (X-ray; 250 A; D/E=377-386), 3PDH (X-ray; 180 A; D=372-389), 3Q01 (X-ray; 210 A; A/B=94-356), 3Q05 (X-ray; 240 A; A/B/C/D=94-356), 3Q06 (X-ray; 320 A; A/B/C/D=96-354), 3SAK (NMR; -; A/B/C/D=319-360), 3TG5 (X-ray; 230 A; B=365-375), 3TS8 (X-ray; 280 A; A/B/C/D=94-356), 3ZME (X-ray; 135 A; A/B=94-312), 4AGL (X-ray; 170 A; A/B=94-312), 4AGM (X-ray; 152 A; A/B=94-312), 4AGN (X-ray; 160 A; A/B=94-312), 4AGO (X-ray; 145 A; A/B=94-312), 4AGP (X-ray; 150 A; A/B=94-312), 4AGQ (X-ray; 142 A; A/B=94-312), 4BUZ (X-ray; 190 A; P=379-386), 4BV2 (X-ray; 330 A; E/H=376-388), 4HFZ (X-ray; 269 A; B/D=15-29), 4HJE (X-ray; 191 A; A/B/C/D=92-291), 4IBQ (X-ray; 180 A; A/B/C/D=94-293), 4IBS (X-ray; 178 A; A/B/C/D=94-293), 4IBT (X-ray; 170 A; A/B/C/D=94-293), 4IBU (X-ray; 170 A; A/B/C/D=94-293), 4IBV (X-ray; 210 A; A=94-293), 4IBW (X-ray; 179 A; A=94-293), 4IBY (X-ray; 145 A; A/B=94-293), 4IBZ (X-ray; 192 A; A/B/C/D=94-293), 4IJT (X-ray; 178 A; A=94-293), 4KVP (X-ray; 150 A; A/B/C/D=94-312), 4LO9 (X-ray; 250 A; A/B/C/D=94-312), 4LOE (X-ray; 185 A; A/B/C/D=94-312), 4LOF (X-ray; 200 A; A=94-312), 4MZI (X-ray; 125 A; A=94-292), 4MZR (X-ray; 290 A; A/B/C/D=94-388), 4QO1 (X-ray; 192 A; B=92-312)

* Cleavage Information

1 [sites]

Source Reference: [PubMed ID: 9111352] Pariat M, Carillo S, Molinari M, Salvat C, Debussche L, Bracco L, Milner J, Piechaczyk M, Proteolysis by calpains: a possible contribution to degradation of p53. Mol Cell Biol. 1997 May;17(5):2806-15.

Cleavage sites (±10aa)


Leu25 Leu

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)

* References

[PubMed ID: 21112961] Marcel V, Tran PL, Sagne C, Martel-Planche G, Vaslin L, Teulade-Fichou MP, Hall J, Mergny JL, Hainaut P, Van Dyck E, G-quadruplex structures in TP53 intron 3: role in alternative splicing and in production of p53 mRNA isoforms. Carcinogenesis. 2011 Mar;32(3):271-8. doi: 10.1093/carcin/bgq253. Epub 2010 Nov

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