Protein:MDM2 |
Protein Summary |
 Gene summary |
| Gene name: MDM2 | ASpdb.0 ID: 4193 | Gene | Gene symbol | MDM2 | Gene ID | 4193 |
| Gene name | MDM2 proto-oncogene |
| Synonyms | ACTFS|HDMX|LSKB|hdm2 |
| Cytomap | 12q15 |
| Type of gene | protein-coding |
| Description | E3 ubiquitin-protein ligase Mdm2MDM2 oncogene, E3 ubiquitin protein ligaseMDM2 proto-oncogene, E3 ubiquitin protein ligaseMdm2, p53 E3 ubiquitin protein ligase homologMdm2, transformed 3T3 cell double minute 2, p53 binding proteindouble minute 2, hum |
| Modification date | 20240407 |
| UniProtAcc | Q00987 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | MDM2 | GO:0000122 | negative regulation of transcription by RNA polymerase II | 9271120|17310983 |
| Gene | MDM2 | GO:0004842 | ubiquitin-protein transferase activity | 9450543 |
| Gene | MDM2 | GO:0005634 | nucleus | 10360174|29295817|30879903 |
| Gene | MDM2 | GO:0005654 | nucleoplasm | 10707090|12915590 |
| Gene | MDM2 | GO:0005730 | nucleolus | 10707090|22869143 |
| Gene | MDM2 | GO:0005737 | cytoplasm | 30879903 |
| Gene | MDM2 | GO:0006511 | ubiquitin-dependent protein catabolic process | 11278372|15314173|16173922|17310983 |
| Gene | MDM2 | GO:0006915 | apoptotic process | 30879903 |
| Gene | MDM2 | GO:0008097 | 5S rRNA binding | 24120868 |
| Gene | MDM2 | GO:0008270 | zinc ion binding | 10722742 |
| Gene | MDM2 | GO:0016567 | protein ubiquitination | 9450543|15878855|19656744|20153724 |
| Gene | MDM2 | GO:0016604 | nuclear body | 10360174 |
| Gene | MDM2 | GO:0016874 | ligase activity | 17142452 |
| Gene | MDM2 | GO:0031648 | protein destabilization | 9529249|10360174|15314173 |
| Gene | MDM2 | GO:0032436 | positive regulation of proteasomal ubiquitin-dependent protein catabolic process | 11278372 |
| Gene | MDM2 | GO:0032991 | protein-containing complex | 9529249|17310983 |
| Gene | MDM2 | GO:0034504 | protein localization to nucleus | 10360174 |
| Gene | MDM2 | GO:0042176 | regulation of protein catabolic process | 9153395 |
| Gene | MDM2 | GO:0043021 | ribonucleoprotein complex binding | 24120868 |
| Gene | MDM2 | GO:0043130 | ubiquitin binding | 29295817 |
| Gene | MDM2 | GO:0043518 | negative regulation of DNA damage response, signal transduction by p53 class mediator | 9529249|10360174 |
| Gene | MDM2 | GO:0045184 | establishment of protein localization | 10360174 |
| Gene | MDM2 | GO:0045892 | negative regulation of DNA-templated transcription | 9271120 |
| Gene | MDM2 | GO:0051726 | regulation of cell cycle | 9529249 |
| Gene | MDM2 | GO:0061630 | ubiquitin protein ligase activity | 15314173|17310983 |
| Gene | MDM2 | GO:0065003 | protein-containing complex assembly | 10608892|12915590 |
| Gene | MDM2 | GO:0071480 | cellular response to gamma radiation | 16213212 |
| Gene | MDM2 | GO:0072717 | cellular response to actinomycin D | 15314173 |
| Gene | MDM2 | GO:1901797 | negative regulation of signal transduction by p53 class mediator | 16173922 |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| Q00987-1 | Q00987-1_4hbm_A.pdb | 4HBM | X-ray | 1.9 | A | 6 | 111 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| Q00987 | MDM2 | Q00987-1 | Q00987-10 | 491 | 436 | 115 | 169 | Deletion | none | none | 114 | 114 |
| Q00987 | MDM2 | Q00987-1 | Q00987-11 | 491 | 497 | 1 | 1 | Substitution | M | MVRSRQM | 1 | 7 |
| Q00987 | MDM2 | Q00987-1 | Q00987-2 | 491 | 296 | 28 | 222 | Deletion | none | none | 27 | 27 |
| Q00987 | MDM2 | Q00987-1 | Q00987-3 | 491 | 270 | 28 | 222 | Deletion | none | none | 27 | 27 |
| Q00987 | MDM2 | Q00987-1 | Q00987-3 | 491 | 270 | 275 | 300 | Deletion | none | none | 79 | 79 |
| Q00987 | MDM2 | Q00987-1 | Q00987-4 | 491 | 218 | 28 | 300 | Deletion | none | none | 27 | 27 |
| Q00987 | MDM2 | Q00987-1 | Q00987-5 | 491 | 321 | 53 | 222 | Deletion | none | none | 52 | 52 |
| Q00987 | MDM2 | Q00987-1 | Q00987-6 | 491 | 132 | 30 | 388 | Deletion | none | none | 29 | 29 |
| Q00987 | MDM2 | Q00987-1 | Q00987-7 | 491 | 102 | 76 | 102 | Substitution | YCSNDLLGDLFGVPSFSVKEHRKIYTM | NDCANLFPLVDLSIRELYISNYITLGI | 76 | 102 |
| Q00987 | MDM2 | Q00987-1 | Q00987-7 | 491 | 102 | 103 | 491 | Deletion | none | none | 102 | 102 |
| Q00987 | MDM2 | Q00987-1 | Q00987-8 | 491 | 430 | 1 | 61 | Deletion | none | none | 0 | 0 |
| Q00987 | MDM2 | Q00987-1 | Q00987-9 | 491 | 446 | 53 | 97 | Deletion | none | none | 52 | 52 |
| Multiple sequence alignment of our canonical and alternatively spliced MDM2 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of MDM2 |
| UniProt-id | ENSG | ENST | ENSP |
| Q00987-1 | ENSG00000135679.27 | ENST00000539479.6 | ENSP00000444430.2 |
| Q00987-11 | ENSG00000135679.27 | ENST00000258149.11 | ENSP00000258149.6 |
| Q00987-2 | ENSG00000135679.27 | ENST00000360430.6 | ENSP00000353611.2 |
| Q00987-4 | ENSG00000135679.27 | ENST00000393413.7 | ENSP00000377065.3 |
| Q00987-5 | ENSG00000135679.27 | ENST00000299252.8 | ENSP00000299252.4 |
| UniProt-id | NM ID | NP ID |
| Q00987-11 | NM_002392.5 | NP_002383.2 |
| Q00987-5 | NM_001278462.1 | NP_001265391.1 |
| Amino acid sequences of our canonical and alternatively spliced MDM2 |
| accession_id | Protein sequence |
| Q00987-1 | MCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVYCSNDLLGDLFGVPS FSVKEHRKIYTMIYRNLVVVNQQESSDSGTSVSENRCHLEGGSDQKDLVQELQEEKPSSSHLVSRPSTSSRRRAISETEENSDELSGERQ RKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLDAGVSEHSGDWLDQDSVSDQFSVEFEVESLDSEDYSLSEEGQELSD EDDEVYQVTVYQAGESDTDSFEEDPEISLADYWKCTSCNEMNPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVP DCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQDKEESVESSLPLNAIEPCVICQGRPKNGCI |
| Q00987-10 | MCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVYCSNDLLGDLFGVPS FSVKEHRKIYTMIYRNLVVVNQQEENSDELSGERQRKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLDAGVSEHSGDW LDQDSVSDQFSVEFEVESLDSEDYSLSEEGQELSDEDDEVYQVTVYQAGESDTDSFEEDPEISLADYWKCTSCNEMNPPLPSHCNRCWAL RENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVPDCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFE |
| Q00987-11 | MVRSRQMCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVYCSNDLLGD LFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDSGTSVSENRCHLEGGSDQKDLVQELQEEKPSSSHLVSRPSTSSRRRAISETEENSDE LSGERQRKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLDAGVSEHSGDWLDQDSVSDQFSVEFEVESLDSEDYSLSEE GQELSDEDDEVYQVTVYQAGESDTDSFEEDPEISLADYWKCTSCNEMNPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAE EGFDVPDCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQDKEESVESSLPLNAIEPCVICQGR |
| Q00987-2 | MCNTNMSVPTDGAVTTSQIPASEQETLDLDAGVSEHSGDWLDQDSVSDQFSVEFEVESLDSEDYSLSEEGQELSDEDDEVYQVTVYQAGE SDTDSFEEDPEISLADYWKCTSCNEMNPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVPDCKKTIVNDSRESCV EENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQDKEESVESSLPLNAIEPCVICQGRPKNGCIVHGKTGHLMACFTCA |
| Q00987-3 | MCNTNMSVPTDGAVTTSQIPASEQETLDLDAGVSEHSGDWLDQDSVSDQFSVEFEVESLDSEDYSLSEEGQELSDEDDEDYWKCTSCNEM NPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVPDCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSS SIIYSSQEDVKEFEREETQDKEESVESSLPLNAIEPCVICQGRPKNGCIVHGKTGHLMACFTCAKKLKKRNKPCPVCRQPIQMIVLTYFP |
| Q00987-4 | MCNTNMSVPTDGAVTTSQIPASEQETLDYWKCTSCNEMNPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVPDCK KTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQDKEESVESSLPLNAIEPCVICQGRPKNGCIVHG |
| Q00987-5 | MCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEDLDAGVSEHSGDWLDQDSVSDQFSVEFEVESLDSEDYS LSEEGQELSDEDDEVYQVTVYQAGESDTDSFEEDPEISLADYWKCTSCNEMNPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENS TQAEEGFDVPDCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQDKEESVESSLPLNAIEPCVI |
| Q00987-6 | MCNTNMSVPTDGAVTTSQIPASEQETLVRQESEDYSQPSTSSSIIYSSQEDVKEFEREETQDKEESVESSLPLNAIEPCVICQGRPKNGC |
| Q00987-7 | MCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVNDCANLFPLVDLSIR |
| Q00987-8 | MTKRLYDEKQQHIVYCSNDLLGDLFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDSGTSVSENRCHLEGGSDQKDLVQELQEEKPSSSH LVSRPSTSSRRRAISETEENSDELSGERQRKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLDAGVSEHSGDWLDQDSV SDQFSVEFEVESLDSEDYSLSEEGQELSDEDDEVYQVTVYQAGESDTDSFEEDPEISLADYWKCTSCNEMNPPLPSHCNRCWALRENWLP EDKGKDKGEISEKAKLENSTQAEEGFDVPDCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQD |
| Q00987-9 | MCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEKIYTMIYRNLVVVNQQESSDSGTSVSENRCHLEGGSDQ KDLVQELQEEKPSSSHLVSRPSTSSRRRAISETEENSDELSGERQRKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLD AGVSEHSGDWLDQDSVSDQFSVEFEVESLDSEDYSLSEEGQELSDEDDEVYQVTVYQAGESDTDSFEEDPEISLADYWKCTSCNEMNPPL PSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVPDCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIY |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| MDM2 (go to UniProt):Q00987 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Q00987 | Domain | 26 | 109 | Note=SWIB/MDM2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01273 | Type=Deletion;Start=28;End=222 |
| Q00987 | Domain | 26 | 109 | Note=SWIB/MDM2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01273 | Type=Deletion;Start=28;End=222 |
| Q00987 | Domain | 26 | 109 | Note=SWIB/MDM2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01273 | Type=Deletion;Start=28;End=300 |
| Q00987 | Domain | 26 | 109 | Note=SWIB/MDM2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01273 | Type=Deletion;Start=53;End=222 |
| Q00987 | Domain | 26 | 109 | Note=SWIB/MDM2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01273 | Type=Deletion;Start=30;End=388 |
| Q00987 | Domain | 26 | 109 | Note=SWIB/MDM2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01273 | Type=Substitution;Start=76;End=102 |
| Q00987 | Domain | 26 | 109 | Note=SWIB/MDM2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01273 | Type=Deletion;Start=103;End=491 |
| Q00987 | Domain | 26 | 109 | Note=SWIB/MDM2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01273 | Type=Deletion;Start=1;End=61 |
| Q00987 | Domain | 26 | 109 | Note=SWIB/MDM2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01273 | Type=Deletion;Start=53;End=97 |
| Q00987 | Zinc finger | 299 | 328 | Note=RanBP2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00322 | Type=Deletion;Start=275;End=300 |
| Q00987 | Zinc finger | 299 | 328 | Note=RanBP2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00322 | Type=Deletion;Start=28;End=300 |
| Q00987 | Zinc finger | 299 | 328 | Note=RanBP2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00322 | Type=Deletion;Start=30;End=388 |
| Q00987 | Zinc finger | 299 | 328 | Note=RanBP2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00322 | Type=Deletion;Start=103;End=491 |
| Q00987 | Zinc finger | 438 | 479 | Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 | Type=Deletion;Start=103;End=491 |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Substitution;Start=1;End=1 |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=28;End=222 |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=28;End=222 |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=28;End=300 |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=53;End=222 |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=30;End=388 |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Substitution;Start=76;End=102 |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=103;End=491 |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=1;End=61 |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=53;End=97 |
| Q00987 | Region | 1 | 101 | Note=Sufficient to promote the mitochondrial pathway of apoptosis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30879903;Dbxref=PMID:30879903 | Type=Substitution;Start=1;End=1 |
| Q00987 | Region | 1 | 101 | Note=Sufficient to promote the mitochondrial pathway of apoptosis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30879903;Dbxref=PMID:30879903 | Type=Deletion;Start=28;End=222 |
| Q00987 | Region | 1 | 101 | Note=Sufficient to promote the mitochondrial pathway of apoptosis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30879903;Dbxref=PMID:30879903 | Type=Deletion;Start=28;End=222 |
| Q00987 | Region | 1 | 101 | Note=Sufficient to promote the mitochondrial pathway of apoptosis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30879903;Dbxref=PMID:30879903 | Type=Deletion;Start=28;End=300 |
| Q00987 | Region | 1 | 101 | Note=Sufficient to promote the mitochondrial pathway of apoptosis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30879903;Dbxref=PMID:30879903 | Type=Deletion;Start=53;End=222 |
| Q00987 | Region | 1 | 101 | Note=Sufficient to promote the mitochondrial pathway of apoptosis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30879903;Dbxref=PMID:30879903 | Type=Deletion;Start=30;End=388 |
| Q00987 | Region | 1 | 101 | Note=Sufficient to promote the mitochondrial pathway of apoptosis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30879903;Dbxref=PMID:30879903 | Type=Substitution;Start=76;End=102 |
| Q00987 | Region | 1 | 101 | Note=Sufficient to promote the mitochondrial pathway of apoptosis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30879903;Dbxref=PMID:30879903 | Type=Deletion;Start=1;End=61 |
| Q00987 | Region | 1 | 101 | Note=Sufficient to promote the mitochondrial pathway of apoptosis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30879903;Dbxref=PMID:30879903 | Type=Deletion;Start=53;End=97 |
| Q00987 | Region | 141 | 187 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=115;End=169 |
| Q00987 | Region | 141 | 187 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=28;End=222 |
| Q00987 | Region | 141 | 187 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=28;End=222 |
| Q00987 | Region | 141 | 187 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=28;End=300 |
| Q00987 | Region | 141 | 187 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=53;End=222 |
| Q00987 | Region | 141 | 187 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=388 |
| Q00987 | Region | 141 | 187 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=103;End=491 |
| Q00987 | Region | 150 | 230 | "Note=Interaction with PYHIN1 and necessary for interaction with RFFL and RNF34;Ontology_term=ECO:0000269 | ECO:0000269;evidence=ECO:0000269|PubMed:16479015 |
| Q00987 | Region | 150 | 230 | "Note=Interaction with PYHIN1 and necessary for interaction with RFFL and RNF34;Ontology_term=ECO:0000269 | ECO:0000269;evidence=ECO:0000269|PubMed:16479015 |
| Q00987 | Region | 150 | 230 | "Note=Interaction with PYHIN1 and necessary for interaction with RFFL and RNF34;Ontology_term=ECO:0000269 | ECO:0000269;evidence=ECO:0000269|PubMed:16479015 |
| Q00987 | Region | 150 | 230 | "Note=Interaction with PYHIN1 and necessary for interaction with RFFL and RNF34;Ontology_term=ECO:0000269 | ECO:0000269;evidence=ECO:0000269|PubMed:16479015 |
| Q00987 | Region | 150 | 230 | "Note=Interaction with PYHIN1 and necessary for interaction with RFFL and RNF34;Ontology_term=ECO:0000269 | ECO:0000269;evidence=ECO:0000269|PubMed:16479015 |
| Q00987 | Region | 150 | 230 | "Note=Interaction with PYHIN1 and necessary for interaction with RFFL and RNF34;Ontology_term=ECO:0000269 | ECO:0000269;evidence=ECO:0000269|PubMed:16479015 |
| Q00987 | Region | 150 | 230 | "Note=Interaction with PYHIN1 and necessary for interaction with RFFL and RNF34;Ontology_term=ECO:0000269 | ECO:0000269;evidence=ECO:0000269|PubMed:16479015 |
| Q00987 | Region | 170 | 306 | Note=Interaction with MTBP;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=28;End=222 |
| Q00987 | Region | 170 | 306 | Note=Interaction with MTBP;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=28;End=222 |
| Q00987 | Region | 170 | 306 | Note=Interaction with MTBP;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=275;End=300 |
| Q00987 | Region | 170 | 306 | Note=Interaction with MTBP;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=28;End=300 |
| Q00987 | Region | 170 | 306 | Note=Interaction with MTBP;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=53;End=222 |
| Q00987 | Region | 170 | 306 | Note=Interaction with MTBP;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=30;End=388 |
| Q00987 | Region | 170 | 306 | Note=Interaction with MTBP;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=103;End=491 |
| Q00987 | Region | 210 | 304 | Note=ARF-binding | Type=Deletion;Start=28;End=222 |
| Q00987 | Region | 210 | 304 | Note=ARF-binding | Type=Deletion;Start=28;End=222 |
| Q00987 | Region | 210 | 304 | Note=ARF-binding | Type=Deletion;Start=275;End=300 |
| Q00987 | Region | 210 | 304 | Note=ARF-binding | Type=Deletion;Start=28;End=300 |
| Q00987 | Region | 210 | 304 | Note=ARF-binding | Type=Deletion;Start=53;End=222 |
| Q00987 | Region | 210 | 304 | Note=ARF-binding | Type=Deletion;Start=30;End=388 |
| Q00987 | Region | 210 | 304 | Note=ARF-binding | Type=Deletion;Start=103;End=491 |
| Q00987 | Region | 211 | 237 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=28;End=222 |
| Q00987 | Region | 211 | 237 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=28;End=222 |
| Q00987 | Region | 211 | 237 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=28;End=300 |
| Q00987 | Region | 211 | 237 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=53;End=222 |
| Q00987 | Region | 211 | 237 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=388 |
| Q00987 | Region | 211 | 237 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=103;End=491 |
| Q00987 | Region | 223 | 232 | Note=Interaction with USP7 | Type=Deletion;Start=28;End=300 |
| Q00987 | Region | 223 | 232 | Note=Interaction with USP7 | Type=Deletion;Start=30;End=388 |
| Q00987 | Region | 223 | 232 | Note=Interaction with USP7 | Type=Deletion;Start=103;End=491 |
| Q00987 | Region | 242 | 331 | Note=Region II | Type=Deletion;Start=275;End=300 |
| Q00987 | Region | 242 | 331 | Note=Region II | Type=Deletion;Start=28;End=300 |
| Q00987 | Region | 242 | 331 | Note=Region II | Type=Deletion;Start=30;End=388 |
| Q00987 | Region | 242 | 331 | Note=Region II | Type=Deletion;Start=103;End=491 |
| Q00987 | Region | 253 | 274 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=28;End=300 |
| Q00987 | Region | 253 | 274 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=388 |
| Q00987 | Region | 253 | 274 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=103;End=491 |
| Q00987 | Region | 276 | 491 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=275;End=300 |
| Q00987 | Region | 276 | 491 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=28;End=300 |
| Q00987 | Region | 276 | 491 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=30;End=388 |
| Q00987 | Region | 276 | 491 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=103;End=491 |
| Q00987 | Region | 371 | 427 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=388 |
| Q00987 | Region | 371 | 427 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=103;End=491 |
| Q00987 | Motif | 179 | 185 | Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=28;End=222 |
| Q00987 | Motif | 179 | 185 | Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=28;End=222 |
| Q00987 | Motif | 179 | 185 | Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=28;End=300 |
| Q00987 | Motif | 179 | 185 | Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=53;End=222 |
| Q00987 | Motif | 179 | 185 | Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=30;End=388 |
| Q00987 | Motif | 179 | 185 | Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=103;End=491 |
| Q00987 | Motif | 190 | 202 | Note=Nuclear export signal | Type=Deletion;Start=28;End=222 |
| Q00987 | Motif | 190 | 202 | Note=Nuclear export signal | Type=Deletion;Start=28;End=222 |
| Q00987 | Motif | 190 | 202 | Note=Nuclear export signal | Type=Deletion;Start=28;End=300 |
| Q00987 | Motif | 190 | 202 | Note=Nuclear export signal | Type=Deletion;Start=53;End=222 |
| Q00987 | Motif | 190 | 202 | Note=Nuclear export signal | Type=Deletion;Start=30;End=388 |
| Q00987 | Motif | 190 | 202 | Note=Nuclear export signal | Type=Deletion;Start=103;End=491 |
| Q00987 | Motif | 466 | 473 | Note=Nucleolar localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=103;End=491 |
| Q00987 | Compositional bias | 145 | 161 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=115;End=169 |
| Q00987 | Compositional bias | 145 | 161 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=28;End=222 |
| Q00987 | Compositional bias | 145 | 161 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=28;End=222 |
| Q00987 | Compositional bias | 145 | 161 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=28;End=300 |
| Q00987 | Compositional bias | 145 | 161 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=53;End=222 |
| Q00987 | Compositional bias | 145 | 161 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=388 |
| Q00987 | Compositional bias | 145 | 161 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=103;End=491 |
| Q00987 | Compositional bias | 162 | 187 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=115;End=169 |
| Q00987 | Compositional bias | 162 | 187 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=28;End=222 |
| Q00987 | Compositional bias | 162 | 187 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=28;End=222 |
| Q00987 | Compositional bias | 162 | 187 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=28;End=300 |
| Q00987 | Compositional bias | 162 | 187 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=53;End=222 |
| Q00987 | Compositional bias | 162 | 187 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=388 |
| Q00987 | Compositional bias | 162 | 187 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=103;End=491 |
| Q00987 | Compositional bias | 211 | 225 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=28;End=222 |
| Q00987 | Compositional bias | 211 | 225 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=28;End=222 |
| Q00987 | Compositional bias | 211 | 225 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=28;End=300 |
| Q00987 | Compositional bias | 211 | 225 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=53;End=222 |
| Q00987 | Compositional bias | 211 | 225 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=388 |
| Q00987 | Compositional bias | 211 | 225 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=103;End=491 |
| Q00987 | Compositional bias | 380 | 408 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=30;End=388 |
| Q00987 | Compositional bias | 380 | 408 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=103;End=491 |
| Q00987 | Compositional bias | 409 | 425 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=103;End=491 |
Gene Isoform Structures and Expression Levels for MDM2 |
| Gene structures of our canonical and alternative spliced genes of MDM2 * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
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| Expression levels of gene isoforms across TCGA. |
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Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of Q00987-1 |
| 3D view using mol* of Q00987-10 |
| 3D view using mol* of Q00987-11 |
| 3D view using mol* of Q00987-2 |
| 3D view using mol* of Q00987-3 |
| 3D view using mol* of Q00987-4 |
| 3D view using mol* of Q00987-5 |
| 3D view using mol* of Q00987-6 |
| 3D view using mol* of Q00987-7 |
| 3D view using mol* of Q00987-8 |
| 3D view using mol* of Q00987-9 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of Q00987-1 |
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| pLDDT distribution across the protein length of Q00987-10 |
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| pLDDT distribution across the protein length of Q00987-11 |
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| pLDDT distribution across the protein length of Q00987-2 |
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| pLDDT distribution across the protein length of Q00987-3 |
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| pLDDT distribution across the protein length of Q00987-4 |
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| pLDDT distribution across the protein length of Q00987-5 |
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| pLDDT distribution across the protein length of Q00987-6 |
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| pLDDT distribution across the protein length of Q00987-7 |
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| pLDDT distribution across the protein length of Q00987-8 |
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| pLDDT distribution across the protein length of Q00987-9 |
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Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of Q00987-1 |
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| Ramachandran plot of Q00987-10 |
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| Ramachandran plot of Q00987-2 |
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| Ramachandran plot of Q00987-5 |
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| Ramachandran plot of Q00987-7 |
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| Ramachandran plot of Q00987-8 |
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| Ramachandran plot of Q00987-9 |
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Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| Q00987-1 | 1.163 | 220 | 1.271 | 425.32 | 0.375 | 0.745 | 0.979 | 2.44 | 0.356 | 6.857 | 1.422 | 51,52,54,55,57,58,59,61,62,67,72,73,75,86,91,93,94 ,96,99,100,103,197,198,200,201,202,204,205 |
| Q00987-10 | 1.091 | 308 | 1.161 | 731.619 | 0.546 | 0.722 | 0.908 | 1.684 | 0.651 | 2.585 | 0.646 | 23,24,25,26,49,50,51,52,54,55,57,58,59,61,62,67,72 ,73,75,91,93,94,96,97,99,100,101,103,104,135,136,1 37,138,139,140,142,143,145,146,147,149,150,219,220 ,221,222 |
| Q00987-11 | 1.107 | 183 | 1.181 | 630.777 | 0.477 | 0.735 | 0.967 | 1.485 | 0.614 | 2.421 | 1.2 | 19,20,21,22,23,24,30,57,60,61,63,64,65,67,68,73,78 ,81,92,97,99,102,105,106,199,201,203,204,205,206,2 07,208 |
| Q00987-2 | 0.924 | 82 | 0.902 | 225.008 | 0.613 | 0.687 | 0.913 | 0.43 | 1.108 | 0.388 | 0.602 | 1,2,3,4,85,86,87,88,90,235,236,237,238,241,244,251 ,261,262,263,264,282,295 |
| Q00987-3 | 0.954 | 99 | 0.997 | 274.743 | 0.635 | 0.596 | 0.788 | 0.424 | 0.906 | 0.468 | 0.44 | 1,2,3,4,5,6,8,212,225,228,230,233,234,235,236,237, 238,267 |
| Q00987-4 | 0.518 | 20 | 0.459 | 37.044 | 0.756 | 0.531 | 0.769 | 0.347 | 0.859 | 0.404 | 0.501 | 44,52,53,54,55,56,57
|
| Q00987-5 | 0.982 | 160 | 1.036 | 492.205 | 0.622 | 0.609 | 0.83 | 0.695 | 0.826 | 0.842 | 0.878 | 102,103,104,105,106,107,108,109,110,112,115,116,11 7,118,119,259,260,261,262,279,281,288,292,296,299, 300,314,315,316,317,318,319,320,321 |
| Q00987-6 | 0.407 | 13 | 0.341 | 23.667 | 0.829 | 0.446 | 0.639 | 0.088 | 0.813 | 0.108 | 0.441 | 110,113,114,115,122,123
|
| Q00987-7 | 1.132 | 88 | 1.221 | 114.562 | 0.409 | 0.775 | 0.986 | 2.954 | 0.387 | 7.642 | 2.173 | 57,61,62,66,67,72,75,81,85,90,93,94,97,98,101,102
|
| Q00987-8 | 1.02 | 331 | 1.069 | 855.099 | 0.54 | 0.669 | 0.864 | 0.885 | 0.835 | 1.061 | 0.828 | 50,51,139,140,141,142,143,144,145,146,202,203,205, 207,208,209,210,211,212,213,214,215,216,217,218,21 9,388,397,401,402,405,406,408,409,410,423,424,425, 426,427,428,429,430 |
| Q00987-9 | 1.026 | 265 | 1.08 | 753.914 | 0.514 | 0.669 | 0.891 | 0.888 | 0.802 | 1.108 | 0.9 | 155,157,160,218,219,220,221,223,224,225,226,227,22 8,229,230,231,232,233,234,235,385,386,399,404,406, 417,418,419,421,422,424,425,426,439,440,441,442,44 3,444,445,446 |
Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of Q00987-1_Q00987-1_4hbm_A.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q00987-1_4hbm_A_Q00987-10.pdb |
| 3D view using mol* of Q00987-1_4hbm_A_Q00987-11.pdb |
| 3D view using mol* of Q00987-1_4hbm_A_Q00987-2.pdb |
| 3D view using mol* of Q00987-1_4hbm_A_Q00987-3.pdb |
| 3D view using mol* of Q00987-1_4hbm_A_Q00987-4.pdb |
| 3D view using mol* of Q00987-1_4hbm_A_Q00987-5.pdb |
| 3D view using mol* of Q00987-1_4hbm_A_Q00987-6.pdb |
| 3D view using mol* of Q00987-1_4hbm_A_Q00987-7.pdb |
| 3D view using mol* of Q00987-1_4hbm_A_Q00987-8.pdb |
| 3D view using mol* of Q00987-1_4hbm_A_Q00987-9.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q00987-1_Q00987-10.pdb |
| 3D view using mol* of Q00987-1_Q00987-11.pdb |
| 3D view using mol* of Q00987-1_Q00987-2.pdb |
| 3D view using mol* of Q00987-1_Q00987-3.pdb |
| 3D view using mol* of Q00987-1_Q00987-4.pdb |
| 3D view using mol* of Q00987-1_Q00987-5.pdb |
| 3D view using mol* of Q00987-1_Q00987-6.pdb |
| 3D view using mol* of Q00987-1_Q00987-7.pdb |
| 3D view using mol* of Q00987-1_Q00987-8.pdb |
| 3D view using mol* of Q00987-1_Q00987-9.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/Q00987-1_vs_Q00987-10.png |
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| ./stats/secondary_structure/figure/Q00987-1_vs_Q00987-11.png |
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| ./stats/secondary_structure/figure/Q00987-1_vs_Q00987-2.png |
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| ./stats/secondary_structure/figure/Q00987-1_vs_Q00987-3.png |
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| ./stats/secondary_structure/figure/Q00987-1_vs_Q00987-4.png |
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| ./stats/secondary_structure/figure/Q00987-1_vs_Q00987-5.png |
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| ./stats/secondary_structure/figure/Q00987-1_vs_Q00987-6.png |
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| ./stats/secondary_structure/figure/Q00987-1_vs_Q00987-7.png |
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| ./stats/secondary_structure/figure/Q00987-1_vs_Q00987-8.png |
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| ./stats/secondary_structure/figure/Q00987-1_vs_Q00987-9.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/Q00987-1_vs_Q00987-10.png |
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| ./stats/relative_asa/Q00987-1_vs_Q00987-11.png |
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| ./stats/relative_asa/Q00987-1_vs_Q00987-2.png |
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| ./stats/relative_asa/Q00987-1_vs_Q00987-3.png |
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| ./stats/relative_asa/Q00987-1_vs_Q00987-4.png |
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| ./stats/relative_asa/Q00987-1_vs_Q00987-5.png |
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| ./stats/relative_asa/Q00987-1_vs_Q00987-6.png |
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| ./stats/relative_asa/Q00987-1_vs_Q00987-7.png |
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| ./stats/relative_asa/Q00987-1_vs_Q00987-8.png |
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| ./stats/relative_asa/Q00987-1_vs_Q00987-9.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Substitution;Start=1;End=1 |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=28;End=222 |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=28;End=222 |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=28;End=300 |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=53;End=222 |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=30;End=388 |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Substitution;Start=76;End=102 |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=103;End=491 |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=1;End=61 |
| Q00987 | Region | 1 | 110 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=53;End=97 |
| Q00987 | Region | 150 | 230 | "Note=Interaction with PYHIN1 and necessary for interaction with RFFL and RNF34;Ontology_term=ECO:0000269 | ECO:0000269;evidence=ECO:0000269|PubMed:16479015 |
| Q00987 | Region | 150 | 230 | "Note=Interaction with PYHIN1 and necessary for interaction with RFFL and RNF34;Ontology_term=ECO:0000269 | ECO:0000269;evidence=ECO:0000269|PubMed:16479015 |
| Q00987 | Region | 150 | 230 | "Note=Interaction with PYHIN1 and necessary for interaction with RFFL and RNF34;Ontology_term=ECO:0000269 | ECO:0000269;evidence=ECO:0000269|PubMed:16479015 |
| Q00987 | Region | 150 | 230 | "Note=Interaction with PYHIN1 and necessary for interaction with RFFL and RNF34;Ontology_term=ECO:0000269 | ECO:0000269;evidence=ECO:0000269|PubMed:16479015 |
| Q00987 | Region | 150 | 230 | "Note=Interaction with PYHIN1 and necessary for interaction with RFFL and RNF34;Ontology_term=ECO:0000269 | ECO:0000269;evidence=ECO:0000269|PubMed:16479015 |
| Q00987 | Region | 150 | 230 | "Note=Interaction with PYHIN1 and necessary for interaction with RFFL and RNF34;Ontology_term=ECO:0000269 | ECO:0000269;evidence=ECO:0000269|PubMed:16479015 |
| Q00987 | Region | 150 | 230 | "Note=Interaction with PYHIN1 and necessary for interaction with RFFL and RNF34;Ontology_term=ECO:0000269 | ECO:0000269;evidence=ECO:0000269|PubMed:16479015 |
| Q00987 | Region | 170 | 306 | Note=Interaction with MTBP;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=28;End=222 |
| Q00987 | Region | 170 | 306 | Note=Interaction with MTBP;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=28;End=222 |
| Q00987 | Region | 170 | 306 | Note=Interaction with MTBP;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=275;End=300 |
| Q00987 | Region | 170 | 306 | Note=Interaction with MTBP;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=28;End=300 |
| Q00987 | Region | 170 | 306 | Note=Interaction with MTBP;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=53;End=222 |
| Q00987 | Region | 170 | 306 | Note=Interaction with MTBP;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=30;End=388 |
| Q00987 | Region | 170 | 306 | Note=Interaction with MTBP;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=103;End=491 |
| Q00987 | Region | 223 | 232 | Note=Interaction with USP7 | Type=Deletion;Start=28;End=300 |
| Q00987 | Region | 223 | 232 | Note=Interaction with USP7 | Type=Deletion;Start=30;End=388 |
| Q00987 | Region | 223 | 232 | Note=Interaction with USP7 | Type=Deletion;Start=103;End=491 |
| Q00987 | Region | 276 | 491 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=275;End=300 |
| Q00987 | Region | 276 | 491 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=28;End=300 |
| Q00987 | Region | 276 | 491 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=30;End=388 |
| Q00987 | Region | 276 | 491 | Note=Necessary for interaction with USP2 | Type=Deletion;Start=103;End=491 |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to MDM2 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| Q00987 | MDM2 | DB02872 | Cis-[4,5-Bis-(4-Bromophenyl)-2-(2-Ethoxy-4-Methoxyphenyl)-4,5-Dihydroimidazol-1-Yl]-[4-(2-Hydroxyethyl)Piperazin-1-Yl]Methanone | experimental | |
| Q00987 | MDM2 | DB14533 | Zinc chloride | approved, investigational | binder |
| Q00987 | MDM2 | DB14487 | Zinc acetate | approved, investigational | |
| Q00987 | MDM2 | DB14548 | Zinc sulfate, unspecified form | approved, experimental | binder |
| Q00987 | MDM2 | DB04144 | Cis-[4,5-Bis-(4-Chlorophenyl)-2-(2-Isopropoxy-4-Methoxyphenyl)-4,5-Dihyd Roimidazol-1-Yl]-Piperazin-1-Yl-Methanone | experimental | |
| Q00987 | MDM2 | DB01593 | Zinc | approved, investigational |
Related Diseases to MDM2 |
| Previous studies relating to the alternative splicing of MDM2 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| MDM2 | 10074928 | Expression of alternatively spliced mdm2 transcripts correlates with stabilized wild-type p53 protein in human glioblastoma cells. | A puzzling finding in various human tumors, including glioblastoma multiforme (GBM), is the stabilization of wild-type (wt) p53 protein. The biological significance of this phenomenon and the mechanism by which it occurs are unexplained. Recent reports have revealed that mdm2 exerts its negative regulation on the p53 signal by directly binding p53 protein and thereby instigating its proteasomal degradation. mdm2 has been shown to exist in alternatively spliced forms in human ovarian and bladder carcinomas, and recently in GBM, with loss or disruption of its p53 binding domain. Here we report that alternatively spliced transcripts of mdm2 are present in 7 of 16 human GBM primary cell cultures and in the established GBM cell lines LN 229 and LN 18. Sequencing demonstrated loss of the amino terminal p53 binding domain in these alternatively spliced mdm2 transcripts, and an out-of-frame splicing in the majority of cases. A significant correlation between the presence of mdm2 splice variants and increased expression of wt p53 protein was observed. Furthermore, in the presence of an mdm2 splice variant, wt p53 stabilization occurred despite coincident MDM2 amplification. Our findings suggest that wt p53 protein stabilization may arise as a consequence of alternative splicing of mdm2. Such a mechanism might account for wt p53 protein accumulation in GBM cells, even in the presence of MDM2 gene amplification. | D001932 | Brain Neoplasms |
| MDM2 | 10074928 | Expression of alternatively spliced mdm2 transcripts correlates with stabilized wild-type p53 protein in human glioblastoma cells. | A puzzling finding in various human tumors, including glioblastoma multiforme (GBM), is the stabilization of wild-type (wt) p53 protein. The biological significance of this phenomenon and the mechanism by which it occurs are unexplained. Recent reports have revealed that mdm2 exerts its negative regulation on the p53 signal by directly binding p53 protein and thereby instigating its proteasomal degradation. mdm2 has been shown to exist in alternatively spliced forms in human ovarian and bladder carcinomas, and recently in GBM, with loss or disruption of its p53 binding domain. Here we report that alternatively spliced transcripts of mdm2 are present in 7 of 16 human GBM primary cell cultures and in the established GBM cell lines LN 229 and LN 18. Sequencing demonstrated loss of the amino terminal p53 binding domain in these alternatively spliced mdm2 transcripts, and an out-of-frame splicing in the majority of cases. A significant correlation between the presence of mdm2 splice variants and increased expression of wt p53 protein was observed. Furthermore, in the presence of an mdm2 splice variant, wt p53 stabilization occurred despite coincident MDM2 amplification. Our findings suggest that wt p53 protein stabilization may arise as a consequence of alternative splicing of mdm2. Such a mechanism might account for wt p53 protein accumulation in GBM cells, even in the presence of MDM2 gene amplification. | D005909 | Glioblastoma |
| MDM2 | 10188733 | Expression of MDM2 during mammary tumorigenesis. | The MDM2 oncoprotein encodes a 90 kDa nuclear phosphoprotein capable of abrogating the growth suppressive functions of p53 and pRb tumor suppressor proteins by direct interaction. Alternative splicing of MDM2 protein coding sequences has been documented during tumor progression in human ovarian and bladder carcinomas. The aim of this study was to determine whether alternative splicing of MDM2 occurs during breast tumorigenesis in mice and humans and whether protein coding sequences were affected. Specimens representing normal and malignant breast tissues from the murine D2 mammary tumor model system and human breast carcinomas were examined. Three distinct mdm2 mRNA transcripts of 3.3, 1.6 and 1.5 kb were detected in normal and malignant murine mammary tissues by Northern blot analysis using a full-length mdm2 cDNA probe. Additional Northern blot analysis using a probe derived from exon 12 of murine mdm2 demonstrated that the 1.5 and 1.6 kb transcripts lack sequences encoding the C-terminus of the protein. No evidence of internal deletions of protein coding sequences of mdm2 was detected in any of the normal mammary tissues or D2 murine mammary tumors examined by reverse transcription PCR (RT-PCR). Three distinct MDM2 transcripts of 6.7, 4.7 and 1.9 kb were detected in malignant human breast tissue by Northern blot analysis using a cDNA probe specific for the complete open reading frame of human MDM2. However, a cDNA probe specific for the last exon of human MDM2 hybridized only to the 6.7 and 4.7 kb transcripts, demonstrating that the 1.9 kb transcript lacked protein coding sequences contained in exon 12. Similarly, no internal deletions were detected in a panel of malignant human breast tissues using RT-PCR and analogous primers within human MDM2. Therefore, breast tumors differ from other solid tumors reported previously in that no internal deletions of MDM2 protein coding sequences were observed. However, the data document the presence of multiple MDM2 mRNA transcripts in both normal and malignant breast tissues. A subset of MDM2 transcripts were shown to lack the last exon which contains sequences coding for the RING and zinc fingers and domains which are targets for caspase-3 mediated proteolytic degradation and are required to target p53 for proteosomal degradation. | D001943 | Breast Neoplasms |
| MDM2 | 10188733 | Expression of MDM2 during mammary tumorigenesis. | The MDM2 oncoprotein encodes a 90 kDa nuclear phosphoprotein capable of abrogating the growth suppressive functions of p53 and pRb tumor suppressor proteins by direct interaction. Alternative splicing of MDM2 protein coding sequences has been documented during tumor progression in human ovarian and bladder carcinomas. The aim of this study was to determine whether alternative splicing of MDM2 occurs during breast tumorigenesis in mice and humans and whether protein coding sequences were affected. Specimens representing normal and malignant breast tissues from the murine D2 mammary tumor model system and human breast carcinomas were examined. Three distinct mdm2 mRNA transcripts of 3.3, 1.6 and 1.5 kb were detected in normal and malignant murine mammary tissues by Northern blot analysis using a full-length mdm2 cDNA probe. Additional Northern blot analysis using a probe derived from exon 12 of murine mdm2 demonstrated that the 1.5 and 1.6 kb transcripts lack sequences encoding the C-terminus of the protein. No evidence of internal deletions of protein coding sequences of mdm2 was detected in any of the normal mammary tissues or D2 murine mammary tumors examined by reverse transcription PCR (RT-PCR). Three distinct MDM2 transcripts of 6.7, 4.7 and 1.9 kb were detected in malignant human breast tissue by Northern blot analysis using a cDNA probe specific for the complete open reading frame of human MDM2. However, a cDNA probe specific for the last exon of human MDM2 hybridized only to the 6.7 and 4.7 kb transcripts, demonstrating that the 1.9 kb transcript lacked protein coding sequences contained in exon 12. Similarly, no internal deletions were detected in a panel of malignant human breast tissues using RT-PCR and analogous primers within human MDM2. Therefore, breast tumors differ from other solid tumors reported previously in that no internal deletions of MDM2 protein coding sequences were observed. However, the data document the presence of multiple MDM2 mRNA transcripts in both normal and malignant breast tissues. A subset of MDM2 transcripts were shown to lack the last exon which contains sequences coding for the RING and zinc fingers and domains which are targets for caspase-3 mediated proteolytic degradation and are required to target p53 for proteosomal degradation. | D008325 | Mammary Neoplasms, Experimental |
| MDM2 | 11307150 | Amplification of the MDM2 gene, but not expression of splice variants of MDM2 MRNA, is associated with prognosis in soft tissue sarcoma. | The MDM2 gene encodes a 90-kDa oncoprotein that is overexpressed in several human carcinomas, osteosarcomas, gliomas and soft tissue sarcomas (STSs). This overexpression is the result of several mechanisms, for example, enhanced transcription or translation, gene amplification and alternative splicing. We found that 19 of 67 (28.4%) STS specimens contained an amplified MDM2 gene. The amplification was more likely to be present in grade 1 tumors than in grade 2 or 3 tumors (58% of grade 1 tumors vs. 15% of grade 2 or 3 tumors, p = 0.001, chi(2) test). Furthermore, patients with tumors that contained an amplified MDM2 gene had a survival estimate (87 months) that was longer than that of patients with tumors that lacked an amplified gene (40 months; p = 0.02, log-rank test). Alternatively and aberrantly spliced MDM2 mRNAs were detected in human STSs by a highly sensitive reverse transcription-polymerase chain reaction method. Of 71 tumor samples, 38 (54%) showed evidence of the spliced forms, which included MDM2-A, MDM2-B and several variants exclusively expressed in STSs. A common feature of all forms was the absence of the MDM2 N-terminal region, which includes the TP53-binding region. Furthermore, the presence of the spliced forms was associated with elevated levels of TP53 (p = 0.01, chi(2) test). Although the presence of spliced forms was associated with late-stage tumor phenotypes (p = 0.05, chi(2) test), we observed no relationship between the presence of splice variants and patient outcome. | D012509 | Sarcoma |
| MDM2 | 14757843 | MDM2 and its splice variant messenger RNAs: expression in tumors and down-regulation using antisense oligonucleotides. | Alternative splicing has an important role in expanding protein diversity. An example of a gene with more than one transcript is the MDM2 oncogene. To date, more than 40 different splice variants have been isolated from both tumor and normal tissues. Here, we review what is known about the alteration of MDM2 mRNA expression, focusing on alternative splicing and potential functions of different MDM2 isoforms. We also discuss the progress that has been made in the development of antisense oligonucleotides targeted to MDM2 for use as a potential cancer therapy. | D009369 | Neoplasms |
| MDM2 | 15315825 | Genomic organisation of the human MDM2 oncogene and relationship to its alternatively spliced mRNAs. | The MDM2 proto-oncogene, which encodes a protein that binds to the p53 tumour suppressor, has been found amplified and overexpressed in a range of human tumours. Although the human MDM2 cDNA sequence has been reported, the genomic organisation of the human gene has not been documented. We have previously reported the detection of five alternative internally deleted MDM2 transcripts in human tumours and suggested these may represent alternatively spliced forms. Here we demonstrate two novel MDM2 transcripts with internal deletions, using RT-PCR followed by sequencing. To definitively ascribe these variant transcript forms to alternative splicing, and to explore associated mechanisms, we have determined the intron--exon organisation of the human genomic sequence. The human MDM2 gene spans approximately 33 kb and is divided into 12 exons. Exon sizes range from 50 to > or =1161 bp and intron sizes vary from 121 to approximately 7000 bp. The positions of intron--exon boundaries are compared with the deletion junctions of the multiple-sized transcripts and discussed in relation to alternative splicing mechanism. | D001749 | Urinary Bladder Neoplasms |
| MDM2 | 15714438 | Alternative splicing of MDM2 mRNA in lung carcinomas and lung cell lines. | The MDM2 gene is overexpressed in several human tumors and its product may be processed into various isoforms. Recently, alternative splicing forms of MDM2 mRNA have been detected in various types of tumors. In this study, lung tissue from human non small cell lung cancers was examined for MDM2 mRNA splicing variants by nested RT-PCR. Of the 117 lung cancer tissue samples analyzed, a total of 31 (26.5%) had splice variants for the MDM2 gene, while 59 (50.4%) had undetectable levels of MDM2 transcript. Further analysis indicated that the predominant variant for 26 of the 31 samples with alternative MDM2 splicing products was MDM2-657, a splice variant lacking exons 3-11. Significant associations were found between the frequency of alternative splicing and the gender and smoking habits of the patients. Approximately 36% of male patients had alternative splicing of MDM2 compared with only 9.5% of female patients (P = 0.008); 44.2% of the smoker patients had alternative MDM2 splice forms versus 16.2% of nonsmokers (P = 0.003). Furthermore, most normal lung cell lines examined possessed only full-length MDM2 mRNA, while among several lung cancer cell lines, only H1355 and CaLu-1 cells lacked alternatively spliced MDM2 transcripts. When H1355 cells were treated in vitro with the cigarette smoke carcinogen benzo[a]pyrene (B[a]P) or the B[a]P metabolite benzo[a]pyrene diolepoxide (BPDE), three MDM2 splicing products were detected by nested RT-PCR. Finally, with the use of several specific inhibitors, we found that BPDE-induced MDM2 mRNA alternative splicing in H1355 cells may occur through the PI3K or MAPK pathway. Overall, our results suggest that carcinogens present in cigarette smoke increase the risk of alternative MDM2 splicing, which is highly associated with lung cancer. | D002277 | Carcinoma |
| MDM2 | 15714438 | Alternative splicing of MDM2 mRNA in lung carcinomas and lung cell lines. | The MDM2 gene is overexpressed in several human tumors and its product may be processed into various isoforms. Recently, alternative splicing forms of MDM2 mRNA have been detected in various types of tumors. In this study, lung tissue from human non small cell lung cancers was examined for MDM2 mRNA splicing variants by nested RT-PCR. Of the 117 lung cancer tissue samples analyzed, a total of 31 (26.5%) had splice variants for the MDM2 gene, while 59 (50.4%) had undetectable levels of MDM2 transcript. Further analysis indicated that the predominant variant for 26 of the 31 samples with alternative MDM2 splicing products was MDM2-657, a splice variant lacking exons 3-11. Significant associations were found between the frequency of alternative splicing and the gender and smoking habits of the patients. Approximately 36% of male patients had alternative splicing of MDM2 compared with only 9.5% of female patients (P = 0.008); 44.2% of the smoker patients had alternative MDM2 splice forms versus 16.2% of nonsmokers (P = 0.003). Furthermore, most normal lung cell lines examined possessed only full-length MDM2 mRNA, while among several lung cancer cell lines, only H1355 and CaLu-1 cells lacked alternatively spliced MDM2 transcripts. When H1355 cells were treated in vitro with the cigarette smoke carcinogen benzo[a]pyrene (B[a]P) or the B[a]P metabolite benzo[a]pyrene diolepoxide (BPDE), three MDM2 splicing products were detected by nested RT-PCR. Finally, with the use of several specific inhibitors, we found that BPDE-induced MDM2 mRNA alternative splicing in H1355 cells may occur through the PI3K or MAPK pathway. Overall, our results suggest that carcinogens present in cigarette smoke increase the risk of alternative MDM2 splicing, which is highly associated with lung cancer. | D008175 | Lung Neoplasms |
| MDM2 | 19273224 | MDM2 and MDM4 splicing: an integral part of the cancer spliceome. | MDM2 and MDM4, the murine double minute proteins, are oncogenes that function as important regulators of various proteins. One fundamental role for these proteins is regulation of the tumor suppressor, p53. Precise regulation of p53 is vital for coordinated malignant suppression and cell survival. Alternative splice forms of MDM2 as well as MDM4 have been associated with various cancers. Indeed, UV irradiation triggers alternative splicing of both MDM2 and MDM4. Coordinated alternative splicing in response to cellular stress or in cancerous cells regulates the posttranscriptional expression of these two genes and likely others. This concert of stress responsive mRNAs comprises the cancer spliceome and provides a fingerprint of coordinated alternative splicing in these aberrant cells. Although various transcripts have been described for both proteins, here we provide a precise catalog of the alternatively spliced transcripts of both genes and the cancers with which they are associated. | D009369 | Neoplasms |
| MDM2 | 21761395 | Identification of spliced variants of the proto-oncogene HDM2 in colorectal cancer. | The human double minute 2 (hdm2) oncogene is a negative regulator of the p53 gene. Expression and alternative splicing of the hdm2 gene may contribute to colorectal cancer development or progression. This study aimed to determine the presence and identification of aberrant mRNA transcripts of hdm2 in colorectal cancer tissues and cell lines, and determine the nature of their association with clinicopathological characteristics and survival of patients. | D015179 | Colorectal Neoplasms |
| MDM2 | 24018792 | In vitro and in silico studies of MDM2/MDMX isoforms predict Nutlin-3A sensitivity in well/de-differentiated liposarcomas. | The molecular marker of well-differentiated/de-differentiated liposarcomas is MDM2 gene amplification coupled with protein overexpression and wild-type TP53. MDMX is a recently identified MDM2 homolog and its presence in this tumor is unexplored. Our aim was to investigate the role of full-length MDM2 and MDMX proteins and their isoforms in surgical specimens of well-differentiated/de-differentiated liposarcomas in view of Nutlin-3A (a MDM2 inhibitor) treatment. Frozen and matched formalin-fixed, paraffin-embedded material from surgical specimens was examined by means of: (1) fluorescence in situ hybridization to determine MDM2 and MDMX gene copy numbers; (2) RT-PCR and densitometry to analyze alternative splicing forms of mdm2 and mdmx; (3) immunoblotting and immunohistochemistry to assess the corresponding translated proteins; and (4) in vitro and in silico assays to determine their affinity for Nutlin-3A. All these cases showed MDM2 gene amplification with an MDMX disomic pattern. In all cases, the full-length mdm2 transcript was associated with the mdm2-b transcript, with ratios ranging from 0.07 to 5.6, and both were translated into protein; mdmx and mdmx-s were co-transcripted, with ratios ranging from 0.1 to 5.6. MDMX-S was frequently more upregulated than MDMX at both transcriptional and protein level. Each case showed different amounts of mdm2, mdm2-b, mdmx, and mdmx-s transcripts and the corresponding proteins. In vitro assays showed that Nutlin-3A was ineffective against MDM2-B and was unable to disrupt the MDMX/TP53 and MSMX-S/TP53 complexes. Molecular simulations confirmed these in vitro findings by showing that MDM2 has high Nutlin-3A affinity, followed by MDMX-S, MDMX, and MDM2-B. Nutlin-3A is predicted to be a good therapeutic option for well-differentiated/de-differentiated liposarcomas. However, our findings predict heterogeneous responses depending on the relative expression of mdm2, mdm2-b, mdmx, and mdmx-s transcripts and proteins. | D008080 | Liposarcoma |
| MDM2 | 24027430 | Stress-induced isoforms of MDM2 and MDM4 correlate with high-grade disease and an altered splicing network in pediatric rhabdomyosarcoma. | Pediatric rhabdomyosarcoma (RMS) is a morphologically and genetically heterogeneous malignancy commonly classified into three histologic subtypes, namely, alveolar, embryonal, and anaplastic. An issue that continues to challenge effective RMS patient prognosis is the dearth of molecular markers predictive of disease stage irrespective of tumor subtype. Our study involving a panel of 70 RMS tumors has identified specific alternative splice variants of the oncogenes Murine Double Minute 2 (MDM2) and MDM4 as potential biomarkers for RMS. Our results have demonstrated the strong association of genotoxic-stress inducible splice forms MDM2-ALT1 (91.6% Intergroup Rhabdomyosarcoma Study Group stage 4 tumors) and MDM4-ALT2 (90.9% MDM4-ALT2-positive T2 stage tumors) with high-risk metastatic RMS. Moreover, MDM2-ALT1-positive metastatic tumors belonged to both the alveolar (50%) and embryonal (41.6%) subtypes, making this the first known molecular marker for high-grade metastatic disease across the most common RMS subtypes. Furthermore, our results show that MDM2-ALT1 expression can function by directly contribute to metastatic behavior and promote the invasion of RMS cells through a matrigel-coated membrane. Additionally, expression of both MDM2-ALT1 and MDM4-ALT2 increased anchorage-independent cell-growth in soft agar assays. Intriguingly, we observed a unique coordination in the splicing of MDM2-ALT1 and MDM4-ALT2 in approximately 24% of tumor samples in a manner similar to genotoxic stress response in cell lines. To further explore splicing network alterations with possible relevance to RMS disease, we used an exon microarray approach to examine stress-inducible splicing in an RMS cell line (Rh30) and observed striking parallels between stress-responsive alternative splicing and constitutive splicing in RMS tumors. | D012208 | Rhabdomyosarcoma |
Clinically important variants in MDM2 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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