Protein:CHEK2 |
Protein Summary |
 Gene summary |
| Gene name: CHEK2 | ASpdb.0 ID: 11200 | Gene | Gene symbol | CHEK2 | Gene ID | 11200 |
| Gene name | checkpoint kinase 2 |
| Synonyms | CDS1|CHK2|HuCds1|LFS2|PP1425|RAD53|TPDS4|hCds1 |
| Cytomap | 22q12.1 |
| Type of gene | protein-coding |
| Description | serine/threonine-protein kinase Chk2CHK2 checkpoint homologcds1 homologcheckpoint-like protein CHK2 |
| Modification date | 20240416 |
| UniProtAcc | O96017 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | CHEK2 | GO:0000781 | chromosome, telomeric region | 15149599 |
| Gene | CHEK2 | GO:0004674 | protein serine/threonine kinase activity | 12717439|16794575 |
| Gene | CHEK2 | GO:0005654 | nucleoplasm | - |
| Gene | CHEK2 | GO:0005794 | Golgi apparatus | - |
| Gene | CHEK2 | GO:0006355 | regulation of DNA-templated transcription | 12717439 |
| Gene | CHEK2 | GO:0006468 | protein phosphorylation | 12717439|18833288 |
| Gene | CHEK2 | GO:0006974 | DNA damage response | 24550317 |
| Gene | CHEK2 | GO:0008630 | intrinsic apoptotic signaling pathway in response to DNA damage | 12402044 |
| Gene | CHEK2 | GO:0016605 | PML body | 12402044 |
| Gene | CHEK2 | GO:0042770 | signal transduction in response to DNA damage | 14744935 |
| Gene | CHEK2 | GO:0042803 | protein homodimerization activity | 16794575 |
| Gene | CHEK2 | GO:0045893 | positive regulation of DNA-templated transcription | 17101782 |
| Gene | CHEK2 | GO:0046777 | protein autophosphorylation | 16794575|18644861 |
| Gene | CHEK2 | GO:0050821 | protein stabilization | 12717439|18833288 |
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 |
| O96017-1 | O96017-1_3i6u_A.pdb | 3I6U | X-ray | 3.0 | A | 89 | 501 |
| 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 |
| O96017 | CHEK2 | O96017-1 | O96017-10 | 543 | 140 | 131 | 147 | Substitution | KRTDKYRTYSKKHFRIF | EFRSYSFYLP | 131 | 140 |
| O96017 | CHEK2 | O96017-1 | O96017-10 | 543 | 140 | 148 | 543 | Deletion | none | none | 140 | 140 |
| O96017 | CHEK2 | O96017-1 | O96017-11 | 543 | 225 | 75 | 392 | Deletion | none | none | 74 | 74 |
| O96017 | CHEK2 | O96017-1 | O96017-12 | 543 | 514 | 337 | 365 | Deletion | none | none | 336 | 336 |
| O96017 | CHEK2 | O96017-1 | O96017-13 | 543 | 322 | 1 | 221 | Deletion | none | none | 0 | 0 |
| O96017 | CHEK2 | O96017-1 | O96017-2 | 543 | 234 | 198 | 224 | Substitution | VFVFFDLTVDDQSVYPKALRDEYIMSK | EKILKIYSLSRFSKIRRGAVAHVFNPS | 198 | 224 |
| O96017 | CHEK2 | O96017-1 | O96017-2 | 543 | 234 | 228 | 234 | Substitution | SGACGEV | GRGWQIT | 228 | 234 |
| O96017 | CHEK2 | O96017-1 | O96017-2 | 543 | 234 | 235 | 543 | Deletion | none | none | 234 | 234 |
| O96017 | CHEK2 | O96017-1 | O96017-3 | 543 | 162 | 107 | 487 | Deletion | none | none | 106 | 106 |
| O96017 | CHEK2 | O96017-1 | O96017-4 | 543 | 452 | 107 | 197 | Deletion | none | none | 106 | 106 |
| O96017 | CHEK2 | O96017-1 | O96017-5 | 543 | 203 | 199 | 203 | Substitution | FVFFD | VPVER | 199 | 203 |
| O96017 | CHEK2 | O96017-1 | O96017-5 | 543 | 203 | 204 | 543 | Deletion | none | none | 203 | 203 |
| O96017 | CHEK2 | O96017-1 | O96017-6 | 543 | 165 | 150 | 165 | Substitution | VGPKNSYIAYIEDHSG | ENLSCPYRIWFNFCLF | 150 | 165 |
| O96017 | CHEK2 | O96017-1 | O96017-6 | 543 | 165 | 166 | 543 | Deletion | none | none | 165 | 165 |
| O96017 | CHEK2 | O96017-1 | O96017-7 | 543 | 339 | 337 | 339 | Substitution | YLH | MKT | 337 | 339 |
| O96017 | CHEK2 | O96017-1 | O96017-7 | 543 | 339 | 340 | 543 | Deletion | none | none | 339 | 339 |
| O96017 | CHEK2 | O96017-1 | O96017-8 | 543 | 289 | 283 | 289 | Substitution | PCIIKIK | DGRGRAV | 283 | 289 |
| O96017 | CHEK2 | O96017-1 | O96017-8 | 543 | 289 | 290 | 543 | Deletion | none | none | 289 | 289 |
| O96017 | CHEK2 | O96017-1 | O96017-9 | 543 | 586 | 107 | 107 | Substitution | E | ETESGHVTQSDLELLLSSDPPASASQSAGIRGVRHHPRPVCSLK | 107 | 150 |
| Multiple sequence alignment of our canonical and alternatively spliced CHEK2 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of CHEK2 |
| UniProt-id | ENSG | ENST | ENSP |
| O96017-1 | ENSG00000183765.24 | ENST00000404276.6 | ENSP00000385747.1 |
| O96017-1 | ENSG00000183765.24 | ENST00000405598.5 | ENSP00000386087.1 |
| O96017-1 | ENSG00000183765.24 | ENST00000650281.1 | ENSP00000497000.1 |
| O96017-12 | ENSG00000183765.24 | ENST00000348295.7 | ENSP00000329012.5 |
| O96017-13 | ENSG00000183765.24 | ENST00000425190.7 | ENSP00000390244.2 |
| O96017-13 | ENSG00000183765.24 | ENST00000649563.1 | ENSP00000496928.1 |
| O96017-4 | ENSG00000183765.24 | ENST00000403642.5 | ENSP00000384919.1 |
| O96017-5 | ENSG00000183765.24 | ENST00000417588.5 | ENSP00000412901.1 |
| O96017-5 | ENSG00000183765.24 | ENST00000439346.6 | ENSP00000396903.2 |
| O96017-6 | ENSG00000183765.24 | ENST00000448511.5 | ENSP00000404567.1 |
| O96017-8 | ENSG00000183765.24 | ENST00000433728.5 | ENSP00000404400.1 |
| O96017-9 | ENSG00000183765.24 | ENST00000382580.6 | ENSP00000372023.2 |
| UniProt-id | NM ID | NP ID |
| O96017-1 | NM_007194.3 | NP_009125.1 |
| O96017-12 | NM_145862.2 | NP_665861.1 |
| O96017-13 | NM_001257387.1 | NP_001244316.1 |
| O96017-13 | XM_011529845.2 | XP_011528147.1 |
| O96017-9 | NM_001005735.1 | NP_001005735.1 |
| Amino acid sequences of our canonical and alternatively spliced CHEK2 |
| accession_id | Protein sequence |
| O96017-1 | MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEDQEPEDQEPEEPTP APWARLWALQDGFANLECVNDNYWFGRDKSCEYCFDEPLLKRTDKYRTYSKKHFRIFREVGPKNSYIAYIEDHSGNGTFVNTELVGKGKR RPLNNNSEIALSLSRNKVFVFFDLTVDDQSVYPKALRDEYIMSKTLGSGACGEVKLAFERKTCKKVAIKIISKRKFAIGSAREADPALNV ETEIEILKKLNHPCIIKIKNFFDAEDYYIVLELMEGGELFDKVVGNKRLKEATCKLYFYQMLLAVQYLHENGIIHRDLKPENVLLSSQEE DCLIKITDFGHSKILGETSLMRTLCGTPTYLAPEVLVSVGTAGYNRAVDCWSLGVILFICLSGYPPFSEHRTQVSLKDQITSGKYNFIPE VWAEVSEKALDLVKKLLVVDPKARFTTEEALRHPWLQDEDMKRKFQDLLSEENESTALPQVLAQPSTSRKRPREGEAEGAETTKRPAVCA |
| O96017-10 | MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEDQEPEDQEPEEPTP |
| O96017-11 | MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEVLVSVGTAGYNRAV DCWSLGVILFICLSGYPPFSEHRTQVSLKDQITSGKYNFIPEVWAEVSEKALDLVKKLLVVDPKARFTTEEALRHPWLQDEDMKRKFQDL |
| O96017-12 | MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEDQEPEDQEPEEPTP APWARLWALQDGFANLECVNDNYWFGRDKSCEYCFDEPLLKRTDKYRTYSKKHFRIFREVGPKNSYIAYIEDHSGNGTFVNTELVGKGKR RPLNNNSEIALSLSRNKVFVFFDLTVDDQSVYPKALRDEYIMSKTLGSGACGEVKLAFERKTCKKVAIKIISKRKFAIGSAREADPALNV ETEIEILKKLNHPCIIKIKNFFDAEDYYIVLELMEGGELFDKVVGNKRLKEATCKLYFYQMLLAVQITDFGHSKILGETSLMRTLCGTPT YLAPEVLVSVGTAGYNRAVDCWSLGVILFICLSGYPPFSEHRTQVSLKDQITSGKYNFIPEVWAEVSEKALDLVKKLLVVDPKARFTTEE |
| O96017-13 | MSKTLGSGACGEVKLAFERKTCKKVAIKIISKRKFAIGSAREADPALNVETEIEILKKLNHPCIIKIKNFFDAEDYYIVLELMEGGELFD KVVGNKRLKEATCKLYFYQMLLAVQYLHENGIIHRDLKPENVLLSSQEEDCLIKITDFGHSKILGETSLMRTLCGTPTYLAPEVLVSVGT AGYNRAVDCWSLGVILFICLSGYPPFSEHRTQVSLKDQITSGKYNFIPEVWAEVSEKALDLVKKLLVVDPKARFTTEEALRHPWLQDEDM |
| O96017-2 | MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEDQEPEDQEPEEPTP APWARLWALQDGFANLECVNDNYWFGRDKSCEYCFDEPLLKRTDKYRTYSKKHFRIFREVGPKNSYIAYIEDHSGNGTFVNTELVGKGKR |
| O96017-3 | MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEDQEPEDQEPEEPTP |
| O96017-4 | MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEDQEPEDQEPEEPTP APWARLWALQDGFANLVFVFFDLTVDDQSVYPKALRDEYIMSKTLGSGACGEVKLAFERKTCKKVAIKIISKRKFAIGSAREADPALNVE TEIEILKKLNHPCIIKIKNFFDAEDYYIVLELMEGGELFDKVVGNKRLKEATCKLYFYQMLLAVQYLHENGIIHRDLKPENVLLSSQEED CLIKITDFGHSKILGETSLMRTLCGTPTYLAPEVLVSVGTAGYNRAVDCWSLGVILFICLSGYPPFSEHRTQVSLKDQITSGKYNFIPEV WAEVSEKALDLVKKLLVVDPKARFTTEEALRHPWLQDEDMKRKFQDLLSEENESTALPQVLAQPSTSRKRPREGEAEGAETTKRPAVCAA |
| O96017-5 | MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEDQEPEDQEPEEPTP APWARLWALQDGFANLECVNDNYWFGRDKSCEYCFDEPLLKRTDKYRTYSKKHFRIFREVGPKNSYIAYIEDHSGNGTFVNTELVGKGKR |
| O96017-6 | MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEDQEPEDQEPEEPTP |
| O96017-7 | MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEDQEPEDQEPEEPTP APWARLWALQDGFANLECVNDNYWFGRDKSCEYCFDEPLLKRTDKYRTYSKKHFRIFREVGPKNSYIAYIEDHSGNGTFVNTELVGKGKR RPLNNNSEIALSLSRNKVFVFFDLTVDDQSVYPKALRDEYIMSKTLGSGACGEVKLAFERKTCKKVAIKIISKRKFAIGSAREADPALNV |
| O96017-8 | MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEDQEPEDQEPEEPTP APWARLWALQDGFANLECVNDNYWFGRDKSCEYCFDEPLLKRTDKYRTYSKKHFRIFREVGPKNSYIAYIEDHSGNGTFVNTELVGKGKR RPLNNNSEIALSLSRNKVFVFFDLTVDDQSVYPKALRDEYIMSKTLGSGACGEVKLAFERKTCKKVAIKIISKRKFAIGSAREADPALNV |
| O96017-9 | MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEDQEPEDQEPEEPTP APWARLWALQDGFANLETESGHVTQSDLELLLSSDPPASASQSAGIRGVRHHPRPVCSLKCVNDNYWFGRDKSCEYCFDEPLLKRTDKYR TYSKKHFRIFREVGPKNSYIAYIEDHSGNGTFVNTELVGKGKRRPLNNNSEIALSLSRNKVFVFFDLTVDDQSVYPKALRDEYIMSKTLG SGACGEVKLAFERKTCKKVAIKIISKRKFAIGSAREADPALNVETEIEILKKLNHPCIIKIKNFFDAEDYYIVLELMEGGELFDKVVGNK RLKEATCKLYFYQMLLAVQYLHENGIIHRDLKPENVLLSSQEEDCLIKITDFGHSKILGETSLMRTLCGTPTYLAPEVLVSVGTAGYNRA VDCWSLGVILFICLSGYPPFSEHRTQVSLKDQITSGKYNFIPEVWAEVSEKALDLVKKLLVVDPKARFTTEEALRHPWLQDEDMKRKFQD |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| CHEK2 (go to UniProt):O96017 |
| 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 |
| O96017 | Domain | 113 | 175 | Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 | Type=Substitution;Start=131;End=147 |
| O96017 | Domain | 113 | 175 | Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 | Type=Deletion;Start=148;End=543 |
| O96017 | Domain | 113 | 175 | Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 | Type=Deletion;Start=75;End=392 |
| O96017 | Domain | 113 | 175 | Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 | Type=Deletion;Start=1;End=221 |
| O96017 | Domain | 113 | 175 | Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 | Type=Deletion;Start=107;End=487 |
| O96017 | Domain | 113 | 175 | Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 | Type=Deletion;Start=107;End=197 |
| O96017 | Domain | 113 | 175 | Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 | Type=Substitution;Start=150;End=165 |
| O96017 | Domain | 113 | 175 | Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 | Type=Deletion;Start=166;End=543 |
| O96017 | Domain | 220 | 486 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=148;End=543 |
| O96017 | Domain | 220 | 486 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=75;End=392 |
| O96017 | Domain | 220 | 486 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=337;End=365 |
| O96017 | Domain | 220 | 486 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=1;End=221 |
| O96017 | Domain | 220 | 486 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Substitution;Start=198;End=224 |
| O96017 | Domain | 220 | 486 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Substitution;Start=228;End=234 |
| O96017 | Domain | 220 | 486 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=235;End=543 |
| O96017 | Domain | 220 | 486 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=107;End=487 |
| O96017 | Domain | 220 | 486 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=204;End=543 |
| O96017 | Domain | 220 | 486 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=166;End=543 |
| O96017 | Domain | 220 | 486 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Substitution;Start=337;End=339 |
| O96017 | Domain | 220 | 486 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=340;End=543 |
| O96017 | Domain | 220 | 486 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Substitution;Start=283;End=289 |
| O96017 | Domain | 220 | 486 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=290;End=543 |
| O96017 | Region | 1 | 66 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=221 |
| O96017 | Region | 368 | 394 | Note=T-loop/activation segment | Type=Deletion;Start=148;End=543 |
| O96017 | Region | 368 | 394 | Note=T-loop/activation segment | Type=Deletion;Start=75;End=392 |
| O96017 | Region | 368 | 394 | Note=T-loop/activation segment | Type=Deletion;Start=235;End=543 |
| O96017 | Region | 368 | 394 | Note=T-loop/activation segment | Type=Deletion;Start=107;End=487 |
| O96017 | Region | 368 | 394 | Note=T-loop/activation segment | Type=Deletion;Start=204;End=543 |
| O96017 | Region | 368 | 394 | Note=T-loop/activation segment | Type=Deletion;Start=166;End=543 |
| O96017 | Region | 368 | 394 | Note=T-loop/activation segment | Type=Deletion;Start=340;End=543 |
| O96017 | Region | 368 | 394 | Note=T-loop/activation segment | Type=Deletion;Start=290;End=543 |
| O96017 | Region | 506 | 538 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=148;End=543 |
| O96017 | Region | 506 | 538 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=235;End=543 |
| O96017 | Region | 506 | 538 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=204;End=543 |
| O96017 | Region | 506 | 538 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=166;End=543 |
| O96017 | Region | 506 | 538 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=340;End=543 |
| O96017 | Region | 506 | 538 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=290;End=543 |
| O96017 | Compositional bias | 7 | 66 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=221 |
Gene Isoform Structures and Expression Levels for CHEK2 |
| Gene structures of our canonical and alternative spliced genes of CHEK2 * 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 O96017-1 |
| 3D view using mol* of O96017-10 |
| 3D view using mol* of O96017-11 |
| 3D view using mol* of O96017-12 |
| 3D view using mol* of O96017-13 |
| 3D view using mol* of O96017-2 |
| 3D view using mol* of O96017-3 |
| 3D view using mol* of O96017-4 |
| 3D view using mol* of O96017-5 |
| 3D view using mol* of O96017-6 |
| 3D view using mol* of O96017-7 |
| 3D view using mol* of O96017-8 |
| 3D view using mol* of O96017-9 |
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 O96017-1 |
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| pLDDT distribution across the protein length of O96017-10 |
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| pLDDT distribution across the protein length of O96017-11 |
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| pLDDT distribution across the protein length of O96017-12 |
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| pLDDT distribution across the protein length of O96017-13 |
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| pLDDT distribution across the protein length of O96017-2 |
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| pLDDT distribution across the protein length of O96017-3 |
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| pLDDT distribution across the protein length of O96017-4 |
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| pLDDT distribution across the protein length of O96017-5 |
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| pLDDT distribution across the protein length of O96017-6 |
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| pLDDT distribution across the protein length of O96017-7 |
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| pLDDT distribution across the protein length of O96017-8 |
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| pLDDT distribution across the protein length of O96017-9 |
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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 O96017-1 |
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| Ramachandran plot of O96017-10 |
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| Ramachandran plot of O96017-11 |
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| Ramachandran plot of O96017-12 |
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| Ramachandran plot of O96017-2 |
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| Ramachandran plot of O96017-4 |
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| Ramachandran plot of O96017-5 |
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| Ramachandran plot of O96017-7 |
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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 |
| O96017-1 | 1.047 | 283 | 1.034 | 821.828 | 0.502 | 0.768 | 1.009 | 0.629 | 1.127 | 0.558 | 0.862 | 99,186,188,197,200,223,224,226,227,228,229,230,231 ,232,234,236,238,245,247,249,286,301,302,303,304,3 05,307,308,342,343,344,345,346,347,348,349,351,352 ,354,367,368,371,372,373,375,376,377,379,380,382,3 83,386,387,390,391,392,394,395,398,399,400,401,402 ,404,405,408,409,412 |
| O96017-10 | 0.576 | 22 | 0.499 | 69.629 | 0.614 | 0.626 | 0.861 | 0.843 | 0.973 | 0.867 | 0.395 | 103,117,125,130,131,133,134,135
|
| O96017-11 | 0.674 | 41 | 0.64 | 109.074 | 0.723 | 0.577 | 0.748 | 0.101 | 0.946 | 0.107 | 1.672 | 106,107,108,109,110,112,113,114,116,121,126,127,12 8,129 |
| O96017-12 | 1.08 | 233 | 1.107 | 730.59 | 0.492 | 0.788 | 0.986 | 0.928 | 0.938 | 0.988 | 1.046 | 230,231,249,251,255,256,274,277,278,280,285,286,28 7,288,299,301,335,338,339,341,342,343,344,346,347, 349,351,352,353,354,355,356,357,362,372,373,375,37 6,377,380,512,513,514 |
| O96017-13 | 1.064 | 157 | 1.014 | 429.436 | 0.453 | 0.794 | 1.041 | 0.598 | 1.235 | 0.484 | 1.098 | 5,6,7,8,9,10,11,13,26,28,65,80,81,82,83,86,87,124, 125,126,128,130,131,133,146,147,148,149,150,151,15 8,161,162,165,166 |
| O96017-2 | 1.003 | 174 | 1.047 | 646.898 | 0.634 | 0.656 | 0.937 | 0.895 | 0.878 | 1.018 | 0.756 | 90,91,92,93,94,95,97,99,109,148,156,157,158,182,18 3,184,185,202,203,204,205,206,207,208,209,210,211, 212,216,217,218,219,220,221,223,225,228,230,231,23 2,233,234 |
| O96017-3 | 0.48 | 14 | 0.314 | 36.358 | 0.689 | 0.607 | 1.095 | 0.497 | 1.231 | 0.404 | 0.442 | 95,96,97,98,99,100
|
| O96017-4 | 1.058 | 185 | 1.073 | 488.432 | 0.454 | 0.782 | 1.053 | 0.847 | 1.031 | 0.821 | 1.309 | 135,136,137,138,139,140,141,143,156,158,195,210,21 1,212,213,214,216,217,255,256,257,258,260,261,263, 267,276,277,280,281,284,288,289,291,292,295,296,29 7,299,300,321 |
| O96017-5 | 0.576 | 15 | 0.534 | 43.218 | 0.776 | 0.609 | 0.815 | 1.06 | 0.598 | 1.772 | 0.724 | 93,94,148,155,156,157,158,183,201,203
|
| O96017-6 | 0.791 | 32 | 0.806 | 149.548 | 0.756 | 0.681 | 0.785 | 1.594 | 0.413 | 3.861 | 0.55 | 96,97,98,99,100,103,104,105,106,115,123,125,144
|
| O96017-7 | 0.961 | 98 | 0.91 | 395.136 | 0.64 | 0.65 | 0.902 | 0.167 | 1.26 | 0.132 | 0.883 | 90,91,92,93,109,148,155,156,204,205,206,207,208,20 9,210,211,212,213,222,223,224,225,229,232,233,235, 250,251,252,255,295,296,298 |
| O96017-8 | 0.899 | 78 | 0.933 | 279.202 | 0.721 | 0.607 | 0.737 | 0.578 | 0.802 | 0.72 | 1.427 | 234,239,244,246,247,248,249,250,251,274,277,278,28 0,281,282,284,285,286,287,288,289 |
| O96017-9 | 1.041 | 290 | 1 | 776.209 | 0.497 | 0.759 | 1.031 | 0.554 | 1.212 | 0.457 | 0.902 | 269,270,271,272,273,274,275,277,290,292,316,320,32 9,342,344,345,346,347,350,351,384,385,386,387,388, 389,390,391,392,394,395,397,410,411,413,414,415,41 6,419,420,422,423,424,425,426,427,429,430,433,434, 435,437,438,441,442,443,444,445,447,448,451,455 |
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 O96017-1_O96017-1_3i6u_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 O96017-1_3i6u_A_O96017-10.pdb |
| 3D view using mol* of O96017-1_3i6u_A_O96017-11.pdb |
| 3D view using mol* of O96017-1_3i6u_A_O96017-12.pdb |
| 3D view using mol* of O96017-1_3i6u_A_O96017-13.pdb |
| 3D view using mol* of O96017-1_3i6u_A_O96017-2.pdb |
| 3D view using mol* of O96017-1_3i6u_A_O96017-3.pdb |
| 3D view using mol* of O96017-1_3i6u_A_O96017-4.pdb |
| 3D view using mol* of O96017-1_3i6u_A_O96017-5.pdb |
| 3D view using mol* of O96017-1_3i6u_A_O96017-6.pdb |
| 3D view using mol* of O96017-1_3i6u_A_O96017-7.pdb |
| 3D view using mol* of O96017-1_3i6u_A_O96017-8.pdb |
| 3D view using mol* of O96017-1_3i6u_A_O96017-9.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of O96017-1_O96017-10.pdb |
| 3D view using mol* of O96017-1_O96017-11.pdb |
| 3D view using mol* of O96017-1_O96017-12.pdb |
| 3D view using mol* of O96017-1_O96017-13.pdb |
| 3D view using mol* of O96017-1_O96017-2.pdb |
| 3D view using mol* of O96017-1_O96017-3.pdb |
| 3D view using mol* of O96017-1_O96017-4.pdb |
| 3D view using mol* of O96017-1_O96017-5.pdb |
| 3D view using mol* of O96017-1_O96017-6.pdb |
| 3D view using mol* of O96017-1_O96017-7.pdb |
| 3D view using mol* of O96017-1_O96017-8.pdb |
| 3D view using mol* of O96017-1_O96017-9.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/O96017-1_vs_O96017-10.png |
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| ./stats/secondary_structure/figure/O96017-1_vs_O96017-11.png |
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| ./stats/secondary_structure/figure/O96017-1_vs_O96017-12.png |
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| ./stats/secondary_structure/figure/O96017-1_vs_O96017-13.png |
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| ./stats/secondary_structure/figure/O96017-1_vs_O96017-2.png |
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| ./stats/secondary_structure/figure/O96017-1_vs_O96017-3.png |
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| ./stats/secondary_structure/figure/O96017-1_vs_O96017-4.png |
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| ./stats/secondary_structure/figure/O96017-1_vs_O96017-5.png |
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| ./stats/secondary_structure/figure/O96017-1_vs_O96017-6.png |
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| ./stats/secondary_structure/figure/O96017-1_vs_O96017-7.png |
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| ./stats/secondary_structure/figure/O96017-1_vs_O96017-8.png |
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| ./stats/secondary_structure/figure/O96017-1_vs_O96017-9.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/O96017-1_vs_O96017-10.png |
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| ./stats/relative_asa/O96017-1_vs_O96017-11.png |
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| ./stats/relative_asa/O96017-1_vs_O96017-12.png |
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| ./stats/relative_asa/O96017-1_vs_O96017-13.png |
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| ./stats/relative_asa/O96017-1_vs_O96017-2.png |
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| ./stats/relative_asa/O96017-1_vs_O96017-3.png |
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| ./stats/relative_asa/O96017-1_vs_O96017-4.png |
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| ./stats/relative_asa/O96017-1_vs_O96017-5.png |
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| ./stats/relative_asa/O96017-1_vs_O96017-6.png |
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| ./stats/relative_asa/O96017-1_vs_O96017-7.png |
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| ./stats/relative_asa/O96017-1_vs_O96017-8.png |
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| ./stats/relative_asa/O96017-1_vs_O96017-9.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to CHEK2 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| O96017 | CHEK2 | DB05149 | XL844 | investigational | |
| O96017 | CHEK2 | DB06486 | Enzastaurin | investigational | |
| O96017 | CHEK2 | DB12010 | Fostamatinib | approved, investigational | inhibitor |
Related Diseases to CHEK2 |
| Previous studies relating to the alternative splicing of CHEK2 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| CHEK2 | 15361853 | Alternative splicing and mutation status of CHEK2 in stage III breast cancer. | The DNA damage checkpoint kinase, CHK2, promotes growth arrest or apoptosis through phosphorylating targets such as Cdc25A, Cdc25C, BRCA1, and p53. Both germline and somatic loss-of-function CHEK2 mutations occur in human tumours, the former linked to the Li-Fraumeni syndrome, and the latter found in diverse types of sporadic malignancies. Here we examined the status of CHK2 by genetic and immunohistochemical analyses in 53 breast carcinomas previously characterized for TP53 status. We identified two CHEK2 mutants, 470T>C (Ile157Thr), and a novel mutation, 1368insA leading to a premature stop codon in exon 13. The truncated protein encoded by CHEK2 carrying the 1368insA was stable yet mislocalized to the cytoplasm in tumour sections and when ectopically expressed in cultured cells. Unexpectedly, we found CHEK2 to be subject to extensive alternative splicing, with some 90 splice variants detected in our tumour series. While all cancers expressed normal-length CHEK2 mRNA together with the spliced transcripts, we demonstrate and/or predict some of these splice variants to lack CHK2 function and/or localize aberrantly. We conclude that cytoplasmic sequestration may represent a novel mechanism to disable CHK2, and propose to further explore the significance of the complex splicing patterns of this tumour suppressor gene in oncogenesis. | D001943 | Breast Neoplasms |
| CHEK2 | 20080130 | Chk2 splice variants express a dominant-negative effect on the wild-type Chk2 kinase activity. | While the majority of RNA transcripts from protein-encoding genes in the human genome are subject to physiological splicing, pathological splicing is increasingly reported in cancer tissue. Previously, we identified >90 different splice variants of Chk2, a gene encoding a serine/threonine kinase propagating the DNA damage signal by phosphorylating and activating several downstream substrates like p53, Cdc25A, and Cdc25C involved in cell cycle arrest and apoptosis. While alternative splice forms of other genes have been reported to exert a dominant-negative effect on the wild-type molecules, the function of Chk2 splice protein variants is still unclear. Here we evaluated the function of four Chk2 splice proteins for which mRNA splice variants were identified in human breast carcinomas. These splice variants were stably expressed as nuclear proteins. Two splice forms (Chk2Delta4 and Chk2del(2-3)) expressed kinase activity while variants Chk2Delta11 and Chk2isoI were essentially kinase inactive. Independent of intrinsic kinase activity, each splice variant impaired wild-type Chk2 activity through heterodimerization. Based on our findings, we suggest alternative splicing as a possible novel mechanism for repression of the Chk2 wild-type function. | D001943 | Breast Neoplasms |
| CHEK2 | 21765476 | CHEK2 genomic and proteomic analyses reveal genetic inactivation or endogenous activation across the 60 cell lines of the US National Cancer Institute. | CHEK2 encodes a serine/threonine kinase (Chk2) activated by ATM in response to DNA double-strand breaks. On the one hand, CHEK2 has been described as a tumor suppressor with proapoptotic, cell-cycle checkpoint and mitotic functions. On the other hand, Chk2 is also commonly activated (phosphorylated at T68) in cancers and precancerous lesions. Here, we report an extensive characterization of CHEK2 across the panel of 60 established cancer cell lines from the NCI Anticancer Screen (the NCI-60) using genomic and proteomic analyses, including exon-specific mRNA expression, DNA copy-number variation (CNV) by aCGH, exome sequencing, as well as western blot analyses for total and activated (pT68-Chk2) Chk2. We show that the high heterogeneity of Chk2 levels in cancer cells is primarily due to its inactivation (owing to low gene expression, alternative splicing, point mutations, copy-number alterations and premature truncation) or reduction of protein levels. Moreover, we observe that a significant percentage of cancer cells (12% of the NCI-60 and HeLa cells) show high endogenous Chk2 activation, which is always associated with p53 inactivation, and which is accompanied by downregulation of the Fanconi anemia and homologous recombination pathways. We also report the presence of activated Chk2 (pT68-Chk2) along with histone γ-H2AX in centrosomes. | D043171 | Chromosomal Instability |
| CHEK2 | 21765476 | CHEK2 genomic and proteomic analyses reveal genetic inactivation or endogenous activation across the 60 cell lines of the US National Cancer Institute. | CHEK2 encodes a serine/threonine kinase (Chk2) activated by ATM in response to DNA double-strand breaks. On the one hand, CHEK2 has been described as a tumor suppressor with proapoptotic, cell-cycle checkpoint and mitotic functions. On the other hand, Chk2 is also commonly activated (phosphorylated at T68) in cancers and precancerous lesions. Here, we report an extensive characterization of CHEK2 across the panel of 60 established cancer cell lines from the NCI Anticancer Screen (the NCI-60) using genomic and proteomic analyses, including exon-specific mRNA expression, DNA copy-number variation (CNV) by aCGH, exome sequencing, as well as western blot analyses for total and activated (pT68-Chk2) Chk2. We show that the high heterogeneity of Chk2 levels in cancer cells is primarily due to its inactivation (owing to low gene expression, alternative splicing, point mutations, copy-number alterations and premature truncation) or reduction of protein levels. Moreover, we observe that a significant percentage of cancer cells (12% of the NCI-60 and HeLa cells) show high endogenous Chk2 activation, which is always associated with p53 inactivation, and which is accompanied by downregulation of the Fanconi anemia and homologous recombination pathways. We also report the presence of activated Chk2 (pT68-Chk2) along with histone γ-H2AX in centrosomes. | D005199 | Fanconi Anemia |
| CHEK2 | 21765476 | CHEK2 genomic and proteomic analyses reveal genetic inactivation or endogenous activation across the 60 cell lines of the US National Cancer Institute. | CHEK2 encodes a serine/threonine kinase (Chk2) activated by ATM in response to DNA double-strand breaks. On the one hand, CHEK2 has been described as a tumor suppressor with proapoptotic, cell-cycle checkpoint and mitotic functions. On the other hand, Chk2 is also commonly activated (phosphorylated at T68) in cancers and precancerous lesions. Here, we report an extensive characterization of CHEK2 across the panel of 60 established cancer cell lines from the NCI Anticancer Screen (the NCI-60) using genomic and proteomic analyses, including exon-specific mRNA expression, DNA copy-number variation (CNV) by aCGH, exome sequencing, as well as western blot analyses for total and activated (pT68-Chk2) Chk2. We show that the high heterogeneity of Chk2 levels in cancer cells is primarily due to its inactivation (owing to low gene expression, alternative splicing, point mutations, copy-number alterations and premature truncation) or reduction of protein levels. Moreover, we observe that a significant percentage of cancer cells (12% of the NCI-60 and HeLa cells) show high endogenous Chk2 activation, which is always associated with p53 inactivation, and which is accompanied by downregulation of the Fanconi anemia and homologous recombination pathways. We also report the presence of activated Chk2 (pT68-Chk2) along with histone γ-H2AX in centrosomes. | D009369 | Neoplasms |
| CHEK2 | 22355270 | Alternative splicing of CHEK2 and codeletion with NF2 promote chromosomal instability in meningioma. | Mutations of the NF2 gene on chromosome 22q are thought to initiate tumorigenesis in nearly 50% of meningiomas, and 22q deletion is the earliest and most frequent large-scale chromosomal abnormality observed in these tumors. In aggressive meningiomas, 22q deletions are generally accompanied by the presence of large-scale segmental abnormalities involving other chromosomes, but the reasons for this association are unknown. We find that large-scale chromosomal alterations accumulate during meningioma progression primarily in tumors harboring 22q deletions, suggesting 22q-associated chromosomal instability. Here we show frequent codeletion of the DNA repair and tumor suppressor gene, CHEK2, in combination with NF2 on chromosome 22q in a majority of aggressive meningiomas. In addition, tumor-specific splicing of CHEK2 in meningioma leads to decreased functional Chk2 protein expression. We show that enforced Chk2 knockdown in meningioma cells decreases DNA repair. Furthermore, Chk2 depletion increases centrosome amplification, thereby promoting chromosomal instability. Taken together, these data indicate that alternative splicing and frequent codeletion of CHEK2 and NF2 contribute to the genomic instability and associated development of aggressive biologic behavior in meningiomas. | D043171 | Chromosomal Instability |
| CHEK2 | 22355270 | Alternative splicing of CHEK2 and codeletion with NF2 promote chromosomal instability in meningioma. | Mutations of the NF2 gene on chromosome 22q are thought to initiate tumorigenesis in nearly 50% of meningiomas, and 22q deletion is the earliest and most frequent large-scale chromosomal abnormality observed in these tumors. In aggressive meningiomas, 22q deletions are generally accompanied by the presence of large-scale segmental abnormalities involving other chromosomes, but the reasons for this association are unknown. We find that large-scale chromosomal alterations accumulate during meningioma progression primarily in tumors harboring 22q deletions, suggesting 22q-associated chromosomal instability. Here we show frequent codeletion of the DNA repair and tumor suppressor gene, CHEK2, in combination with NF2 on chromosome 22q in a majority of aggressive meningiomas. In addition, tumor-specific splicing of CHEK2 in meningioma leads to decreased functional Chk2 protein expression. We show that enforced Chk2 knockdown in meningioma cells decreases DNA repair. Furthermore, Chk2 depletion increases centrosome amplification, thereby promoting chromosomal instability. Taken together, these data indicate that alternative splicing and frequent codeletion of CHEK2 and NF2 contribute to the genomic instability and associated development of aggressive biologic behavior in meningiomas. | D018450 | Disease Progression |
| CHEK2 | 22355270 | Alternative splicing of CHEK2 and codeletion with NF2 promote chromosomal instability in meningioma. | Mutations of the NF2 gene on chromosome 22q are thought to initiate tumorigenesis in nearly 50% of meningiomas, and 22q deletion is the earliest and most frequent large-scale chromosomal abnormality observed in these tumors. In aggressive meningiomas, 22q deletions are generally accompanied by the presence of large-scale segmental abnormalities involving other chromosomes, but the reasons for this association are unknown. We find that large-scale chromosomal alterations accumulate during meningioma progression primarily in tumors harboring 22q deletions, suggesting 22q-associated chromosomal instability. Here we show frequent codeletion of the DNA repair and tumor suppressor gene, CHEK2, in combination with NF2 on chromosome 22q in a majority of aggressive meningiomas. In addition, tumor-specific splicing of CHEK2 in meningioma leads to decreased functional Chk2 protein expression. We show that enforced Chk2 knockdown in meningioma cells decreases DNA repair. Furthermore, Chk2 depletion increases centrosome amplification, thereby promoting chromosomal instability. Taken together, these data indicate that alternative splicing and frequent codeletion of CHEK2 and NF2 contribute to the genomic instability and associated development of aggressive biologic behavior in meningiomas. | D008577 | Meningeal Neoplasms |
| CHEK2 | 22355270 | Alternative splicing of CHEK2 and codeletion with NF2 promote chromosomal instability in meningioma. | Mutations of the NF2 gene on chromosome 22q are thought to initiate tumorigenesis in nearly 50% of meningiomas, and 22q deletion is the earliest and most frequent large-scale chromosomal abnormality observed in these tumors. In aggressive meningiomas, 22q deletions are generally accompanied by the presence of large-scale segmental abnormalities involving other chromosomes, but the reasons for this association are unknown. We find that large-scale chromosomal alterations accumulate during meningioma progression primarily in tumors harboring 22q deletions, suggesting 22q-associated chromosomal instability. Here we show frequent codeletion of the DNA repair and tumor suppressor gene, CHEK2, in combination with NF2 on chromosome 22q in a majority of aggressive meningiomas. In addition, tumor-specific splicing of CHEK2 in meningioma leads to decreased functional Chk2 protein expression. We show that enforced Chk2 knockdown in meningioma cells decreases DNA repair. Furthermore, Chk2 depletion increases centrosome amplification, thereby promoting chromosomal instability. Taken together, these data indicate that alternative splicing and frequent codeletion of CHEK2 and NF2 contribute to the genomic instability and associated development of aggressive biologic behavior in meningiomas. | D008579 | Meningioma |
Clinically important variants in CHEK2 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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