{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O96017","secondaryAccessions":["A8K3Y9","B7ZBF3","B7ZBF4","B7ZBF5","Q6QA03","Q6QA04","Q6QA05","Q6QA06","Q6QA07","Q6QA08","Q6QA10","Q6QA11","Q6QA12","Q6QA13","Q9HBS5","Q9HCQ8","Q9UGF0","Q9UGF1"],"uniProtkbId":"CHK2_HUMAN","entryAudit":{"firstPublicDate":"2000-05-30","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1999-05-01","entryVersion":258,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Serine/threonine-protein kinase Chk2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37943659"}],"value":"2.7.11.1"}]},"alternativeNames":[{"fullName":{"value":"CHK2 checkpoint homolog"}},{"fullName":{"value":"Cds1 homolog"},"shortNames":[{"value":"Hucds1"},{"value":"hCds1"}]},{"fullName":{"value":"Checkpoint kinase 2"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:16627"}],"value":"CHEK2"},"synonyms":[{"value":"CDS1"},{"value":"CHK2"},{"value":"RAD53"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9Z265"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10097108"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10724175"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11298456"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12402044"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12607004"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12717439"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12810724"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16163388"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17101782"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17380128"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17715138"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18317453"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18644861"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18728393"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20364141"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25361978"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25619829"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37943659"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9836640"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9889122"}],"value":"Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest, activation of DNA repair and apoptosis in response to the presence of DNA double-strand breaks. May also negatively regulate cell cycle progression during unperturbed cell cycles. Following activation, phosphorylates numerous effectors preferentially at the consensus sequence [L-X-R-X-X-S/T] (PubMed:37943659). Regulates cell cycle checkpoint arrest through phosphorylation of CDC25A, CDC25B and CDC25C, inhibiting their activity. Inhibition of CDC25 phosphatase activity leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression. May also phosphorylate NEK6 which is involved in G2/M cell cycle arrest. Regulates DNA repair through phosphorylation of BRCA2, enhancing the association of RAD51 with chromatin which promotes DNA repair by homologous recombination. Also stimulates the transcription of genes involved in DNA repair (including BRCA2) through the phosphorylation and activation of the transcription factor FOXM1. Regulates apoptosis through the phosphorylation of p53/TP53, MDM4 and PML. Phosphorylation of p53/TP53 at 'Ser-20' by CHEK2 may alleviate inhibition by MDM2, leading to accumulation of active p53/TP53. Phosphorylation of MDM4 may also reduce degradation of p53/TP53. Also controls the transcription of pro-apoptotic genes through phosphorylation of the transcription factor E2F1. Tumor suppressor, it may also have a DNA damage-independent function in mitotic spindle assembly by phosphorylating BRCA1. Its absence may be a cause of the chromosomal instability observed in some cancer cells. Promotes the CCAR2-SIRT1 association and is required for CCAR2-mediated SIRT1 inhibition (PubMed:25361978). Under oxidative stress, promotes ATG7 ubiquitination by phosphorylating the E3 ubiquitin ligase TRIM32 at 'Ser-55' leading to positive regulation of the autophagosme assembly (PubMed:37943659)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32001251"}],"value":"(Microbial infection) Phosphorylates herpes simplex virus 1/HHV-1 protein ICP0 and thus activates its SUMO-targeted ubiquitin ligase activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17989"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:11604"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83421"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37943659"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1"}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15342622"}],"value":"Activated through phosphorylation at Thr-68 by ATM in response to DNA double-strand breaks. Activation is modulated by several mediators including MDC1 and TP53BP1. Induces homodimerization with exchange of the T-loop/activation segment between protomers and transphosphorylation of the protomers. The autophosphorylated kinase dimer is fully active. Negatively regulated by PPM1D through dephosphorylation of Thr-68"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10724175"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11298456"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12364621"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12607004"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12810724"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16794575"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18644861"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24825908"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25361978"}],"value":"Homodimer. Homodimerization is part of the activation process but the dimer may dissociate following activation. Interacts with PML. Interacts with TP53. Interacts with RB1; phosphorylates RB1. Interacts with BRCA1. Interacts (phosphorylated at Thr-68) with MDC1; requires ATM-mediated phosphorylation of CHEK2. Interacts with TP53BP1; modulates CHEK2 phosphorylation at Thr-68 in response to ionizing radiation. Interacts with CDC25A; phosphorylates CDC25A and mediates its degradation in response to ionizing radiation. Interacts with CUL1; mediates CHEK2 ubiquitination and regulation. Interacts with CDKN2AIP. Interacts (via protein kinase domain) with CCAR2 (via N-terminus). Interacts with SIRT1"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"Q9NY61","geneName":"AATF","intActId":"EBI-372428"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"Q9UQ88-1","geneName":"CDK11A","intActId":"EBI-11579223"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"O96017","geneName":"CHEK2","intActId":"EBI-1180783"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"Q9Y248","geneName":"GINS2","intActId":"EBI-747491"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"Q13007","geneName":"IL24","intActId":"EBI-3915542"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"Q96KN1","geneName":"LRATD2","intActId":"EBI-9057780"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"P56645","geneName":"PER3","intActId":"EBI-2827813"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"P53350","geneName":"PLK1","intActId":"EBI-476768"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"O15355","geneName":"PPM1G","intActId":"EBI-725702"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"Q15172","geneName":"PPP2R5A","intActId":"EBI-641666"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"Q15173","geneName":"PPP2R5B","intActId":"EBI-1369497"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"Q13362-1","geneName":"PPP2R5C","intActId":"EBI-1266170"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"Q13362-2","geneName":"PPP2R5C","intActId":"EBI-1266173"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"Q13362-3","geneName":"PPP2R5C","intActId":"EBI-1266176"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"Q16537","geneName":"PPP2R5E","intActId":"EBI-968374"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"P06400","geneName":"RB1","intActId":"EBI-491274"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"Q5VTR2","geneName":"RNF20","intActId":"EBI-2372238"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"Q93009","geneName":"USP7","intActId":"EBI-302474"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"P55072","geneName":"VCP","intActId":"EBI-355164"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"P18887","geneName":"XRCC1","intActId":"EBI-947466"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"P0C6X7","geneName":"rep","chainId":"PRO_0000037319","intActId":"EBI-25487926"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"P06725","geneName":"UL83","intActId":"EBI-9545359"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"O96017","intActId":"EBI-1180783"},"interactantTwo":{"uniProtKBAccession":"P27958","chainId":"PRO_0000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nucleoplasm","id":"SL-0190"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["O96017-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"synonyms":[{"value":"ins2"}],"isoformIds":["O96017-2"],"sequenceIds":["VSP_014564","VSP_014567","VSP_014568"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"synonyms":[{"value":"del2-12"}],"isoformIds":["O96017-3"],"sequenceIds":["VSP_014559"],"isoformSequenceStatus":"Described"},{"name":{"value":"4"},"synonyms":[{"value":"del2-3"}],"isoformIds":["O96017-4"],"sequenceIds":["VSP_014558"],"isoformSequenceStatus":"Described"},{"name":{"value":"5"},"synonyms":[{"value":"del4"}],"isoformIds":["O96017-5"],"sequenceIds":["VSP_014565","VSP_014566"],"isoformSequenceStatus":"Described"},{"name":{"value":"6"},"synonyms":[{"value":"sub3"}],"isoformIds":["O96017-6"],"sequenceIds":["VSP_014562","VSP_014563"],"isoformSequenceStatus":"Described"},{"name":{"value":"7"},"synonyms":[{"value":"del9-12"}],"isoformIds":["O96017-7"],"sequenceIds":["VSP_014572","VSP_014573"],"isoformSequenceStatus":"Described"},{"name":{"value":"8"},"synonyms":[{"value":"del7"}],"isoformIds":["O96017-8"],"sequenceIds":["VSP_014569","VSP_014570"],"isoformSequenceStatus":"Described"},{"name":{"value":"9"},"synonyms":[{"value":"insx"}],"isoformIds":["O96017-9"],"sequenceIds":["VSP_014557"],"isoformSequenceStatus":"Described"},{"name":{"value":"10"},"synonyms":[{"value":"iso2"}],"isoformIds":["O96017-10"],"sequenceIds":["VSP_014560","VSP_014561"],"isoformSequenceStatus":"Described"},{"name":{"value":"11"},"synonyms":[{"value":"iso1"}],"isoformIds":["O96017-11"],"sequenceIds":["VSP_014556"],"isoformSequenceStatus":"Described"},{"name":{"value":"12"},"synonyms":[{"value":"del9"}],"isoformIds":["O96017-12"],"sequenceIds":["VSP_014571"],"isoformSequenceStatus":"Described"},{"name":{"value":"13"},"isoformIds":["O96017-13"],"sequenceIds":["VSP_045148"],"isoformSequenceStatus":"Described"}]},{"texts":[{"value":"High expression is found in testis, spleen, colon and peripheral blood leukocytes. Low expression is found in other tissues"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10973490"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11390408"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15342622"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16311512"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16481012"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17715138"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18644861"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19164942"}],"value":"Phosphorylated. Phosphorylated at Ser-73 by PLK3 in response to DNA damage, promoting phosphorylation at Thr-68 by ATM and the G2/M transition checkpoint. Phosphorylation at Thr-68 induces homodimerization. Autophosphorylates at Thr-383 and Thr-387 in the T-loop/activation segment upon dimerization to become fully active and phosphorylate its substrates like for instance CDC25C. DNA damage-induced autophosphorylation at Ser-379 induces CUL1-mediated ubiquitination and regulates the pro-apoptotic function. Phosphorylation at Ser-456 also regulates ubiquitination. Phosphorylated by PLK4"}],"commentType":"PTM"},{"texts":[{"value":"Ubiquitinated. CUL1-mediated ubiquitination regulates the pro-apoptotic function. Ubiquitination may also regulate protein stability. Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Tumor predisposition syndrome 4","diseaseAccession":"DI-02882","acronym":"TPDS4","description":"A disorder characterized by an increased risk for developing various types of benign and/or malignant neoplasms that arise at an accelerated rate and in different organs.","diseaseCrossReference":{"database":"MIM","id":"609265"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11719428"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Prostate cancer","diseaseAccession":"DI-02663","acronym":"PC","description":"A malignancy originating in tissues of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma.","diseaseCrossReference":{"database":"MIM","id":"176807"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12533788"}]},"note":{"texts":[{"value":"Disease susceptibility is associated with variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Osteogenic sarcoma","diseaseAccession":"DI-02109","acronym":"OSRC","description":"A sarcoma originating in bone-forming cells, affecting the ends of long bones.","diseaseCrossReference":{"database":"MIM","id":"259500"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11746983"}]},"note":{"texts":[{"value":"The gene represented in this entry may be involved in disease pathogenesis"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Breast cancer","diseaseAccession":"DI-02602","acronym":"BC","description":"A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case.","diseaseCrossReference":{"database":"MIM","id":"114480"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12094328"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12454775"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12610780"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15818573"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21618645"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25619829"}]},"note":{"texts":[{"value":"Disease susceptibility is associated with variants affecting the gene represented in this entry"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Lacks enzymatic activity"}],"commentType":"MISCELLANEOUS","molecule":"Isoform 2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Lacks enzymatic activity"}],"commentType":"MISCELLANEOUS","molecule":"Isoform 4"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Lacks enzymatic activity"}],"commentType":"MISCELLANEOUS","molecule":"Isoform 7"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Retains low level of catalytic activity"}],"commentType":"MISCELLANEOUS","molecule":"Isoform 9"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Lacks enzymatic activity"}],"commentType":"MISCELLANEOUS","molecule":"Isoform 10"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Lacks enzymatic activity"}],"commentType":"MISCELLANEOUS","molecule":"Isoform 12"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the protein kinase superfamily. 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CHK2 subfamily"}],"commentType":"SIMILARITY"},{"commentType":"WEB RESOURCE","resourceName":"Atlas of Genetics and Cytogenetics in Oncology and Haematology","resourceUrl":"https://atlasgeneticsoncology.org/gene/312/CHEK2","ftp":false}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":543,"modifier":"EXACT"}},"description":"Serine/threonine-protein kinase Chk2","featureId":"PRO_0000085858"},{"type":"Domain","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"FHA","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00086"}]},{"type":"Domain","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":486,"modifier":"EXACT"}},"description":"Protein 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