{"database":"JPOST Repository","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Csv":["https://storage.jpostdb.org/JPST003727/files/P4171_all_combined.csv","https://storage.jpostdb.org/JPST003727/files/P4171_DMTMM_CALM1_CHK2_XL.csv"],"Raw":["https://storage.jpostdb.org/JPST003727/files/P4551_01.raw","https://storage.jpostdb.org/JPST003727/files/P4551_03.raw","https://storage.jpostdb.org/JPST003727/files/P4171_03.raw","https://storage.jpostdb.org/JPST003727/files/P4171_05.raw","https://storage.jpostdb.org/JPST003727/files/P4551_04.raw","https://storage.jpostdb.org/JPST003727/files/P4551_02.raw","https://storage.jpostdb.org/JPST003727/files/P4171_01.raw","https://storage.jpostdb.org/JPST003727/files/P4171_02.raw","https://storage.jpostdb.org/JPST003727/files/P4171_04.raw"],"Mgf":["https://storage.jpostdb.org/JPST003727/files/P4551_03.mgf","https://storage.jpostdb.org/JPST003727/files/P4551_01.mgf","https://storage.jpostdb.org/JPST003727/files/P4171_05.mgf","https://storage.jpostdb.org/JPST003727/files/P4171_03.mgf","https://storage.jpostdb.org/JPST003727/files/P4551_02.mgf","https://storage.jpostdb.org/JPST003727/files/P4171_01.mgf","https://storage.jpostdb.org/JPST003727/files/P4171_04.mgf","https://storage.jpostdb.org/JPST003727/files/P4171_02.mgf"],"Fasta":["https://storage.jpostdb.org/JPST003727/files/P4171_ChrisD_CALM1__CHK2.fasta"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Prof. James Murphy"],"species":["Homo Sapiens (human)"],"full_dataset_link":["https://repository.jpostdb.org/entry/JPST003727"],"submitter_affiliation":["WEHI"],"sample_protocol":[""],"repository":["jPOST"],"data_protocol":[""],"pubmed_abstract":["Calmodulin (CaM) serves an essential role in eukaryotic cells as a Ca2+ sensor. Ca2+ binding leads to conformation changes in CaM that enable engagement of a repertoire of enzymes and the regulation of their catalytic activities. Classically, Ca2+-CaM binds to an inhibitory pseudosubstrate sequence C-terminal to the kinase domain in members of the Ca2+-CaM-dependent protein kinase (CAMK) family and relieves inhibition to promote catalytic activity. Here, we report an unexpected mechanism by which CaM can bind CHK2 kinase to inhibit its kinase activity. Using biochemical, biophysical and structural mass spectrometry, we identify a direct interaction of Ca2+-CaM with the CHK2 kinase domain that suppresses CHK2 catalytic activity in vitro and identify K373 in CHK2 as crucial for cell proliferation in human cells following DNA damage. Our findings add direct suppression of kinase activity to the repertoire of CaM's functions, complementing the paradigmatic mechanism of promoting kinase activity through autoinhibitory domain sequestration."],"pubmed_title":["Unconventional binding of calmodulin to CHK2 kinase inhibits catalytic activity."],"pubmed_authors":["Horne Christopher R CR, Wang Tingting T, Young Samuel N SN, Dite Toby A TA, Nyvall Hunter G HG, Suresh Sushant S, Davies Katherine A KA, Gonzalez Castro Abner A, Vaibhav Vineet V, Mather Lucy J LJ, Dagley Laura F LF, Belousoff Matthew J MJ, Manning Gerard G, Means Anthony R AR, Burke John E JE, Petersen Janni J, Scott John W JW, Murphy James M JM"],"additional_accession":[]},"is_claimable":false,"name":"Calmodulin and CHK2 kinase crosslinking","description":"Recombinant proteins were mixed and then crosslinked either with DMTMM or by SDA and UV exposure. Complexes were resolved by SDS-PAGE, excised and tryptic peptides identified by MS.","dates":{"publication":"Sat Mar 28 00:00:00 GMT 2026"},"accession":"PXD062332","cross_references":{"TAXONOMY":["9606"],"pubmed":["41003242"]}}