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O96017

- CHK2_HUMAN

UniProt

O96017 - CHK2_HUMAN

Protein

Serine/threonine-protein kinase Chk2

Gene

CHEK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    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]. 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.17 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    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-68.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei249 – 2491ATP
    Active sitei347 – 3471Proton acceptor
    Binding sitei368 – 3681ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi227 – 2348ATP
    Nucleotide bindingi302 – 3087ATP
    Nucleotide bindingi351 – 3522ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB
    6. protein kinase binding Source: UniProtKB
    7. protein serine/threonine kinase activity Source: UniProtKB
    8. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. cellular protein catabolic process Source: UniProtKB
    2. cellular response to DNA damage stimulus Source: UniProtKB
    3. DNA damage checkpoint Source: UniProtKB
    4. DNA damage induced protein phosphorylation Source: UniProtKB
    5. double-strand break repair Source: UniProtKB
    6. G2/M transition of mitotic cell cycle Source: UniProtKB
    7. intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
    8. positive regulation of transcription, DNA-templated Source: UniProtKB
    9. protein autophosphorylation Source: UniProtKB
    10. protein phosphorylation Source: UniProtKB
    11. protein stabilization Source: UniProtKB
    12. regulation of protein catabolic process Source: UniProtKB
    13. regulation of transcription, DNA-templated Source: UniProtKB
    14. replicative senescence Source: BHF-UCL
    15. response to gamma radiation Source: Ensembl
    16. signal transduction in response to DNA damage Source: MGI
    17. signal transduction involved in intra-S DNA damage checkpoint Source: UniProtKB
    18. spindle assembly involved in mitosis Source: UniProtKB
    19. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Cell cycle, Cell division, DNA damage, DNA repair, Mitosis, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    ReactomeiREACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_897. G2/M DNA damage checkpoint.
    SignaLinkiO96017.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase Chk2 (EC:2.7.11.1)
    Alternative name(s):
    CHK2 checkpoint homolog
    Cds1 homolog
    Short name:
    Hucds1
    Short name:
    hCds1
    Checkpoint kinase 2
    Gene namesi
    Name:CHEK2
    Synonyms:CDS1, CHK2, RAD53
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:16627. CHEK2.

    Subcellular locationi

    Isoform 2 : Nucleus
    Note: Isoform 10 is present throughout the cell.
    NucleusPML body. Nucleusnucleoplasm
    Note: Recruited into PML bodies together with TP53.

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. PML body Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Li-Fraumeni syndrome 2 (LFS2) [MIM:609265]: A highly penetrant familial cancer syndrome that in its classic form is defined by the existence of a proband affected by a sarcoma before 45 years with a first degree relative affected by any tumor before 45 years and another first degree relative with any tumor before 45 years or a sarcoma at any age. Other clinical definitions for LFS have been proposed (PubMed:8118819 and PubMed:8718514) and called Li-Fraumeni like syndrome (LFL). In these families affected relatives develop a diverse set of malignancies at unusually early ages. Four types of cancers account for 80% of tumors occurring in TP53 germline mutation carriers: breast cancers, soft tissue and bone sarcomas, brain tumors (astrocytomas) and adrenocortical carcinomas. Less frequent tumors include choroid plexus carcinoma or papilloma before the age of 15, rhabdomyosarcoma before the age of 5, leukemia, Wilms tumor, malignant phyllodes tumor, colorectal and gastric cancers.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti145 – 1451R → W in colon cancer and LFS2; does not cause protein abrogation in familial colorectal cancer; loss of the ability to interact with and phosphorylate CDC25A and to promote CDC25A degradation in response to ionizing radiation. 5 Publications
    VAR_008554
    Prostate cancer (PC) [MIM:176807]: 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.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Osteogenic sarcoma (OSRC) [MIM:259500]: A sarcoma originating in bone-forming cells, affecting the ends of long bones.
    Note: The gene represented in this entry may be involved in disease pathogenesis.
    Breast cancer (BC) [MIM:114480]: 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.2 Publications
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi68 – 681T → A: Loss of activation and phosphorylation. 2 Publications
    Mutagenesisi73 – 731S → A: Impaired activation, phosphorylation by ATM and G2/M transition checkpoint. 1 Publication
    Mutagenesisi347 – 3471D → A: Loss of kinase activity and of the ability to phosphorylate CDC25A. 2 Publications
    Mutagenesisi368 – 3681D → N: Loss of autophosphorylation activity. 1 Publication
    Mutagenesisi379 – 3791S → A: Abrogates autophosphorylation at Ser-379 and prevents ubiquitination. 1 Publication
    Mutagenesisi383 – 3831T → A: Loss of phosphorylation in response to ionizing radiation. 1 Publication
    Mutagenesisi387 – 3871T → A: Loss of phosphorylation in response to ionizing radiation. 1 Publication
    Mutagenesisi456 – 4561S → A: Increased ubiquitination and degradation by the proteasome. 1 Publication

    Keywords - Diseasei

    Disease mutation, Li-Fraumeni syndrome, Tumor suppressor

    Organism-specific databases

    MIMi114480. phenotype.
    176807. phenotype.
    259500. phenotype.
    604373. gene+phenotype.
    609265. phenotype.
    Orphaneti1331. Familial prostate cancer.
    145. Hereditary breast and ovarian cancer syndrome.
    524. Li-Fraumeni syndrome.
    668. Osteosarcoma.
    PharmGKBiPA404.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 543543Serine/threonine-protein kinase Chk2PRO_0000085858Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei62 – 621Phosphoserine; by PLK32 Publications
    Modified residuei68 – 681Phosphothreonine; by ATM and MLTK5 Publications
    Modified residuei73 – 731Phosphoserine; by PLK32 Publications
    Modified residuei379 – 3791Phosphoserine; by autocatalysis2 Publications
    Modified residuei383 – 3831Phosphothreonine; by autocatalysis2 Publications
    Modified residuei387 – 3871Phosphothreonine; by autocatalysis2 Publications
    Modified residuei456 – 4561Phosphoserine2 Publications

    Post-translational modificationi

    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 PLK4.8 Publications
    Ubiquitinated. CUL1-mediated ubiquitination regulates the pro-apoptotic function. Ubiquitination may also regulate protein stability. Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination.

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO96017.
    PaxDbiO96017.
    PRIDEiO96017.

    PTM databases

    PhosphoSiteiO96017.

    Expressioni

    Tissue specificityi

    High expression is found in testis, spleen, colon and peripheral blood leukocytes. Low expression is found in other tissues.

    Gene expression databases

    ArrayExpressiO96017.
    BgeeiO96017.
    GenevestigatoriO96017.

    Organism-specific databases

    HPAiCAB002030.
    HPA001878.

    Interactioni

    Subunit structurei

    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.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself6EBI-1180783,EBI-1180783
    P279583EBI-1180783,EBI-6904388From a different organism.
    AATFQ9NY614EBI-1180783,EBI-372428
    GINS2Q9Y2482EBI-1180783,EBI-747491
    PER3P566452EBI-1180783,EBI-2827813
    PLK1P533506EBI-1180783,EBI-476768
    PPP2R5AQ151722EBI-1180783,EBI-641666
    PPP2R5BQ151732EBI-1180783,EBI-1369497
    PPP2R5CQ13362-13EBI-1180783,EBI-1266170
    PPP2R5CQ13362-22EBI-1180783,EBI-1266173
    PPP2R5CQ13362-34EBI-1180783,EBI-1266176
    PPP2R5EQ165373EBI-1180783,EBI-968374
    RB1P064003EBI-1180783,EBI-491274
    VCPP550722EBI-1180783,EBI-355164
    XRCC1P188878EBI-1180783,EBI-947466

    Protein-protein interaction databases

    BioGridi116369. 60 interactions.
    DIPiDIP-24270N.
    IntActiO96017. 25 interactions.
    MINTiMINT-124588.

    Structurei

    Secondary structure

    1
    543
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi94 – 985
    Beta strandi100 – 1034
    Beta strandi106 – 1083
    Beta strandi110 – 1189
    Beta strandi122 – 1243
    Helixi128 – 1325
    Helixi135 – 1384
    Beta strandi144 – 1507
    Beta strandi154 – 1629
    Beta strandi168 – 1703
    Beta strandi180 – 1823
    Beta strandi187 – 1937
    Beta strandi197 – 2037
    Helixi209 – 2113
    Helixi214 – 2196
    Beta strandi220 – 2289
    Beta strandi230 – 23910
    Turni240 – 2434
    Beta strandi244 – 2518
    Helixi253 – 2564
    Helixi270 – 27910
    Beta strandi288 – 30215
    Beta strandi307 – 3093
    Helixi310 – 3134
    Helixi314 – 3163
    Helixi321 – 34020
    Helixi350 – 3523
    Beta strandi353 – 3619
    Beta strandi364 – 3663
    Helixi369 – 3713
    Helixi379 – 3857
    Helixi388 – 3903
    Helixi393 – 3986
    Turni399 – 4035
    Helixi407 – 42216
    Beta strandi429 – 4313
    Helixi436 – 4427
    Helixi449 – 4524
    Helixi457 – 46610
    Turni471 – 4733
    Helixi477 – 4815
    Helixi484 – 4863
    Helixi489 – 50214
    Turni504 – 5063

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GXCX-ray2.70A/D/G/J64-212[»]
    2CN5X-ray2.25A210-531[»]
    2CN8X-ray2.70A210-531[»]
    2W0JX-ray2.05A210-531[»]
    2W7XX-ray2.07A210-531[»]
    2WTCX-ray3.00A210-531[»]
    2WTDX-ray2.75A210-531[»]
    2WTIX-ray2.50A210-531[»]
    2WTJX-ray2.10A210-531[»]
    2XBJX-ray2.30A210-531[»]
    2XK9X-ray2.35A210-531[»]
    2XM8X-ray3.40A210-531[»]
    2XM9X-ray2.50A210-531[»]
    2YCFX-ray1.77A210-530[»]
    2YCQX-ray2.05A210-531[»]
    2YCRX-ray2.20A210-531[»]
    2YCSX-ray2.35A210-531[»]
    2YIQX-ray1.89A210-531[»]
    2YIRX-ray2.10A210-531[»]
    2YITX-ray2.20A210-531[»]
    3I6UX-ray3.00A/B84-502[»]
    3I6WX-ray3.25A/B/C/D/E/F/G/H70-512[»]
    3VA4X-ray1.54C63-73[»]
    4A9RX-ray2.85A210-531[»]
    4A9SX-ray2.66A210-531[»]
    4A9TX-ray2.70A210-531[»]
    4A9UX-ray2.48A210-531[»]
    4BDAX-ray2.60A210-531[»]
    4BDBX-ray2.50A210-531[»]
    4BDCX-ray3.00A210-531[»]
    4BDDX-ray2.67A210-531[»]
    4BDEX-ray2.55A210-531[»]
    4BDFX-ray2.70A210-531[»]
    4BDGX-ray2.84A210-531[»]
    4BDHX-ray2.70A210-531[»]
    4BDIX-ray2.32A210-531[»]
    4BDJX-ray3.01A210-531[»]
    4BDKX-ray3.30A210-531[»]
    ProteinModelPortaliO96017.
    SMRiO96017. Positions 89-509.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO96017.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini113 – 17563FHAPROSITE-ProRule annotationAdd
    BLAST
    Domaini220 – 486267Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni368 – 39427T-loop/activation segmentAdd
    BLAST

    Sequence similaritiesi

    Contains 1 FHA domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG108055.
    KOiK06641.
    OMAiKFAIGSE.
    OrthoDBiEOG7C5M7Z.
    PhylomeDBiO96017.
    TreeFamiTF101082.

    Family and domain databases

    Gene3Di2.60.200.20. 1 hit.
    InterProiIPR000253. FHA_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR008984. SMAD_FHA_domain.
    [Graphical view]
    PfamiPF00498. FHA. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00240. FHA. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49879. SSF49879. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50006. FHA_DOMAIN. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (13)i

    Sequence statusi: Complete.

    This entry describes 13 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O96017-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSRESDVEAQ QSHGSSACSQ PHGSVTQSQG SSSQSQGISS SSTSTMPNSS    50
    QSSHSSSGTL SSLETVSTQE LYSIPEDQEP EDQEPEEPTP APWARLWALQ 100
    DGFANLECVN DNYWFGRDKS CEYCFDEPLL KRTDKYRTYS KKHFRIFREV 150
    GPKNSYIAYI EDHSGNGTFV NTELVGKGKR RPLNNNSEIA LSLSRNKVFV 200
    FFDLTVDDQS VYPKALRDEY IMSKTLGSGA CGEVKLAFER KTCKKVAIKI 250
    ISKRKFAIGS AREADPALNV ETEIEILKKL NHPCIIKIKN FFDAEDYYIV 300
    LELMEGGELF DKVVGNKRLK EATCKLYFYQ MLLAVQYLHE NGIIHRDLKP 350
    ENVLLSSQEE DCLIKITDFG HSKILGETSL MRTLCGTPTY LAPEVLVSVG 400
    TAGYNRAVDC WSLGVILFIC LSGYPPFSEH RTQVSLKDQI TSGKYNFIPE 450
    VWAEVSEKAL DLVKKLLVVD PKARFTTEEA LRHPWLQDED MKRKFQDLLS 500
    EENESTALPQ VLAQPSTSRK RPREGEAEGA ETTKRPAVCA AVL 543
    Length:543
    Mass (Da):60,915
    Last modified:May 1, 1999 - v1
    Checksum:i28890ACF3C1F3408
    GO
    Isoform 2 (identifier: O96017-2) [UniParc]FASTAAdd to Basket

    Also known as: ins2

    The sequence of this isoform differs from the canonical sequence as follows:
         198-224: VFVFFDLTVDDQSVYPKALRDEYIMSK → EKILKIYSLSRFSKIRRGAVAHVFNPS
         228-234: SGACGEV → GRGWQIT
         235-543: Missing.

    Note: Lacks enzymatic activity.

    Show »
    Length:234
    Mass (Da):26,084
    Checksum:i46766F331DD13DA8
    GO
    Isoform 3 (identifier: O96017-3) [UniParc]FASTAAdd to Basket

    Also known as: del2-12

    The sequence of this isoform differs from the canonical sequence as follows:
         107-487: Missing.

    Show »
    Length:162
    Mass (Da):17,370
    Checksum:iD3BF7E0BC0DB0EC1
    GO
    Isoform 4 (identifier: O96017-4) [UniParc]FASTAAdd to Basket

    Also known as: del2-3

    The sequence of this isoform differs from the canonical sequence as follows:
         107-197: Missing.

    Note: Lacks enzymatic activity.

    Show »
    Length:452
    Mass (Da):50,203
    Checksum:i96F7C353E4F3C85B
    GO
    Isoform 5 (identifier: O96017-5) [UniParc]FASTAAdd to Basket

    Also known as: del4

    The sequence of this isoform differs from the canonical sequence as follows:
         199-203: FVFFD → VPVER
         204-543: Missing.

    Show »
    Length:203
    Mass (Da):22,594
    Checksum:i9D1ED8844633607E
    GO
    Isoform 6 (identifier: O96017-6) [UniParc]FASTAAdd to Basket

    Also known as: sub3

    The sequence of this isoform differs from the canonical sequence as follows:
         150-165: VGPKNSYIAYIEDHSG → ENLSCPYRIWFNFCLF
         166-543: Missing.

    Show »
    Length:165
    Mass (Da):18,706
    Checksum:i795CC81539178CF0
    GO
    Isoform 7 (identifier: O96017-7) [UniParc]FASTAAdd to Basket

    Also known as: del9-12

    The sequence of this isoform differs from the canonical sequence as follows:
         337-339: YLH → MKT
         340-543: Missing.

    Note: Lacks enzymatic activity.

    Show »
    Length:339
    Mass (Da):38,125
    Checksum:iCAE0E58DF0308393
    GO
    Isoform 8 (identifier: O96017-8) [UniParc]FASTAAdd to Basket

    Also known as: del7

    The sequence of this isoform differs from the canonical sequence as follows:
         283-289: PCIIKIK → DGRGRAV
         290-543: Missing.

    Show »
    Length:289
    Mass (Da):32,142
    Checksum:i630D0AF3AE5114E6
    GO
    Isoform 9 (identifier: O96017-9) [UniParc]FASTAAdd to Basket

    Also known as: insx

    The sequence of this isoform differs from the canonical sequence as follows:
         107-107: E → ETESGHVTQSDLELLLSSDPPASASQSAGIRGVRHHPRPVCSLK

    Note: Retains low level of catalytic activity.

    Show »
    Length:586
    Mass (Da):65,419
    Checksum:i55BDE42C9A0F98A7
    GO
    Isoform 10 (identifier: O96017-10) [UniParc]FASTAAdd to Basket

    Also known as: iso2

    The sequence of this isoform differs from the canonical sequence as follows:
         131-147: KRTDKYRTYSKKHFRIF → EFRSYSFYLP
         148-543: Missing.

    Note: Lacks enzymatic activity.

    Show »
    Length:140
    Mass (Da):15,420
    Checksum:i54BBB0152B5668D5
    GO
    Isoform 11 (identifier: O96017-11) [UniParc]FASTAAdd to Basket

    Also known as: iso1

    The sequence of this isoform differs from the canonical sequence as follows:
         75-392: Missing.

    Show »
    Length:225
    Mass (Da):24,396
    Checksum:i57F0155780C96BA2
    GO
    Isoform 12 (identifier: O96017-12) [UniParc]FASTAAdd to Basket

    Also known as: del9

    The sequence of this isoform differs from the canonical sequence as follows:
         337-365: Missing.

    Note: Lacks enzymatic activity.

    Show »
    Length:514
    Mass (Da):57,526
    Checksum:i8B99B81830B8092F
    GO
    Isoform 13 (identifier: O96017-13) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-221: Missing.

    Show »
    Length:322
    Mass (Da):36,157
    Checksum:iD31257F4B9652438
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti17 – 171A → S in an osteogenic sarcoma sample; somatic mutation; might influence susceptibility to breast cancer; does not cause protein abrogation in familial colorectal cancer. 1 Publication
    VAR_019101
    Natural varianti59 – 591T → K in multiple cancers. 1 Publication
    VAR_026630
    Natural varianti64 – 641E → K in prostate cancer; somatic mutation. 1 Publication
    VAR_019107
    Natural varianti85 – 851P → L in an osteogenic sarcoma sample; neutral allele among Ashkenazi Jewish women. 3 Publications
    Corresponds to variant rs17883862 [ dbSNP | Ensembl ].
    VAR_019102
    Natural varianti117 – 1171R → G.3 Publications
    Corresponds to variant rs28909982 [ dbSNP | Ensembl ].
    VAR_022461
    Natural varianti137 – 1371R → Q Might influence susceptibility to breast cancer; does not cause protein abrogation in familial colorectal cancer. 2 Publications
    VAR_022462
    Natural varianti145 – 1451R → P in prostate cancer; somatic mutation. 1 Publication
    VAR_019108
    Natural varianti145 – 1451R → W in colon cancer and LFS2; does not cause protein abrogation in familial colorectal cancer; loss of the ability to interact with and phosphorylate CDC25A and to promote CDC25A degradation in response to ionizing radiation. 5 Publications
    VAR_008554
    Natural varianti157 – 1571I → T Might influence susceptibility to different types of cancer; does not cause protein abrogation in familial colorectal cancer; loss of the ability to interact with and phosphorylate CDC25A and to promote CDC25A degradation in response to ionizing radiation. 13 Publications
    Corresponds to variant rs17879961 [ dbSNP | Ensembl ].
    VAR_008555
    Natural varianti167 – 1671G → R in prostate cancer; somatic mutation. 1 Publication
    VAR_019109
    Natural varianti180 – 1801R → C in prostate cancer; somatic mutation. 2 Publications
    Corresponds to variant rs77130927 [ dbSNP | Ensembl ].
    VAR_019103
    Natural varianti180 – 1801R → H in prostate cancer; somatic mutation. 3 Publications
    Corresponds to variant rs137853009 [ dbSNP | Ensembl ].
    VAR_019110
    Natural varianti181 – 1811R → C in prostate cancer; somatic mutation. 1 Publication
    Corresponds to variant rs137853010 [ dbSNP | Ensembl ].
    VAR_019104
    Natural varianti181 – 1811R → H in prostate cancer; somatic mutation. 1 Publication
    Corresponds to variant rs121908701 [ dbSNP | Ensembl ].
    VAR_019105
    Natural varianti239 – 2391E → K in prostate cancer; germline mutation. 1 Publication
    VAR_019106
    Natural varianti251 – 2511I → F in prostate cancer; germline mutation. 1 Publication
    VAR_019111
    Natural varianti318 – 3181R → H in prostate cancer; somatic mutation. 1 Publication
    Corresponds to variant rs143611747 [ dbSNP | Ensembl ].
    VAR_019112
    Natural varianti323 – 3231T → P in prostate cancer; somatic mutation. 1 Publication
    VAR_019113
    Natural varianti327 – 3271Y → C in prostate cancer; somatic mutation. 1 Publication
    VAR_019114
    Natural varianti347 – 3471D → N.
    Corresponds to variant rs28909980 [ dbSNP | Ensembl ].
    VAR_029154
    Natural varianti371 – 3711H → Y Confers a moderate risk of breast cancer; partially reduces kinase activity. 1 Publication
    VAR_066012
    Natural varianti406 – 4061R → H.
    Corresponds to variant rs299671 [ dbSNP | Ensembl ].
    VAR_024572
    Natural varianti428 – 4281S → F May increase breast cancer risk. 1 Publication
    Corresponds to variant rs137853011 [ dbSNP | Ensembl ].
    VAR_022463
    Natural varianti436 – 4361L → M.1 Publication
    Corresponds to variant rs17882922 [ dbSNP | Ensembl ].
    VAR_021117
    Natural varianti446 – 4461N → K.1 Publication
    Corresponds to variant rs17880867 [ dbSNP | Ensembl ].
    VAR_021118
    Natural varianti447 – 4471F → I.1 Publication
    Corresponds to variant rs17881473 [ dbSNP | Ensembl ].
    VAR_021119
    Natural varianti448 – 4481I → S.1 Publication
    Corresponds to variant rs17886163 [ dbSNP | Ensembl ].
    VAR_021120
    Natural varianti476 – 4761T → K in prostate cancer; somatic mutation. 1 Publication
    VAR_019115
    Natural varianti500 – 5001S → C.
    Corresponds to variant rs28909981 [ dbSNP | Ensembl ].
    VAR_029155
    Natural varianti501 – 5011E → K.1 Publication
    Corresponds to variant rs17883172 [ dbSNP | Ensembl ].
    VAR_021121
    Natural varianti512 – 5121L → V.1 Publication
    Corresponds to variant rs17882942 [ dbSNP | Ensembl ].
    VAR_021122

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 221221Missing in isoform 13. 1 PublicationVSP_045148Add
    BLAST
    Alternative sequencei75 – 392318Missing in isoform 11. 1 PublicationVSP_014556Add
    BLAST
    Alternative sequencei107 – 487381Missing in isoform 3. 1 PublicationVSP_014559Add
    BLAST
    Alternative sequencei107 – 19791Missing in isoform 4. 1 PublicationVSP_014558Add
    BLAST
    Alternative sequencei107 – 1071E → ETESGHVTQSDLELLLSSDP PASASQSAGIRGVRHHPRPV CSLK in isoform 9. 2 PublicationsVSP_014557
    Alternative sequencei131 – 14717KRTDK…HFRIF → EFRSYSFYLP in isoform 10. 1 PublicationVSP_014560Add
    BLAST
    Alternative sequencei148 – 543396Missing in isoform 10. 1 PublicationVSP_014561Add
    BLAST
    Alternative sequencei150 – 16516VGPKN…EDHSG → ENLSCPYRIWFNFCLF in isoform 6. 1 PublicationVSP_014562Add
    BLAST
    Alternative sequencei166 – 543378Missing in isoform 6. 1 PublicationVSP_014563Add
    BLAST
    Alternative sequencei198 – 22427VFVFF…YIMSK → EKILKIYSLSRFSKIRRGAV AHVFNPS in isoform 2. 2 PublicationsVSP_014564Add
    BLAST
    Alternative sequencei199 – 2035FVFFD → VPVER in isoform 5. 1 PublicationVSP_014565
    Alternative sequencei204 – 543340Missing in isoform 5. 1 PublicationVSP_014566Add
    BLAST
    Alternative sequencei228 – 2347SGACGEV → GRGWQIT in isoform 2. 2 PublicationsVSP_014567
    Alternative sequencei235 – 543309Missing in isoform 2. 2 PublicationsVSP_014568Add
    BLAST
    Alternative sequencei283 – 2897PCIIKIK → DGRGRAV in isoform 8. 1 PublicationVSP_014569
    Alternative sequencei290 – 543254Missing in isoform 8. 1 PublicationVSP_014570Add
    BLAST
    Alternative sequencei337 – 36529Missing in isoform 12. 2 PublicationsVSP_014571Add
    BLAST
    Alternative sequencei337 – 3393YLH → MKT in isoform 7. 1 PublicationVSP_014572
    Alternative sequencei340 – 543204Missing in isoform 7. 1 PublicationVSP_014573Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF086904 mRNA. Translation: AAC83693.1.
    AJ131197 mRNA. Translation: CAA10319.1.
    AF096279 mRNA. Translation: AAD11784.1.
    AY551295 mRNA. Translation: AAS58456.1.
    AY551296 mRNA. Translation: AAS58457.1.
    AY551297 mRNA. Translation: AAS58458.1.
    AY551298 mRNA. Translation: AAS58459.1.
    AY551299 mRNA. Translation: AAS58460.1.
    AY551300 mRNA. Translation: AAS58461.1.
    AY551301 mRNA. Translation: AAS58462.1.
    AY551302 mRNA. Translation: AAS58463.1.
    AY551303 mRNA. Translation: AAS58464.1.
    AY551304 mRNA. Translation: AAS58465.1.
    AY551305 mRNA. Translation: AAS58466.1.
    CR456418 mRNA. Translation: CAG30304.1.
    AF174135 mRNA. Translation: AAD48504.1.
    AB040105 mRNA. Translation: BAB17231.1.
    AK290754 mRNA. Translation: BAF83443.1.
    AF217975 mRNA. Translation: AAG17218.1.
    AY800241 Genomic DNA. Translation: AAV41895.1.
    AL121825, AL117330 Genomic DNA. Translation: CAH73823.1.
    AL117330, AL121825 Genomic DNA. Translation: CAH73875.1.
    AL121825, AL117330 Genomic DNA. Translation: CAX11957.1.
    AL121825, AL117330 Genomic DNA. Translation: CAX11958.1.
    AL121825, AL117330 Genomic DNA. Translation: CAX11959.1.
    AL117330, AL121825 Genomic DNA. Translation: CAX14026.1.
    AL117330, AL121825 Genomic DNA. Translation: CAX14027.1.
    AL117330, AL121825 Genomic DNA. Translation: CAX14028.1.
    CH471095 Genomic DNA. Translation: EAW59755.1.
    BC004207 mRNA. Translation: AAH04207.1.
    CCDSiCCDS13843.1. [O96017-1]
    CCDS13844.1. [O96017-12]
    CCDS33629.1. [O96017-9]
    CCDS58798.1. [O96017-13]
    RefSeqiNP_001005735.1. NM_001005735.1. [O96017-9]
    NP_001244316.1. NM_001257387.1. [O96017-13]
    NP_009125.1. NM_007194.3. [O96017-1]
    NP_665861.1. NM_145862.2. [O96017-12]
    UniGeneiHs.291363.
    Hs.505297.

    Genome annotation databases

    EnsembliENST00000328354; ENSP00000329178; ENSG00000183765. [O96017-1]
    ENST00000348295; ENSP00000329012; ENSG00000183765. [O96017-12]
    ENST00000382580; ENSP00000372023; ENSG00000183765. [O96017-9]
    ENST00000402731; ENSP00000384835; ENSG00000183765. [O96017-12]
    ENST00000403642; ENSP00000384919; ENSG00000183765. [O96017-4]
    ENST00000404276; ENSP00000385747; ENSG00000183765. [O96017-1]
    ENST00000405598; ENSP00000386087; ENSG00000183765. [O96017-1]
    ENST00000417588; ENSP00000412901; ENSG00000183765. [O96017-5]
    ENST00000433728; ENSP00000404400; ENSG00000183765. [O96017-8]
    ENST00000448511; ENSP00000404567; ENSG00000183765. [O96017-6]
    GeneIDi11200.
    KEGGihsa:11200.
    UCSCiuc003ads.1. human. [O96017-1]
    uc003adt.1. human. [O96017-9]
    uc003adv.1. human. [O96017-12]
    uc010gvh.1. human. [O96017-4]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF086904 mRNA. Translation: AAC83693.1 .
    AJ131197 mRNA. Translation: CAA10319.1 .
    AF096279 mRNA. Translation: AAD11784.1 .
    AY551295 mRNA. Translation: AAS58456.1 .
    AY551296 mRNA. Translation: AAS58457.1 .
    AY551297 mRNA. Translation: AAS58458.1 .
    AY551298 mRNA. Translation: AAS58459.1 .
    AY551299 mRNA. Translation: AAS58460.1 .
    AY551300 mRNA. Translation: AAS58461.1 .
    AY551301 mRNA. Translation: AAS58462.1 .
    AY551302 mRNA. Translation: AAS58463.1 .
    AY551303 mRNA. Translation: AAS58464.1 .
    AY551304 mRNA. Translation: AAS58465.1 .
    AY551305 mRNA. Translation: AAS58466.1 .
    CR456418 mRNA. Translation: CAG30304.1 .
    AF174135 mRNA. Translation: AAD48504.1 .
    AB040105 mRNA. Translation: BAB17231.1 .
    AK290754 mRNA. Translation: BAF83443.1 .
    AF217975 mRNA. Translation: AAG17218.1 .
    AY800241 Genomic DNA. Translation: AAV41895.1 .
    AL121825 , AL117330 Genomic DNA. Translation: CAH73823.1 .
    AL117330 , AL121825 Genomic DNA. Translation: CAH73875.1 .
    AL121825 , AL117330 Genomic DNA. Translation: CAX11957.1 .
    AL121825 , AL117330 Genomic DNA. Translation: CAX11958.1 .
    AL121825 , AL117330 Genomic DNA. Translation: CAX11959.1 .
    AL117330 , AL121825 Genomic DNA. Translation: CAX14026.1 .
    AL117330 , AL121825 Genomic DNA. Translation: CAX14027.1 .
    AL117330 , AL121825 Genomic DNA. Translation: CAX14028.1 .
    CH471095 Genomic DNA. Translation: EAW59755.1 .
    BC004207 mRNA. Translation: AAH04207.1 .
    CCDSi CCDS13843.1. [O96017-1 ]
    CCDS13844.1. [O96017-12 ]
    CCDS33629.1. [O96017-9 ]
    CCDS58798.1. [O96017-13 ]
    RefSeqi NP_001005735.1. NM_001005735.1. [O96017-9 ]
    NP_001244316.1. NM_001257387.1. [O96017-13 ]
    NP_009125.1. NM_007194.3. [O96017-1 ]
    NP_665861.1. NM_145862.2. [O96017-12 ]
    UniGenei Hs.291363.
    Hs.505297.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GXC X-ray 2.70 A/D/G/J 64-212 [» ]
    2CN5 X-ray 2.25 A 210-531 [» ]
    2CN8 X-ray 2.70 A 210-531 [» ]
    2W0J X-ray 2.05 A 210-531 [» ]
    2W7X X-ray 2.07 A 210-531 [» ]
    2WTC X-ray 3.00 A 210-531 [» ]
    2WTD X-ray 2.75 A 210-531 [» ]
    2WTI X-ray 2.50 A 210-531 [» ]
    2WTJ X-ray 2.10 A 210-531 [» ]
    2XBJ X-ray 2.30 A 210-531 [» ]
    2XK9 X-ray 2.35 A 210-531 [» ]
    2XM8 X-ray 3.40 A 210-531 [» ]
    2XM9 X-ray 2.50 A 210-531 [» ]
    2YCF X-ray 1.77 A 210-530 [» ]
    2YCQ X-ray 2.05 A 210-531 [» ]
    2YCR X-ray 2.20 A 210-531 [» ]
    2YCS X-ray 2.35 A 210-531 [» ]
    2YIQ X-ray 1.89 A 210-531 [» ]
    2YIR X-ray 2.10 A 210-531 [» ]
    2YIT X-ray 2.20 A 210-531 [» ]
    3I6U X-ray 3.00 A/B 84-502 [» ]
    3I6W X-ray 3.25 A/B/C/D/E/F/G/H 70-512 [» ]
    3VA4 X-ray 1.54 C 63-73 [» ]
    4A9R X-ray 2.85 A 210-531 [» ]
    4A9S X-ray 2.66 A 210-531 [» ]
    4A9T X-ray 2.70 A 210-531 [» ]
    4A9U X-ray 2.48 A 210-531 [» ]
    4BDA X-ray 2.60 A 210-531 [» ]
    4BDB X-ray 2.50 A 210-531 [» ]
    4BDC X-ray 3.00 A 210-531 [» ]
    4BDD X-ray 2.67 A 210-531 [» ]
    4BDE X-ray 2.55 A 210-531 [» ]
    4BDF X-ray 2.70 A 210-531 [» ]
    4BDG X-ray 2.84 A 210-531 [» ]
    4BDH X-ray 2.70 A 210-531 [» ]
    4BDI X-ray 2.32 A 210-531 [» ]
    4BDJ X-ray 3.01 A 210-531 [» ]
    4BDK X-ray 3.30 A 210-531 [» ]
    ProteinModelPortali O96017.
    SMRi O96017. Positions 89-509.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116369. 60 interactions.
    DIPi DIP-24270N.
    IntActi O96017. 25 interactions.
    MINTi MINT-124588.

    Chemistry

    BindingDBi O96017.
    ChEMBLi CHEMBL2527.
    GuidetoPHARMACOLOGYi 1988.

    PTM databases

    PhosphoSitei O96017.

    Proteomic databases

    MaxQBi O96017.
    PaxDbi O96017.
    PRIDEi O96017.

    Protocols and materials databases

    DNASUi 11200.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000328354 ; ENSP00000329178 ; ENSG00000183765 . [O96017-1 ]
    ENST00000348295 ; ENSP00000329012 ; ENSG00000183765 . [O96017-12 ]
    ENST00000382580 ; ENSP00000372023 ; ENSG00000183765 . [O96017-9 ]
    ENST00000402731 ; ENSP00000384835 ; ENSG00000183765 . [O96017-12 ]
    ENST00000403642 ; ENSP00000384919 ; ENSG00000183765 . [O96017-4 ]
    ENST00000404276 ; ENSP00000385747 ; ENSG00000183765 . [O96017-1 ]
    ENST00000405598 ; ENSP00000386087 ; ENSG00000183765 . [O96017-1 ]
    ENST00000417588 ; ENSP00000412901 ; ENSG00000183765 . [O96017-5 ]
    ENST00000433728 ; ENSP00000404400 ; ENSG00000183765 . [O96017-8 ]
    ENST00000448511 ; ENSP00000404567 ; ENSG00000183765 . [O96017-6 ]
    GeneIDi 11200.
    KEGGi hsa:11200.
    UCSCi uc003ads.1. human. [O96017-1 ]
    uc003adt.1. human. [O96017-9 ]
    uc003adv.1. human. [O96017-12 ]
    uc010gvh.1. human. [O96017-4 ]

    Organism-specific databases

    CTDi 11200.
    GeneCardsi GC22M029083.
    HGNCi HGNC:16627. CHEK2.
    HPAi CAB002030.
    HPA001878.
    MIMi 114480. phenotype.
    176807. phenotype.
    259500. phenotype.
    604373. gene+phenotype.
    609265. phenotype.
    neXtProti NX_O96017.
    Orphaneti 1331. Familial prostate cancer.
    145. Hereditary breast and ovarian cancer syndrome.
    524. Li-Fraumeni syndrome.
    668. Osteosarcoma.
    PharmGKBi PA404.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG108055.
    KOi K06641.
    OMAi KFAIGSE.
    OrthoDBi EOG7C5M7Z.
    PhylomeDBi O96017.
    TreeFami TF101082.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    Reactomei REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_897. G2/M DNA damage checkpoint.
    SignaLinki O96017.

    Miscellaneous databases

    EvolutionaryTracei O96017.
    GeneWikii CHEK2.
    GenomeRNAii 11200.
    NextBioi 42629.
    PROi O96017.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O96017.
    Bgeei O96017.
    Genevestigatori O96017.

    Family and domain databases

    Gene3Di 2.60.200.20. 1 hit.
    InterProi IPR000253. FHA_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR008984. SMAD_FHA_domain.
    [Graphical view ]
    Pfami PF00498. FHA. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00240. FHA. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49879. SSF49879. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50006. FHA_DOMAIN. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Linkage of ATM to cell cycle regulation by the Chk2 protein kinase."
      Matsuoka S., Huang M., Elledge S.J.
      Science 282:1893-1897(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN PHOSPHORYLATION OF CDC25C, MUTAGENESIS OF ASP-347.
    2. "A human homologue of the checkpoint kinase Cds1 directly inhibits Cdc25 phosphatase."
      Blasina A., van de Weyer I., Laus M.C., Luyten W.H.M.L., Parker A.E., McGowan C.H.
      Curr. Biol. 9:1-10(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN MITOSIS.
    3. "A human Cds1-related kinase that functions downstream of ATM protein in the cellular response to DNA damage."
      Brown A.L., Lee C.-H., Schwarz J.K., Mitiku N., Piwnica-Worms H., Chung J.H.
      Proc. Natl. Acad. Sci. U.S.A. 96:3745-3750(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN PHOSPHORYLATION OF CDC25C.
    4. "Alternative splicing and mutation status of CHEK2 in stage III breast cancer."
      Staalesen V., Falck J., Geisler S., Bartkova J., Boerresen-Dale A.-L., Lukas J., Lillehaug J.R., Bartek J., Lonning P.E.
      Oncogene 23:8535-8544(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6; 7; 8; 9; 10; 11 AND 12), SUBCELLULAR LOCATION.
      Tissue: Mammary gland.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
    6. "Chk2/HuCds1 cell cycle checkpoint protein kinase from human colon carcinoma HT29 cells: regulation by autophosphorylation and DNA-dependent protein kinase and inhibition by cell cycle regulatory drugs."
      Shao R.-G., Zhang H., Yu Q., Pommier Y.
      Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Colon carcinoma.
    7. "An alternative spliced Chk2."
      Ogawa A., Okabe-Nakamura A.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12).
      Tissue: T-cell.
    8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    9. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 13).
    10. NIEHS SNPs program
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-85; THR-157; MET-436; LYS-446; ILE-447; SER-448; LYS-501 AND VAL-512.
    11. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    13. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Muscle.
    14. "hCds1-mediated phosphorylation of BRCA1 regulates the DNA damage response."
      Lee J.S., Collins K.M., Brown A.L., Lee C.H., Chung J.H.
      Nature 404:201-204(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF BRCA1, INTERACTION WITH BRCA1.
    15. "Ataxia telangiectasia-mutated phosphorylates Chk2 in vivo and in vitro."
      Matsuoka S., Rotman G., Ogawa A., Shiloh Y., Tamai K., Elledge S.J.
      Proc. Natl. Acad. Sci. U.S.A. 97:10389-10394(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-68 BY ATM.
    16. "The hCds1 (Chk2)-FHA domain is essential for a chain of phosphorylation events on hCds1 that is induced by ionizing radiation."
      Lee C.H., Chung J.H.
      J. Biol. Chem. 276:30537-30541(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-383 AND THR-387, MUTAGENESIS OF THR-383 AND THR-387.
    17. "The ATM-Chk2-Cdc25A checkpoint pathway guards against radioresistant DNA synthesis."
      Falck J., Mailand N., Syljuaasen R.G., Bartek J., Lukas J.
      Nature 410:842-847(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN INTRA S-PHASE CHECKPOINT, FUNCTION IN PHOSPHORYLATION OF CDC25A, INTERACTION WITH CDC25A, MUTAGENESIS OF ASP-347, CHARACTERIZATION OF VARIANT COLON CANCER TRP-145, CHARACTERIZATION OF VARIANT THR-157.
    18. Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO BC.
    19. "Phosphorylation of threonine 68 promotes oligomerization and autophosphorylation of the Chk2 protein kinase via the forkhead-associated domain."
      Ahn J.Y., Li X., Davis H.L., Canman C.E.
      J. Biol. Chem. 277:19389-19395(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMODIMERIZATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF THR-68.
    20. "PML-dependent apoptosis after DNA damage is regulated by the checkpoint kinase hCds1/Chk2."
      Yang S., Kuo C., Bisi J.E., Kim M.K.
      Nat. Cell Biol. 4:865-870(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN APOPTOSIS, FUNCTION IN PHOSPHORYLATION OF PML, SUBCELLULAR LOCATION.
    21. "53BP1, a mediator of the DNA damage checkpoint."
      Wang B., Matsuoka S., Carpenter P.B., Elledge S.J.
      Science 298:1435-1438(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TP53BP1.
    22. "The promyelocytic leukemia protein protects p53 from Mdm2-mediated inhibition and degradation."
      Louria-Hayon I., Grossman T., Sionov R.V., Alsheich O., Pandolfi P.P., Haupt Y.
      J. Biol. Chem. 278:33134-33141(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PML AND TP53, SUBCELLULAR LOCATION.
    23. "Chk2 activates E2F-1 in response to DNA damage."
      Stevens C., Smith L., La Thangue N.B.
      Nat. Cell Biol. 5:401-409(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSCRIPTION REGULATION, FUNCTION IN APOPTOSIS, FUNCTION IN PHOSPHORYLATION OF E2F1.
    24. "MDC1 is coupled to activated CHK2 in mammalian DNA damage response pathways."
      Lou Z., Minter-Dykhouse K., Wu X., Chen J.
      Nature 421:957-961(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA DAMAGE RESPONSE, INTERACTION WITH MDC1.
    25. Cited for: REVIEW ON PHOSPHORYLATION OF TP53 AND OTHER SUBSTRATES.
    26. "The stress kinase MRK contributes to regulation of DNA damage checkpoints through a p38gamma-independent pathway."
      Tosti E., Waldbaum L., Warshaw G., Gross E.A., Ruggieri R.
      J. Biol. Chem. 279:47652-47660(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, PHOSPHORYLATION AT THR-68 BY MLTK, MUTAGENESIS OF THR-68 AND ASP-368.
    27. "ATM and Chk2-dependent phosphorylation of MDMX contribute to p53 activation after DNA damage."
      Chen L., Gilkes D.M., Pan Y., Lane W.S., Chen J.
      EMBO J. 24:3411-3422(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TP53 ACTIVATION, FUNCTION IN PHOSPHORYLATION OF MDM4.
    28. "Regulation of the antioncogenic Chk2 kinase by the oncogenic Wip1 phosphatase."
      Fujimoto H., Onishi N., Kato N., Takekawa M., Xu X.Z., Kosugi A., Kondo T., Imamura M., Oishi I., Yoda A., Minami Y.
      Cell Death Differ. 13:1170-1180(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-68, DEPHOSPHORYLATION AT THR-68 BY PPM1D.
    29. "Priming phosphorylation of Chk2 by polo-like kinase 3 (Plk3) mediates its full activation by ATM and a downstream checkpoint in response to DNA damage."
      Bahassi el M., Myer D.L., McKenney R.J., Hennigan R.F., Stambrook P.J.
      Mutat. Res. 596:166-176(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-62; THR-68 AND SER-73, MUTAGENESIS OF SER-73.
    30. "Phosphorylation of pRB at Ser612 by Chk1/2 leads to a complex between pRB and E2F-1 after DNA damage."
      Inoue Y., Kitagawa M., Taya Y.
      EMBO J. 26:2083-2093(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF RB1.
    31. "Stability of checkpoint kinase 2 is regulated via phosphorylation at serine 456."
      Kass E.M., Ahn J., Tanaka T., Freed-Pastor W.A., Keezer S., Prives C.
      J. Biol. Chem. 282:30311-30321(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN APOPTOSIS, PHOSPHORYLATION AT SER-456, UBIQUITINATION, MUTAGENESIS OF SER-456.
    32. "Chk2 mediates stabilization of the FoxM1 transcription factor to stimulate expression of DNA repair genes."
      Tan Y., Raychaudhuri P., Costa R.H.
      Mol. Cell. Biol. 27:1007-1016(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA REPAIR, FUNCTION IN PHOSPHORYLATION OF FOXM1.
    33. "Nek6 is involved in G2/M phase cell cycle arrest through DNA damage-induced phosphorylation."
      Lee M.Y., Kim H.J., Kim M.A., Jee H.J., Kim A.J., Bae Y.S., Park J.I., Chung J.H., Yun J.
      Cell Cycle 7:2705-2709(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF NEK6.
    34. "Regulation of Chk2 ubiquitination and signaling through autophosphorylation of serine 379."
      Lovly C.M., Yan L., Ryan C.E., Takada S., Piwnica-Worms H.
      Mol. Cell. Biol. 28:5874-5885(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN APOPTOSIS, PHOSPHORYLATION AT SER-379, MUTAGENESIS OF SER-379, UBIQUITINATION, INTERACTION WITH CUL1.
    35. "The checkpoint kinases Chk1 and Chk2 regulate the functional associations between hBRCA2 and Rad51 in response to DNA damage."
      Bahassi E.M., Ovesen J.L., Riesenberg A.L., Bernstein W.Z., Hasty P.E., Stambrook P.J.
      Oncogene 27:3977-3985(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RAD51-MEDIATED DNA REPAIR, FUNCTION IN PHOSPHORYLATION OF BRCA2.
    36. "Polo-like kinase 4 phosphorylates Chk2."
      Petrinac S., Ganuelas M.L., Bonni S., Nantais J., Hudson J.W.
      Cell Cycle 8:327-329(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY PLK4.
    37. "The CHK2-BRCA1 tumour suppressor pathway ensures chromosomal stability in human somatic cells."
      Stolz A., Ertych N., Kienitz A., Vogel C., Schneider V., Fritz B., Jacob R., Dittmar G., Weichert W., Petersen I., Bastians H.
      Nat. Cell Biol. 12:492-499(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF BRCA1, FUNCTION IN CHROMOSOMAL STABILITY.
    38. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    39. "A recurrent CHEK2 p.H371Y mutation is associated with breast cancer risk in Chinese women."
      Liu Y., Liao J., Xu Y., Chen W., Liu D., Ouyang T., Li J., Wang T., Fan Z., Fan T., Lin B., Xu X., Xie Y.
      Hum. Mutat. 32:1000-1003(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO BC, VARIANTS CYS-180 AND TYR-371, CHARACTERIZATION OF VARIANT TYR-371.
    40. "The E3 ligase RNF8 regulates KU80 removal and NHEJ repair."
      Feng L., Chen J.
      Nat. Struct. Mol. Biol. 19:201-206(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY RNF8.
    41. "Structural and functional versatility of the FHA domain in DNA-damage signaling by the tumor suppressor kinase Chk2."
      Li J., Williams B.L., Haire L.F., Goldberg M., Wilker E., Durocher D., Yaffe M.B., Jackson S.P., Smerdon S.J.
      Mol. Cell 9:1045-1054(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 64-212.
    42. "Trans-activation of the DNA-damage signalling protein kinase Chk2 by T-loop exchange."
      Oliver A.W., Paul A., Boxall K.J., Barrie S.E., Aherne G.W., Garrett M.D., Mittnacht S., Pearl L.H.
      EMBO J. 25:3179-3190(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 210-531 IN COMPLEX WITH ADP AND INHIBITOR, HOMODIMERIZATION, AUTOPHOSPHORYLATION.
    43. "Structure and activation mechanism of the CHK2 DNA damage checkpoint kinase."
      Cai Z., Chehab N.H., Pavletich N.P.
      Mol. Cell 35:818-829(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 84-502 OF HOMODIMER.
    44. Cited for: VARIANT THR-157, VARIANT COLON CANCER TRP-145.
    45. "Mutation analysis of the CHK2 gene in families with hereditary breast cancer."
      Allinen M., Huusko P., Maentyniemi S., Launonen V., Winqvist R.
      Br. J. Cancer 85:209-212(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT THR-157.
    46. "Destabilization of CHK2 by a missense mutation associated with Li-Fraumeni Syndrome."
      Lee S.B., Kim S.H., Bell D.W., Wahrer D.C.R., Schiripo T.A., Jorczak M.M., Sgroi D.C., Garber J.E., Li F.P., Nichols K.E., Varley J.M., Godwin A.K., Shannon K.M., Harlow E., Haber D.A.
      Cancer Res. 61:8062-8067(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LFS2 TRP-145.
    47. Cited for: VARIANT MULTIPLE CANCERS LYS-59.
    48. "CHEK2 variants in susceptibility to breast cancer and evidence of retention of the wild type allele in tumours."
      Sodha N., Bullock S., Taylor R., Mitchell G., Guertl-Lackner B., Williams R.D., Bevan S., Bishop K., McGuire S., Houlston R.S., Eeles R.A.
      Br. J. Cancer 87:1445-1448(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GLY-117; GLN-137 AND HIS-180.
    49. "Mutations of the CHK2 gene are found in some osteosarcomas, but are rare in breast, lung, and ovarian tumors."
      Miller C.W., Ikezoe T., Krug U., Hofmann W.K., Tavor S., Vegesna V., Tsukasaki K., Takeuchi S., Koeffler H.P.
      Genes Chromosomes Cancer 33:17-21(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS OSTEOSARCOMA SER-17 AND LEU-85.
    50. Cited for: VARIANTS PROSTATE CANCER LYS-64; PRO-145; ARG-167; CYS-180; HIS-180; CYS-181; HIS-181; LYS-239; PHE-251; HIS-318; PRO-323; CYS-327 AND LYS-476, VARIANT THR-157.
    51. Cited for: VARIANTS GLY-117; TRP-145 AND THR-157.
    52. Cited for: VARIANT THR-157.
    53. Cited for: VARIANT THR-157.
    54. "Frequency of CHEK2 mutations in a population based, case-control study of breast cancer in young women."
      Friedrichsen D.M., Malone K.E., Doody D.R., Daling J.R., Ostrander E.A.
      Breast Cancer Res. 6:R629-R635(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TRP-145 AND THR-157.
    55. Cited for: VARIANT THR-157.
    56. Cited for: VARIANT THR-157.
    57. Cited for: VARIANT THR-157.
    58. "Functional and genomic approaches reveal an ancient CHEK2 allele associated with breast cancer in the Ashkenazi Jewish population."
      Shaag A., Walsh T., Renbaum P., Kirchhoff T., Nafa K., Shiovitz S., Mandell J.B., Welcsh P., Lee M.K., Ellis N., Offit K., Levy-Lahad E., King M.-C.
      Hum. Mol. Genet. 14:555-563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LEU-85 AND PHE-428.
    59. Cited for: VARIANT THR-157.
    60. "Homozygosity for a CHEK2*1100delC mutation identified in familial colorectal cancer does not lead to a severe clinical phenotype."
      van Puijenbroek M., van Asperen C.J., van Mil A., Devilee P., van Wezel T., Morreau H.
      J. Pathol. 206:198-204(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GLY-117; GLN-137; TRP-145; THR-157 AND HIS-180.

    Entry informationi

    Entry nameiCHK2_HUMAN
    AccessioniPrimary (citable) accession number: O96017
    Secondary accession number(s): A8K3Y9
    , B7ZBF3, B7ZBF4, B7ZBF5, Q6QA03, Q6QA04, Q6QA05, Q6QA06, Q6QA07, Q6QA08, Q6QA10, Q6QA11, Q6QA12, Q6QA13, Q9HBS5, Q9HCQ8, Q9UGF0, Q9UGF1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 175 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3