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Protein

Serine/threonine-protein kinase Chk2

Gene

CHEK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Promotes the CCAR2-SIRT1 association and is required for CCAR2-mediated SIRT1 inhibition (PubMed:25361978).By similarity19 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

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

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • cellular protein catabolic process Source: UniProtKB
  • cellular response to bisphenol A Source: Ensembl
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to drug Source: Ensembl
  • DNA damage checkpoint Source: UniProtKB
  • DNA damage induced protein phosphorylation Source: UniProtKB
  • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  • double-strand break repair Source: UniProtKB
  • G2/M transition of mitotic cell cycle Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
  • mitotic spindle assembly Source: UniProtKB
  • negative regulation of cell cycle arrest Source: Ensembl
  • negative regulation of DNA damage checkpoint Source: Ensembl
  • peptidyl-serine phosphorylation Source: Ensembl
  • positive regulation of anoikis Source: Ensembl
  • positive regulation of protein phosphorylation Source: Ensembl
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • protein stabilization Source: UniProtKB
  • regulation of protein catabolic process Source: UniProtKB
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • regulation of transcription, DNA-templated Source: UniProtKB
  • replicative cell aging Source: CACAO
  • replicative senescence Source: BHF-UCL
  • response to doxorubicin Source: Ensembl
  • response to gamma radiation Source: Ensembl
  • signal transduction in response to DNA damage Source: MGI
  • signal transduction involved in intra-S DNA damage checkpoint Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

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.
ReactomeiR-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-6804757. Regulation of TP53 Degradation.
R-HSA-6804760. Regulation of TP53 Activity through Methylation.
R-HSA-69473. G2/M DNA damage checkpoint.
R-HSA-69541. Stabilization of p53.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
SignaLinkiO96017.
SIGNORiO96017.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:16627. CHEK2.

Subcellular locationi

Isoform 2 :
  • Nucleus

  • Note: Isoform 10 is present throughout the cell.

GO - Cellular componenti

  • Golgi apparatus Source: HPA
  • nucleoplasm Source: HPA
  • PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Li-Fraumeni syndrome 2 (LFS2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:609265
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. 6 Publications
Corresponds to variant rs137853007 [ dbSNP | Ensembl ].
VAR_008554
Prostate cancer (PC)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:176807
Osteogenic sarcoma (OSRC)
The gene represented in this entry may be involved in disease pathogenesis.
Disease descriptionA sarcoma originating in bone-forming cells, affecting the ends of long bones.
See also OMIM:259500
Breast cancer (BC)3 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.1 Publication
Disease descriptionA 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.
See also OMIM:114480
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti390 – 3901Y → C in BC; does not phosphorylate p53/TP53. 1 Publication
Corresponds to variant rs200928781 [ dbSNP | Ensembl ].
VAR_073020

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

MalaCardsiCHEK2.
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.

Chemistry

ChEMBLiCHEMBL2527.
GuidetoPHARMACOLOGYi1988.

Polymorphism and mutation databases

BioMutaiCHEK2.

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 PLK31 Publication
Modified residuei68 – 681Phosphothreonine; by ATM and MLTK4 Publications
Modified residuei73 – 731Phosphoserine; by PLK31 Publication
Modified residuei379 – 3791Phosphoserine; by autocatalysis1 Publication
Modified residuei383 – 3831Phosphothreonine; by autocatalysis1 Publication
Modified residuei387 – 3871Phosphothreonine; by autocatalysis1 Publication
Modified residuei456 – 4561Phosphoserine1 Publication

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

EPDiO96017.
MaxQBiO96017.
PeptideAtlasiO96017.
PRIDEiO96017.

PTM databases

iPTMnetiO96017.
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

BgeeiENSG00000183765.
ExpressionAtlasiO96017. baseline and differential.
GenevisibleiO96017. HS.

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. Interacts with CDKN2AIP. Interacts (via protein kinase domain) with CCAR2 (via N-terminus). Interacts with SIRT1.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself6EBI-1180783,EBI-1180783
P279583EBI-1180783,EBI-6904388From a different organism.
AATFQ9NY614EBI-1180783,EBI-372428
CDK11AQ9UQ88-12EBI-1180783,EBI-11579223
FAM84BQ96KN13EBI-1180783,EBI-9057780
GINS2Q9Y2482EBI-1180783,EBI-747491
IL24Q130073EBI-1180783,EBI-3915542
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
RNF20Q5VTR23EBI-1180783,EBI-2372238
VCPP550722EBI-1180783,EBI-355164
XRCC1P188878EBI-1180783,EBI-947466

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116369. 95 interactions.
DIPiDIP-24270N.
IntActiO96017. 106 interactions.
MINTiMINT-124588.

Chemistry

BindingDBiO96017.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

GeneTreeiENSGT00800000124190.
HOGENOMiHOG000233016.
HOVERGENiHBG108055.
InParanoidiO96017.
KOiK06641.
OMAiSRAVDCW.
OrthoDBiEOG091G0DVW.
PhylomeDBiO96017.
TreeFamiTF101082.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR000253. FHA_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 2 hits.
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. AlignAdd to basket

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

        10         20         30         40         50
MSRESDVEAQ QSHGSSACSQ PHGSVTQSQG SSSQSQGISS SSTSTMPNSS
60 70 80 90 100
QSSHSSSGTL SSLETVSTQE LYSIPEDQEP EDQEPEEPTP APWARLWALQ
110 120 130 140 150
DGFANLECVN DNYWFGRDKS CEYCFDEPLL KRTDKYRTYS KKHFRIFREV
160 170 180 190 200
GPKNSYIAYI EDHSGNGTFV NTELVGKGKR RPLNNNSEIA LSLSRNKVFV
210 220 230 240 250
FFDLTVDDQS VYPKALRDEY IMSKTLGSGA CGEVKLAFER KTCKKVAIKI
260 270 280 290 300
ISKRKFAIGS AREADPALNV ETEIEILKKL NHPCIIKIKN FFDAEDYYIV
310 320 330 340 350
LELMEGGELF DKVVGNKRLK EATCKLYFYQ MLLAVQYLHE NGIIHRDLKP
360 370 380 390 400
ENVLLSSQEE DCLIKITDFG HSKILGETSL MRTLCGTPTY LAPEVLVSVG
410 420 430 440 450
TAGYNRAVDC WSLGVILFIC LSGYPPFSEH RTQVSLKDQI TSGKYNFIPE
460 470 480 490 500
VWAEVSEKAL DLVKKLLVVD PKARFTTEEA LRHPWLQDED MKRKFQDLLS
510 520 530 540
EENESTALPQ VLAQPSTSRK RPREGEAEGA ETTKRPAVCA AVL
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
Corresponds to variant rs137853008 [ dbSNP | Ensembl ].
VAR_019101
Natural varianti59 – 591T → K in multiple cancers. 1 Publication
Corresponds to variant rs149991239 [ dbSNP | Ensembl ].
VAR_026630
Natural varianti64 – 641E → K in prostate cancer; somatic mutation. 1 Publication
Corresponds to variant rs141568342 [ dbSNP | Ensembl ].
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
Corresponds to variant rs368570187 [ dbSNP | Ensembl ].
VAR_022462
Natural varianti145 – 1451R → P in prostate cancer; somatic mutation. 1 Publication
Corresponds to variant rs587781667 [ dbSNP | Ensembl ].
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. 6 Publications
Corresponds to variant rs137853007 [ dbSNP | Ensembl ].
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. 14 Publications
Corresponds to variant rs17879961 [ dbSNP | Ensembl ].
VAR_008555
Natural varianti167 – 1671G → R in prostate cancer; somatic mutation. 1 Publication
Corresponds to variant rs72552322 [ dbSNP | Ensembl ].
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
Corresponds to variant rs121908702 [ dbSNP | Ensembl ].
VAR_019106
Natural varianti251 – 2511I → F in prostate cancer; germline mutation. 1 Publication
Corresponds to variant rs587780189 [ dbSNP | Ensembl ].
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
Corresponds to variant rs587780194 [ dbSNP | Ensembl ].
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
Corresponds to variant rs531398630 [ dbSNP | Ensembl ].
VAR_066012
Natural varianti390 – 3901Y → C in BC; does not phosphorylate p53/TP53. 1 Publication
Corresponds to variant rs200928781 [ dbSNP | Ensembl ].
VAR_073020
Natural varianti406 – 4061R → H.
Corresponds to variant rs200649225 [ 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:
EMBLi
GenBanki
DDBJi
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]
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]
XP_011528147.1. XM_011529845.2. [O96017-13]
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.
UCSCiuc003adt.2. human. [O96017-1]

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:
EMBLi
GenBanki
DDBJi
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]
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]
XP_011528147.1. XM_011529845.2. [O96017-13]
UniGeneiHs.291363.
Hs.505297.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi116369. 95 interactions.
DIPiDIP-24270N.
IntActiO96017. 106 interactions.
MINTiMINT-124588.

Chemistry

BindingDBiO96017.
ChEMBLiCHEMBL2527.
GuidetoPHARMACOLOGYi1988.

PTM databases

iPTMnetiO96017.
PhosphoSiteiO96017.

Polymorphism and mutation databases

BioMutaiCHEK2.

Proteomic databases

EPDiO96017.
MaxQBiO96017.
PeptideAtlasiO96017.
PRIDEiO96017.

Protocols and materials databases

DNASUi11200.
Structural Biology KnowledgebaseSearch...

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.
UCSCiuc003adt.2. human. [O96017-1]

Organism-specific databases

CTDi11200.
GeneCardsiCHEK2.
HGNCiHGNC:16627. CHEK2.
HPAiCAB002030.
HPA001878.
MalaCardsiCHEK2.
MIMi114480. phenotype.
176807. phenotype.
259500. phenotype.
604373. gene+phenotype.
609265. phenotype.
neXtProtiNX_O96017.
Orphaneti1331. Familial prostate cancer.
145. Hereditary breast and ovarian cancer syndrome.
524. Li-Fraumeni syndrome.
668. Osteosarcoma.
PharmGKBiPA404.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00800000124190.
HOGENOMiHOG000233016.
HOVERGENiHBG108055.
InParanoidiO96017.
KOiK06641.
OMAiSRAVDCW.
OrthoDBiEOG091G0DVW.
PhylomeDBiO96017.
TreeFamiTF101082.

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-6804757. Regulation of TP53 Degradation.
R-HSA-6804760. Regulation of TP53 Activity through Methylation.
R-HSA-69473. G2/M DNA damage checkpoint.
R-HSA-69541. Stabilization of p53.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
SignaLinkiO96017.
SIGNORiO96017.

Miscellaneous databases

EvolutionaryTraceiO96017.
GeneWikiiCHEK2.
GenomeRNAii11200.
PROiO96017.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000183765.
ExpressionAtlasiO96017. baseline and differential.
GenevisibleiO96017. HS.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR000253. FHA_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 2 hits.
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]
ProtoNetiSearch...

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: September 7, 2016
This is version 196 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.