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O96017

- CHK2_HUMAN

UniProt

O96017 - CHK2_HUMAN

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Protein

Serine/threonine-protein kinase Chk2

Gene
CHEK2, CDS1, CHK2, RAD53
Organism
Homo sapiens (Human)
Status
Reviewed - 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.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
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.
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.3 Publications
Isoform 4 : Nucleus 3 Publications
Isoform 7 : Nucleus 3 Publications
Isoform 9 : Nucleus 3 Publications
Isoform 12 : Nucleus 3 Publications
NucleusPML body. Nucleusnucleoplasm
Note: Recruited into PML bodies together with TP53.3 Publications

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. PML body Source: UniProtKB
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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
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.
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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry (1 Publication).2 Publications

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 PLK31 Publication
Modified residuei68 – 681Phosphothreonine; by ATM and MLTK3 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 PLK4.10 Publications
Ubiquitinated. CUL1-mediated ubiquitination regulates the pro-apoptotic function. Ubiquitination may also regulate protein stability. Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination.3 Publications

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.8 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. 24 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.

Miscellaneous databases

EvolutionaryTraceiO96017.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini113 – 17563FHAAdd
BLAST
Domaini220 – 486267Protein kinaseAdd
BLAST

Region

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

Sequence similaritiesi

Contains 1 FHA domain.

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. 6 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. 14 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. VSP_045148Add
BLAST
Alternative sequencei75 – 392318Missing in isoform 11. VSP_014556Add
BLAST
Alternative sequencei107 – 487381Missing in isoform 3. VSP_014559Add
BLAST
Alternative sequencei107 – 19791Missing in isoform 4. VSP_014558Add
BLAST
Alternative sequencei107 – 1071E → ETESGHVTQSDLELLLSSDP PASASQSAGIRGVRHHPRPV CSLK in isoform 9. VSP_014557
Alternative sequencei131 – 14717KRTDK…HFRIF → EFRSYSFYLP in isoform 10. VSP_014560Add
BLAST
Alternative sequencei148 – 543396Missing in isoform 10. VSP_014561Add
BLAST
Alternative sequencei150 – 16516VGPKN…EDHSG → ENLSCPYRIWFNFCLF in isoform 6. VSP_014562Add
BLAST
Alternative sequencei166 – 543378Missing in isoform 6. VSP_014563Add
BLAST
Alternative sequencei198 – 22427VFVFF…YIMSK → EKILKIYSLSRFSKIRRGAV AHVFNPS in isoform 2. VSP_014564Add
BLAST
Alternative sequencei199 – 2035FVFFD → VPVER in isoform 5. VSP_014565
Alternative sequencei204 – 543340Missing in isoform 5. VSP_014566Add
BLAST
Alternative sequencei228 – 2347SGACGEV → GRGWQIT in isoform 2. VSP_014567
Alternative sequencei235 – 543309Missing in isoform 2. VSP_014568Add
BLAST
Alternative sequencei283 – 2897PCIIKIK → DGRGRAV in isoform 8. VSP_014569
Alternative sequencei290 – 543254Missing in isoform 8. VSP_014570Add
BLAST
Alternative sequencei337 – 36529Missing in isoform 12. VSP_014571Add
BLAST
Alternative sequencei337 – 3393YLH → MKT in isoform 7. VSP_014572
Alternative sequencei340 – 543204Missing in isoform 7. VSP_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]
ENST00000382566; ENSP00000372007; ENSG00000183765. [O96017-8]
ENST00000382578; ENSP00000372021; ENSG00000183765. [O96017-4]
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]
ENST00000544772; ENSP00000442458; ENSG00000183765. [O96017-13]
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. 24 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 ]
ENST00000382566 ; ENSP00000372007 ; ENSG00000183765 . [O96017-8 ]
ENST00000382578 ; ENSP00000372021 ; ENSG00000183765 . [O96017-4 ]
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 ]
ENST00000544772 ; ENSP00000442458 ; ENSG00000183765 . [O96017-13 ]
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

« Hide 'large scale' publications
  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 BY ATM AT THR-68.
  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: September 3, 2014
This is version 174 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

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