O14757 (CHK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase Chk1
EC=2.7.11.1

Alternative name(s):
CHK1 checkpoint homolog
Cell cycle checkpoint kinase
Checkpoint kinase-1

Gene names

Name:	CHEK1
Synonyms:	CHK1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	476 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome. Recognizes the substrate consensus sequence [R-X-X-S/T]. Binds to and phosphorylates CDC25A, CDC25B and CDC25C. Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C. Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis of CDC25A. Phosphorylation of CDC25A at 'Ser-76' primes the protein for subsequent phosphorylation at 'Ser-79', 'Ser-82' and 'Ser-88' by NEK11, which is required for polyubiquitination and degradation of CDCD25A. Inhibition of CDC25 leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression. Also phosphorylates NEK6. Binds to and phosphorylates RAD51 at 'Thr-309', which promotes the release of RAD51 from BRCA2 and enhances the association of RAD51 with chromatin, thereby promoting DNA repair by homologous recombination. Phosphorylates multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and promotes cell cycle arrest and suppression of cellular proliferation. Also promotes repair of DNA cross-links through phosphorylation of FANCE. Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A. This may enhance chromatin assembly both in the presence or absence of DNA damage. May also play a role in replication fork maintenance through regulation of PCNA. May regulate the transcription of genes that regulate cell-cycle progression through the phosphorylation of histones. Phosphorylates histone H3.1 (to form H3T11ph), which leads to epigenetic inhibition of a subset of genes. May also phosphorylate RB1 to promote its interaction with the E2F family of transcription factors and subsequent cell cycle arrest. Ref.1 Ref.9 Ref.12 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.25 Ref.27 Ref.30 Ref.32 Ref.36 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.46 Ref.47 Ref.48 Ref.50 Ref.55 Ref.58
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated through phosphorylation by ATR or ATM in response to DNA damage or inhibition of DNA replication. Activation is modulated by several mediators including CLSPN, BRCA1 and FEM1B.
Subunit structure	Interacts (phosphorylated by ATR) with RAD51. Interacts with and phosphorylates CLSPN, an adapter protein that regulates the ATR-dependent phosphorylation of CHEK1. Interacts with BRCA1. Interacts with and phosphorylates CDC25A, CDC25B and CDC25C. Interacts with FBXO6, which regulates CHEK1. Interacts with PPM1D, which regulates CHEK1 through dephosphorylation. Interacts with TIMELESS; DNA damage-dependent. Interacts with FEM1B; activates CHEK1 in response to stress. Interacts with TLK1. Interacts with XPO1 and YWHAZ. Ref.1 Ref.17 Ref.24 Ref.26 Ref.33 Ref.35 Ref.37 Ref.38 Ref.41 Ref.53 Ref.56
Subcellular location	Nucleus. Cytoplasm. Cytoplasm › cytoskeleton › centrosome. Note: Nuclear export is mediated at least in part by XPO1/CRM1. Also localizes to the centrosome specifically during interphase, where it may protect centrosomal CDC2 kinase from inappropriate activation by cytoplasmic CDC25B. Ref.1 Ref.2 Ref.17 Ref.24 Ref.32 Ref.34
Tissue specificity	Expressed ubiquitously with the most abundant expression in thymus, testis, small intestine and colon. Ref.1 Ref.2
Domain	The autoinhibitory region (AIR) inhibits the activity of the kinase domain. Ref.31
Post-translational modification	Phosphorylated by ATR in a RAD17-dependent manner in response to ultraviolet irradiation and inhibition of DNA replication. Phosphorylated by ATM in response to ionizing irradiation. ATM and ATR can both phosphorylate Ser-317 and Ser-345 and this results in enhanced kinase activity. Phosphorylation at Ser-345 induces a change in the conformation of the protein, activates the kinase activity and is a prerequisite for interaction with FBXO6 and subsequent ubiquitination at Lys-436. Phosphorylation at Ser-345 also increases binding to 14-3-3 proteins and promotes nuclear retention. Conversely, dephosphorylation at Ser-345 by PPM1D may contribute to exit from checkpoint mediated cell cycle arrest. Phosphorylation at Ser-280 by AKT1/PKB, may promote mono and/or diubiquitination. Also phosphorylated at undefined residues during mitotic arrest, resulting in decreased activity. Ref.1 Ref.9 Ref.11 Ref.12 Ref.13 Ref.16 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24 Ref.27 Ref.29 Ref.30 Ref.31 Ref.33 Ref.35 Ref.36 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.45 Ref.47 Ref.49 Ref.50 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.57 Ubiquitinated. Mono or diubiquitination promotes nuclear exclusion By similarity. The activated form (phosphorylated on Ser-345) is polyubiquitinated at Lys-436 by some SCF-type E3 ubiquitin ligase complex containing FBXO6 promoting its degradation. Ubiquitination and degradation are required to terminate the checkpoint and ensure that activated CHEK1 does not accumulate as cells progress through S phase, when replication forks encounter transient impediments during normal DNA replication. Ref.1 Ref.9 Ref.11 Ref.12 Ref.13 Ref.16 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24 Ref.27 Ref.29 Ref.30 Ref.31 Ref.33 Ref.35 Ref.36 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.45 Ref.47 Ref.49 Ref.50 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.57
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. NIM1 subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle DNA damage DNA repair
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA damage induced protein phosphorylation Inferred from direct assay Ref.41. Source: UniProtKB DNA repair Inferred from mutant phenotype Ref.53. Source: UniProtKB DNA replication Traceable author statement. Source: Reactome cellular response to mechanical stimulus Inferred from expression pattern. Source: UniProtKB chromatin-mediated maintenance of transcription Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of mitosis Inferred from direct assay Ref.32. Source: UniProtKB regulation of double-strand break repair via homologous recombination Inferred from direct assay Ref.38. Source: UniProtKB regulation of histone H3-K9 acetylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of mitotic centrosome separation Inferred from direct assay Ref.32. Source: UniProtKB regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage Inferred from sequence or structural similarity. Source: UniProtKB replicative senescence Non-traceable author statement. Source: BHF-UCL
Cellular component	centrosome Inferred from direct assay Ref.32. Source: UniProtKB chromatin Inferred from sequence or structural similarity. Source: UniProtKB condensed nuclear chromosome Inferred from direct assay Ref.2. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW histone kinase activity (H3-T11 specific) Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction Ref.38Ref.56Ref.53. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRCA1	P38398	3	EBI-974488,EBI-349905
CDC25C	P30307	2	EBI-974488,EBI-974439
CLSPN	Q9HAW4	5	EBI-974488,EBI-1369377
RAD51	Q06609	3	EBI-974488,EBI-297202
TIMELESS	Q9UNS1	2	EBI-974488,EBI-2212315

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 476

476

Serine/threonine-protein kinase Chk1

PRO_0000085848

Regions

Domain

9 – 265

257

Protein kinase

Nucleotide binding

15 – 23

9

ATP By similarity

Region

1 – 265

265

Interaction with CLSPN By similarity

Region

391 – 476

86

Autoinhibitory region

Sites

Active site

130

1

Proton acceptor

Binding site

38

1

ATP By similarity

Amino acid modifications

Modified residue

279

1

Phosphothreonine Ref.52 Ref.54

Modified residue

280

1

Phosphoserine; by PKB/AKT1 By similarity

Modified residue

284

1

Phosphoserine Ref.52

Modified residue

286

1

Phosphoserine Ref.49 Ref.51 Ref.52

Modified residue

296

1

Phosphoserine Ref.33 Ref.51 Ref.54

Modified residue

301

1

Phosphoserine Ref.49 Ref.51 Ref.57

Modified residue

307

1

Phosphoserine Ref.54

Modified residue

308

1

Phosphoserine Ref.45 Ref.49

Modified residue

317

1

Phosphoserine; by ATM and ATR Ref.13 Ref.16 Ref.19 Ref.20 Ref.22 Ref.24 Ref.29 Ref.33 Ref.35 Ref.45 Ref.49

Modified residue

331

1

Phosphoserine Ref.49

Modified residue

345

1

Phosphoserine; by ATM and ATR Ref.11 Ref.13 Ref.16 Ref.19 Ref.23 Ref.24 Ref.30 Ref.31 Ref.33 Ref.35 Ref.39 Ref.53

Modified residue

468

1

Phosphoserine Ref.49

Cross-link

436

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.44 Ref.53

Natural variations

Natural variant

156

1

R → Q. Ref.5
Corresponds to variant rs3731410 [ dbSNP | Ensembl ].

VAR_021123

Natural variant

223

1

E → V. Ref.63
Corresponds to variant rs35817404 [ dbSNP | Ensembl ].

VAR_040407

Natural variant

312

1

V → M. Ref.63
Corresponds to variant rs34097480 [ dbSNP | Ensembl ].

VAR_040408

Natural variant

471

1

I → V. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7 Ref.8
Corresponds to variant rs506504 [ dbSNP | Ensembl ].

VAR_024571

Experimental info

Mutagenesis

38

1

K → R: Abolishes kinase activity. Ref.16 Ref.31

Mutagenesis

130

1

D → A: Abolishes kinase activity. Ref.1 Ref.9 Ref.12 Ref.13 Ref.14 Ref.21 Ref.22 Ref.32

Mutagenesis

317

1

S → A: Abrogates interaction with RAD51; when associated with A-345. Reduces phosphorylation and impairs activation by hydroxyurea and ionizing radiation. Abrogates nuclear retention upon checkpoint activation. Impairs interaction with FBXO6. Ref.13 Ref.19 Ref.22 Ref.24 Ref.38

Mutagenesis

317

1

S → E: Enhances interaction with RAD51; when associated with E-345. Ref.13 Ref.19 Ref.22 Ref.24 Ref.38

Mutagenesis

344

1

F → A: Impairs nuclear export. Ref.24

Mutagenesis

345

1

S → A: Abrogates interaction with RAD51; when associated with A-317. Reduces phosphorylation and impairs activation by hydroxyurea and ionizing radiation. Impairs interaction with YWHAZ which is required for nuclear retention after checkpoint activation. Ref.13 Ref.19 Ref.22 Ref.24 Ref.38 Ref.53

Mutagenesis

345

1

S → E: Enhances interaction with RAD51; when associated with E-317. Ref.13 Ref.19 Ref.22 Ref.24 Ref.38 Ref.53

Mutagenesis

353

1

M → A: Impairs nuclear export. Ref.24

Mutagenesis

357

1

S → A: No effect on phosphorylation induced by hydroxyurea. Ref.13

Mutagenesis

366

1

S → A: No effect on phosphorylation induced by hydroxyurea. Ref.13

Mutagenesis

372

1

R → E in 3RE mutant. Disrupts the folding and/or conformation, allowing increased accessibility to FBXO6 component of SCF-type E3 ubiquitin ligase complex; when associated with E-376 and E-379. Ref.53

Mutagenesis

376

1

R → E in 3RE mutant. Disrupts the folding and/or conformation, allowing increased accessibility to FBXO6 component of SCF-type E3 ubiquitin ligase complex; when associated with E-372 and E-379. Ref.53

Mutagenesis

379

1

R → E in 3RE mutant. Disrupts the folding and/or conformation, allowing increased accessibility to FBXO6 component of SCF-type E3 ubiquitin ligase complex; when associated with E-372 and E-376. Ref.53

Mutagenesis

436

1

K → R: Enhances stability of the protein, probably by preventing ubiquitination at this site. Ref.53

Mutagenesis

468

1

S → A: No effect on phosphorylation induced by hydroxyurea. Ref.13

Secondary structure

1

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476

Helix Strand Turn

Details...

Helix

4 – 7

4

Beta strand

9 – 16

8

Beta strand

22 – 28

7

Turn

29 – 31

3

Beta strand

34 – 41

8

Helix

49 – 61

13

Beta strand

70 – 74

5

Beta strand

79 – 85

7

Helix

92 – 95

4

Turn

98 – 100

3

Helix

104 – 123

20

Helix

133 – 135

3

Beta strand

136 – 138

3

Beta strand

144 – 146

3

Helix

171 – 173

3

Helix

176 – 180

5

Helix

186 – 203

18

Beta strand

209 – 211

3

Helix

216 – 222

7

Helix

231 – 233

3

Helix

237 – 245

9

Turn

250 – 252

3

Helix

256 – 259

4

Turn

263 – 266

4

Sequences

	Sequence		Length	Mass (Da)
	O14757 [UniParc]. Last modified January 11, 2011. Version 2. Checksum: 0ABD0FAB67E60F67	FASTA	476	54,434
	10 20 30 40 50 60 MAVPFVEDWD LVQTLGEGAY GEVQLAVNRV TEEAVAVKIV DMKRAVDCPE NIKKEICINK 70 80 90 100 110 120 MLNHENVVKF YGHRREGNIQ YLFLEYCSGG ELFDRIEPDI GMPEPDAQRF FHQLMAGVVY 130 140 150 160 170 180 LHGIGITHRD IKPENLLLDE RDNLKISDFG LATVFRYNNR ERLLNKMCGT LPYVAPELLK 190 200 210 220 230 240 RREFHAEPVD VWSCGIVLTA MLAGELPWDQ PSDSCQEYSD WKEKKTYLNP WKKIDSAPLA 250 260 270 280 290 300 LLHKILVENP SARITIPDIK KDRWYNKPLK KGAKRPRVTS GGVSESPSGF SKHIQSNLDF 310 320 330 340 350 360 SPVNSASSEE NVKYSSSQPE PRTGLSLWDT SPSYIDKLVQ GISFSQPTCP DHMLLNSQLL 370 380 390 400 410 420 GTPGSSQNPW QRLVKRMTRF FTKLDADKSY QCLKETCEKL GYQWKKSCMN QVTISTTDRR 430 440 450 460 470 NNKLIFKVNL LEMDDKILVD FRLSKGDGLE FKRHFLKIKG KLIDIVSSQK IWLPAT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA damage to Cdk regulation through Cdc25." Sanchez Y., Wong C., Thoma R.S., Richman R., Wu Z., Piwnica-Worms H., Elledge S.J. Science 277:1497-1501(1997) [PubMed: 9278511] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN PHOSPHORYLATION OF CDC25A; CDC25B AND CDC25C, INTERACTION WITH CDC25A; CDC25B AND CDC25C, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-130, VARIANT VAL-471.
[2]	"Atm-dependent interactions of a mammalian chk1 homolog with meiotic chromosomes." Flaggs G., Plug A.W., Dunks K.M., Mundt K.E., Ford J.C., Quiggle M.R.E., Taylor E.M., Westphal C.H., Ashley T., Hoekstra M.F., Carr A.M. Curr. Biol. 7:977-986(1997) [PubMed: 9382850] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT VAL-471.
[3]	"Analysis of the candidate target genes for mutation in microsatellite instability-positive cancers of the colorectum, stomach, and endometrium." Semba S., Ouyang H., Han S.-Y., Kato Y., Horii A. Int. J. Oncol. 16:731-737(2000) [PubMed: 10717241] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-471.
[4]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-471. Tissue: Testis.
[5]	NIEHS SNPs program Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-156 AND VAL-471.
[6]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed: 16554811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-471.
[8]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-471. Tissue: Bone marrow and Muscle.
[9]	"The human homologs of checkpoint kinases Chk1 and Cds1 (Chk2) phosphorylate p53 at multiple DNA damage-inducible sites." Shieh S.-Y., Ahn J., Tamai K., Taya Y., Prives C. Genes Dev. 14:289-300(2000) [PubMed: 10673501] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF TP53, MUTAGENESIS OF ASP-130.
[10]	Erratum Shieh S.-Y., Ahn J., Tamai K., Taya Y., Prives C. Genes Dev. 14:750-750(2000)
[11]	"Chk1 is an essential kinase that is regulated by Atr and required for the G(2)/M DNA damage checkpoint." Liu Q., Guntuku S., Cui X.-S., Matsuoka S., Cortez D., Tamai K., Luo G., Carattini-Rivera S., DeMayo F., Bradley A., Donehower L.A., Elledge S.J. Genes Dev. 14:1448-1459(2000) [PubMed: 10859164] [Abstract] Cited for: PHOSPHORYLATION AT SER-345 BY ATR.
[12]	"Activation of mammalian Chk1 during DNA replication arrest: a role for Chk1 in the intra-S phase checkpoint monitoring replication origin firing." Feijoo C., Hall-Jackson C., Wu R., Jenkins D., Leitch J., Gilbert D.M., Smythe C. J. Cell Biol. 154:913-923(2001) [PubMed: 11535615] [Abstract] Cited for: FUNCTION IN DNA REPLICATION, PHOSPHORYLATION BY ATR, MUTAGENESIS OF ASP-130.
[13]	"ATR-mediated checkpoint pathways regulate phosphorylation and activation of human Chk1." Zhao H., Piwnica-Worms H. Mol. Cell. Biol. 21:4129-4139(2001) [PubMed: 11390642] [Abstract] Cited for: PHOSPHORYLATION AT SER-317 AND SER-345, MUTAGENESIS OF ASP-130; SER-317; SER-345; SER-357; SER-366 AND SER-468.
[14]	"Determination of substrate motifs for human Chk1 and hCds1/Chk2 by the oriented peptide library approach." O'Neill T., Giarratani L., Chen P., Iyer L., Lee C.-H., Bobiak M., Kanai F., Zhou B.-B., Chung J.H., Rathbun G.A. J. Biol. Chem. 277:16102-16115(2002) [PubMed: 11821419] [Abstract] Cited for: SUBSTRATE SPECIFICITY, MUTAGENESIS OF ASP-130.
[15]	Erratum O'Neill T., Giarratani L., Chen P., Iyer L., Lee C.-H., Bobiak M., Kanai F., Zhou B.-B., Chung J.H., Rathbun G.A. J. Biol. Chem. 277:35776-35777(2002)
[16]	"An ATR- and Chk1-dependent S checkpoint inhibits replicon initiation following UVC-induced DNA damage." Heffernan T.P., Simpson D.A., Frank A.R., Heinloth A.N., Paules R.S., Cordeiro-Stone M., Kaufmann W.K. Mol. Cell. Biol. 22:8552-8561(2002) [PubMed: 12446774] [Abstract] Cited for: FUNCTION IN DNA DAMAGE RESPONSE, PHOSPHORYLATION AT SER-317 AND SER-345, MUTAGENESIS OF LYS-38.
[17]	"BRCA1 regulates the G2/M checkpoint by activating Chk1 kinase upon DNA damage." Yarden R.I., Pardo-Reoyo S., Sgagias M., Cowan K.H., Brody L.C. Nat. Genet. 30:285-289(2002) [PubMed: 11836499] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH BRCA1.
[18]	"Disruption of the checkpoint kinase 1/cell division cycle 25A pathway abrogates ionizing radiation-induced S and G2 checkpoints." Zhao H., Watkins J.L., Piwnica-Worms H. Proc. Natl. Acad. Sci. U.S.A. 99:14795-14800(2002) [PubMed: 12399544] [Abstract] Cited for: FUNCTION IN DNA DAMAGE RESPONSE.
[19]	"Chk1 regulates the S phase checkpoint by coupling the physiological turnover and ionizing radiation-induced accelerated proteolysis of Cdc25A." Soerensen C.S., Syljuaesen R.G., Falck J., Schroeder T., Roennstrand L., Khanna K.K., Zhou B.-B., Bartek J., Lukas J. Cancer Cell 3:247-258(2003) [PubMed: 12676583] [Abstract] Cited for: FUNCTION IN CDC25A TURNOVER, PHOSPHORYLATION AT SER-317 AND SER-345, MUTAGENESIS OF SER-317 AND SER-345.
[20]	"Human tousled like kinases are targeted by an ATM- and Chk1-dependent DNA damage checkpoint." Groth A., Lukas J., Nigg E.A., Sillje H.H.W., Wernstedt C., Bartek J., Hansen K. EMBO J. 22:1676-1687(2003) [PubMed: 12660173] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF TLK1, PHOSPHORYLATION AT SER-317.
[21]	"SCFbeta-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase." Jin J., Shirogane T., Xu L., Nalepa G., Qin J., Elledge S.J., Harper J.W. Genes Dev. 17:3062-3074(2003) [PubMed: 14681206] [Abstract] Cited for: FUNCTION IN CDC25A TURNOVER, MUTAGENESIS OF ASP-130.
[22]	"Ataxia-telangiectasia-mutated (ATM) and NBS1-dependent phosphorylation of Chk1 on ser-317 in response to ionizing radiation." Gatei M., Sloper K., Soerensen C., Syljuaesen R., Falck J., Hobson K., Savage K., Lukas J., Zhou B.-B., Bartek J., Khanna K.K. J. Biol. Chem. 278:14806-14811(2003) [PubMed: 12588868] [Abstract] Cited for: PHOSPHORYLATION AT SER-317, MUTAGENESIS OF ASP-130; SER-317 AND SER-345.
[23]	"Chk1 mediates S and G2 arrests through Cdc25A degradation in response to DNA-damaging agents." Xiao Z., Chen Z., Gunasekera A.H., Sowin T.J., Rosenberg S.H., Fesik S., Zhang H. J. Biol. Chem. 278:21767-21773(2003) [PubMed: 12676925] [Abstract] Cited for: FUNCTION IN CDC25A TURNOVER, PHOSPHORYLATION AT SER-345.
[24]	"Regulation of Chk1 includes chromatin association and 14-3-3 binding following phosphorylation on ser-345." Jiang K., Pereira E., Maxfield M., Russell B., Goudelock D.M., Sanchez Y. J. Biol. Chem. 278:25207-25217(2003) [PubMed: 12676962] [Abstract] Cited for: INTERACTION WITH YWHAZ AND XPO1, SUBCELLULAR LOCATION, ASSOCIATION WITH CHROMATIN, PHOSPHORYLATION AT SER-317 AND SER-345, MUTAGENESIS OF SER-317; PHE-344; SER-345 AND MET-353.
[25]	"Phosphorylation at serine 75 is required for UV-mediated degradation of human Cdc25A phosphatase at the S-phase checkpoint." Hassepass I., Voit R., Hoffmann I. J. Biol. Chem. 278:29824-29829(2003) [PubMed: 12759351] [Abstract] Cited for: FUNCTION IN CDC25A TURNOVER.
[26]	"Human claspin is required for replication checkpoint control." Chini C.C.S., Chen J. J. Biol. Chem. 278:30057-30062(2003) [PubMed: 12766152] [Abstract] Cited for: INTERACTION WITH CLSPN.
[27]	"Chk1 kinase negatively regulates mitotic function of Cdc25A phosphatase through 14-3-3 binding." Chen M.-S., Ryan C.E., Piwnica-Worms H. Mol. Cell. Biol. 23:7488-7497(2003) [PubMed: 14559997] [Abstract] Cited for: FUNCTION IN MITOSIS, FUNCTION IN PHOSPHORYLATION OF CDC25A.
[28]	"Suppression of tousled-like kinase activity after DNA damage or replication block requires ATM, NBS1 and Chk1." Krause D.R., Jonnalagadda J.C., Gatei M.H., Sillje H.H.W., Zhou B.-B., Nigg E.A., Khanna K. Oncogene 22:5927-5937(2003) [PubMed: 12955071] [Abstract] Cited for: REGULATION OF TLK1.
[29]	"MSH2 and ATR form a signaling module and regulate two branches of the damage response to DNA methylation." Wang Y., Qin J. Proc. Natl. Acad. Sci. U.S.A. 100:15387-15392(2003) [PubMed: 14657349] [Abstract] Cited for: PHOSPHORYLATION AT SER-317.
[30]	"The DNA crosslink-induced S-phase checkpoint depends on ATR-CHK1 and ATR-NBS1-FANCD2 pathways." Pichierri P., Rosselli F. EMBO J. 23:1178-1187(2004) [PubMed: 14988723] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-345.
[31]	"Differential mode of regulation of the checkpoint kinases CHK1 and CHK2 by their regulatory domains." Ng C.-P., Lee H.C., Ho C.W., Arooz T., Siu W.Y., Lau A., Poon R.Y.C. J. Biol. Chem. 279:8808-8819(2004) [PubMed: 14681223] [Abstract] Cited for: DOMAIN, MITOTIC PHOSPHORYLATION, PHOSPHORYLATION AT SER-345, MUTAGENESIS OF LYS-38.
[32]	"Centrosome-associated Chk1 prevents premature activation of cyclin-B-Cdk1 kinase." Kraemer A., Mailand N., Lukas C., Syljuaesen R.G., Wilkinson C.J., Nigg E.A., Bartek J., Lukas J. Nat. Cell Biol. 6:884-891(2004) [PubMed: 15311285] [Abstract] Cited for: FUNCTION IN MITOSIS, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-130.
[33]	"DNA-dependent phosphorylation of Chk1 and claspin in a human cell-free system." Clarke C.A.L., Clarke P.R. Biochem. J. 388:705-712(2005) [PubMed: 15707391] [Abstract] Cited for: INTERACTION WITH CLSPN, PHOSPHORYLATION AT SER-296; SER-317 AND SER-345.
[34]	"Lack of PTEN sequesters CHK1 and initiates genetic instability." Puc J., Keniry M., Li H.S., Pandita T.K., Choudhury A.D., Memeo L., Mansukhani M., Murty V.V.V.S., Gaciong Z., Meek S.E.M., Piwnica-Worms H., Hibshoosh H., Parsons R. Cancer Cell 7:193-204(2005) [PubMed: 15710331] [Abstract] Cited for: SUBCELLULAR LOCATION.
[35]	"PPM1D dephosphorylates Chk1 and p53 and abrogates cell cycle checkpoints." Lu X., Nannenga B., Donehower L.A. Genes Dev. 19:1162-1174(2005) [PubMed: 15870257] [Abstract] Cited for: INTERACTION WITH PPM1D, PHOSPHORYLATION AT SER-317 AND SER-345, DEPHOSPHORYLATION BY PPM1D.
[36]	"p53 C-terminal phosphorylation by CHK1 and CHK2 participates in the regulation of DNA-damage-induced C-terminal acetylation." Ou Y.-H., Chung P.-H., Sun T.-P., Shieh S.-Y. Mol. Biol. Cell 16:1684-1695(2005) [PubMed: 15659650] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF TP53, FUNCTION IN TP53-DEPENDENT TRANSCRIPTION.
[37]	"Coupling of human circadian and cell cycles by the timeless protein." Uensal-Kacmaz K., Mullen T.E., Kaufmann W.K., Sancar A. Mol. Cell. Biol. 25:3109-3116(2005) [PubMed: 15798197] [Abstract] Cited for: INTERACTION WITH TIMELESS.
[38]	"The cell-cycle checkpoint kinase Chk1 is required for mammalian homologous recombination repair." Soerensen C.S., Hansen L.T., Dziegielewski J., Syljuaesen R.G., Lundin C., Bartek J., Helleday T. Nat. Cell Biol. 7:195-201(2005) [PubMed: 15665856] [Abstract] Cited for: FUNCTION IN HOMOLOGOUS RECOMBINATION REPAIR, FUNCTION IN PHOSPHORYLATION OF RAD51, INTERACTION WITH RAD51, MUTAGENESIS OF SER-317 AND SER-345.
[39]	"DNA damage-induced mitotic catastrophe is mediated by the Chk1-dependent mitotic exit DNA damage checkpoint." Huang X., Tran T., Zhang L., Hatcher R., Zhang P. Proc. Natl. Acad. Sci. U.S.A. 102:1065-1070(2005) [PubMed: 15650047] [Abstract] Cited for: FUNCTION IN MITOTIC EXIT, PHOSPHORYLATION AT SER-345.
[40]	"14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1, resulting in p53 activation." Jin Y., Dai M.S., Lu S.Z., Xu Y., Luo Z., Zhao Y., Lu H. EMBO J. 25:1207-1218(2006) [PubMed: 16511572] [Abstract] Cited for: FUNCTION IN TP53 ACTIVATION, FUNCTION IN PHOSPHORYLATION OF MDM4.
[41]	"Repeated phosphopeptide motifs in human Claspin are phosphorylated by Chk1 and mediate Claspin function." Chini C.C., Chen J. J. Biol. Chem. 281:33276-33282(2006) [PubMed: 16963448] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CLSPN, INTERACTION WITH CLSPN.
[42]	"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: 17380128] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF RB1.
[43]	"Chk1-mediated phosphorylation of FANCE is required for the Fanconi anemia/BRCA pathway." Wang X., Kennedy R.D., Ray K., Stuckert P., Ellenberger T., D'Andrea A.D. Mol. Cell. Biol. 27:3098-3108(2007) [PubMed: 17296736] [Abstract] Cited for: FUNCTION IN DNA CROSS-LINKS REPAIR, FUNCTION IN PHOSPHORYLATION OF FANCE.
[44]	"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry." Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D. Proteomics 7:868-874(2007) [PubMed: 17370265] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-436, MASS SPECTROMETRY. Tissue: Mammary cancer.
[45]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308 AND SER-317, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[46]	"Chk1 suppresses a caspase-2 apoptotic response to DNA damage that bypasses p53, Bcl-2, and caspase-3." Sidi S., Sanda T., Kennedy R.D., Hagen A.T., Jette C.A., Hoffmans R., Pascual J., Imamura S., Kishi S., Amatruda J.F., Kanki J.P., Green D.R., D'Andrea A.A., Look A.T. Cell 133:864-877(2008) [PubMed: 18510930] [Abstract] Cited for: FUNCTION IN APOPTOSIS.
[47]	"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: 18728393] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF NEK6.
[48]	"Chk1 and Claspin potentiate PCNA ubiquitination." Yang X.H., Shiotani B., Classon M., Zou L. Genes Dev. 22:1147-1152(2008) [PubMed: 18451105] [Abstract] Cited for: FUNCTION IN REPLICATION FORK MAINTENANCE, FUNCTION IN PCNA UBIQUITINATION.
[49]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286; SER-301; SER-308; SER-317; SER-331 AND SER-468, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[50]	"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: 18317453] [Abstract] Cited for: FUNCTION IN RAD51-MEDIATED DNA REPAIR, FUNCTION IN PHOSPHORYLATION OF BRCA2 AND RAD51.
[51]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286; SER-296 AND SER-301, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[52]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-279; SER-280; SER-284 AND SER-286, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[53]	"The F box protein Fbx6 regulates Chk1 stability and cellular sensitivity to replication stress." Zhang Y.-W., Brognard J., Coughlin C., You Z., Dolled-Filhart M., Aslanian A., Manning G., Abraham R.T., Hunter T. Mol. Cell 35:442-453(2009) [PubMed: 19716789] [Abstract] Cited for: PHOSPHORYLATION AT SER-345, UBIQUITINATION AT LYS-436, INTERACTION WITH FBXO6, MUTAGENESIS OF SER-345; ARG-372; ARG-376; ARG-379 AND LYS-436.
[54]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-279; SER-280; SER-296 AND SER-307, MASS SPECTROMETRY.
[55]	"NEK11 regulates CDC25A degradation and the IR-induced G2/M checkpoint." Melixetian M., Klein D.K., Soerensen C.S., Helin K. Nat. Cell Biol. 11:1247-1253(2009) [PubMed: 19734889] [Abstract] Cited for: FUNCTION IN NEK11 PHOSPHORYLATION.
[56]	"Human FEM1B is required for Rad9 recruitment and CHK1 activation in response to replication stress." Sun T.P., Shieh S.Y. Oncogene 28:1971-1981(2009) [PubMed: 19330022] [Abstract] Cited for: INTERACTION WITH FEM1B.
[57]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-301, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[58]	"NEK11: linking CHK1 and CDC25A in DNA damage checkpoint signaling." Soerensen C.S., Melixetian M., Klein D.K., Helin K. Cell Cycle 9:450-455(2010) [PubMed: 20090422] [Abstract] Cited for: FUNCTION IN CDC25A DEGRADATION.
[59]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[60]	"The 1.7 A crystal structure of human cell cycle checkpoint kinase Chk1: implications for Chk1 regulation." Chen P., Luo C., Deng Y., Ryan K., Register J., Margosiak S., Tempczyk-Russell A., Nguyen B., Myers P., Lundgren K., Kan C.-C., O'Connor P.M. Cell 100:681-692(2000) [PubMed: 10761933] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-289.
[61]	"Structural basis for Chk1 inhibition by UCN-01." Zhao B., Bower M.J., McDevitt P.J., Zhao H., Davis S.T., Johanson K.O., Green S.M., Concha N.O., Zhou B.-B.S. J. Biol. Chem. 277:46609-46615(2002) [PubMed: 12244092] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-289.
[62]	"Structure-based design of novel Chk1 inhibitors: insights into hydrogen bonding and protein-ligand affinity." Foloppe N., Fisher L.M., Howes R., Kierstan P., Potter A., Robertson A.G.S., Surgenor A.E. J. Med. Chem. 48:4332-4345(2005) [PubMed: 15974586] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-289.
[63]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-223 AND MET-312.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF016582 mRNA. Translation: AAC51736.1.
AF032874 mRNA. Translation: AAB88852.1.
AB032387 Genomic DNA. Translation: BAA84577.1.
AK292549 mRNA. Translation: BAF85238.1.
AF527555 Genomic DNA. Translation: AAM78553.1.
AP001132 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67644.1.
BC004202 mRNA. Translation: AAH04202.1.
BC017575 mRNA. Translation: AAH17575.1.

IPI

IPI00023664.

RefSeq

NP_001107593.1. NM_001114121.2.
NP_001107594.1. NM_001114122.2.
NP_001231775.1. NM_001244846.1.
NP_001265.2. NM_001274.5.

UniGene

Hs.24529.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IA8	X-ray	1.70	A	1-289	[»]
1NVQ	X-ray	2.00	A	1-289	[»]
1NVR	X-ray	1.80	A	1-289	[»]
1NVS	X-ray	1.80	A	1-289	[»]
1ZLT	X-ray	1.74	A	1-289	[»]
1ZYS	X-ray	1.70	A	1-273	[»]
2AYP	X-ray	2.90	A	1-269	[»]
2BR1	X-ray	2.00	A	1-289	[»]
2BRB	X-ray	2.10	A	1-289	[»]
2BRG	X-ray	2.10	A	1-289	[»]
2BRH	X-ray	2.10	A	1-289	[»]
2BRM	X-ray	2.20	A	1-289	[»]
2BRN	X-ray	2.80	A	1-289	[»]
2BRO	X-ray	2.20	A	1-289	[»]
2C3J	X-ray	2.10	A	1-289	[»]
2C3K	X-ray	2.60	A	1-289	[»]
2C3L	X-ray	2.35	A	1-289	[»]
2CGU	X-ray	2.50	A	1-289	[»]
2CGV	X-ray	2.60	A	1-289	[»]
2CGW	X-ray	2.20	A	1-289	[»]
2CGX	X-ray	2.20	A	1-289	[»]
2E9N	X-ray	2.50	A	2-270	[»]
2E9O	X-ray	2.10	A	2-270	[»]
2E9P	X-ray	2.60	A	2-270	[»]
2E9U	X-ray	2.00	A	2-270	[»]
2E9V	X-ray	2.00	A/B	2-269	[»]
2GDO	X-ray	3.00	A	1-289	[»]
2GHG	X-ray	3.50	A	2-270	[»]
2HOG	X-ray	1.90	A	2-307	[»]
2HXL	X-ray	1.80	A	2-307	[»]
2HXQ	X-ray	2.00	A	2-307	[»]
2HY0	X-ray	1.70	A	2-307	[»]
2QHM	X-ray	2.00	A	1-307	[»]
2QHN	X-ray	1.70	A	1-307	[»]
2R0U	X-ray	1.90	A	1-307	[»]
2WMQ	X-ray	2.48	A	1-289	[»]
2WMR	X-ray	2.43	A	1-289	[»]
2WMS	X-ray	2.70	A	1-289	[»]
2WMT	X-ray	2.55	A	1-289	[»]
2WMU	X-ray	2.60	A	1-289	[»]
2WMV	X-ray	2.01	A	1-289	[»]
2WMW	X-ray	2.43	A	1-289	[»]
2WMX	X-ray	2.45	A	1-289	[»]
2X8D	X-ray	1.90	A	1-289	[»]
2X8E	X-ray	2.50	A	1-276	[»]
2X8I	X-ray	1.92	A	1-289	[»]
2XEY	X-ray	2.70	A	1-289	[»]
2XEZ	X-ray	2.25	A	1-289	[»]
2XF0	X-ray	2.40	A	1-289	[»]
2YWP	X-ray	2.90	A	2-270	[»]
3F9N	X-ray	1.90	A	2-307	[»]
3JVR	X-ray	1.76	A	2-272	[»]
3JVS	X-ray	1.90	A	2-272	[»]
3NLB	X-ray	1.90	A	1-289	[»]
3OT3	X-ray	1.44	A	2-274	[»]
3OT8	X-ray	1.65	A	2-274	[»]
3PA3	X-ray	1.40	A	2-274	[»]
3PA4	X-ray	1.59	A	2-274	[»]
3PA5	X-ray	1.70	A	2-274	[»]

ProteinModelPortal

O14757.

SMR

O14757. Positions 3-447.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24182N.

IntAct

O14757. 13 interactions.

MINT

MINT-1179072.

STRING

O14757.

PTM databases

PhosphoSite

O14757.

Proteomic databases

PRIDE

O14757.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000278916; ENSP00000278916; ENSG00000149554.
ENST00000428830; ENSP00000412504; ENSG00000149554.
ENST00000438015; ENSP00000388648; ENSG00000149554.

GeneID

1111.

KEGG

hsa:1111.

Organism-specific databases

CTD

1111.

GeneCards

GC11P125495.

H-InvDB

HIX0201657.

HGNC

HGNC:1925. CHEK1.

HPA

CAB002049.

MIM

603078. gene.

neXtProt

NX_O14757.

PharmGKB

PA110.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG10563.

HOVERGEN

HBG002590.

InParanoid

O14757.

OMA

GGFSKHI.

PhylomeDB

O14757.

Enzyme and pathway databases

BRENDA

2.7.11.1. 2681.

Pathway_Interaction_DB

circadianpathway. Circadian rhythm pathway.

Reactome

REACT_111102. Signal Transduction.
REACT_1538. Cell Cycle Checkpoints.

Gene expression databases

ArrayExpress

O14757.

Bgee

O14757.

CleanEx

HS_CHEK1.

Genevestigator

O14757.

GermOnline

ENSG00000149554. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_kinase-like_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR002290. Ser/Thr_kinase_dom.
[Graphical view]

KO

K02216.

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

O14757.

NextBio

4608.

SOURCE

Search...

Entry information

Entry name

CHK1_HUMAN

Accession

Primary (citable) accession number: O14757
Secondary accession number(s): A8K934

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 11, 2011
Last modified:	January 25, 2012
This is version 141 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.