UniProtKB - O14757 (CHK1_HUMAN)
Serine/threonine-protein kinase Chk1
CHEK1
Functioni
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 (PubMed:11535615, PubMed:12446774, PubMed:12399544, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15665856, PubMed:15650047, PubMed:32357935).
May also negatively regulate cell cycle progression during unperturbed cell cycles (PubMed:11535615, PubMed:12446774, PubMed:12399544, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15665856, PubMed:15650047).
This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome (PubMed:11535615, PubMed:12446774, PubMed:12399544, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15665856, PubMed:15650047).
Recognizes the substrate consensus sequence [R-X-X-S/T] (PubMed:11535615, PubMed:12446774, PubMed:12399544, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15665856, PubMed:15650047).
Binds to and phosphorylates CDC25A, CDC25B and CDC25C (PubMed:9278511, PubMed:12676583, PubMed:14681206, PubMed:12676925, PubMed:12759351, PubMed:19734889, PubMed:14559997).
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 (PubMed:9278511).
Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis of CDC25A (PubMed:9278511, PubMed:12676583, PubMed:14681206, PubMed:12676925, PubMed:12759351, PubMed:19734889).
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 (PubMed:9278511, PubMed:19734889, PubMed:20090422).
Inhibition of CDC25 leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression (PubMed:9278511).
Also phosphorylates NEK6 (PubMed:18728393).
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 (PubMed:15665856).
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 (PubMed:10673501, PubMed:15659650, PubMed:16511572).
Also promotes repair of DNA cross-links through phosphorylation of FANCE (PubMed:17296736).
Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A (PubMed:12660173, PubMed:12955071).
This may enhance chromatin assembly both in the presence or absence of DNA damage (PubMed:12660173, PubMed:12955071).
May also play a role in replication fork maintenance through regulation of PCNA (PubMed:18451105).
May regulate the transcription of genes that regulate cell-cycle progression through the phosphorylation of histones (By similarity).
Phosphorylates histone H3.1 (to form H3T11ph), which leads to epigenetic inhibition of a subset of genes (By similarity).
May also phosphorylate RB1 to promote its interaction with the E2F family of transcription factors and subsequent cell cycle arrest (PubMed:17380128).
Phosphorylates SPRTN, promoting SPRTN recruitment to chromatin (PubMed:31316063).
Reduces replication stress and activates the G2/M checkpoint, by phosphorylating and inactivating PABIR1/FAM122A and promoting the serine/threonine-protein phosphatase 2A-mediated dephosphorylation and stabilization of WEE1 levels and activity (PubMed:33108758).
By similarity27 PublicationsEndogenous repressor of isoform 1, interacts with, and antagonizes CHK1 to promote the S to G2/M phase transition.
1 PublicationCatalytic activityi
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 38 | ATPPROSITE-ProRule annotation | 1 | |
Active sitei | 130 | Proton acceptor | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 15 – 23 | ATPPROSITE-ProRule annotation | 9 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- histone kinase activity (H3-T11 specific) Source: UniProtKB
- protein domain specific binding Source: CAFA
- protein kinase activity Source: CACAO
- protein serine/threonine/tyrosine kinase activity Source: RHEA
- protein serine/threonine kinase activity Source: UniProtKB
- protein serine kinase activity Source: RHEA
GO - Biological processi
- apoptotic process Source: UniProtKB
- apoptotic process involved in development Source: Ensembl
- cellular response to caffeine Source: Ensembl
- cellular response to DNA damage stimulus Source: UniProtKB
- cellular response to mechanical stimulus Source: UniProtKB
- DNA damage checkpoint signaling Source: UniProtKB
- DNA damage induced protein phosphorylation Source: UniProtKB
- DNA repair Source: UniProtKB
- DNA replication Source: Reactome
- epigenetic maintenance of chromatin in transcription-competent conformation Source: UniProtKB
- G2/M transition of mitotic cell cycle Source: Ensembl
- inner cell mass cell proliferation Source: Ensembl
- intracellular signal transduction Source: GO_Central
- mitotic G2/M transition checkpoint Source: UniProtKB
- mitotic G2 DNA damage checkpoint signaling Source: UniProtKB
- negative regulation of DNA biosynthetic process Source: Ensembl
- negative regulation of G0 to G1 transition Source: Reactome
- negative regulation of mitotic nuclear division Source: UniProtKB
- nucleus organization Source: Ensembl
- peptidyl-threonine phosphorylation Source: UniProtKB
- positive regulation of cell cycle Source: CAFA
- protein phosphorylation Source: UniProtKB
- regulation of cell population proliferation Source: Ensembl
- regulation of double-strand break repair via homologous recombination Source: UniProtKB
- regulation of histone H3-K9 acetylation Source: UniProtKB
- regulation of mitotic centrosome separation Source: UniProtKB
- regulation of signal transduction by p53 class mediator Source: Reactome
- regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage Source: UniProtKB
- replicative senescence Source: BHF-UCL
Keywordsi
Molecular function | Kinase, Serine/threonine-protein kinase, Transferase |
Biological process | Cell cycle, DNA damage, DNA repair |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 2.7.11.1, 2681 |
PathwayCommonsi | O14757 |
Reactomei | R-HSA-1433557, Signaling by SCF-KIT R-HSA-176187, Activation of ATR in response to replication stress R-HSA-5693607, Processing of DNA double-strand break ends R-HSA-5693616, Presynaptic phase of homologous DNA pairing and strand exchange R-HSA-6796648, TP53 Regulates Transcription of DNA Repair Genes R-HSA-6804756, Regulation of TP53 Activity through Phosphorylation R-HSA-69473, G2/M DNA damage checkpoint R-HSA-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A R-HSA-75035, Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex R-HSA-8953750, Transcriptional Regulation by E2F6 |
SignaLinki | O14757 |
SIGNORi | O14757 |
Names & Taxonomyi
Protein namesi | Recommended name: Serine/threonine-protein kinase Chk1 (EC:2.7.11.15 Publications)Alternative name(s): CHK1 checkpoint homolog Cell cycle checkpoint kinase Checkpoint kinase-1 |
Gene namesi | Name:CHEK1 Synonyms:CHK1 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:1925, CHEK1 |
MIMi | 603078, gene |
neXtProti | NX_O14757 |
VEuPathDBi | HostDB:ENSG00000149554 |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Cytoskeleton
- centrosome 1 Publication
Nucleus
- Nucleus 5 Publications
Other locations
- Chromosome 3 Publications
Note: Nuclear export is mediated at least in part by XPO1/CRM1 (PubMed:12676962). Also localizes to the centrosome specifically during interphase, where it may protect centrosomal CDC2 kinase from inappropriate activation by cytoplasmic CDC25B (PubMed:15311285). Proteolytic cleavage at the C-terminus by SPRTN promotes removal from chromatin (PubMed:31316063).3 Publications
Cytoskeleton
- centrosome Source: UniProtKB
Cytosol
- cytosol Source: Reactome
Extracellular region or secreted
- extracellular space Source: UniProtKB
Nucleus
- condensed nuclear chromosome Source: UniProtKB
- nucleoplasm Source: HPA
- nucleus Source: UniProtKB
Other locations
- chromatin Source: UniProtKB
- cytoplasm Source: CAFA
- intracellular membrane-bounded organelle Source: HPA
- protein-containing complex Source: CAFA
- replication fork Source: Ensembl
Keywords - Cellular componenti
Chromosome, Cytoplasm, Cytoskeleton, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 38 | K → R: Abolishes kinase activity. 2 Publications | 1 | |
Mutagenesisi | 130 | D → A: Abolishes kinase activity. 8 Publications | 1 | |
Mutagenesisi | 132 | K → R: Strong reduction of chromatin-associated CHK1 ubiquitination. 1 Publication | 1 | |
Mutagenesisi | 317 | 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. 5 Publications | 1 | |
Mutagenesisi | 317 | S → E: Enhances interaction with RAD51; when associated with E-345. 5 Publications | 1 | |
Mutagenesisi | 344 | F → A: Impairs nuclear export. 1 Publication | 1 | |
Mutagenesisi | 345 | 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. 6 Publications | 1 | |
Mutagenesisi | 345 | S → E: Enhances interaction with RAD51; when associated with E-317. 6 Publications | 1 | |
Mutagenesisi | 353 | M → A: Impairs nuclear export. 1 Publication | 1 | |
Mutagenesisi | 357 | S → A: No effect on phosphorylation induced by hydroxyurea. 1 Publication | 1 | |
Mutagenesisi | 366 | S → A: No effect on phosphorylation induced by hydroxyurea. 1 Publication | 1 | |
Mutagenesisi | 372 | 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. 1 Publication | 1 | |
Mutagenesisi | 376 | 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. 1 Publication | 1 | |
Mutagenesisi | 379 | 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. 1 Publication | 1 | |
Mutagenesisi | 436 | K → R: Enhances stability of the protein, probably by preventing ubiquitination at this site. 1 Publication | 1 | |
Mutagenesisi | 468 | S → A: No effect on phosphorylation induced by hydroxyurea. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 1111 |
OpenTargetsi | ENSG00000149554 |
PharmGKBi | PA110 |
Miscellaneous databases
Pharosi | O14757, Tchem |
Chemistry databases
ChEMBLi | CHEMBL4630 |
DrugBanki | DB07647, (2R)-1-[(5,6-DIPHENYL-7H-PYRROLO[2,3-D]PYRIMIDIN-4-YL)AMINO]PROPAN-2-OL DB07648, (2R)-3-{[(4Z)-5,6-DIPHENYL-6,7-DIHYDRO-4H-PYRROLO[2,3-D]PYRIMIDIN-4-YLIDENE]AMINO}PROPANE-1,2-DIOL DB07037, (2S)-1-AMINO-3-[(5-NITROQUINOLIN-8-YL)AMINO]PROPAN-2-OL DB07243, (3-ENDO)-8-METHYL-8-AZABICYCLO[3.2.1]OCT-3-YL 1H-PYRROLO[2,3-B]PYRIDINE-3-CARBOXYLATE DB07078, (3Z)-6-(4-HYDROXY-3-METHOXYPHENYL)-3-(1H-PYRROL-2-YLMETHYLENE)-1,3-DIHYDRO-2H-INDOL-2-ONE DB07654, (5,6-DIPHENYL-FURO[2,3-D]PYRIMIDIN-4-YLAMINO)-ACETIC DB07213, (5-{3-[5-(PIPERIDIN-1-YLMETHYL)-1H-INDOL-2-YL]-1H-INDAZOL-6-YL}-2H-1,2,3-TRIAZOL-4-YL)METHANOL DB07314, 1-(5-CHLORO-2,4-DIMETHOXYPHENYL)-3-(5-CYANOPYRAZIN-2-YL)UREA DB07228, 1-(5-CHLORO-2-METHOXYPHENYL)-3-{6-[2-(DIMETHYLAMINO)-1-METHYLETHOXY]PYRAZIN-2-YL}UREA DB08781, 1-[(2S)-4-(5-BROMO-1H-PYRAZOLO[3,4-B]PYRIDIN-4-YL)MORPHOLIN-2-YL]METHANAMINE DB08774, 1-[(2S)-4-(5-phenyl-1H-pyrazolo[3,4-b]pyridin-4-yl)morpholin-2-yl]methanamine DB07311, 18-CHLORO-11,12,13,14-TETRAHYDRO-1H,10H-8,4-(AZENO)-9,15,1,3,6-BENZODIOXATRIAZACYCLOHEPTADECIN-2-ONE DB07034, 2,2'-{[9-(HYDROXYIMINO)-9H-FLUORENE-2,7-DIYL]BIS(OXY)}DIACETIC ACID DB07038, 2-(cyclohexylamino)benzoic acid DB08779, 2-(methylsulfanyl)-5-(thiophen-2-ylmethyl)-1H-imidazol-4-ol DB08393, 2-[(5,6-DIPHENYLFURO[2,3-D]PYRIMIDIN-4-YL)AMINO]ETHANOL DB08392, 2-[5,6-BIS-(4-METHOXY-PHENYL)-FURO[2,3-D]PYRIMIDIN-4-YLAMINO]-ETHANOL DB07959, 3-(1H-BENZIMIDAZOL-2-YL)-1H-INDAZOLE DB07075, 3-(5-{[4-(AMINOMETHYL)PIPERIDIN-1-YL]METHYL}-1H-INDOL-2-YL)-1H-INDAZOLE-6-CARBONITRILE DB07025, 3-(5-{[4-(AMINOMETHYL)PIPERIDIN-1-YL]METHYL}-1H-INDOL-2-YL)QUINOLIN-2(1H)-ONE DB07655, 3-AMINO-3-BENZYL-[4.3.0]BICYCLO-1,6-DIAZANONAN-2-ONE DB07320, 4-(6-{[(4-METHYLCYCLOHEXYL)AMINO]METHYL}-1,4-DIHYDROINDENO[1,2-C]PYRAZOL-3-YL)BENZOIC ACID DB07336, 4-[3-(1H-BENZIMIDAZOL-2-YL)-1H-INDAZOL-6-YL]-2-METHOXYPHENOL DB08777, 5,6,7,8-TETRAHYDRO[1]BENZOTHIENO[2,3-D]PYRIMIDIN-4(3H)-ONE DB07158, 5-ETHYL-3-METHYL-1,5-DIHYDRO-4H-PYRAZOLO[4,3-C]QUINOLIN-4-ONE DB08780, 6-MORPHOLIN-4-YL-9H-PURINE DB08778, [4-amino-2-(tert-butylamino)-1,3-thiazol-5-yl](phenyl)methanone DB06852, CHIR-124 DB06486, Enzastaurin DB12010, Fostamatinib DB08776, N-(4-OXO-5,6,7,8-TETRAHYDRO-4H-[1,3]THIAZOLO[5,4-C]AZEPIN-2-YL)ACETAMIDE DB07653, N-(5,6-DIPHENYLFURO[2,3-D]PYRIMIDIN-4-YL)GLYCINE DB06876, N-{5-[4-(4-METHYLPIPERAZIN-1-YL)PHENYL]-1H-PYRROLO[2,3-B]PYRIDIN-3-YL}NICOTINAMIDE DB08683, REL-(9R,12S)-9,10,11,12-TETRAHYDRO-9,12-EPOXY-1H-DIINDOLO[1,2,3-FG:3',2',1'-KL]PYRROLO[3,4-I][1,6]BENZODIAZOCINE-1,3(2H)-DIONE DB05149, XL844 |
DrugCentrali | O14757 |
GuidetoPHARMACOLOGYi | 1987 |
Genetic variation databases
BioMutai | CHEK1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000085848 | 1 – 476 | Serine/threonine-protein kinase Chk1Add BLAST | 476 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Cross-linki | 132 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication | ||
Modified residuei | 280 | PhosphoserineCombined sources | 1 | |
Modified residuei | 286 | PhosphoserineCombined sources | 1 | |
Modified residuei | 296 | PhosphoserineCombined sources1 Publication | 1 | |
Modified residuei | 301 | PhosphoserineCombined sources | 1 | |
Modified residuei | 317 | Phosphoserine; by ATM and ATR9 Publications | 1 | |
Modified residuei | 331 | PhosphoserineCombined sources | 1 | |
Modified residuei | 345 | Phosphoserine; by ATM and ATR13 Publications | 1 | |
Cross-linki | 436 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication | ||
Modified residuei | 467 | PhosphoserineCombined sources | 1 | |
Modified residuei | 468 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Keywords - PTMi
Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
CPTACi | CPTAC-3223 CPTAC-3282 CPTAC-922 |
EPDi | O14757 |
jPOSTi | O14757 |
MassIVEi | O14757 |
MaxQBi | O14757 |
PaxDbi | O14757 |
PeptideAtlasi | O14757 |
PRIDEi | O14757 |
ProteomicsDBi | 27577 48208 [O14757-1] 48209 [O14757-2] |
PTM databases
iPTMneti | O14757 |
MetOSitei | O14757 |
PhosphoSitePlusi | O14757 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000149554, Expressed in secondary oocyte and 169 other tissues |
ExpressionAtlasi | O14757, baseline and differential |
Genevisiblei | O14757, HS |
Organism-specific databases
HPAi | ENSG00000149554, Tissue enhanced (bone marrow, lymphoid tissue, seminal vesicle) |
Interactioni
Subunit structurei
Interacts (phosphorylated by ATR) with RAD51 (PubMed:15665856).
Interacts with and phosphorylates CLSPN, an adapter protein that regulates the ATR-dependent phosphorylation of CHEK1 (PubMed:16963448).
Interacts with BRCA1 (PubMed:11836499).
Interacts with and phosphorylates CDC25A, CDC25B and CDC25C (PubMed:9278511).
Interacts with FBXO6, which regulates CHEK1 (PubMed:19716789).
Interacts with PPM1D, which regulates CHEK1 through dephosphorylation (PubMed:15870257).
Interacts with TIMELESS; DNA damage-dependent (PubMed:15798197).
Interacts with FEM1B; activates CHEK1 in response to stress (PubMed:19330022).
Interacts with TLK1 (PubMed:12660173).
Interacts with XPO1 and YWHAZ (PubMed:12676962).
Interacts with CDK5RAP3; antagonizes CHEK1 (PubMed:19223857).
13 PublicationsIsoform 1 associates with isoform 2, the interaction is disrupted upon phosphorylation by ATR.
1 PublicationBinary interactionsi
O14757
GO - Molecular functioni
- protein domain specific binding Source: CAFA
Protein-protein interaction databases
BioGRIDi | 107536, 196 interactors |
CORUMi | O14757 |
DIPi | DIP-24182N |
ELMi | O14757 |
IntActi | O14757, 55 interactors |
MINTi | O14757 |
STRINGi | 9606.ENSP00000388648 |
Chemistry databases
BindingDBi | O14757 |
Miscellaneous databases
RNActi | O14757, protein |
Structurei
Secondary structure
3D structure databases
SMRi | O14757 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | O14757 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 9 – 265 | Protein kinasePROSITE-ProRule annotationAdd BLAST | 257 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 265 | Interaction with CLSPNBy similarityAdd BLAST | 265 | |
Regioni | 270 – 327 | DisorderedSequence analysisAdd BLAST | 58 | |
Regioni | 391 – 476 | Autoinhibitory regionAdd BLAST | 86 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 281 – 327 | Polar residuesSequence analysisAdd BLAST | 47 |
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0590, Eukaryota |
GeneTreei | ENSGT00940000159682 |
InParanoidi | O14757 |
OMAi | HVEYIFL |
PhylomeDBi | O14757 |
TreeFami | TF351441 |
Family and domain databases
CDDi | cd14069, STKc_Chk1, 1 hit |
InterProi | View protein in InterPro IPR034670, Chk1_catalytic_dom IPR011009, Kinase-like_dom_sf IPR000719, Prot_kinase_dom IPR017441, Protein_kinase_ATP_BS IPR008271, Ser/Thr_kinase_AS |
Pfami | View protein in Pfam PF00069, Pkinase, 1 hit |
SMARTi | View protein in SMART SM00220, S_TKc, 1 hit |
SUPFAMi | SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in PROSITE PS00107, PROTEIN_KINASE_ATP, 1 hit PS50011, PROTEIN_KINASE_DOM, 1 hit PS00108, PROTEIN_KINASE_ST, 1 hit |
s (3+)i Sequence
Sequence statusi: Complete.
This entry describes 3 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 3 described isoforms and 7 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MAVPFVEDWD LVQTLGEGAY GEVQLAVNRV TEEAVAVKIV DMKRAVDCPE
60 70 80 90 100
NIKKEICINK MLNHENVVKF YGHRREGNIQ YLFLEYCSGG ELFDRIEPDI
110 120 130 140 150
GMPEPDAQRF FHQLMAGVVY LHGIGITHRD IKPENLLLDE RDNLKISDFG
160 170 180 190 200
LATVFRYNNR ERLLNKMCGT LPYVAPELLK RREFHAEPVD VWSCGIVLTA
210 220 230 240 250
MLAGELPWDQ PSDSCQEYSD WKEKKTYLNP WKKIDSAPLA LLHKILVENP
260 270 280 290 300
SARITIPDIK KDRWYNKPLK KGAKRPRVTS GGVSESPSGF SKHIQSNLDF
310 320 330 340 350
SPVNSASSEE NVKYSSSQPE PRTGLSLWDT SPSYIDKLVQ GISFSQPTCP
360 370 380 390 400
DHMLLNSQLL GTPGSSQNPW QRLVKRMTRF FTKLDADKSY QCLKETCEKL
410 420 430 440 450
GYQWKKSCMN QVTISTTDRR NNKLIFKVNL LEMDDKILVD FRLSKGDGLE
460 470
FKRHFLKIKG KLIDIVSSQK IWLPAT
Computationally mapped potential isoform sequencesi
There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketE9PKQ3 | E9PKQ3_HUMAN | CHK1 checkpoint homolog | CHEK1 | 206 | Annotation score: | ||
E7EPP6 | E7EPP6_HUMAN | Serine/threonine-protein kinase Chk... | CHEK1 | 492 | Annotation score: | ||
E9PJI4 | E9PJI4_HUMAN | Serine/threonine-protein kinase Chk... | CHEK1 | 170 | Annotation score: | ||
E9PQW7 | E9PQW7_HUMAN | Serine/threonine-protein kinase Chk... | CHEK1 | 127 | Annotation score: | ||
A0A087WT52 | A0A087WT52_HUMAN | Serine/threonine-protein kinase Chk... | CHEK1 | 110 | Annotation score: | ||
E9PPA5 | E9PPA5_HUMAN | Serine/threonine-protein kinase Chk... | CHEK1 | 192 | Annotation score: | ||
E9PRU7 | E9PRU7_HUMAN | Serine/threonine-protein kinase Chk... | CHEK1 | 117 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 163 | L → S in BAG56691 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 220 | D → G in BAG61665 (PubMed:22184239).Curated | 1 | |
Sequence conflicti | 381 | F → L in BAG61665 (PubMed:22184239).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_021123 | 156 | R → Q1 PublicationCorresponds to variant dbSNP:rs3731410Ensembl. | 1 | |
Natural variantiVAR_040407 | 223 | E → V1 PublicationCorresponds to variant dbSNP:rs35817404Ensembl. | 1 | |
Natural variantiVAR_040408 | 312 | V → M1 PublicationCorresponds to variant dbSNP:rs34097480Ensembl. | 1 | |
Natural variantiVAR_024571 | 471 | I → V8 PublicationsCorresponds to variant dbSNP:rs506504EnsemblClinVar. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_044008 | 1 – 94 | Missing in isoform 2. 2 PublicationsAdd BLAST | 94 | |
Alternative sequenceiVSP_044009 | 95 – 97 | RIE → MEK in isoform 2. 2 Publications | 3 | |
Alternative sequenceiVSP_045075 | 412 – 445 | Missing in isoform 3. 1 PublicationAdd BLAST | 34 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF016582 mRNA Translation: AAC51736.1 AF032874 mRNA Translation: AAB88852.1 AB032387 Genomic DNA Translation: BAA84577.1 JF289264 mRNA Translation: AEB71796.1 AK292549 mRNA Translation: BAF85238.1 AK293143 mRNA Translation: BAG56691.1 AK299783 mRNA Translation: BAG61665.1 AF527555 Genomic DNA Translation: AAM78553.1 AB451222 mRNA Translation: BAG70036.1 AB451345 mRNA Translation: BAG70159.1 AP001132 Genomic DNA No translation available. CH471065 Genomic DNA Translation: EAW67644.1 BC004202 mRNA Translation: AAH04202.1 BC017575 mRNA Translation: AAH17575.1 |
CCDSi | CCDS58191.1 [O14757-3] CCDS81645.1 [O14757-2] CCDS8459.1 [O14757-1] |
RefSeqi | NP_001107593.1, NM_001114121.2 [O14757-1] NP_001107594.1, NM_001114122.2 [O14757-1] NP_001231775.1, NM_001244846.1 [O14757-3] NP_001265.2, NM_001274.5 [O14757-1] NP_001317357.1, NM_001330428.1 [O14757-2] XP_016872635.1, XM_017017146.1 [O14757-1] |
Genome annotation databases
Ensembli | ENST00000278916; ENSP00000278916; ENSG00000149554 [O14757-3] ENST00000428830; ENSP00000412504; ENSG00000149554 ENST00000438015; ENSP00000388648; ENSG00000149554 ENST00000524737; ENSP00000432890; ENSG00000149554 ENST00000532449; ENSP00000481616; ENSG00000149554 ENST00000534070; ENSP00000435371; ENSG00000149554 ENST00000544373; ENSP00000442317; ENSG00000149554 [O14757-2] |
GeneIDi | 1111 |
KEGGi | hsa:1111 |
MANE-Selecti | ENST00000438015.7; ENSP00000388648.1; NM_001114122.3; NP_001107594.1 |
UCSCi | uc001qcf.5, human [O14757-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Web resourcesi
NIEHS-SNPs |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF016582 mRNA Translation: AAC51736.1 AF032874 mRNA Translation: AAB88852.1 AB032387 Genomic DNA Translation: BAA84577.1 JF289264 mRNA Translation: AEB71796.1 AK292549 mRNA Translation: BAF85238.1 AK293143 mRNA Translation: BAG56691.1 AK299783 mRNA Translation: BAG61665.1 AF527555 Genomic DNA Translation: AAM78553.1 AB451222 mRNA Translation: BAG70036.1 AB451345 mRNA Translation: BAG70159.1 AP001132 Genomic DNA No translation available. CH471065 Genomic DNA Translation: EAW67644.1 BC004202 mRNA Translation: AAH04202.1 BC017575 mRNA Translation: AAH17575.1 |
CCDSi | CCDS58191.1 [O14757-3] CCDS81645.1 [O14757-2] CCDS8459.1 [O14757-1] |
RefSeqi | NP_001107593.1, NM_001114121.2 [O14757-1] NP_001107594.1, NM_001114122.2 [O14757-1] NP_001231775.1, NM_001244846.1 [O14757-3] NP_001265.2, NM_001274.5 [O14757-1] NP_001317357.1, NM_001330428.1 [O14757-2] XP_016872635.1, XM_017017146.1 [O14757-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
2YDI | X-ray | 1.60 | A | 1-289 | [»] | |
2YDJ | X-ray | 1.85 | A/B | 1-276 | [»] | |
2YDK | X-ray | 1.90 | A | 1-276 | [»] | |
2YER | X-ray | 1.83 | A | 1-276 | [»] | |
2YEX | X-ray | 1.30 | A | 1-276 | [»] | |
2YM3 | X-ray | 2.01 | A | 1-289 | [»] | |
2YM4 | X-ray | 2.35 | A | 1-289 | [»] | |
2YM5 | X-ray | 2.03 | A | 1-289 | [»] | |
2YM6 | X-ray | 2.01 | A | 1-289 | [»] | |
2YM7 | X-ray | 1.81 | A | 1-289 | [»] | |
2YM8 | X-ray | 2.07 | 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 | [»] | |
3TKH | X-ray | 1.79 | A | 1-307 | [»] | |
3TKI | X-ray | 1.60 | A | 1-307 | [»] | |
3U9N | X-ray | 1.85 | A | 2-274 | [»] | |
4FSM | X-ray | 2.30 | A | 2-280 | [»] | |
4FSN | X-ray | 2.10 | A | 4-280 | [»] | |
4FSQ | X-ray | 2.40 | A | 2-280 | [»] | |
4FSR | X-ray | 2.50 | A | 2-280 | [»] | |
4FST | X-ray | 1.90 | A | 2-270 | [»] | |
4FSU | X-ray | 2.10 | A | 2-280 | [»] | |
4FSW | X-ray | 2.30 | A | 2-280 | [»] | |
4FSY | X-ray | 2.30 | A | 2-280 | [»] | |
4FSZ | X-ray | 2.30 | A | 2-280 | [»] | |
4FT0 | X-ray | 2.30 | A | 2-280 | [»] | |
4FT3 | X-ray | 2.50 | A | 2-280 | [»] | |
4FT5 | X-ray | 2.40 | A | 2-280 | [»] | |
4FT7 | X-ray | 2.20 | A | 2-280 | [»] | |
4FT9 | X-ray | 2.20 | A | 2-280 | [»] | |
4FTA | X-ray | 2.40 | A | 2-280 | [»] | |
4FTC | X-ray | 2.00 | A | 2-280 | [»] | |
4FTI | X-ray | 2.20 | A | 2-280 | [»] | |
4FTJ | X-ray | 2.20 | A | 2-280 | [»] | |
4FTK | X-ray | 2.30 | A | 2-280 | [»] | |
4FTL | X-ray | 2.50 | A | 2-280 | [»] | |
4FTM | X-ray | 1.90 | A | 2-280 | [»] | |
4FTN | X-ray | 2.02 | A | 2-280 | [»] | |
4FTO | X-ray | 2.10 | A | 2-280 | [»] | |
4FTQ | X-ray | 2.00 | A | 2-280 | [»] | |
4FTR | X-ray | 2.25 | A | 2-280 | [»] | |
4FTT | X-ray | 2.30 | A | 2-280 | [»] | |
4FTU | X-ray | 2.10 | A | 2-280 | [»] | |
4GH2 | X-ray | 2.03 | A | 2-280 | [»] | |
4HYH | X-ray | 1.70 | A | 1-289 | [»] | |
4HYI | X-ray | 1.40 | A | 1-289 | [»] | |
4JIK | X-ray | 1.90 | A | 2-274 | [»] | |
4QYE | X-ray | 2.05 | A | 1-289 | [»] | |
4QYF | X-ray | 2.15 | A | 1-289 | [»] | |
4QYG | X-ray | 1.75 | A/B | 1-289 | [»] | |
4QYH | X-ray | 1.90 | A/B | 1-289 | [»] | |
4RVK | X-ray | 1.85 | A | 1-289 | [»] | |
4RVL | X-ray | 1.85 | A | 1-289 | [»] | |
4RVM | X-ray | 1.86 | A | 1-289 | [»] | |
5DLS | X-ray | 2.15 | A | 1-289 | [»] | |
5F4N | X-ray | 1.91 | A | 1-273 | [»] | |
5OOP | X-ray | 1.70 | A | 1-289 | [»] | |
5OOR | X-ray | 1.90 | A | 1-289 | [»] | |
5OOT | X-ray | 2.10 | A | 1-289 | [»] | |
5OP2 | X-ray | 1.90 | A | 1-289 | [»] | |
5OP4 | X-ray | 2.00 | A | 1-289 | [»] | |
5OP5 | X-ray | 1.90 | A | 1-289 | [»] | |
5OP7 | X-ray | 1.80 | A | 1-289 | [»] | |
5OPB | X-ray | 1.55 | A | 1-289 | [»] | |
5OPR | X-ray | 1.95 | A | 1-289 | [»] | |
5OPS | X-ray | 2.00 | A | 1-289 | [»] | |
5OPU | X-ray | 1.55 | A | 1-289 | [»] | |
5OPV | X-ray | 1.90 | A | 1-289 | [»] | |
5OQ5 | X-ray | 1.40 | A | 1-289 | [»] | |
5OQ6 | X-ray | 1.95 | A | 1-289 | [»] | |
5OQ7 | X-ray | 2.10 | A/B | 1-289 | [»] | |
5OQ8 | X-ray | 2.00 | A | 1-289 | [»] | |
5WI2 | X-ray | 2.50 | A/B | 377-476 | [»] | |
6FC8 | X-ray | 1.61 | A | 1-276 | [»] | |
6FCF | X-ray | 1.85 | A | 1-276 | [»] | |
6FCK | X-ray | 1.90 | A | 1-276 | [»] | |
7AKM | X-ray | 1.93 | A/B | 2-287 | [»] | |
7AKO | X-ray | 1.80 | A/B | 2-289 | [»] | |
7BJD | X-ray | 2.00 | A | 1-289 | [»] | |
7BJE | X-ray | 1.80 | A | 1-289 | [»] | |
7BJH | X-ray | 1.80 | A | 1-289 | [»] | |
7BJJ | X-ray | 1.80 | A | 1-289 | [»] | |
7BJM | X-ray | 2.30 | A | 1-289 | [»] | |
7BJO | X-ray | 2.30 | A | 1-289 | [»] | |
7BJR | X-ray | 1.90 | A | 1-289 | [»] | |
7BJX | X-ray | 2.40 | A/B | 1-289 | [»] | |
7BK1 | X-ray | 2.00 | A | 1-289 | [»] | |
7BK2 | X-ray | 2.00 | A | 1-289 | [»] | |
7BK3 | X-ray | 2.00 | A | 1-289 | [»] | |
7BKN | X-ray | 2.74 | A | 1-289 | [»] | |
7BKO | X-ray | 2.30 | A | 1-289 | [»] | |
7MCK | X-ray | 1.65 | A | 1-289 | [»] | |
SMRi | O14757 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 107536, 196 interactors |
CORUMi | O14757 |
DIPi | DIP-24182N |
ELMi | O14757 |
IntActi | O14757, 55 interactors |
MINTi | O14757 |
STRINGi | 9606.ENSP00000388648 |
Chemistry databases
BindingDBi | O14757 |
ChEMBLi | CHEMBL4630 |
DrugBanki | DB07647, (2R)-1-[(5,6-DIPHENYL-7H-PYRROLO[2,3-D]PYRIMIDIN-4-YL)AMINO]PROPAN-2-OL DB07648, (2R)-3-{[(4Z)-5,6-DIPHENYL-6,7-DIHYDRO-4H-PYRROLO[2,3-D]PYRIMIDIN-4-YLIDENE]AMINO}PROPANE-1,2-DIOL DB07037, (2S)-1-AMINO-3-[(5-NITROQUINOLIN-8-YL)AMINO]PROPAN-2-OL DB07243, (3-ENDO)-8-METHYL-8-AZABICYCLO[3.2.1]OCT-3-YL 1H-PYRROLO[2,3-B]PYRIDINE-3-CARBOXYLATE DB07078, (3Z)-6-(4-HYDROXY-3-METHOXYPHENYL)-3-(1H-PYRROL-2-YLMETHYLENE)-1,3-DIHYDRO-2H-INDOL-2-ONE DB07654, (5,6-DIPHENYL-FURO[2,3-D]PYRIMIDIN-4-YLAMINO)-ACETIC DB07213, (5-{3-[5-(PIPERIDIN-1-YLMETHYL)-1H-INDOL-2-YL]-1H-INDAZOL-6-YL}-2H-1,2,3-TRIAZOL-4-YL)METHANOL DB07314, 1-(5-CHLORO-2,4-DIMETHOXYPHENYL)-3-(5-CYANOPYRAZIN-2-YL)UREA DB07228, 1-(5-CHLORO-2-METHOXYPHENYL)-3-{6-[2-(DIMETHYLAMINO)-1-METHYLETHOXY]PYRAZIN-2-YL}UREA DB08781, 1-[(2S)-4-(5-BROMO-1H-PYRAZOLO[3,4-B]PYRIDIN-4-YL)MORPHOLIN-2-YL]METHANAMINE DB08774, 1-[(2S)-4-(5-phenyl-1H-pyrazolo[3,4-b]pyridin-4-yl)morpholin-2-yl]methanamine DB07311, 18-CHLORO-11,12,13,14-TETRAHYDRO-1H,10H-8,4-(AZENO)-9,15,1,3,6-BENZODIOXATRIAZACYCLOHEPTADECIN-2-ONE DB07034, 2,2'-{[9-(HYDROXYIMINO)-9H-FLUORENE-2,7-DIYL]BIS(OXY)}DIACETIC ACID DB07038, 2-(cyclohexylamino)benzoic acid DB08779, 2-(methylsulfanyl)-5-(thiophen-2-ylmethyl)-1H-imidazol-4-ol DB08393, 2-[(5,6-DIPHENYLFURO[2,3-D]PYRIMIDIN-4-YL)AMINO]ETHANOL DB08392, 2-[5,6-BIS-(4-METHOXY-PHENYL)-FURO[2,3-D]PYRIMIDIN-4-YLAMINO]-ETHANOL DB07959, 3-(1H-BENZIMIDAZOL-2-YL)-1H-INDAZOLE DB07075, 3-(5-{[4-(AMINOMETHYL)PIPERIDIN-1-YL]METHYL}-1H-INDOL-2-YL)-1H-INDAZOLE-6-CARBONITRILE DB07025, 3-(5-{[4-(AMINOMETHYL)PIPERIDIN-1-YL]METHYL}-1H-INDOL-2-YL)QUINOLIN-2(1H)-ONE DB07655, 3-AMINO-3-BENZYL-[4.3.0]BICYCLO-1,6-DIAZANONAN-2-ONE DB07320, 4-(6-{[(4-METHYLCYCLOHEXYL)AMINO]METHYL}-1,4-DIHYDROINDENO[1,2-C]PYRAZOL-3-YL)BENZOIC ACID DB07336, 4-[3-(1H-BENZIMIDAZOL-2-YL)-1H-INDAZOL-6-YL]-2-METHOXYPHENOL DB08777, 5,6,7,8-TETRAHYDRO[1]BENZOTHIENO[2,3-D]PYRIMIDIN-4(3H)-ONE DB07158, 5-ETHYL-3-METHYL-1,5-DIHYDRO-4H-PYRAZOLO[4,3-C]QUINOLIN-4-ONE DB08780, 6-MORPHOLIN-4-YL-9H-PURINE DB08778, [4-amino-2-(tert-butylamino)-1,3-thiazol-5-yl](phenyl)methanone DB06852, CHIR-124 DB06486, Enzastaurin DB12010, Fostamatinib DB08776, N-(4-OXO-5,6,7,8-TETRAHYDRO-4H-[1,3]THIAZOLO[5,4-C]AZEPIN-2-YL)ACETAMIDE DB07653, N-(5,6-DIPHENYLFURO[2,3-D]PYRIMIDIN-4-YL)GLYCINE DB06876, N-{5-[4-(4-METHYLPIPERAZIN-1-YL)PHENYL]-1H-PYRROLO[2,3-B]PYRIDIN-3-YL}NICOTINAMIDE DB08683, REL-(9R,12S)-9,10,11,12-TETRAHYDRO-9,12-EPOXY-1H-DIINDOLO[1,2,3-FG:3',2',1'-KL]PYRROLO[3,4-I][1,6]BENZODIAZOCINE-1,3(2H)-DIONE DB05149, XL844 |
DrugCentrali | O14757 |
GuidetoPHARMACOLOGYi | 1987 |
PTM databases
iPTMneti | O14757 |
MetOSitei | O14757 |
PhosphoSitePlusi | O14757 |
Genetic variation databases
BioMutai | CHEK1 |
Proteomic databases
CPTACi | CPTAC-3223 CPTAC-3282 CPTAC-922 |
EPDi | O14757 |
jPOSTi | O14757 |
MassIVEi | O14757 |
MaxQBi | O14757 |
PaxDbi | O14757 |
PeptideAtlasi | O14757 |
PRIDEi | O14757 |
ProteomicsDBi | 27577 48208 [O14757-1] 48209 [O14757-2] |
Protocols and materials databases
Antibodypediai | 3671, 1848 antibodies from 48 providers |
CPTCi | O14757, 6 antibodies |
DNASUi | 1111 |
Genome annotation databases
Organism-specific databases
CTDi | 1111 |
DisGeNETi | 1111 |
GeneCardsi | CHEK1 |
HGNCi | HGNC:1925, CHEK1 |
HPAi | ENSG00000149554, Tissue enhanced (bone marrow, lymphoid tissue, seminal vesicle) |
MIMi | 603078, gene |
neXtProti | NX_O14757 |
OpenTargetsi | ENSG00000149554 |
PharmGKBi | PA110 |
VEuPathDBi | HostDB:ENSG00000149554 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0590, Eukaryota |
GeneTreei | ENSGT00940000159682 |
InParanoidi | O14757 |
OMAi | HVEYIFL |
PhylomeDBi | O14757 |
TreeFami | TF351441 |
Enzyme and pathway databases
BRENDAi | 2.7.11.1, 2681 |
PathwayCommonsi | O14757 |
Reactomei | R-HSA-1433557, Signaling by SCF-KIT R-HSA-176187, Activation of ATR in response to replication stress R-HSA-5693607, Processing of DNA double-strand break ends R-HSA-5693616, Presynaptic phase of homologous DNA pairing and strand exchange R-HSA-6796648, TP53 Regulates Transcription of DNA Repair Genes R-HSA-6804756, Regulation of TP53 Activity through Phosphorylation R-HSA-69473, G2/M DNA damage checkpoint R-HSA-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A R-HSA-75035, Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex R-HSA-8953750, Transcriptional Regulation by E2F6 |
SignaLinki | O14757 |
SIGNORi | O14757 |
Miscellaneous databases
BioGRID-ORCSi | 1111, 826 hits in 1082 CRISPR screens |
ChiTaRSi | CHEK1, human |
EvolutionaryTracei | O14757 |
GeneWikii | CHEK1 |
GenomeRNAii | 1111 |
Pharosi | O14757, Tchem |
PROi | PR:O14757 |
RNActi | O14757, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000149554, Expressed in secondary oocyte and 169 other tissues |
ExpressionAtlasi | O14757, baseline and differential |
Genevisiblei | O14757, HS |
Family and domain databases
CDDi | cd14069, STKc_Chk1, 1 hit |
InterProi | View protein in InterPro IPR034670, Chk1_catalytic_dom IPR011009, Kinase-like_dom_sf IPR000719, Prot_kinase_dom IPR017441, Protein_kinase_ATP_BS IPR008271, Ser/Thr_kinase_AS |
Pfami | View protein in Pfam PF00069, Pkinase, 1 hit |
SMARTi | View protein in SMART SM00220, S_TKc, 1 hit |
SUPFAMi | SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in PROSITE PS00107, PROTEIN_KINASE_ATP, 1 hit PS50011, PROTEIN_KINASE_DOM, 1 hit PS00108, PROTEIN_KINASE_ST, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CHK1_HUMAN | |
Accessioni | O14757Primary (citable) accession number: O14757 Secondary accession number(s): A8K934 H2BI51 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 30, 2000 |
Last sequence update: | January 11, 2011 | |
Last modified: | February 23, 2022 | |
This is version 236 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | 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. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human and mouse protein kinases
Human and mouse protein kinases: classification and index - Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families