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. 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.

Isoform 2: Endogenous repressor of isoform 1, interacts with, and antagonizes CHK1 to promote the S to G2/M phase transition.

Catalytic activityⁱ

ATP + a protein = ADP + a phosphoprotein.

Activity regulationⁱ

Activated through phosphorylation predominantly by ATR but also by ATM in response to DNA damage or inhibition of DNA replication. Activation is modulated by several mediators including CLSPN, BRCA1 and FEM1B.

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
Inferred from direct assayⁱ
- 18243098
kinase activity Source: Reactome
protein domain specific binding
Source: CAFA
Inferred from physical interactionⁱ
- 26296656
protein kinase activity
Source: CACAO
Inferred from mutant phenotypeⁱ
- 22024163
protein serine/threonine kinase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 16963448

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

apoptotic process
Source: UniProtKB
Inferred from direct assayⁱ
- 23028632
cell cycle Source: UniProtKB-KW
cellular response to DNA damage stimulus
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 20932473
cellular response to mechanical stimulus
Source: UniProtKB
Inferred from expression patternⁱ
- 19593445
chromatin-mediated maintenance of transcription Source: UniProtKB
DNA damage checkpoint
Source: UniProtKB
Inferred from direct assayⁱ
- 16963448
DNA damage induced protein phosphorylation
Source: UniProtKB
Inferred from direct assayⁱ
- 16963448
DNA repair
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 19716789
DNA replication Source: Reactome
intracellular signal transduction
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
negative regulation of G0 to G1 transition Source: Reactome
negative regulation of mitotic nuclear division
Source: UniProtKB
Inferred from direct assayⁱ
- 15311285
peptidyl-threonine phosphorylation
Source: UniProtKB
Inferred from direct assayⁱ
- 15665856
positive regulation of cell cycle
Source: CAFA
Inferred from direct assayⁱ
- 26296656
protein phosphorylation
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
regulation of double-strand break repair via homologous recombination
Source: UniProtKB
Inferred from direct assayⁱ
- 15665856
regulation of histone H3-K9 acetylation Source: UniProtKB
regulation of mitotic centrosome separation
Source: UniProtKB
Inferred from direct assayⁱ
- 15311285
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
Non-traceable author statementⁱ
- 15149599
signal transduction involved in G2 DNA damage checkpoint
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 20932473

View the complete GO annotation on QuickGO ...

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
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:2.7.11.1) 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	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 11

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000149554.12
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:1925 CHEK1
MIMⁱ	603078 gene
neXtProtⁱ	NX_O14757

Keywords - Cellular componentⁱ

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	38	K → R: Abolishes kinase activity. 2 Publications	1
Mutagenesisⁱ	130	D → A: Abolishes kinase activity. 8 Publications	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

DisGeNET More...DisGeNETⁱ	1111
Open Targets More...OpenTargetsⁱ	ENSG00000149554
PharmGKBⁱ	PA110

Chemistry databases

ChEMBLⁱ	CHEMBL4630
Drug and drug target database More...DrugBankⁱ	DB07037 (2S)-1-AMINO-3-[(5-NITROQUINOLIN-8-YL)AMINO]PROPAN-2-OL DB07228 1-(5-CHLORO-2-METHOXYPHENYL)-3-{6-[2-(DIMETHYLAMINO)-1-METHYLETHOXY]PYRAZIN-2-YL}UREA DB07038 2-(cyclohexylamino)benzoic acid DB08779 2-(methylsulfanyl)-5-(thiophen-2-ylmethyl)-1H-imidazol-4-ol 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 DB06852 4-[(3S)-1-AZABICYCLO[2.2.2]OCT-3-YLAMINO]-3-(1H-BENZIMIDAZOL-2-YL)-6-CHLOROQUINOLIN-2(1H)-ONE DB07336 4-[3-(1H-BENZIMIDAZOL-2-YL)-1H-INDAZOL-6-YL]-2-METHOXYPHENOL DB08780 6-MORPHOLIN-4-YL-9H-PURINE DB05149 XL844
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	1987

Polymorphism and mutation databases

BioMutaⁱ	CHEK1

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	Length
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 ATR12 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

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.15 Publications

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.By similarity12 Publications

Keywords - PTMⁱ

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	O14757
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	O14757
PaxDbⁱ	O14757
PeptideAtlas More...PeptideAtlasⁱ	O14757
PRIDEⁱ	O14757
ProteomicsDBⁱ	48208 48209 [O14757-2]

PTM databases

iPTMnetⁱ	O14757
PhosphoSitePlusⁱ	O14757

Expressionⁱ

Tissue specificityⁱ

Expressed ubiquitously with the most abundant expression in thymus, testis, small intestine and colon.2 Publications

Gene expression databases

Bgeeⁱ	ENSG00000149554 Expressed in 152 organ(s), highest expression level in secondary oocyte
CleanExⁱ	HS_CHEK1
ExpressionAtlasⁱ	O14757 baseline and differential
Genevisibleⁱ	O14757 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA044364

HPAⁱ

HPA044364

Interactionⁱ

Subunit structureⁱ

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. Isoform 1 associates with isoform 2, the interaction is disrupted upon phosphorylation by ATR. Interacts with CDK5RAP3; antagonizes CHEK1 (PubMed:19223857).12 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
BRCA1	P38398	3	EBI-974488,EBI-349905
CDC25C	P30307	2	EBI-974488,EBI-974439
CLSPN	Q9HAW4	5	EBI-974488,EBI-1369377
ERRFI1	Q9UJM3	2	EBI-974488,EBI-2941912
HSP90AB1	P08238	3	EBI-974488,EBI-352572
MEN1	O00255	2	EBI-974488,EBI-592789
RAD51	Q06609	3	EBI-974488,EBI-297202
RB1	P06400	3	EBI-974488,EBI-491274
SMURF1	Q9HCE7-2	4	EBI-974488,EBI-9845742
TIMELESS	Q9UNS1	2	EBI-974488,EBI-2212315
YWHAG	P61981	7	EBI-974488,EBI-359832

GO - Molecular functionⁱ

protein domain specific binding
Source: CAFA
Inferred from physical interactionⁱ
- 26296656

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	107536, 159 interactors
CORUMⁱ	O14757
Database of interacting proteins More...DIPⁱ	DIP-24182N
ELMⁱ	O14757
IntActⁱ	O14757, 37 interactors
Molecular INTeraction database More...MINTⁱ	O14757
STRINGⁱ	9606.ENSP00000388648

Chemistry databases

BindingDBⁱ

O14757

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	3 – 8	Combined sources	6
Beta strandⁱ	9 – 17	Combined sources	9
Beta strandⁱ	19 – 28	Combined sources	10
Turnⁱ	29 – 31	Combined sources	3
Beta strandⁱ	34 – 41	Combined sources	8
Helixⁱ	42 – 44	Combined sources	3
Helixⁱ	48 – 60	Combined sources	13
Beta strandⁱ	70 – 76	Combined sources	7
Beta strandⁱ	79 – 85	Combined sources	7
Beta strandⁱ	88 – 91	Combined sources	4
Helixⁱ	92 – 95	Combined sources	4
Turnⁱ	98 – 100	Combined sources	3
Helixⁱ	104 – 123	Combined sources	20
Beta strandⁱ	125 – 127	Combined sources	3
Helixⁱ	133 – 135	Combined sources	3
Beta strandⁱ	136 – 138	Combined sources	3
Beta strandⁱ	144 – 146	Combined sources	3
Helixⁱ	149 – 151	Combined sources	3
Beta strandⁱ	153 – 157	Combined sources	5
Helixⁱ	171 – 173	Combined sources	3
Helixⁱ	176 – 179	Combined sources	4
Beta strandⁱ	182 – 184	Combined sources	3
Helixⁱ	186 – 203	Combined sources	18
Beta strandⁱ	209 – 211	Combined sources	3
Beta strandⁱ	213 – 215	Combined sources	3
Helixⁱ	216 – 222	Combined sources	7
Beta strandⁱ	227 – 229	Combined sources	3
Helixⁱ	231 – 233	Combined sources	3
Helixⁱ	236 – 245	Combined sources	10
Turnⁱ	250 – 252	Combined sources	3
Helixⁱ	256 – 259	Combined sources	4
Turnⁱ	263 – 266	Combined sources	4
Beta strandⁱ	379 – 384	Combined sources	6
Helixⁱ	386 – 399	Combined sources	14
Beta strandⁱ	403 – 417	Combined sources	15
Beta strandⁱ	423 – 432	Combined sources	10
Beta strandⁱ	434 – 446	Combined sources	13
Helixⁱ	448 – 461	Combined sources	14
Helixⁱ	463 – 465	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	O14757
SMRⁱ	O14757
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	O14757

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	391 – 476	Autoinhibitory regionAdd BLAST		86

Domainⁱ

The autoinhibitory region (AIR) inhibits the activity of the kinase domain.1 Publication

Sequence similaritiesⁱ

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. NIM1 subfamily.Curated

Phylogenomic databases

eggNOGⁱ	KOG0590 Eukaryota ENOG410XQ0D LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00680000099954
HOGENOMⁱ	HOG000216658
HOVERGENⁱ	HBG002590
InParanoidⁱ	O14757
KEGG Orthology (KO) More...KOⁱ	K02216
OMAⁱ	NRQTEEA
PhylomeDBⁱ	O14757
TreeFamⁱ	TF351441

Family and domain databases

Conserved Domains Database More...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
Pfam protein domain database More...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

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 3 described isoforms and 10 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: O14757-1) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
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

Length:476

Mass (Da):54,434

Last modified:January 11, 2011 - v2

Checksum:ⁱ0ABD0FAB67E60F67

GO

Isoform 2 (identifier: O14757-2) [UniParc]FASTA Add to basket

Also known as: Chk1-short, Chk1-S

The sequence of this isoform differs from the canonical sequence as follows:
1-94: Missing.
95-97: RIE → MEK

« Hide

        10         20         30         40         50
MEKPDIGMPE PDAQRFFHQL MAGVVYLHGI GITHRDIKPE NLLLDERDNL 
        60         70         80         90        100
KISDFGLATV FRYNNRERLL NKMCGTLPYV APELLKRREF HAEPVDVWSC 
       110        120        130        140        150
GIVLTAMLAG ELPWDQPSDS CQEYSDWKEK KTYLNPWKKI DSAPLALLHK 
       160        170        180        190        200
ILVENPSARI TIPDIKKDRW YNKPLKKGAK RPRVTSGGVS ESPSGFSKHI 
       210        220        230        240        250
QSNLDFSPVN SASSEENVKY SSSQPEPRTG LSLWDTSPSY IDKLVQGISF 
       260        270        280        290        300
SQPTCPDHML LNSQLLGTPG SSQNPWQRLV KRMTRFFTKL DADKSYQCLK 
       310        320        330        340        350
ETCEKLGYQW KKSCMNQVTI STTDRRNNKL IFKVNLLEMD DKILVDFRLS 
       360        370        380 
KGDGLEFKRH FLKIKGKLID IVSSQKIWLP AT

Show »

Length:382

Mass (Da):43,703

Checksum:ⁱ3ECD01BEC168F007

GO

Isoform 3 (identifier: O14757-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
412-445: Missing.

« Hide

        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 
GYQWKKSCMN QGDGLEFKRH FLKIKGKLID IVSSQKIWLP AT

Note: No experimental confirmation available.

Show »

Length:442

Mass (Da):50,415

Checksum:ⁱ05680C63BD1287B6

GO

Computationally mapped potential isoform sequencesⁱ

There are 10 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

E7EPP6	E7EPP6_HUMAN	Serine/threonine-protein kinase Chk... Serine/threonine-protein kinase Chk1	CHEK1	492	Annotation score:
J3KN87	J3KN87_HUMAN	Serine/threonine-protein kinase Chk... Serine/threonine-protein kinase Chk1	CHEK1	432	Annotation score:
E9PKQ3	E9PKQ3_HUMAN	Serine/threonine-protein kinase Chk... Serine/threonine-protein kinase Chk1	CHEK1	204	Annotation score:
E9PJI4	E9PJI4_HUMAN	Serine/threonine-protein kinase Chk... Serine/threonine-protein kinase Chk1	CHEK1	170	Annotation score:
E9PPA5	E9PPA5_HUMAN	Serine/threonine-protein kinase Chk... Serine/threonine-protein kinase Chk1	CHEK1	192	Annotation score:
E9PQW7	E9PQW7_HUMAN	Serine/threonine-protein kinase Chk... Serine/threonine-protein kinase Chk1	CHEK1	127	Annotation score:
E9PM65	E9PM65_HUMAN	Serine/threonine-protein kinase Chk... Serine/threonine-protein kinase Chk1	CHEK1	42	Annotation score:
A0A087WT52	A0A087WT52_HUMAN	Serine/threonine-protein kinase Chk... Serine/threonine-protein kinase Chk1	CHEK1	110	Annotation score:
E9PRU7	E9PRU7_HUMAN	Serine/threonine-protein kinase Chk... Serine/threonine-protein kinase Chk1	CHEK1	117	Annotation score:
A0A087WY91	A0A087WY91_HUMAN	Serine/threonine-protein kinase Chk... Serine/threonine-protein kinase Chk1	CHEK1	89	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	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	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	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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS58191.1 [O14757-3] CCDS81645.1 [O14757-2] CCDS8459.1 [O14757-1]
NCBI Reference Sequences More...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]
UniGeneⁱ	Hs.24529 Hs.595920

Genome annotation databases

Ensemblⁱ	ENST00000428830; ENSP00000412504; ENSG00000149554 [O14757-1] ENST00000438015; ENSP00000388648; ENSG00000149554 [O14757-1] ENST00000524737; ENSP00000432890; ENSG00000149554 [O14757-1] ENST00000532449; ENSP00000481616; ENSG00000149554 [O14757-3] ENST00000534070; ENSP00000435371; ENSG00000149554 [O14757-1] ENST00000544373; ENSP00000442317; ENSG00000149554 [O14757-2]
GeneIDⁱ	1111
KEGGⁱ	hsa:1111
UCSC genome browser More...UCSCⁱ	uc001qcf.5 human [O14757-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
O14757	Serine/threonine-protein kinase Chk1		RAT		476	UniRef90_O14757
Serine/threonine-protein kinase Chk1		MOUSE		476
serine/threonine-protein kinase Chk1 isoform X1		URSMA		499
Uncharacterized protein (Fragment)		AILME		454
Uncharacterized protein		MACFA		488
+99
O14757-2	Serine/threonine-protein kinase Chk1		HUMAN		492	UniRef90_E7EPP6
Uncharacterized protein		MACMU		493
Uncharacterized protein		MACFA		382
Uncharacterized protein		CERAT		493
Uncharacterized protein		MACNE		493
+24
O14757-3	Serine/threonine-protein kinase Chk1 isoform 1		HETGA		476	UniRef90_O14757-3
Uncharacterized protein		Cebus capucinus imitator		442
Uncharacterized protein		COLAP		442
serine/threonine-protein kinase Chk1 isoform X2		ODORO		442
CHEK1 isoform 4		PANTR		442
+29

Protein	Similar proteins		Species	Score	Length	Source
O14757	Serine/threonine-protein kinase Chk1		RAT		476	UniRef50_O14757
Serine/threonine-protein kinase Chk1		MOUSE		476
serine/threonine-protein kinase Chk1 isoform X1		URSMA		499
Uncharacterized protein (Fragment)		AILME		454
Uncharacterized protein		MACFA		488
+214
O14757-3	Serine/threonine-protein kinase Chk1		XENLA		474	UniRef50_O14757-3
Serine/threonine-protein kinase Chk1 isoform 1		HETGA		476
Uncharacterized protein		MANLE		442
Uncharacterized protein		COLAP		442
Uncharacterized protein		RHIRO		442
+68

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]
UniGeneⁱ	Hs.24529 Hs.595920

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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	[»]
ProteinModelPortalⁱ	O14757
SMRⁱ	O14757
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	107536, 159 interactors
CORUMⁱ	O14757
DIPⁱ	DIP-24182N
ELMⁱ	O14757
IntActⁱ	O14757, 37 interactors
MINTⁱ	O14757
STRINGⁱ	9606.ENSP00000388648

Chemistry databases

BindingDBⁱ	O14757
ChEMBLⁱ	CHEMBL4630
DrugBankⁱ	DB07037 (2S)-1-AMINO-3-[(5-NITROQUINOLIN-8-YL)AMINO]PROPAN-2-OL DB07228 1-(5-CHLORO-2-METHOXYPHENYL)-3-{6-[2-(DIMETHYLAMINO)-1-METHYLETHOXY]PYRAZIN-2-YL}UREA DB07038 2-(cyclohexylamino)benzoic acid DB08779 2-(methylsulfanyl)-5-(thiophen-2-ylmethyl)-1H-imidazol-4-ol 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 DB06852 4-[(3S)-1-AZABICYCLO[2.2.2]OCT-3-YLAMINO]-3-(1H-BENZIMIDAZOL-2-YL)-6-CHLOROQUINOLIN-2(1H)-ONE DB07336 4-[3-(1H-BENZIMIDAZOL-2-YL)-1H-INDAZOL-6-YL]-2-METHOXYPHENOL DB08780 6-MORPHOLIN-4-YL-9H-PURINE DB05149 XL844
GuidetoPHARMACOLOGYⁱ	1987

PTM databases

iPTMnetⁱ	O14757
PhosphoSitePlusⁱ	O14757

Polymorphism and mutation databases

BioMutaⁱ	CHEK1

BioMutaⁱ

CHEK1

Proteomic databases

EPDⁱ	O14757
MaxQBⁱ	O14757
PaxDbⁱ	O14757
PeptideAtlasⁱ	O14757
PRIDEⁱ	O14757
ProteomicsDBⁱ	48208 48209 [O14757-2]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	1111
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000428830; ENSP00000412504; ENSG00000149554 [O14757-1] ENST00000438015; ENSP00000388648; ENSG00000149554 [O14757-1] ENST00000524737; ENSP00000432890; ENSG00000149554 [O14757-1] ENST00000532449; ENSP00000481616; ENSG00000149554 [O14757-3] ENST00000534070; ENSP00000435371; ENSG00000149554 [O14757-1] ENST00000544373; ENSP00000442317; ENSG00000149554 [O14757-2]
GeneIDⁱ	1111
KEGGⁱ	hsa:1111
UCSCⁱ	uc001qcf.5 human [O14757-1]

Organism-specific databases

CTDⁱ	1111
DisGeNETⁱ	1111
EuPathDBⁱ	HostDB:ENSG00000149554.12
GeneCardsⁱ	CHEK1
H-InvDBⁱ	HIX0201657
HGNCⁱ	HGNC:1925 CHEK1
HPAⁱ	HPA044364
MIMⁱ	603078 gene
neXtProtⁱ	NX_O14757
OpenTargetsⁱ	ENSG00000149554
PharmGKBⁱ	PA110
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0590 Eukaryota ENOG410XQ0D LUCA
GeneTreeⁱ	ENSGT00680000099954
HOGENOMⁱ	HOG000216658
HOVERGENⁱ	HBG002590
InParanoidⁱ	O14757
KOⁱ	K02216
OMAⁱ	NRQTEEA
PhylomeDBⁱ	O14757
TreeFamⁱ	TF351441

Enzyme and pathway databases

BRENDAⁱ	2.7.11.1 2681
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

ChiTaRSⁱ	CHEK1 human
EvolutionaryTraceⁱ	O14757
GeneWikiⁱ	CHEK1
GenomeRNAiⁱ	1111
Protein Ontology More...PROⁱ	PR:O14757
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000149554 Expressed in 152 organ(s), highest expression level in secondary oocyte
CleanExⁱ	HS_CHEK1
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
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CHK1_HUMAN
Accessionⁱ	O14757Primary (citable) accession number: O14757 Secondary accession number(s): A8K934 , B4DDD0, B4DSK3, B5BTY6, F5H7S4, H2BI51
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
	Last sequence update:	January 11, 2011
	Last modified:	November 7, 2018
	This is version 215 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, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
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
Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM
Human and mouse protein kinases
Human and mouse protein kinases: classification and index

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - O14757 (CHK1_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Serine/threonine-protein kinase Chk1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytoskeleton

Nucleus

Other locations

Cytoskeleton

Cytosol

Extracellular region or secreted

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ