Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - O14757 (CHK1_HUMAN)

Protein

Serine/threonine-protein kinase Chk1

Gene

CHEK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei38ATPPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei130Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi15 – 23ATPPROSITE-ProRule annotation9

<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

  • ATP binding Source: UniProtKB-KW
  • histone kinase activity (H3-T11 specific) Source: UniProtKB
  • kinase activity Source: Reactome
  • protein domain specific binding Source: CAFA
  • protein kinase activity Source: CACAO
  • protein serine/threonine kinase activity Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, DNA damage, DNA repair
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.11.1 2681

Reactome - a knowledgebase of biological pathways and processes

More...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

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		O14757

SIGNOR Signaling Network Open Resource

More...SIGNORi		O14757

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CHEK1
Synonyms:CHK1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000149554.12

Human Gene Nomenclature Database

More...HGNCi		HGNC:1925 CHEK1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		603078 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_O14757

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi38K → R: Abolishes kinase activity. 2 Publications1
Mutagenesisi130D → A: Abolishes kinase activity. 8 Publications1
Mutagenesisi317S → 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 Publications1
Mutagenesisi317S → E: Enhances interaction with RAD51; when associated with E-345. 5 Publications1
Mutagenesisi344F → A: Impairs nuclear export. 1 Publication1
Mutagenesisi345S → 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 Publications1
Mutagenesisi345S → E: Enhances interaction with RAD51; when associated with E-317. 6 Publications1
Mutagenesisi353M → A: Impairs nuclear export. 1 Publication1
Mutagenesisi357S → A: No effect on phosphorylation induced by hydroxyurea. 1 Publication1
Mutagenesisi366S → A: No effect on phosphorylation induced by hydroxyurea. 1 Publication1
Mutagenesisi372R → 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 Publication1
Mutagenesisi376R → 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 Publication1
Mutagenesisi379R → 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 Publication1
Mutagenesisi436K → R: Enhances stability of the protein, probably by preventing ubiquitination at this site. 1 Publication1
Mutagenesisi468S → A: No effect on phosphorylation induced by hydroxyurea. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		1111

Open Targets

More...OpenTargetsi		ENSG00000149554

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA110

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...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

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		CHEK1

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000858481 – 476Serine/threonine-protein kinase Chk1Add BLAST476

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei280PhosphoserineCombined sources1
Modified residuei286PhosphoserineCombined sources1
Modified residuei296PhosphoserineCombined sources1 Publication1
Modified residuei301PhosphoserineCombined sources1
Modified residuei317Phosphoserine; by ATM and ATR9 Publications1
Modified residuei331PhosphoserineCombined sources1
Modified residuei345Phosphoserine; by ATM and ATR12 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki436Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei467PhosphoserineCombined sources1
Modified residuei468PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...EPDi		O14757

MaxQB - The MaxQuant DataBase

More...MaxQBi		O14757

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		O14757

PeptideAtlas

More...PeptideAtlasi		O14757

PRoteomics IDEntifications database

More...PRIDEi		O14757

ProteomicsDB human proteome resource

More...ProteomicsDBi		48208
48209 [O14757-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O14757

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		O14757

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000149554 Expressed in 152 organ(s), highest expression level in secondary oocyte

CleanEx database of gene expression profiles

More...CleanExi		HS_CHEK1

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		O14757 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O14757 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA044364

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		107536, 159 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		O14757

Database of interacting proteins

More...DIPi		DIP-24182N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		O14757

Protein interaction database and analysis system

More...IntActi		O14757, 37 interactors

Molecular INTeraction database

More...MINTi		O14757

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000388648

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		O14757

<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

1476
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		O14757

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		O14757

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		O14757

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini9 – 265Protein kinasePROSITE-ProRule annotationAdd BLAST257

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 265Interaction with CLSPNBy similarityAdd BLAST265
Regioni391 – 476Autoinhibitory regionAdd BLAST86

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

<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

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0590 Eukaryota
ENOG410XQ0D LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000159682

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000216658

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG002590

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O14757

KEGG Orthology (KO)

More...KOi		K02216

Identification of Orthologs from Complete Genome Data

More...OMAi		NRQTEEA

Database for complete collections of gene phylogenies

More...PhylomeDBi		O14757

TreeFam database of animal gene trees

More...TreeFami		TF351441

Family and domain databases

Conserved Domains Database

More...CDDi		cd14069 STKc_Chk1, 1 hit

Integrated resource of protein families, domains and functional sites

More...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

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

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

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

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

« Hide
        10         20         30         40         50
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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0ABD0FAB67E60F67
GO
Isoform 2 (identifier: O14757-2) [UniParc]FASTAAdd 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

Show »
Length:382
Mass (Da):43,703
Checksum:i3ECD01BEC168F007
GO
Isoform 3 (identifier: O14757-3) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:442
Mass (Da):50,415
Checksum:i05680C63BD1287B6
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 10 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7EPP6E7EPP6_HUMAN
Serine/threonine-protein kinase Chk...
CHEK1
492Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3KN87J3KN87_HUMAN
Serine/threonine-protein kinase Chk...
CHEK1
432Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PKQ3E9PKQ3_HUMAN
Serine/threonine-protein kinase Chk...
CHEK1
204Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PJI4E9PJI4_HUMAN
Serine/threonine-protein kinase Chk...
CHEK1
170Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PQW7E9PQW7_HUMAN
Serine/threonine-protein kinase Chk...
CHEK1
127Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PPA5E9PPA5_HUMAN
Serine/threonine-protein kinase Chk...
CHEK1
192Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PM65E9PM65_HUMAN
Serine/threonine-protein kinase Chk...
CHEK1
42Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087WT52A0A087WT52_HUMAN
Serine/threonine-protein kinase Chk...
CHEK1
110Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087WY91A0A087WY91_HUMAN
Serine/threonine-protein kinase Chk...
CHEK1
89Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PRU7E9PRU7_HUMAN
Serine/threonine-protein kinase Chk...
CHEK1
117Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti163L → S in BAG56691 (PubMed:14702039).Curated1
Sequence conflicti220D → G in BAG61665 (PubMed:22184239).Curated1
Sequence conflicti381F → L in BAG61665 (PubMed:22184239).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_021123156R → Q1 PublicationCorresponds to variant dbSNP:rs3731410Ensembl.1
Natural variantiVAR_040407223E → V1 PublicationCorresponds to variant dbSNP:rs35817404Ensembl.1
Natural variantiVAR_040408312V → M1 PublicationCorresponds to variant dbSNP:rs34097480Ensembl.1
Natural variantiVAR_024571471I → V8 PublicationsCorresponds to variant dbSNP:rs506504EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0440081 – 94Missing in isoform 2. 2 PublicationsAdd BLAST94
Alternative sequenceiVSP_04400995 – 97RIE → MEK in isoform 2. 2 Publications3
Alternative sequenceiVSP_045075412 – 445Missing in isoform 3. 1 PublicationAdd BLAST34

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.24529
Hs.595920

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...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]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1111

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:1111

UCSC genome browser

More...UCSCi		uc001qcf.5 human [O14757-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

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
CCDSiCCDS58191.1 [O14757-3]
CCDS81645.1 [O14757-2]
CCDS8459.1 [O14757-1]
RefSeqiNP_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]
UniGeneiHs.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 entryMethodResolution (Å)ChainPositionsPDBsum
1IA8X-ray1.70A1-289[»]
1NVQX-ray2.00A1-289[»]
1NVRX-ray1.80A1-289[»]
1NVSX-ray1.80A1-289[»]
1ZLTX-ray1.74A1-289[»]
1ZYSX-ray1.70A1-273[»]
2AYPX-ray2.90A1-269[»]
2BR1X-ray2.00A1-289[»]
2BRBX-ray2.10A1-289[»]
2BRGX-ray2.10A1-289[»]
2BRHX-ray2.10A1-289[»]
2BRMX-ray2.20A1-289[»]
2BRNX-ray2.80A1-289[»]
2BROX-ray2.20A1-289[»]
2C3JX-ray2.10A1-289[»]
2C3KX-ray2.60A1-289[»]
2C3LX-ray2.35A1-289[»]
2CGUX-ray2.50A1-289[»]
2CGVX-ray2.60A1-289[»]
2CGWX-ray2.20A1-289[»]
2CGXX-ray2.20A1-289[»]
2E9NX-ray2.50A2-270[»]
2E9OX-ray2.10A2-270[»]
2E9PX-ray2.60A2-270[»]
2E9UX-ray2.00A2-270[»]
2E9VX-ray2.00A/B2-269[»]
2GDOX-ray3.00A1-289[»]
2GHGX-ray3.50A2-270[»]
2HOGX-ray1.90A2-307[»]
2HXLX-ray1.80A2-307[»]
2HXQX-ray2.00A2-307[»]
2HY0X-ray1.70A2-307[»]
2QHMX-ray2.00A1-307[»]
2QHNX-ray1.70A1-307[»]
2R0UX-ray1.90A1-307[»]
2WMQX-ray2.48A1-289[»]
2WMRX-ray2.43A1-289[»]
2WMSX-ray2.70A1-289[»]
2WMTX-ray2.55A1-289[»]
2WMUX-ray2.60A1-289[»]
2WMVX-ray2.01A1-289[»]
2WMWX-ray2.43A1-289[»]
2WMXX-ray2.45A1-289[»]
2X8DX-ray1.90A1-289[»]
2X8EX-ray2.50A1-276[»]
2X8IX-ray1.92A1-289[»]
2XEYX-ray2.70A1-289[»]
2XEZX-ray2.25A1-289[»]
2XF0X-ray2.40A1-289[»]
2YDIX-ray1.60A1-289[»]
2YDJX-ray1.85A/B1-276[»]
2YDKX-ray1.90A1-276[»]
2YERX-ray1.83A1-276[»]
2YEXX-ray1.30A1-276[»]
2YM3X-ray2.01A1-289[»]
2YM4X-ray2.35A1-289[»]
2YM5X-ray2.03A1-289[»]
2YM6X-ray2.01A1-289[»]
2YM7X-ray1.81A1-289[»]
2YM8X-ray2.07A1-289[»]
2YWPX-ray2.90A2-270[»]
3F9NX-ray1.90A2-307[»]
3JVRX-ray1.76A2-272[»]
3JVSX-ray1.90A2-272[»]
3NLBX-ray1.90A1-289[»]
3OT3X-ray1.44A2-274[»]
3OT8X-ray1.65A2-274[»]
3PA3X-ray1.40A2-274[»]
3PA4X-ray1.59A2-274[»]
3PA5X-ray1.70A2-274[»]
3TKHX-ray1.79A1-307[»]
3TKIX-ray1.60A1-307[»]
3U9NX-ray1.85A2-274[»]
4FSMX-ray2.30A2-280[»]
4FSNX-ray2.10A4-280[»]
4FSQX-ray2.40A2-280[»]
4FSRX-ray2.50A2-280[»]
4FSTX-ray1.90A2-270[»]
4FSUX-ray2.10A2-280[»]
4FSWX-ray2.30A2-280[»]
4FSYX-ray2.30A2-280[»]
4FSZX-ray2.30A2-280[»]
4FT0X-ray2.30A2-280[»]
4FT3X-ray2.50A2-280[»]
4FT5X-ray2.40A2-280[»]
4FT7X-ray2.20A2-280[»]
4FT9X-ray2.20A2-280[»]
4FTAX-ray2.40A2-280[»]
4FTCX-ray2.00A2-280[»]
4FTIX-ray2.20A2-280[»]
4FTJX-ray2.20A2-280[»]
4FTKX-ray2.30A2-280[»]
4FTLX-ray2.50A2-280[»]
4FTMX-ray1.90A2-280[»]
4FTNX-ray2.02A2-280[»]
4FTOX-ray2.10A2-280[»]
4FTQX-ray2.00A2-280[»]
4FTRX-ray2.25A2-280[»]
4FTTX-ray2.30A2-280[»]
4FTUX-ray2.10A2-280[»]
4GH2X-ray2.03A2-280[»]
4HYHX-ray1.70A1-289[»]
4HYIX-ray1.40A1-289[»]
4JIKX-ray1.90A2-274[»]
4QYEX-ray2.05A1-289[»]
4QYFX-ray2.15A1-289[»]
4QYGX-ray1.75A/B1-289[»]
4QYHX-ray1.90A/B1-289[»]
4RVKX-ray1.85A1-289[»]
4RVLX-ray1.85A1-289[»]
4RVMX-ray1.86A1-289[»]
5DLSX-ray2.15A1-289[»]
5F4NX-ray1.91A1-273[»]
5OOPX-ray1.70A1-289[»]
5OORX-ray1.90A1-289[»]
5OOTX-ray2.10A1-289[»]
5OP2X-ray1.90A1-289[»]
5OP4X-ray2.00A1-289[»]
5OP5X-ray1.90A1-289[»]
5OP7X-ray1.80A1-289[»]
5OPBX-ray1.55A1-289[»]
5OPRX-ray1.95A1-289[»]
5OPSX-ray2.00A1-289[»]
5OPUX-ray1.55A1-289[»]
5OPVX-ray1.90A1-289[»]
5OQ5X-ray1.40A1-289[»]
5OQ6X-ray1.95A1-289[»]
5OQ7X-ray2.10A/B1-289[»]
5OQ8X-ray2.00A1-289[»]
5WI2X-ray2.50A/B377-476[»]
6FC8X-ray1.61A1-276[»]
6FCFX-ray1.85A1-276[»]
6FCKX-ray1.90A1-276[»]
ProteinModelPortaliO14757
SMRiO14757
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107536, 159 interactors
CORUMiO14757
DIPiDIP-24182N
ELMiO14757
IntActiO14757, 37 interactors
MINTiO14757
STRINGi9606.ENSP00000388648

Chemistry databases

BindingDBiO14757
ChEMBLiCHEMBL4630
DrugBankiDB07037 (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
GuidetoPHARMACOLOGYi1987

PTM databases

iPTMnetiO14757
PhosphoSitePlusiO14757

Polymorphism and mutation databases

BioMutaiCHEK1

Proteomic databases

EPDiO14757
MaxQBiO14757
PaxDbiO14757
PeptideAtlasiO14757
PRIDEiO14757
ProteomicsDBi48208
48209 [O14757-2]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		1111
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000428830; 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]
GeneIDi1111
KEGGihsa:1111
UCSCiuc001qcf.5 human [O14757-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1111
DisGeNETi1111
EuPathDBiHostDB:ENSG00000149554.12

GeneCards: human genes, protein and diseases

More...GeneCardsi		CHEK1

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0201657
HGNCiHGNC:1925 CHEK1
HPAiHPA044364
MIMi603078 gene
neXtProtiNX_O14757
OpenTargetsiENSG00000149554
PharmGKBiPA110

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0590 Eukaryota
ENOG410XQ0D LUCA
GeneTreeiENSGT00940000159682
HOGENOMiHOG000216658
HOVERGENiHBG002590
InParanoidiO14757
KOiK02216
OMAiNRQTEEA
PhylomeDBiO14757
TreeFamiTF351441

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-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
SignaLinkiO14757
SIGNORiO14757

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		CHEK1 human
EvolutionaryTraceiO14757

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		CHEK1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		1111

Protein Ontology

More...PROi		PR:O14757

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000149554 Expressed in 152 organ(s), highest expression level in secondary oocyte
CleanExiHS_CHEK1
ExpressionAtlasiO14757 baseline and differential
GenevisibleiO14757 HS

Family and domain databases

CDDicd14069 STKc_Chk1, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCHK1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O14757
Secondary accession number(s): A8K934
, B4DDD0, B4DSK3, B5BTY6, F5H7S4, H2BI51
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 11, 2011
Last modified: December 5, 2018
This is version 216 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again