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Entry version 103 (18 Sep 2019)
Sequence version 2 (27 Sep 2005)
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Protein

Serine/threonine-protein kinase Chk1

Gene

chek1

Organism
Xenopus laevis (African clawed frog)
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]. Phosphorylates wee1 at 'Ser-549' and cdc25c at 'Ser-287', which creates binding sites for 14-3-3 proteins which activate wee1 and inhibit cdc25c. Phosphorylates cdc25a at 'Ser-504' which prevents the interaction of cdc25a with CDK2-cyclin E1, CDC2-cyclin A1 and CDC2-cyclin B1. This inhibitory effect does not require 14-3-3 protein binding. Activation of wee1 and inhibition of CDC25 results in increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and consequent inhibition of cell cycle progression. May promote DNA repair, regulate chromatin assembly and the transcription of genes that regulate cell-cycle progression. May also play a role in replication fork maintenance.10 Publications

<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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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 by atr or atm in response to DNA damage or inhibition of DNA replication.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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 acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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

GO - Biological processi

<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 functionDevelopmental protein, Kinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, DNA damage
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.11.1 6725

<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
Checkpoint kinase-1
Short name:
xChk1
<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>OrganismiXenopus laevis (African clawed frog)
<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 identifieri8355 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

Xenopus laevis and tropicalis biology and genomics resource

More...
Xenbasei
XB-GENE-866102 chek1

<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 & Seán O’Donoghue; 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>Mutagenesisi54K → A: Abolishes interaction with CLSPN. Abrogates phosphorylation at S-344 and kinase activation during checkpoint signaling. 1 Publication1
Mutagenesisi129R → A: Abolishes interaction with CLSPN, abrogates phosphorylation at S-344 and abolishes kinase activity. 1 Publication1
Mutagenesisi135N → A: Abolishes kinase activity; no effect on interaction with CLSPN. 3 Publications1
Mutagenesisi148D → A: Abolishes kinase activity. 1 Publication1
Mutagenesisi153T → A: Abolishes interaction with CLSPN. Abrogates phosphorylation at S-344 and kinase activation during checkpoint signaling. 1 Publication1
Mutagenesisi162R → A: Abolishes interaction with CLSPN and kinase activation during checkpoint signaling. No effect on phosphorylation at S-344. 1 Publication1
Mutagenesisi314T → A: Abrogates phosphorylation and activation during checkpoint signaling; when associated with A-344; A-356 and A-365. 2 Publications1
Mutagenesisi314T → D: Impairs autoinhibition by the AIR domain; when associated with D-344; D-356 and D-365. 2 Publications1
Mutagenesisi314T → E: Impairs autoinhibition by the AIR domain; when associated with E-344; E-356 and E-365. 2 Publications1
Mutagenesisi344S → A: Abrogates phosphorylation and activation during checkpoint signaling; when associated with A-314; A-356 and A-365. 2 Publications1
Mutagenesisi344S → D: Impairs autoinhibition by the AIR domain; when associated with D-314; D-356 and D-365. 2 Publications1
Mutagenesisi344S → E: Impairs autoinhibition by the AIR domain; when associated with E-314; E-356 and E-365. 2 Publications1
Mutagenesisi356S → A: Abrogates phosphorylation and activation during checkpoint signaling; when associated with A-314; A-344 and A-365. 2 Publications1
Mutagenesisi356S → D: Impairs autoinhibition by the AIR domain; when associated with D-314; D-344 and D-365. 2 Publications1
Mutagenesisi356S → E: Impairs autoinhibition by the AIR domain; when associated with E-314; E-344 and E-365. 2 Publications1
Mutagenesisi365S → A: Abrogates phosphorylation and activation during checkpoint signaling; when associated with A-314; A-344 and A-356. 2 Publications1
Mutagenesisi365S → D: Impairs autoinhibition by the AIR domain; when associated with D-314; D-344 and D-356. 2 Publications1
Mutagenesisi365S → E: Impairs autoinhibition by the AIR domain; when associated with E-314; E-344 and E-356. 2 Publications1
Mutagenesisi374 – 380Missing : Induces hyperphosphorylation and enhances kinase activity. 1 Publication7
Mutagenesisi374 – 375KR → AA: Impairs autoinhibition and abrogates nuclear localization. 1 Publication2
Mutagenesisi377T → A: Induces hyperphosphorylation and enhances kinase activity and cell cycle arrest. Abolishes interaction with CLSPN. 2 Publications1
Mutagenesisi377T → E: Enhances kinase activity. 2 Publications1
Mutagenesisi451 – 452KR → AA: Enhances kinase activity. 1 Publication2
Mutagenesisi456 – 458KIK → AAA: Enhances kinase activity and abrogates nuclear localization. 1 Publication3

<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_00000858521 – 474Serine/threonine-protein kinase Chk1Add BLAST474

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 residuei314Phosphothreonine; by ATR1 Publication1
Modified residuei344Phosphoserine; by ATR5 Publications1
Modified residuei356Phosphoserine; by ATR1 Publication1
Modified residuei365Phosphoserine; by ATR1 Publication1

<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 atm in response to ionizing irradiation (By similarity). Phosphorylated by atr at Thr-314, Ser-344, Ser-356 and Ser-365 in response to various stimuli that cause checkpoint activation. Phosphorylation impairs binding of the C-terminal autoinhibitory region (AIR) to the kinase domain and thereby enhances kinase activity.By similarity9 Publications

Keywords - PTMi

Phosphoprotein

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q6DE87

<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 the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed throughout development. Transiently activated by ATR-mediated phosphorylation from the midblastula transition (MBT) to the initial gastrula stage. Developmentally regulated activation of the DNA replication checkpoint may occur as the nucleo-cytoplasmic ratio increases and maternal replication factors are depleted. Elongation of the embryonic cell cycle may allow time for the transcription of genes that initiate the switch from maternal to zygotic control of embryogenesis.5 Publications

<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 with and phosphorylates clspn, an adapter protein that regulates the ATR-dependent phosphorylation of chek1.

3 Publications

<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

3D structure databases

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

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SMRi
Q6DE87

Database of comparative protein structure models

More...
ModBasei
Search...

<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 CLSPNAdd BLAST265
Regioni360 – 474Autoinhibitory regionAdd BLAST115
Regioni367 – 474Required for nuclear localizationAdd BLAST108

<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) binds to the kinase domain and inhibits its activity.2 Publications

<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

KEGG Orthology (KO)

More...
KOi
K02216

Database of Orthologous Groups

More...
OrthoDBi
698464at2759

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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<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.

Q6DE87-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAVPFVEDWD LVQTLGEGAY GEVQLAVNRK TEEAVAVKIV DMTRAADCPE
60 70 80 90 100
NIKKEICINR MLSHTNIVRF YGHRREGNIQ YLFLEYCRGG ELFDRIEPDV
110 120 130 140 150
GMPEQDAQKF FQQLIAGVEY LHSIGITHRD IKPENLLLDE RDQLKISDFG
160 170 180 190 200
LATVFRHNGK ERLLNKMCGT LPYVAPELIK SRAFHADPVD VWSCGIVLTA
210 220 230 240 250
MLAGELPWDQ PNEVCQEYCD WKEKNHYLTP WKKISATPLA LLCKMLTENP
260 270 280 290 300
QSRITIPDIK KDRWFTEIIK KGLKRSRVIS GGSSDSSVLC KQIRSDIDIS
310 320 330 340 350
HFSHSEEKTA LSSTQPEPRT ALATWDSNSS YIDNLVQGKG ISFSQPACPD
360 370 380 390 400
NMLLNSQLIG TPGSSQNVWQ RLVKRMTRFF TKVNAESSYS NLMDTCEKMG
410 420 430 440 450
YVLKKSCANE VTLSTTDRRN NKLIFKVNLV EMEDRILLDF RLSKGDGLEF
460 470
KRHFLKIKKK MDAVVAVQKV LPDT
Length:474
Mass (Da):53,975
Last modified:September 27, 2005 - 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:iB6D09B14838F1C0A
GO

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 conflicti165N → S in AAC64262 (PubMed:9744884).Curated1
Sequence conflicti165N → S in BAA34058 (PubMed:10068474).Curated1
Sequence conflicti230 – 231Missing in BAA34058 (PubMed:10068474).Curated2
Sequence conflicti232K → E in AAF00098 (PubMed:10982403).Curated1
Sequence conflicti238P → L in BAA34058 (PubMed:10068474).Curated1
Sequence conflicti243C → G in AAC64262 (PubMed:9744884).Curated1
Sequence conflicti243C → G in BAA34058 (PubMed:10068474).Curated1
Sequence conflicti307Missing in AAF00098 (PubMed:10982403).Curated1
Sequence conflicti307Missing in AAH77249 (Ref. 4) Curated1
Sequence conflicti331 – 333YID → DIN in AAC64262 (PubMed:9744884).Curated3
Sequence conflicti331 – 333YID → DIN in BAA34058 (PubMed:10068474).Curated3
Sequence conflicti472 – 473PD → SA in AAC64262 (PubMed:9744884).Curated2
Sequence conflicti472 – 473PD → SA in BAA34058 (PubMed:10068474).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF053120 mRNA Translation: AAC64262.1
AB019218 mRNA Translation: BAA34058.1
AF117816 mRNA Translation: AAF00098.1
BC077249 mRNA Translation: AAH77249.1

NCBI Reference Sequences

More...
RefSeqi
NP_001082039.1, NM_001088570.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
398191

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
xla:398191

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053120 mRNA Translation: AAC64262.1
AB019218 mRNA Translation: BAA34058.1
AF117816 mRNA Translation: AAF00098.1
BC077249 mRNA Translation: AAH77249.1
RefSeqiNP_001082039.1, NM_001088570.1

3D structure databases

SMRiQ6DE87
ModBaseiSearch...

PTM databases

iPTMnetiQ6DE87

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi398191
KEGGixla:398191

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
398191
XenbaseiXB-GENE-866102 chek1

Phylogenomic databases

KOiK02216
OrthoDBi698464at2759

Enzyme and pathway databases

BRENDAi2.7.11.1 6725

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...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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_XENLA
<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: Q6DE87
Secondary accession number(s): Q78CK1, Q78DQ2, Q9YI18
<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: September 27, 2005
Last sequence update: September 27, 2005
Last modified: September 18, 2019
This is version 103 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

<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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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