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Q8AYC9 (CHK1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase Chk1

EC=2.7.11.1
Alternative name(s):
CHK1 checkpoint homolog
Checkpoint kinase-1
Gene names
Name:CHEK1
Synonyms:CHK1
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome. Recognizes the substrate consensus sequence [R-X-X-S/T]. Binds to and phosphorylates CDC25A, CDC25B and CDC25C. This inhibits their activity through proteasomal degradation, nucleo-cytoplasmic shuttling and inhibition by proteins of the 13-3-3 family. Inhibition of CDC25 leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks 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 By similarity. Ref.1

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Activated through phosphorylation by ATR or ATM in response to DNA damage or inhibition of DNA replication By similarity.

Subunit structure

Interacts with and phosphorylates CLSPN, an adapter protein that regulates the ATR-dependent phosphorylation of CHEK1 By similarity.

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity.

Domain

The autoinhibitory region (AIR) inhibits the activity of the kinase domain By similarity.

Post-translational modification

Phosphorylated by ATR in a RAD17-dependent manner in response to ultraviolet irradiation and inhibition of DNA replication. Phosphorylated by ATM in response to ionizing irradiation By similarity. Phosphorylation at Ser-345 induces a change in the conformation of the protein and activates the kinase activity. Phosphorylation at Ser-345 also increases binding to 14-3-3 proteins and promotes nuclear retention. Ref.1

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
DNA damage
DNA repair
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

DNA damage induced protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

DNA repair

Traceable author statement. Source: Reactome

G2 DNA damage checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin-mediated maintenance of transcription

Inferred from sequence or structural similarity. Source: UniProtKB

double-strand break repair

Traceable author statement. Source: Reactome

double-strand break repair via homologous recombination

Traceable author statement. Source: Reactome

histone H3-T11 phosphorylation

Inferred from sequence or structural similarity. Source: GOC

negative regulation of mitosis

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-threonine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of double-strand break repair via homologous recombination

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of histone H3-K9 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of mitotic centrosome separation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcentrosome

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin

Inferred from sequence or structural similarity. Source: UniProtKB

condensed nuclear chromosome

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

histone kinase activity (H3-T11 specific)

Inferred from sequence or structural similarity. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 476476Serine/threonine-protein kinase Chk1
PRO_0000085851

Regions

Domain9 – 265257Protein kinase
Nucleotide binding15 – 239ATP By similarity
Region1 – 265265Interaction with CLSPN By similarity
Region391 – 47686Autoinhibitory region By similarity

Sites

Active site1301Proton acceptor By similarity
Binding site381ATP By similarity

Amino acid modifications

Modified residue2801Phosphoserine; by PKB/AKT1 By similarity
Modified residue2961Phosphoserine By similarity
Modified residue3171Phosphoserine; by ATM and ATR By similarity
Modified residue3451Phosphoserine Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8AYC9 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 0E54EE2196EF0C15

FASTA47653,849
        10         20         30         40         50         60 
MAVPFVEDWD LVQTLGEGAY GEVQLAVNRR TEEAVAVKIV DMKRAADCPE NIKKEICINK 

        70         80         90        100        110        120 
MLNHENVVKF YGHRREGATQ YLFLEYCSGG ELFDRIEPDI GMPEPEAQRF FQQLIAGVVY 

       130        140        150        160        170        180 
LHSMGITHRD LKPENLLLDE RDNLKISDFG LATVFKHNGR ERLLNKMCGT LPYVAPELLR 

       190        200        210        220        230        240 
RPEFRAEPVD VWACGVVLTA MLAGELPWDQ PSDSCQEYSD WKERKTYLAP WRKIDSAPLA 

       250        260        270        280        290        300 
LLHKILTENP TARITIPDIK KDRWYCRPLK KGTKRGRVSS GGVTESPGAL PKHIRSDTDF 

       310        320        330        340        350        360 
SPVKSALGED KASYSTSQPE PGTGGALWDS STGSIDRLVQ GISFSQPACP EHMLLNSQLL 

       370        380        390        400        410        420 
GTPGSSQSPW QRLVRRMTRF FTKLDADGSY RSLRDVCEKM GYGWKQSCTN QVTISTTDRR 

       430        440        450        460        470 
NNKLIFKVNL LEMESRILVD FRLSKGDGLE FKRHFLKIKG KLSDVVSTQK VWLPPP 

« Hide

References

[1]"Chk1-deficient tumour cells are viable but exhibit multiple checkpoint and survival defects."
Zachos G., Rainey M.D., Gillespie D.A.F.
EMBO J. 22:713-723(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION AT SER-345.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF525027 mRNA. Translation: AAN33019.1.
RefSeqNP_989676.1. NM_204345.1.
UniGeneGga.4288.
Gga.48286.

3D structure databases

ProteinModelPortalQ8AYC9.
SMRQ8AYC9. Positions 3-272.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid675270. 1 interaction.
STRING9031.ENSGALP00000040314.

Proteomic databases

PaxDbQ8AYC9.
PRIDEQ8AYC9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID374260.
KEGGgga:374260.

Organism-specific databases

CTD3703.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000216658.
HOVERGENHBG002590.
InParanoidQ8AYC9.
KOK02216.
PhylomeDBQ8AYC9.

Enzyme and pathway databases

ReactomeREACT_115612. DNA replication and repair.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20813751.
PROQ8AYC9.

Entry information

Entry nameCHK1_CHICK
AccessionPrimary (citable) accession number: Q8AYC9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families