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O35280 (CHK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. 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, 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 By similarity. 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. Ref.5 Ref.6 Ref.7 Ref.10

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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 By similarity.

Subunit structure

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 By similarity.

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Note: Nuclear export is mediated at least in part by XPO1/CRM1. Also localizes to the centrosome specifically during interphase, where it may protect centrosomal CDC2 kinase from inappropriate activation by cytoplasmic CDC25B By similarity. Ref.4 Ref.8

Tissue specificity

Found in all adult tissues tested. Elevated expression in testis, lung and spleen. 15.5 day old embryos show ubiquitous expression with strong expression in brain, liver, kidney, pancreas, intestine, thymus and lung. Ref.1

Developmental stage

In the testis, present in cells undergoing meiosis I. Not detected in peripheral cells in seminiferous tubules that are undergoing pre-meiotic DNA synthesis or in late condensing or mature sperm. Ref.4

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. 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. Ref.8 Ref.9

Ubiquitinated. Mono or diubiquitination promotes nuclear exclusion. 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 By similarity. 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 similarity. Ref.8 Ref.9

Disruption phenotype

Mice die of apoptosis at the blastocyst stage. Ref.5

Miscellaneous

Haploinsufficient for the suppression of genomic instability and tumor progression.

Sequence similarities

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

Contains 1 protein kinase domain.

Sequence caution

The sequence AAH37613.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCell cycle
DNA damage
DNA repair
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage checkpoint

Inferred from direct assay PubMed 12529385. Source: MGI

DNA damage induced protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

DNA repair

Inferred from direct assay PubMed 15364958. Source: MGI

G2 DNA damage checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

G2/M transition of mitotic cell cycle

Inferred from mutant phenotype Ref.6. Source: MGI

cellular response to DNA damage stimulus

Inferred from direct assay PubMed 11790307PubMed 12529385. Source: MGI

cellular response to caffeine

Inferred from electronic annotation. Source: Ensembl

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

chromatin-mediated maintenance of transcription

Inferred from mutant phenotype Ref.10. Source: UniProtKB

histone H3-T11 phosphorylation

Inferred from direct assay Ref.10. 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

protein phosphorylation

Inferred from direct assay PubMed 15364958. Source: MGI

regulation of cell proliferation

Inferred from mutant phenotype PubMed 21737879. Source: MGI

regulation of double-strand break repair via homologous recombination

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of gene expression

Inferred from genetic interaction PubMed 21737879. Source: MGI

regulation of histone H3-K9 acetylation

Inferred from direct assay Ref.10. 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 mutant phenotype Ref.10. Source: UniProtKB

   Cellular_componentcentrosome

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin

Inferred from direct assay Ref.10. Source: UniProtKB

chromosome, telomeric region

Inferred from electronic annotation. Source: Ensembl

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 direct assay PubMed 11555636. Source: MGI

replication fork

Inferred from direct assay PubMed 15364958. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

histone kinase activity (H3-T11 specific)

Inferred from direct assay Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 15364958. Source: MGI

protein kinase activity

Inferred from mutant phenotype PubMed 15364958. Source: MGI

protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O35280-1)

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.
Isoform 2 (identifier: O35280-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: Missing.
     95-97: RIE → MEK
Note: No experimental confirmation available. 3 initiator methionines can be considered. If this isoform were to start at the first ATG, it would produce a 28 amino acid-long peptide, sharing the first 22 amino acids with the canonical sequence (isoform 1) and differing in the last 6 residues (VQLAVN -> ARHRDA). An initiation at this site could target the mRNA to nonsense-mediated mRNA decay and, in this case, the peptide would be produced at very low levels. The second possible translation initiation site would lead to the synthesis of the sequence shown in this entry as isoform 2. However, the Kozak sequence for this site is not optimal. Finally the third potential initiator methionine corresponds to position 167 in isoform 1 and would lead to the synthesis of a 310 amino acid-long protein identical to isoform 1 residues 167 through 476.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 476476Serine/threonine-protein kinase Chk1
PRO_0000085849

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 Ref.8
Modified residue2861Phosphoserine By similarity
Modified residue2961Phosphoserine By similarity
Modified residue3011Phosphoserine By similarity
Modified residue3171Phosphoserine; by ATM and ATR Ref.9
Modified residue3451Phosphoserine; by ATR Ref.8
Cross-link436Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence1 – 9494Missing in isoform 2.
VSP_015791
Alternative sequence95 – 973RIE → MEK in isoform 2.
VSP_015792

Experimental info

Mutagenesis2801S → A: Enhances cell cycle arrest. Ref.8
Mutagenesis2801S → E: Promotes mono and/or diubiquitination and nuclear exclusion. Reduces phosphorylation at S-345. Ref.8
Sequence conflict331E → Q in AAC53334. Ref.1
Sequence conflict501E → Q in AAC53334. Ref.1
Sequence conflict219 – 2235SDWKE → LIVKK in AAB88853. Ref.4
Sequence conflict2521A → S in AAB88853. Ref.4
Sequence conflict3651S → F in AAC53334. Ref.1
Sequence conflict449 – 4502LE → YN in AAB88853. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 27, 2005. Version 2.
Checksum: 0642D238EB3C5BE3

FASTA47654,381
        10         20         30         40         50         60 
MAVPFVEDWD LVQTLGEGAY GEVQLAVNRI TEEAVAVKIV DMKRAIDCPE NIKKEICINK 

        70         80         90        100        110        120 
MLSHENVVKF YGHRREGHIQ YLFLEYCSGG ELFDRIEPDI GMPEQDAQRF FHQLMAGVVY 

       130        140        150        160        170        180 
LHGIGITHRD IKPENLLLDE RDNLKISDFG LATVFRHNNR ERLLNKMCGT LPYVAPELLK 

       190        200        210        220        230        240 
RKEFHAEPVD VWSCGIVLTA MLAGELPWDQ PSDSCQEYSD WKEKKTYLNP WKKIDSAPLA 

       250        260        270        280        290        300 
LLHKILVETP SARITIPDIK KDRWYNKPLN RGAKRPRATS GGMSESSSGF SKHIHSNLDF 

       310        320        330        340        350        360 
SPVNNGSSEE TVKFSSSQPE PRTGLSLWDT GPSNVDKLVQ GISFSQPTCP EHMLVNSQLL 

       370        380        390        400        410        420 
GTPGSSQNPW QRLVKRMTRF FTKLDADKSY QCLKETFEKL GYQWKKSCMN QVTVSTTDRR 

       430        440        450        460        470 
NNKLIFKINL VEMDEKILVD FRLSKGDGLE FKRHFLKIKG KLSDVVSSQK VWFPVT 

« Hide

Isoform 2 [UniParc].

Checksum: 506D80B1AF404B7D
Show »

FASTA38243,627

References

« Hide 'large scale' references
[1]"Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA damage to Cdk regulation through Cdc25."
Sanchez Y., Wong C., Thoma R.S., Richman R., Wu Z., Piwnica-Worms H., Elledge S.J.
Science 277:1497-1501(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Embryo and Testis.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Mammary gland.
[4]"Atm-dependent interactions of a mammalian chk1 homolog with meiotic chromosomes."
Flaggs G., Plug A.W., Dunks K.M., Mundt K.E., Ford J.C., Quiggle M.R.E., Taylor E.M., Westphal C.H., Ashley T., Hoekstra M.F., Carr A.M.
Curr. Biol. 7:977-986(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 204-450 (ISOFORMS 1/2), SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[5]"Aberrant cell cycle checkpoint function and early embryonic death in Chk1(-/-) mice."
Takai H., Tominaga K., Motoyama N., Minamishima Y.A., Nagahama H., Tsukiyama T., Ikeda K., Nakayama K., Nakanishi M., Nakayama K.
Genes Dev. 14:1439-1447(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[6]"Chk1 is an essential kinase that is regulated by Atr and required for the G(2)/M DNA damage checkpoint."
Liu Q., Guntuku S., Cui X.-S., Matsuoka S., Cortez D., Tamai K., Luo G., Carattini-Rivera S., DeMayo F., Bradley A., Donehower L.A., Elledge S.J.
Genes Dev. 14:1448-1459(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN G2/M DNA DAMAGE CHECKPOINT.
[7]"Chk1 is haploinsufficient for multiple functions critical to tumor suppression."
Lam M.H., Liu Q., Elledge S.J., Rosen J.M.
Cancer Cell 6:45-59(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Lack of PTEN sequesters CHK1 and initiates genetic instability."
Puc J., Keniry M., Li H.S., Pandita T.K., Choudhury A.D., Memeo L., Mansukhani M., Murty V.V.V.S., Gaciong Z., Meek S.E.M., Piwnica-Worms H., Hibshoosh H., Parsons R.
Cancer Cell 7:193-204(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, UBIQUITINATION, PHOSPHORYLATION AT SER-280 AND SER-345, MUTAGENESIS OF SER-280.
[9]"Mice lacking protein phosphatase 5 are defective in ataxia telangiectasia mutated (ATM)-mediated cell cycle arrest."
Yong W., Bao S., Chen H., Li D., Sanchez E.R., Shou W.
J. Biol. Chem. 282:14690-14694(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-317.
[10]"Chk1 is a histone H3 threonine 11 kinase that regulates DNA damage-induced transcriptional repression."
Shimada M., Niida H., Zineldeen D.H., Tagami H., Tanaka M., Saito H., Nakanishi M.
Cell 132:221-232(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN EPIGENETIC REGULATION OF TRANSCRIPTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF016583 mRNA. Translation: AAC53334.1.
AK011258 mRNA. Translation: BAB27500.1.
AK033179 mRNA. Translation: BAC28185.1.
AK045336 mRNA. Translation: BAC32315.1.
BC037613 mRNA. Translation: AAH37613.1. Different initiation.
AF032875 mRNA. Translation: AAB88853.1.
CCDSCCDS22972.1. [O35280-1]
RefSeqNP_031717.2. NM_007691.5. [O35280-1]
UniGeneMm.16753.

3D structure databases

ProteinModelPortalO35280.
SMRO35280. Positions 2-448.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198694. 5 interactions.
IntActO35280. 1 interaction.
MINTMINT-1340615.

PTM databases

PhosphoSiteO35280.

Proteomic databases

MaxQBO35280.
PRIDEO35280.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034625; ENSMUSP00000034625; ENSMUSG00000032113. [O35280-1]
ENSMUST00000172702; ENSMUSP00000134388; ENSMUSG00000032113. [O35280-1]
GeneID12649.
KEGGmmu:12649.
UCSCuc009otv.1. mouse. [O35280-1]
uc009otx.2. mouse. [O35280-2]

Organism-specific databases

CTD1111.
MGIMGI:1202065. Chek1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00730000111032.
HOGENOMHOG000216658.
HOVERGENHBG002590.
InParanoidO35280.
KOK02216.
OMAGGFSKHI.
OrthoDBEOG712TWF.
PhylomeDBO35280.
TreeFamTF351441.

Enzyme and pathway databases

BRENDA2.7.11.1. 3474.
ReactomeREACT_188804. Cell Cycle.

Gene expression databases

ArrayExpressO35280.
BgeeO35280.
CleanExMM_CHEK1.
GenevestigatorO35280.

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

NextBio281856.
PROO35280.
SOURCESearch...

Entry information

Entry nameCHK1_MOUSE
AccessionPrimary (citable) accession number: O35280
Secondary accession number(s): O54925, Q8CI40, Q9D0N2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 27, 2005
Last modified: July 9, 2014
This is version 138 of the entry and version 2 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot