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O35280

- CHK1_MOUSE

UniProt

O35280 - CHK1_MOUSE

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Protein

Serine/threonine-protein kinase Chk1

Gene
Chek1, Chk1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. 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.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme 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 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381ATP By similarity
Active sitei130 – 1301Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 239ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. histone kinase activity (H3-T11 specific) Source: UniProtKB
  3. protein binding Source: MGI
  4. protein kinase activity Source: MGI
  5. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. cellular response to caffeine Source: Ensembl
  2. cellular response to DNA damage stimulus Source: MGI
  3. cellular response to mechanical stimulus Source: Ensembl
  4. chromatin-mediated maintenance of transcription Source: UniProtKB
  5. DNA damage checkpoint Source: MGI
  6. DNA damage induced protein phosphorylation Source: UniProtKB
  7. DNA repair Source: MGI
  8. G2/M transition of mitotic cell cycle Source: MGI
  9. G2 DNA damage checkpoint Source: UniProtKB
  10. histone H3-T11 phosphorylation Source: GOC
  11. negative regulation of mitosis Source: UniProtKB
  12. peptidyl-threonine phosphorylation Source: UniProtKB
  13. protein phosphorylation Source: MGI
  14. regulation of cell proliferation Source: MGI
  15. regulation of double-strand break repair via homologous recombination Source: UniProtKB
  16. regulation of gene expression Source: MGI
  17. regulation of histone H3-K9 acetylation Source: UniProtKB
  18. regulation of mitotic centrosome separation Source: UniProtKB
  19. regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, DNA damage, DNA repair

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 3474.
ReactomeiREACT_188578. Signaling by SCF-KIT.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase Chk1 (EC:2.7.11.1)
Alternative name(s):
CHK1 checkpoint homolog
Checkpoint kinase-1
Gene namesi
Name:Chek1
Synonyms:Chk1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:1202065. Chek1.

Subcellular locationi

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.2 Publications

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. chromatin Source: UniProtKB
  3. chromosome, telomeric region Source: Ensembl
  4. condensed nuclear chromosome Source: UniProtKB
  5. cytoplasm Source: UniProtKB-SubCell
  6. nucleoplasm Source: Reactome
  7. nucleus Source: MGI
  8. replication fork Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice die of apoptosis at the blastocyst stage.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi280 – 2801S → A: Enhances cell cycle arrest. 1 Publication
Mutagenesisi280 – 2801S → E: Promotes mono and/or diubiquitination and nuclear exclusion. Reduces phosphorylation at S-345. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 476476Serine/threonine-protein kinase Chk1PRO_0000085849Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei280 – 2801Phosphoserine; by PKB/AKT11 Publication
Modified residuei286 – 2861Phosphoserine By similarity
Modified residuei296 – 2961Phosphoserine By similarity
Modified residuei301 – 3011Phosphoserine By similarity
Modified residuei317 – 3171Phosphoserine; by ATM and ATR1 Publication
Modified residuei345 – 3451Phosphoserine; by ATR1 Publication
Cross-linki436 – 436Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

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.2 Publications
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.2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO35280.
PRIDEiO35280.

PTM databases

PhosphoSiteiO35280.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

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.1 Publication

Gene expression databases

ArrayExpressiO35280.
BgeeiO35280.
CleanExiMM_CHEK1.
GenevestigatoriO35280.

Interactioni

Subunit structurei

Interacts (phosphorylated by ATR) with RAD51. Interacts with and phosphorylates CLSPN, an adapter protein that regulates the ATR-dependent phosphorylation of CHEK1. Interacts with BRCA1. Interacts with and phosphorylates CDC25A, CDC25B and CDC25C. Interacts with FBXO6, which regulates CHEK1. Interacts with PPM1D, which regulates CHEK1 through dephosphorylation. Interacts with TIMELESS; DNA damage-dependent. Interacts with FEM1B; activates CHEK1 in response to stress. Interacts with TLK1. Interacts with XPO1 and YWHAZ By similarity.

Protein-protein interaction databases

BioGridi198694. 5 interactions.
IntActiO35280. 1 interaction.
MINTiMINT-1340615.

Structurei

3D structure databases

ProteinModelPortaliO35280.
SMRiO35280. Positions 2-448.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 265257Protein kinaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 265265Interaction with CLSPN By similarityAdd
BLAST
Regioni391 – 47686Autoinhibitory region By similarityAdd
BLAST

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00730000111032.
HOGENOMiHOG000216658.
HOVERGENiHBG002590.
InParanoidiO35280.
KOiK02216.
OMAiGGFSKHI.
OrthoDBiEOG712TWF.
PhylomeDBiO35280.
TreeFamiTF351441.

Family and domain databases

InterProiIPR011009. 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]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O35280-1) [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

MAVPFVEDWD LVQTLGEGAY GEVQLAVNRI TEEAVAVKIV DMKRAIDCPE    50
NIKKEICINK MLSHENVVKF YGHRREGHIQ YLFLEYCSGG ELFDRIEPDI 100
GMPEQDAQRF FHQLMAGVVY LHGIGITHRD IKPENLLLDE RDNLKISDFG 150
LATVFRHNNR ERLLNKMCGT LPYVAPELLK RKEFHAEPVD VWSCGIVLTA 200
MLAGELPWDQ PSDSCQEYSD WKEKKTYLNP WKKIDSAPLA LLHKILVETP 250
SARITIPDIK KDRWYNKPLN RGAKRPRATS GGMSESSSGF SKHIHSNLDF 300
SPVNNGSSEE TVKFSSSQPE PRTGLSLWDT GPSNVDKLVQ GISFSQPTCP 350
EHMLVNSQLL GTPGSSQNPW QRLVKRMTRF FTKLDADKSY QCLKETFEKL 400
GYQWKKSCMN QVTVSTTDRR NNKLIFKINL VEMDEKILVD FRLSKGDGLE 450
FKRHFLKIKG KLSDVVSSQK VWFPVT 476
Length:476
Mass (Da):54,381
Last modified:September 27, 2005 - v2
Checksum:i0642D238EB3C5BE3
GO
Isoform 2 (identifier: O35280-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:382
Mass (Da):43,627
Checksum:i506D80B1AF404B7D
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9494Missing in isoform 2. VSP_015791Add
BLAST
Alternative sequencei95 – 973RIE → MEK in isoform 2. VSP_015792

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331E → Q in AAC53334. 1 Publication
Sequence conflicti50 – 501E → Q in AAC53334. 1 Publication
Sequence conflicti219 – 2235SDWKE → LIVKK in AAB88853. 1 Publication
Sequence conflicti252 – 2521A → S in AAB88853. 1 Publication
Sequence conflicti365 – 3651S → F in AAC53334. 1 Publication
Sequence conflicti449 – 4502LE → YN in AAB88853. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS22972.1. [O35280-1]
RefSeqiNP_031717.2. NM_007691.5. [O35280-1]
UniGeneiMm.16753.

Genome annotation databases

EnsembliENSMUST00000034625; ENSMUSP00000034625; ENSMUSG00000032113. [O35280-1]
ENSMUST00000172702; ENSMUSP00000134388; ENSMUSG00000032113. [O35280-1]
GeneIDi12649.
KEGGimmu:12649.
UCSCiuc009otv.1. mouse. [O35280-1]
uc009otx.2. mouse. [O35280-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS22972.1. [O35280-1 ]
RefSeqi NP_031717.2. NM_007691.5. [O35280-1 ]
UniGenei Mm.16753.

3D structure databases

ProteinModelPortali O35280.
SMRi O35280. Positions 2-448.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198694. 5 interactions.
IntActi O35280. 1 interaction.
MINTi MINT-1340615.

PTM databases

PhosphoSitei O35280.

Proteomic databases

MaxQBi O35280.
PRIDEi O35280.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034625 ; ENSMUSP00000034625 ; ENSMUSG00000032113 . [O35280-1 ]
ENSMUST00000172702 ; ENSMUSP00000134388 ; ENSMUSG00000032113 . [O35280-1 ]
GeneIDi 12649.
KEGGi mmu:12649.
UCSCi uc009otv.1. mouse. [O35280-1 ]
uc009otx.2. mouse. [O35280-2 ]

Organism-specific databases

CTDi 1111.
MGIi MGI:1202065. Chek1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00730000111032.
HOGENOMi HOG000216658.
HOVERGENi HBG002590.
InParanoidi O35280.
KOi K02216.
OMAi GGFSKHI.
OrthoDBi EOG712TWF.
PhylomeDBi O35280.
TreeFami TF351441.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 3474.
Reactomei REACT_188578. Signaling by SCF-KIT.

Miscellaneous databases

NextBioi 281856.
PROi O35280.
SOURCEi Search...

Gene expression databases

ArrayExpressi O35280.
Bgeei O35280.
CleanExi MM_CHEK1.
Genevestigatori O35280.

Family and domain databases

InterProi IPR011009. 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 ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.
  11. "Mammalian TIMELESS is involved in period determination and DNA damage-dependent phase advancing of the circadian clock."
    Engelen E., Janssens R.C., Yagita K., Smits V.A., van der Horst G.T., Tamanini F.
    PLoS ONE 8:E56623-E56623(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIMELESS.

Entry informationi

Entry nameiCHK1_MOUSE
AccessioniPrimary (citable) accession number: O35280
Secondary accession number(s): O54925, Q8CI40, Q9D0N2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 27, 2005
Last modified: September 3, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Haploinsufficient for the suppression of genomic instability and tumor progression.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi