O35280 (CHK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	476 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton › centrosome 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 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
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 process	Cell cycle DNA damage DNA repair
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 caffeine Inferred from electronic annotation. Source: Compara cellular response to mechanical stimulus Inferred from electronic annotation. Source: Compara chromatin-mediated maintenance of transcription Inferred from mutant phenotype Ref.10. Source: UniProtKB negative regulation of mitosis Inferred from sequence or structural similarity. Source: UniProtKB regulation of S phase Inferred from electronic annotation. Source: Compara 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 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_component	centrosome 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: Compara 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 replication fork Inferred from direct assay PubMed 15364958. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW histone kinase activity (H3-T11 specific) Inferred from direct assay Ref.10. 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 476	476	Serine/threonine-protein kinase Chk1		PRO_0000085849
Regions
	Domain	9 – 265	257	Protein kinase
	Nucleotide binding	15 – 23	9	ATP By similarity
	Region	1 – 265	265	Interaction with CLSPN By similarity
	Region	391 – 476	86	Autoinhibitory region By similarity
Sites
	Active site	130	1	Proton acceptor By similarity
	Binding site	38	1	ATP By similarity
Amino acid modifications
	Modified residue	280	1	Phosphoserine; by PKB/AKT1 Ref.8
	Modified residue	286	1	Phosphoserine By similarity
	Modified residue	296	1	Phosphoserine By similarity
	Modified residue	301	1	Phosphoserine By similarity
	Modified residue	317	1	Phosphoserine; by ATM and ATR Ref.9
	Modified residue	345	1	Phosphoserine; by ATR Ref.8
	Cross-link	436		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Natural variations
	Alternative sequence	1 – 94	94	Missing in isoform 2.		VSP_015791
	Alternative sequence	95 – 97	3	RIE → MEK in isoform 2.		VSP_015792
Experimental info
	Mutagenesis	280	1	S → A: Enhances cell cycle arrest. Ref.8
	Mutagenesis	280	1	S → E: Promotes mono and/or diubiquitination and nuclear exclusion. Reduces phosphorylation at S-345. Ref.8
	Sequence conflict	33	1	E → Q in AAC53334. Ref.1
	Sequence conflict	50	1	E → Q in AAC53334. Ref.1
	Sequence conflict	219 – 223	5	SDWKE → LIVKK in AAB88853. Ref.4
	Sequence conflict	252	1	A → S in AAB88853. Ref.4
	Sequence conflict	365	1	S → F in AAC53334. Ref.1
	Sequence conflict	449 – 450	2	LE → YN in AAB88853. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 27, 2005. Version 2. Checksum: 0642D238EB3C5BE3	FASTA	476	54,381
	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
	Isoform 2 [UniParc]. Checksum: 506D80B1AF404B7D	FASTA	382	43,627
	10 20 30 40 50 60 MEKPDIGMPE QDAQRFFHQL MAGVVYLHGI GITHRDIKPE NLLLDERDNL KISDFGLATV 70 80 90 100 110 120 FRHNNRERLL NKMCGTLPYV APELLKRKEF HAEPVDVWSC GIVLTAMLAG ELPWDQPSDS 130 140 150 160 170 180 CQEYSDWKEK KTYLNPWKKI DSAPLALLHK ILVETPSARI TIPDIKKDRW YNKPLNRGAK 190 200 210 220 230 240 RPRATSGGMS ESSSGFSKHI HSNLDFSPVN NGSSEETVKF SSSQPEPRTG LSLWDTGPSN 250 260 270 280 290 300 VDKLVQGISF SQPTCPEHML VNSQLLGTPG SSQNPWQRLV KRMTRFFTKL DADKSYQCLK 310 320 330 340 350 360 ETFEKLGYQW KKSCMNQVTV STTDRRNNKL IFKINLVEMD EKILVDFRLS KGDGLEFKRH 370 380 FLKIKGKLSD VVSSQKVWFP VT

References

	« Hide 'large scale' referencesShow '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. , 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]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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.
IPI	IPI00229735. IPI00387390.
RefSeq	NP_031717.2. NM_007691.5.
UniGene	Mm.16753.
3D structure databases
ProteinModelPortal	O35280.
SMR	O35280. Positions 2-304.
ModBase	Search...
Protein-protein interaction databases
IntAct	O35280. 1 interaction.
MINT	MINT-1340615.
PTM databases
PhosphoSite	O35280.
Proteomic databases
PRIDE	O35280.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034625; ENSMUSP00000034625; ENSMUSG00000032113. ENSMUST00000172702; ENSMUSP00000134388; ENSMUSG00000032113.
GeneID	12649.
KEGG	mmu:12649.
UCSC	uc009otv.1. mouse. uc009otx.2. mouse.
Organism-specific databases
CTD	1111.
MGI	MGI:1202065. Chek1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00680000099954.
HOGENOM	HOG000216658.
HOVERGEN	HBG002590.
InParanoid	O35280.
KO	K02216.
OMA	GGFSKHI.
OrthoDB	EOG4001JD.
Enzyme and pathway databases
BRENDA	2.7.11.1. 3474.
Reactome	REACT_118161. Cell Cycle.
Gene expression databases
ArrayExpress	O35280.
Bgee	O35280.
CleanEx	MM_CHEK1.
Genevestigator	O35280.
GermOnline	ENSMUSG00000032113. Mus musculus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	281856.
SOURCE	Search...

Entry information

Entry name

CHK1_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program