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UniProtKB - O14757 (CHK1_HUMAN)

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Protein

Serine/threonine-protein kinase Chk1

Gene

CHEK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C. Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis of CDC25A. Phosphorylation of CDC25A at 'Ser-76' primes the protein for subsequent phosphorylation at 'Ser-79', 'Ser-82' and 'Ser-88' by NEK11, which is required for polyubiquitination and degradation of CDCD25A. 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 at 'Ser-743', 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. 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.
Isoform 2: Endogenous repressor of isoform 1, interacts with, and antagonizes CHK1 to promote the S to G2/M phase transition.

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei38ATPPROSITE-ProRule annotation1
Active sitei130Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi15 – 23ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • histone kinase activity (H3-T11 specific) Source: UniProtKB
  • kinase activity Source: Reactome
  • protein domain specific binding Source: CAFA
  • protein kinase activity Source: CACAO
  • protein serine/threonine kinase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to mechanical stimulus Source: UniProtKB
  • chromatin-mediated maintenance of transcription Source: UniProtKB
  • DNA damage checkpoint Source: UniProtKB
  • DNA damage induced protein phosphorylation Source: UniProtKB
  • DNA repair Source: UniProtKB
  • DNA replication Source: Reactome
  • G2 DNA damage checkpoint Source: UniProtKB
  • intracellular signal transduction Source: GO_Central
  • negative regulation of mitotic nuclear division Source: UniProtKB
  • peptidyl-threonine phosphorylation Source: UniProtKB
  • positive regulation of cell cycle Source: CAFA
  • regulation of double-strand break repair via homologous recombination Source: UniProtKB
  • regulation of histone H3-K9 acetylation Source: UniProtKB
  • regulation of mitotic centrosome separation Source: UniProtKB
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage Source: UniProtKB
  • replicative senescence Source: BHF-UCL
Complete GO annotation...

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, DNA damage, DNA repair
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-1433557. Signaling by SCF-KIT.
R-HSA-176187. Activation of ATR in response to replication stress.
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
SignaLinkiO14757.
SIGNORiO14757.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase Chk1 (EC:2.7.11.1)
Alternative name(s):
CHK1 checkpoint homolog
Cell cycle checkpoint kinase
Checkpoint kinase-1
Gene namesi
Name:CHEK1
Synonyms:CHK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:1925. CHEK1.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • chromatin Source: UniProtKB
  • condensed nuclear chromosome Source: UniProtKB
  • cytoplasm Source: CAFA
  • cytosol Source: Reactome
  • extracellular space Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • protein complex Source: CAFA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi38K → R: Abolishes kinase activity. 2 Publications1
Mutagenesisi130D → A: Abolishes kinase activity. 8 Publications1
Mutagenesisi317S → A: Abrogates interaction with RAD51; when associated with A-345. Reduces phosphorylation and impairs activation by hydroxyurea and ionizing radiation. Abrogates nuclear retention upon checkpoint activation. Impairs interaction with FBXO6. 5 Publications1
Mutagenesisi317S → E: Enhances interaction with RAD51; when associated with E-345. 5 Publications1
Mutagenesisi344F → A: Impairs nuclear export. 1 Publication1
Mutagenesisi345S → A: Abrogates interaction with RAD51; when associated with A-317. Reduces phosphorylation and impairs activation by hydroxyurea and ionizing radiation. Impairs interaction with YWHAZ which is required for nuclear retention after checkpoint activation. 6 Publications1
Mutagenesisi345S → E: Enhances interaction with RAD51; when associated with E-317. 6 Publications1
Mutagenesisi353M → A: Impairs nuclear export. 1 Publication1
Mutagenesisi357S → A: No effect on phosphorylation induced by hydroxyurea. 1 Publication1
Mutagenesisi366S → A: No effect on phosphorylation induced by hydroxyurea. 1 Publication1
Mutagenesisi372R → E in 3RE mutant. Disrupts the folding and/or conformation, allowing increased accessibility to FBXO6 component of SCF-type E3 ubiquitin ligase complex; when associated with E-376 and E-379. 1 Publication1
Mutagenesisi376R → E in 3RE mutant. Disrupts the folding and/or conformation, allowing increased accessibility to FBXO6 component of SCF-type E3 ubiquitin ligase complex; when associated with E-372 and E-379. 1 Publication1
Mutagenesisi379R → E in 3RE mutant. Disrupts the folding and/or conformation, allowing increased accessibility to FBXO6 component of SCF-type E3 ubiquitin ligase complex; when associated with E-372 and E-376. 1 Publication1
Mutagenesisi436K → R: Enhances stability of the protein, probably by preventing ubiquitination at this site. 1 Publication1
Mutagenesisi468S → A: No effect on phosphorylation induced by hydroxyurea. 1 Publication1

Organism-specific databases

DisGeNETi1111.
OpenTargetsiENSG00000149554.
PharmGKBiPA110.

Chemistry databases

ChEMBLiCHEMBL4630.
DrugBankiDB07037. (2S)-1-AMINO-3-[(5-NITROQUINOLIN-8-YL)AMINO]PROPAN-2-OL.
DB07228. 1-(5-CHLORO-2-METHOXYPHENYL)-3-{6-[2-(DIMETHYLAMINO)-1-METHYLETHOXY]PYRAZIN-2-YL}UREA.
DB07038. 2-(cyclohexylamino)benzoic acid.
DB08779. 2-(methylsulfanyl)-5-(thiophen-2-ylmethyl)-1H-imidazol-4-ol.
DB07959. 3-(1H-BENZIMIDAZOL-2-YL)-1H-INDAZOLE.
DB07075. 3-(5-{[4-(AMINOMETHYL)PIPERIDIN-1-YL]METHYL}-1H-INDOL-2-YL)-1H-INDAZOLE-6-CARBONITRILE.
DB07025. 3-(5-{[4-(AMINOMETHYL)PIPERIDIN-1-YL]METHYL}-1H-INDOL-2-YL)QUINOLIN-2(1H)-ONE.
DB06852. 4-[(3S)-1-AZABICYCLO[2.2.2]OCT-3-YLAMINO]-3-(1H-BENZIMIDAZOL-2-YL)-6-CHLOROQUINOLIN-2(1H)-ONE.
DB07336. 4-[3-(1H-BENZIMIDAZOL-2-YL)-1H-INDAZOL-6-YL]-2-METHOXYPHENOL.
DB08780. 6-MORPHOLIN-4-YL-9H-PURINE.
DB05149. XL844.
GuidetoPHARMACOLOGYi1987.

Polymorphism and mutation databases

BioMutaiCHEK1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000858481 – 476Serine/threonine-protein kinase Chk1Add BLAST476

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei280PhosphoserineCombined sources1
Modified residuei286PhosphoserineCombined sources1
Modified residuei296PhosphoserineCombined sources1 Publication1
Modified residuei301PhosphoserineCombined sources1
Modified residuei317Phosphoserine; by ATM and ATR9 Publications1
Modified residuei331PhosphoserineCombined sources1
Modified residuei345Phosphoserine; by ATM and ATR12 Publications1
Cross-linki436Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei467PhosphoserineCombined sources1
Modified residuei468PhosphoserineCombined sources1

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.15 Publications
Ubiquitinated. Mono or diubiquitination promotes nuclear exclusion (By similarity). 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. 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 similarity12 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO14757.
MaxQBiO14757.
PaxDbiO14757.
PeptideAtlasiO14757.
PRIDEiO14757.

PTM databases

iPTMnetiO14757.
PhosphoSitePlusiO14757.

Expressioni

Tissue specificityi

Expressed ubiquitously with the most abundant expression in thymus, testis, small intestine and colon.2 Publications

Gene expression databases

BgeeiENSG00000149554.
CleanExiHS_CHEK1.
ExpressionAtlasiO14757. baseline and differential.
GenevisibleiO14757. HS.

Organism-specific databases

HPAiHPA044364.

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. Isoform 1 associates with isoform 2, the interaction is disrupted upon phosphorylation by ATR. Interacts with CDK5RAP3; antagonizes CHEK1 (PubMed:19223857).12 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein domain specific binding Source: CAFA
Complete GO annotation...

Protein-protein interaction databases

BioGridi107536. 110 interactors.
DIPiDIP-24182N.
IntActiO14757. 36 interactors.
MINTiMINT-1179072.
STRINGi9606.ENSP00000388648.

Chemistry databases

BindingDBiO14757.

Structurei

Secondary structure

1476
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 8Combined sources6
Beta strandi9 – 17Combined sources9
Beta strandi19 – 28Combined sources10
Turni29 – 31Combined sources3
Beta strandi34 – 41Combined sources8
Helixi42 – 44Combined sources3
Helixi48 – 60Combined sources13
Beta strandi70 – 76Combined sources7
Beta strandi79 – 85Combined sources7
Beta strandi88 – 91Combined sources4
Helixi92 – 95Combined sources4
Turni98 – 100Combined sources3
Helixi104 – 123Combined sources20
Beta strandi125 – 127Combined sources3
Helixi133 – 135Combined sources3
Beta strandi136 – 138Combined sources3
Beta strandi144 – 146Combined sources3
Helixi149 – 151Combined sources3
Beta strandi153 – 157Combined sources5
Helixi171 – 173Combined sources3
Helixi176 – 179Combined sources4
Beta strandi182 – 184Combined sources3
Helixi186 – 203Combined sources18
Beta strandi209 – 211Combined sources3
Beta strandi213 – 215Combined sources3
Helixi216 – 222Combined sources7
Beta strandi227 – 229Combined sources3
Helixi231 – 233Combined sources3
Helixi236 – 245Combined sources10
Turni250 – 252Combined sources3
Helixi256 – 259Combined sources4
Turni263 – 266Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IA8X-ray1.70A1-289[»]
1NVQX-ray2.00A1-289[»]
1NVRX-ray1.80A1-289[»]
1NVSX-ray1.80A1-289[»]
1ZLTX-ray1.74A1-289[»]
1ZYSX-ray1.70A1-273[»]
2AYPX-ray2.90A1-269[»]
2BR1X-ray2.00A1-289[»]
2BRBX-ray2.10A1-289[»]
2BRGX-ray2.10A1-289[»]
2BRHX-ray2.10A1-289[»]
2BRMX-ray2.20A1-289[»]
2BRNX-ray2.80A1-289[»]
2BROX-ray2.20A1-289[»]
2C3JX-ray2.10A1-289[»]
2C3KX-ray2.60A1-289[»]
2C3LX-ray2.35A1-289[»]
2CGUX-ray2.50A1-289[»]
2CGVX-ray2.60A1-289[»]
2CGWX-ray2.20A1-289[»]
2CGXX-ray2.20A1-289[»]
2E9NX-ray2.50A2-270[»]
2E9OX-ray2.10A2-270[»]
2E9PX-ray2.60A2-270[»]
2E9UX-ray2.00A2-270[»]
2E9VX-ray2.00A/B2-269[»]
2GDOX-ray3.00A1-289[»]
2GHGX-ray3.50A2-270[»]
2HOGX-ray1.90A2-307[»]
2HXLX-ray1.80A2-307[»]
2HXQX-ray2.00A2-307[»]
2HY0X-ray1.70A2-307[»]
2QHMX-ray2.00A1-307[»]
2QHNX-ray1.70A1-307[»]
2R0UX-ray1.90A1-307[»]
2WMQX-ray2.48A1-289[»]
2WMRX-ray2.43A1-289[»]
2WMSX-ray2.70A1-289[»]
2WMTX-ray2.55A1-289[»]
2WMUX-ray2.60A1-289[»]
2WMVX-ray2.01A1-289[»]
2WMWX-ray2.43A1-289[»]
2WMXX-ray2.45A1-289[»]
2X8DX-ray1.90A1-289[»]
2X8EX-ray2.50A1-276[»]
2X8IX-ray1.92A1-289[»]
2XEYX-ray2.70A1-289[»]
2XEZX-ray2.25A1-289[»]
2XF0X-ray2.40A1-289[»]
2YDIX-ray1.60A1-289[»]
2YDJX-ray1.85A/B1-276[»]
2YDKX-ray1.90A1-276[»]
2YERX-ray1.83A1-276[»]
2YEXX-ray1.30A1-276[»]
2YM3X-ray2.01A1-289[»]
2YM4X-ray2.35A1-289[»]
2YM5X-ray2.03A1-289[»]
2YM6X-ray2.01A1-289[»]
2YM7X-ray1.81A1-289[»]
2YM8X-ray2.07A1-289[»]
2YWPX-ray2.90A2-270[»]
3F9NX-ray1.90A2-307[»]
3JVRX-ray1.76A2-272[»]
3JVSX-ray1.90A2-272[»]
3NLBX-ray1.90A1-289[»]
3OT3X-ray1.44A2-274[»]
3OT8X-ray1.65A2-274[»]
3PA3X-ray1.40A2-274[»]
3PA4X-ray1.59A2-274[»]
3PA5X-ray1.70A2-274[»]
3TKHX-ray1.79A1-307[»]
3TKIX-ray1.60A1-307[»]
3U9NX-ray1.85A2-274[»]
4FSMX-ray2.30A2-280[»]
4FSNX-ray2.10A4-280[»]
4FSQX-ray2.40A2-280[»]
4FSRX-ray2.50A2-280[»]
4FSTX-ray1.90A2-270[»]
4FSUX-ray2.10A2-280[»]
4FSWX-ray2.30A2-280[»]
4FSYX-ray2.30A2-280[»]
4FSZX-ray2.30A2-280[»]
4FT0X-ray2.30A2-280[»]
4FT3X-ray2.50A2-280[»]
4FT5X-ray2.40A2-280[»]
4FT7X-ray2.20A2-280[»]
4FT9X-ray2.20A2-280[»]
4FTAX-ray2.40A2-280[»]
4FTCX-ray2.00A2-280[»]
4FTIX-ray2.20A2-280[»]
4FTJX-ray2.20A2-280[»]
4FTKX-ray2.30A2-280[»]
4FTLX-ray2.50A2-280[»]
4FTMX-ray1.90A2-280[»]
4FTNX-ray2.02A2-280[»]
4FTOX-ray2.10A2-280[»]
4FTQX-ray2.00A2-280[»]
4FTRX-ray2.25A2-280[»]
4FTTX-ray2.30A2-280[»]
4FTUX-ray2.10A2-280[»]
4GH2X-ray2.03A2-280[»]
4HYHX-ray1.70A1-289[»]
4HYIX-ray1.40A1-289[»]
4JIKX-ray1.90A2-274[»]
4QYEX-ray2.05A1-289[»]
4QYFX-ray2.15A1-289[»]
4QYGX-ray1.75A/B1-289[»]
4QYHX-ray1.90A/B1-289[»]
4RVKX-ray1.85A1-289[»]
4RVLX-ray1.85A1-289[»]
4RVMX-ray1.86A1-289[»]
5DLSX-ray2.15A1-289[»]
5F4NX-ray1.91A1-273[»]
ProteinModelPortaliO14757.
SMRiO14757.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14757.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 265Protein kinasePROSITE-ProRule annotationAdd BLAST257

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 265Interaction with CLSPNBy similarityAdd BLAST265
Regioni391 – 476Autoinhibitory regionAdd BLAST86

Domaini

The autoinhibitory region (AIR) inhibits the activity of the kinase domain.1 Publication

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0590. Eukaryota.
ENOG410XQ0D. LUCA.
GeneTreeiENSGT00870000136514.
HOGENOMiHOG000216658.
HOVERGENiHBG002590.
InParanoidiO14757.
KOiK02216.
OMAiAQPADIW.
PhylomeDBiO14757.
TreeFamiTF351441.

Family and domain databases

CDDicd14069. STKc_Chk1. 1 hit.
InterProiView protein in InterPro
IPR034670. Chk1_catalytic_dom.
IPR011009. Kinase-like_dom.
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. 2 hits.
PROSITEiView protein in PROSITE
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O14757-1) [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

        10         20         30         40         50
MAVPFVEDWD LVQTLGEGAY GEVQLAVNRV TEEAVAVKIV DMKRAVDCPE 
        60         70         80         90        100
NIKKEICINK MLNHENVVKF YGHRREGNIQ YLFLEYCSGG ELFDRIEPDI 
       110        120        130        140        150
GMPEPDAQRF FHQLMAGVVY LHGIGITHRD IKPENLLLDE RDNLKISDFG 
       160        170        180        190        200
LATVFRYNNR ERLLNKMCGT LPYVAPELLK RREFHAEPVD VWSCGIVLTA 
       210        220        230        240        250
MLAGELPWDQ PSDSCQEYSD WKEKKTYLNP WKKIDSAPLA LLHKILVENP 
       260        270        280        290        300
SARITIPDIK KDRWYNKPLK KGAKRPRVTS GGVSESPSGF SKHIQSNLDF 
       310        320        330        340        350
SPVNSASSEE NVKYSSSQPE PRTGLSLWDT SPSYIDKLVQ GISFSQPTCP 
       360        370        380        390        400
DHMLLNSQLL GTPGSSQNPW QRLVKRMTRF FTKLDADKSY QCLKETCEKL 
       410        420        430        440        450
GYQWKKSCMN QVTISTTDRR NNKLIFKVNL LEMDDKILVD FRLSKGDGLE 
       460        470 
FKRHFLKIKG KLIDIVSSQK IWLPAT
Length:476
Mass (Da):54,434
Last modified:January 11, 2011 - v2
Checksum:i0ABD0FAB67E60F67
GO
Isoform 2 (identifier: O14757-2) [UniParc]FASTAAdd to basket
Also known as: Chk1-short, Chk1-S

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: Missing.
     95-97: RIE → MEK

Show »
Length:382
Mass (Da):43,703
Checksum:i3ECD01BEC168F007
GO
Isoform 3 (identifier: O14757-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     412-445: Missing.

Note: No experimental confirmation available.
Show »
Length:442
Mass (Da):50,415
Checksum:i05680C63BD1287B6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti163L → S in BAG56691 (PubMed:14702039).Curated1
Sequence conflicti220D → G in BAG61665 (PubMed:22184239).Curated1
Sequence conflicti381F → L in BAG61665 (PubMed:22184239).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_021123156R → Q1 PublicationCorresponds to variant dbSNP:rs3731410Ensembl.1
Natural variantiVAR_040407223E → V1 PublicationCorresponds to variant dbSNP:rs35817404Ensembl.1
Natural variantiVAR_040408312V → M1 PublicationCorresponds to variant dbSNP:rs34097480Ensembl.1
Natural variantiVAR_024571471I → V8 PublicationsCorresponds to variant dbSNP:rs506504Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0440081 – 94Missing in isoform 2. 2 PublicationsAdd BLAST94
Alternative sequenceiVSP_04400995 – 97RIE → MEK in isoform 2. 2 Publications3
Alternative sequenceiVSP_045075412 – 445Missing in isoform 3. 1 PublicationAdd BLAST34

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF016582 mRNA. Translation: AAC51736.1.
AF032874 mRNA. Translation: AAB88852.1.
AB032387 Genomic DNA. Translation: BAA84577.1.
JF289264 mRNA. Translation: AEB71796.1.
AK292549 mRNA. Translation: BAF85238.1.
AK293143 mRNA. Translation: BAG56691.1.
AK299783 mRNA. Translation: BAG61665.1.
AF527555 Genomic DNA. Translation: AAM78553.1.
AB451222 mRNA. Translation: BAG70036.1.
AB451345 mRNA. Translation: BAG70159.1.
AP001132 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67644.1.
BC004202 mRNA. Translation: AAH04202.1.
BC017575 mRNA. Translation: AAH17575.1.
CCDSiCCDS58191.1. [O14757-3]
CCDS81645.1. [O14757-2]
CCDS8459.1. [O14757-1]
RefSeqiNP_001107593.1. NM_001114121.2. [O14757-1]
NP_001107594.1. NM_001114122.2. [O14757-1]
NP_001231775.1. NM_001244846.1. [O14757-3]
NP_001265.2. NM_001274.5. [O14757-1]
NP_001317357.1. NM_001330428.1. [O14757-2]
XP_016872635.1. XM_017017146.1. [O14757-1]
UniGeneiHs.24529.
Hs.595920.

Genome annotation databases

EnsembliENST00000428830; ENSP00000412504; ENSG00000149554. [O14757-1]
ENST00000438015; ENSP00000388648; ENSG00000149554. [O14757-1]
ENST00000524737; ENSP00000432890; ENSG00000149554. [O14757-1]
ENST00000532449; ENSP00000481616; ENSG00000149554. [O14757-3]
ENST00000534070; ENSP00000435371; ENSG00000149554. [O14757-1]
ENST00000544373; ENSP00000442317; ENSG00000149554. [O14757-2]
GeneIDi1111.
KEGGihsa:1111.
UCSCiuc001qcf.5. human. [O14757-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiCHK1_HUMAN
AccessioniPrimary (citable) accession number: O14757
Secondary accession number(s): A8K934
, B4DDD0, B4DSK3, B5BTY6, F5H7S4, H2BI51
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 11, 2011
Last modified: June 7, 2017
This is version 201 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families