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Protein

Serine/threonine-protein kinase grp

Gene

grp

Organism
Drosophila melanogaster (Fruit fly)
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. May phosphorylate the CDC25 phosphatase stg, which promotes its degradation. This results in increased inhibitory tyrosine phosphorylation of Cdk1-cyclin complexes and consequent inhibition of cell cycle progression.11 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511ATPPROSITE-ProRule annotationBy similarity
Active sitei143 – 1431Proton acceptorCurated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi28 – 369ATPPROSITE-ProRule annotationBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein kinase activity Source: BHF-UCL
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • cell cycle arrest Source: FlyBase
  • cell cycle checkpoint Source: UniProtKB
  • cellularization Source: FlyBase
  • centrosome separation Source: FlyBase
  • DNA damage checkpoint Source: UniProtKB
  • embryonic development via the syncytial blastoderm Source: FlyBase
  • female meiosis chromosome segregation Source: FlyBase
  • imaginal disc development Source: FlyBase
  • mitotic cell cycle checkpoint Source: FlyBase
  • mitotic DNA replication checkpoint Source: FlyBase
  • mitotic G2 DNA damage checkpoint Source: FlyBase
  • protein phosphorylation Source: UniProtKB
  • regulation of syncytial blastoderm mitotic cell cycle Source: UniProtKB
  • response to radiation Source: FlyBase
  • spindle assembly Source: FlyBase
  • wound healing Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, DNA damage

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-176187. Activation of ATR in response to replication stress.
R-DME-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-DME-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
SignaLinkiO61661.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase grp (EC:2.7.11.1)
Alternative name(s):
Chk1 homolog
Protein grapes
Gene namesi
Name:grpImported
ORF Names:CG17161Imported
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0261278. grp.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: FlyBase
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi143 – 1431D → A: Abolishes kinase activity. 1 Publication
Mutagenesisi189 – 1891P → L: Impaired cell cycle arrest in response to the DNA synthesis inhibitor hydroxyurea (HU). 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 512512Serine/threonine-protein kinase grpPRO_0000085855Add
BLAST

Post-translational modificationi

Phosphorylated in a MEI-41/ATR dependent manner in response to DNA damage or the presence of unreplicated DNA.1 Publication

Proteomic databases

PaxDbiO61661.

Expressioni

Developmental stagei

Expressed both maternally and zygotically. Maternally supplied mRNA is degraded during progression from nuclear stage 12 to nuclear stage 13. Zygotic expression is seen at reduced levels later in embryogenesis and during larval development. Higher expression is seen in pupae, coincident with ovarian differentiation. May be activated during the syncytial blastoderm divisions which precede cellularization, the Drosophila equivalent of the midblastula transition (MBT). Developmentally regulated activation of the DNA replication checkpoint may occur as the nucleo-cytoplasmic ratio increases and maternal replication factors are depleted. Elongation of the embryonic cell cycle may allow time for the transcription of genes that initiate the switch from maternal to zygotic control of embryogenesis.2 Publications

Gene expression databases

BgeeiO61661.
ExpressionAtlasiO61661. differential.
GenevisibleiO61661. DM.

Interactioni

Protein-protein interaction databases

BioGridi61001. 37 interactions.
IntActiO61661. 25 interactions.
MINTiMINT-328549.
STRINGi7227.FBpp0080441.

Structurei

3D structure databases

ProteinModelPortaliO61661.
SMRiO61661. Positions 18-317.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 279258Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0590. Eukaryota.
ENOG410XQ0D. LUCA.
GeneTreeiENSGT00680000099954.
InParanoidiO61661.
KOiK02216.
OMAiICSPKAK.
OrthoDBiEOG712TWF.
PhylomeDBiO61661.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
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]

Sequencei

Sequence statusi: Complete.

O61661-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATLTEAGT GPAATREFVE GWTLAQTLGE GAYGEVKLLI NRQTGEAVAM
60 70 80 90 100
KMVDLKKHPD AANSVRKEVC IQKMLQDKHI LRFFGKRSQG SVEYIFLEYA
110 120 130 140 150
AGGELFDRIE PDVGMPQHEA QRYFTQLLSG LNYLHQRGIA HRDLKPENLL
160 170 180 190 200
LDEHDNVKIS DFGMATMFRC KGKERLLDKR CGTLPYVAPE VLQKAYHAQP
210 220 230 240 250
ADLWSCGVIL VTMLAGELPW DQPSTNCTEF TNWRDNDHWQ LQTPWSKLDT
260 270 280 290 300
LAISLLRKLL ATSPGTRLTL EKTLDHKWCN MQFADNERSY DLVDSAAALE
310 320 330 340 350
ICSPKAKRQR LQSSAHLSNG LDDSISRNYC SQPMPTMRSD DDFNVRLGSG
360 370 380 390 400
RSKEDGGDRQ TLAQEARLSY SFSQPALLDD LLLATQMNQT QNASQNYFQR
410 420 430 440 450
LVRRMTRFFV TTRWDDTIKR LVGTIERLGG YTCKFGDDGV VTVSTVDRNK
460 470 480 490 500
LRLVFKAHII EMDGKILVDC RLSKGCGLEF KRRFIKIKNA LEDIVLKGPT
510
TWPIAIATNS VP
Length:512
Mass (Da):57,833
Last modified:October 10, 2003 - v2
Checksum:i504CAB3C0B642EA0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 494EAVA → GGCG in AAC13566 (PubMed:9197245).Curated
Sequence conflicti197 – 1982HA → QP in AAC13566 (PubMed:9197245).Curated
Sequence conflicti260 – 2601L → LL in AAC13566 (PubMed:9197245).Curated
Sequence conflicti339 – 3391S → T in AAC13566 (PubMed:9197245).Curated
Sequence conflicti352 – 3598SKEDGGDR → IQGGWRRP in AAC13566 (PubMed:9197245).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF057041 mRNA. Translation: AAC13566.1.
AE014134 Genomic DNA. Translation: AAF53551.2.
AE014134 Genomic DNA. Translation: AAF53552.2.
AE014134 Genomic DNA. Translation: AAN10952.1.
AY051961 mRNA. Translation: AAK93385.1.
RefSeqiNP_477011.1. NM_057663.4.
NP_723985.1. NM_165171.3.
NP_723986.1. NM_165172.3.
UniGeneiDm.7018.

Genome annotation databases

EnsemblMetazoaiFBtr0080884; FBpp0080441; FBgn0261278.
FBtr0080885; FBpp0080442; FBgn0261278.
FBtr0080886; FBpp0080443; FBgn0261278.
GeneIDi34993.
KEGGidme:Dmel_CG17161.
UCSCiCG17161-RB. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF057041 mRNA. Translation: AAC13566.1.
AE014134 Genomic DNA. Translation: AAF53551.2.
AE014134 Genomic DNA. Translation: AAF53552.2.
AE014134 Genomic DNA. Translation: AAN10952.1.
AY051961 mRNA. Translation: AAK93385.1.
RefSeqiNP_477011.1. NM_057663.4.
NP_723985.1. NM_165171.3.
NP_723986.1. NM_165172.3.
UniGeneiDm.7018.

3D structure databases

ProteinModelPortaliO61661.
SMRiO61661. Positions 18-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61001. 37 interactions.
IntActiO61661. 25 interactions.
MINTiMINT-328549.
STRINGi7227.FBpp0080441.

Proteomic databases

PaxDbiO61661.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0080884; FBpp0080441; FBgn0261278.
FBtr0080885; FBpp0080442; FBgn0261278.
FBtr0080886; FBpp0080443; FBgn0261278.
GeneIDi34993.
KEGGidme:Dmel_CG17161.
UCSCiCG17161-RB. d. melanogaster.

Organism-specific databases

CTDi2922.
FlyBaseiFBgn0261278. grp.

Phylogenomic databases

eggNOGiKOG0590. Eukaryota.
ENOG410XQ0D. LUCA.
GeneTreeiENSGT00680000099954.
InParanoidiO61661.
KOiK02216.
OMAiICSPKAK.
OrthoDBiEOG712TWF.
PhylomeDBiO61661.

Enzyme and pathway databases

ReactomeiR-DME-176187. Activation of ATR in response to replication stress.
R-DME-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-DME-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
SignaLinkiO61661.

Miscellaneous databases

GenomeRNAii34993.
PROiO61661.

Gene expression databases

BgeeiO61661.
ExpressionAtlasiO61661. differential.
GenevisibleiO61661. DM.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila grapes gene is related to checkpoint gene chk1/rad27 and is required for late syncytial division fidelity."
    Fogarty P., Campbell S.D., Abu-Shumays R., de Saint Phalle B., Yu K.R., Uy G.L., Goldberg M.L., Sullivan W.
    Curr. Biol. 7:418-426(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication.
  5. "The Drosophila maternal-effect mutation grapes causes a metaphase arrest at nuclear cycle 13."
    Fogarty P., Kalpin R.F., Sullivan W.
    Development 120:2131-2142(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "DNA-replication checkpoint control at the Drosophila midblastula transition."
    Sibon O.C.M., Stevenson V.A., Theurkauf W.E.
    Nature 388:93-97(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
  7. "The Drosophila ATM homologue Mei-41 has an essential checkpoint function at the midblastula transition."
    Sibon O.C.M., Laurencon A., Hawley R., Theurkauf W.E.
    Curr. Biol. 9:302-312(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Drosophila grapes/CHK1 mutants are defective in cyclin proteolysis and coordination of mitotic events."
    Su T.T., Campbell S.D., O'Farrell P.H.
    Curr. Biol. 9:919-922(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "The grapes checkpoint coordinates nuclear envelope breakdown and chromosome condensation."
    Yu K.R., Saint R.B., Sullivan W.
    Nat. Cell Biol. 2:609-615(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. Cited for: MUTAGENESIS OF ASP-143.
  11. "Control of cleavage cycles in Drosophila embryos by fruhstart."
    Grosshans J., Mueller H.A.J., Wieschaus E.
    Dev. Cell 5:285-294(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Relative contribution of DNA repair, cell cycle checkpoints, and cell death to survival after DNA damage in Drosophila larvae."
    Jaklevic B.R., Su T.T.
    Curr. Biol. 14:23-32(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "The Drosophila Grp/Chk1 DNA damage checkpoint controls entry into anaphase."
    Royou A., Macias H., Sullivan W.
    Curr. Biol. 15:334-339(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Grp/DChk1 is required for G2-M checkpoint activation in Drosophila S2 cells, whereas Dmnk/DChk2 is dispensable."
    de Vries H.I., Uyetake L., Lemstra W., Brunsting J.F., Su T.T., Kampinga H.H., Sibon O.C.M.
    J. Cell Sci. 118:1833-1842(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION.
  15. "Regulation of mitosis in response to damaged or incompletely replicated DNA require different levels of grapes (Drosophila Chk1)."
    Purdy A., Uyetake L., Cordeiro M.G., Su T.T.
    J. Cell Sci. 118:3305-3315(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  16. "Drosophila Claspin is required for the G2 arrest that is induced by DNA replication stress but not by DNA double-strand breaks."
    Lee E.M., Trinh T.T., Shim H.J., Park S.Y., Nguyen T.T., Kim M.J., Song Y.H.
    DNA Repair 11:741-752(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF PRO-189.

Entry informationi

Entry nameiCHK1_DROME
AccessioniPrimary (citable) accession number: O61661
Secondary accession number(s): A4V0S9, Q960N7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: October 10, 2003
Last modified: June 8, 2016
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

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.