CDC7_MOUSE
ID CDC7_MOUSE Reviewed; 564 AA.
AC Q9Z0H0; Q9WUV1; Q9Z2Y7;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Cell division cycle 7-related protein kinase;
DE Short=CDC7-related kinase;
DE Short=muCdc7;
DE EC=2.7.11.1;
GN Name=Cdc7; Synonyms=Cdc7l1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Liver;
RX PubMed=9722556; DOI=10.1074/jbc.273.36.23248;
RA Kim J., Sato N., Yamada M., Arai K., Masai H.;
RT "Growth regulation of the expression of mouse cDNA and gene encoding a
RT serine/threonine kinase related to Saccharomyces cerevisiae CDC7 essential
RT for G1/S transition. Structure, chromosomal localization, and expression of
RT mouse gene for s. cerevisiae Cdc7-related kinase.";
RL J. Biol. Chem. 273:23248-23257(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10199953; DOI=10.1007/s004120050348;
RA Faul T., Staib C., Nanda I., Schmid M., Grummt F.;
RT "Identification and characterization of mouse homologue to yeast Cdc7
RT protein and chromosomal localization of the cognate mouse gene Cdc7l.";
RL Chromosoma 108:26-31(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH DBF4.
RC STRAIN=C57BL/6J; TISSUE=Egg, and Embryo;
RX PubMed=10517317; DOI=10.1007/s004380051078;
RA Lepke M., Puetter V., Staib C., Kneissl M., Berger C., Hoehn K., Nanda I.,
RA Schmid M., Grummt F.;
RT "Identification, characterization and chromosomal localization of the
RT cognate human and murine DBF4 genes.";
RL Mol. Gen. Genet. 262:220-229(1999).
CC -!- FUNCTION: Seems to phosphorylate critical substrates that regulate the
CC G1/S phase transition and/or DNA replication. Can phosphorylate MCM2
CC and MCM3.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Forms a complex with either DBF4/DBF4A or DBF4B, leading to
CC the activation of the kinase activity.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9Z0H0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z0H0-2; Sequence=VSP_004864;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC7 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AB019388; BAA34347.1; -; Genomic_DNA.
DR EMBL; AB018575; BAA33881.1; -; mRNA.
DR EMBL; AB018574; BAA33880.1; -; mRNA.
DR EMBL; AJ007661; CAB40539.1; -; mRNA.
DR EMBL; AK145921; BAE26752.1; -; mRNA.
DR EMBL; CH466529; EDL20174.1; -; Genomic_DNA.
DR EMBL; BC072666; AAH72666.1; -; mRNA.
DR CCDS; CCDS19498.1; -. [Q9Z0H0-1]
DR CCDS; CCDS71628.1; -. [Q9Z0H0-2]
DR RefSeq; NP_001258495.1; NM_001271566.1. [Q9Z0H0-1]
DR RefSeq; NP_001258496.1; NM_001271567.1. [Q9Z0H0-2]
DR RefSeq; NP_001258497.1; NM_001271568.1.
DR RefSeq; NP_033993.2; NM_009863.3. [Q9Z0H0-1]
DR AlphaFoldDB; Q9Z0H0; -.
DR SMR; Q9Z0H0; -.
DR BioGRID; 198629; 6.
DR IntAct; Q9Z0H0; 1.
DR MINT; Q9Z0H0; -.
DR STRING; 10090.ENSMUSP00000031221; -.
DR iPTMnet; Q9Z0H0; -.
DR PhosphoSitePlus; Q9Z0H0; -.
DR EPD; Q9Z0H0; -.
DR MaxQB; Q9Z0H0; -.
DR PaxDb; Q9Z0H0; -.
DR PRIDE; Q9Z0H0; -.
DR ProteomicsDB; 281514; -. [Q9Z0H0-1]
DR ProteomicsDB; 281515; -. [Q9Z0H0-2]
DR Antibodypedia; 3628; 322 antibodies from 36 providers.
DR DNASU; 12545; -.
DR Ensembl; ENSMUST00000031221; ENSMUSP00000031221; ENSMUSG00000029283. [Q9Z0H0-1]
DR Ensembl; ENSMUST00000117196; ENSMUSP00000112392; ENSMUSG00000029283. [Q9Z0H0-2]
DR Ensembl; ENSMUST00000118261; ENSMUSP00000113385; ENSMUSG00000029283. [Q9Z0H0-1]
DR GeneID; 12545; -.
DR KEGG; mmu:12545; -.
DR UCSC; uc008ylw.2; mouse. [Q9Z0H0-1]
DR UCSC; uc008ylx.2; mouse. [Q9Z0H0-2]
DR CTD; 8317; -.
DR MGI; MGI:1309511; Cdc7.
DR VEuPathDB; HostDB:ENSMUSG00000029283; -.
DR eggNOG; KOG1167; Eukaryota.
DR GeneTree; ENSGT00550000075011; -.
DR HOGENOM; CLU_000288_118_1_1; -.
DR InParanoid; Q9Z0H0; -.
DR OMA; FYTKMDV; -.
DR OrthoDB; 1361975at2759; -.
DR PhylomeDB; Q9Z0H0; -.
DR TreeFam; TF101052; -.
DR BRENDA; 2.7.11.1; 3474.
DR Reactome; R-MMU-176187; Activation of ATR in response to replication stress.
DR Reactome; R-MMU-68962; Activation of the pre-replicative complex.
DR BioGRID-ORCS; 12545; 22 hits in 115 CRISPR screens.
DR PRO; PR:Q9Z0H0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9Z0H0; protein.
DR Bgee; ENSMUSG00000029283; Expressed in otic placode and 247 other tissues.
DR ExpressionAtlas; Q9Z0H0; baseline and differential.
DR Genevisible; Q9Z0H0; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0044770; P:cell cycle phase transition; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Isopeptide bond; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..564
FT /note="Cell division cycle 7-related protein kinase"
FT /id="PRO_0000085764"
FT DOMAIN 52..564
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 460..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 171
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 58..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00311"
FT CROSSLNK 260
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00311"
FT VAR_SEQ 267..298
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9722556"
FT /id="VSP_004864"
FT CONFLICT 38
FT /note="I -> F (in Ref. 1; BAA34347/BAA33881/BAA33880)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="C -> G (in Ref. 1; BAA34347/BAA33881/BAA33880)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="F -> S (in Ref. 1; BAA34347/BAA33881/BAA33880)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="D -> N (in Ref. 1; BAA34347/BAA33881/BAA33880)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="K -> R (in Ref. 1; BAA34347/BAA33881/BAA33880)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="A -> V (in Ref. 1; BAA34347/BAA33881/BAA33880)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 564 AA; 62770 MW; 82BD6617F70FB240 CRC64;
MEEPMAFSSL RGSDRCPADD SLKKYEQSVK LSGIKRDIEE LCEAVPQLVN VFKIKDKIGE
GTFSSVYLAT AQLQEGHEEK IALKHLIPTS HPMRIAAELQ CLTVAGGQDN VMGLKYCFRK
NDHVVIAMPY LEHESFLDIL NSLSFQEVRE YMYNLFVALK RIHQFGIVHR DVKPSNFLYN
RRLKKYALVD FGLAQGTRDT KIELLKFVQS EAQQEDCSRN KYHGVVGHKG LLSRPAPKTV
DQQCTPKTSV KRSYTQVHIK QGKDGKERSV GLSVQRSVFG ERNFNIHSSI SHESPAEKLI
KQSKTVDIIS RKLATKKTAI STKAMNSVMR ETARSCPAVL TCDCYGSDRV CSVCLSRRQQ
VAPRAGTPGF RAPEVLTKCP DQTTAIDMWS AGVIFLSLLS GRYPFYKASD DLTALAQIMT
IRGSRETIQA AKAFGKSVLC SKEVPAQDLR ALCERLRGLD STTPRSASGP PGNASYDPAA
SKNTDHKASR VQAAQAQHSE DSLYKRDNDG YWSHPKDCTS NSEGWDSVPD EAYDLLDKLL
DLNPASRITA EAALLHAFFK DMCS
