CDC6_MOUSE
ID CDC6_MOUSE Reviewed; 562 AA.
AC O89033; Q3TMD0; Q8C3S5; Q9CZT0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Cell division control protein 6 homolog;
DE AltName: Full=CDC6-related protein;
DE AltName: Full=p62(cdc6);
GN Name=Cdc6;
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 [MRNA].
RX PubMed=9774682; DOI=10.1128/mcb.18.11.6679;
RA Hateboer G., Wobst A., Petersen B.O., Le Cam L., Vigo E., Sardet C.,
RA Helin K.;
RT "Cell cycle-regulated expression of mammalian CDC6 is dependent on E2F.";
RL Mol. Cell. Biol. 18:6679-6697(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Strub A., Staib C., Grummt F.;
RT "A mouse related protein to human Cdc6.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-68; SER-72; SER-75 AND
RP SER-421, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in the initiation of DNA replication. Also
CC participates in checkpoint controls that ensure DNA replication is
CC completed before mitosis is initiated.
CC -!- SUBUNIT: Interacts with PCNA, ORC1, cyclin-CDK (By similarity).
CC Interacts with HUWE1 (By similarity). Interacts with ANKRD17 (By
CC similarity). Interacts with GRWD1; origin binding of GRWD1 is dependent
CC on CDC6 (By similarity). Interacts with CDT1; are mutually dependent on
CC one another for loading MCM complexes onto chromatin (By similarity).
CC Interacts with TTC4 (By similarity). Interacts (via Cy motif) with
CC CCNF; the interaction takes place during G2 and M phase (By
CC similarity). Interacts with CDH1 (By similarity).
CC {ECO:0000250|UniProtKB:Q99741}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99741}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q99741}. Note=The protein is nuclear in G1 and
CC cytoplasmic in S-phase cells. {ECO:0000250|UniProtKB:Q99741}.
CC -!- PTM: Ubiquitinated by the SCF(CCNF) E3 ubiquitin-protein ligase
CC complex. {ECO:0000250|UniProtKB:Q99741}.
CC -!- SIMILARITY: Belongs to the CDC6/cdc18 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA08752.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA11110.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ009559; CAA08752.1; ALT_INIT; mRNA.
DR EMBL; AJ223087; CAA11110.1; ALT_INIT; mRNA.
DR EMBL; AK012192; BAB28090.1; -; mRNA.
DR EMBL; AK085020; BAC39341.1; -; mRNA.
DR EMBL; AK166003; BAE38512.1; -; mRNA.
DR EMBL; BC052434; AAH52434.1; -; mRNA.
DR CCDS; CCDS25368.1; -.
DR RefSeq; NP_001020950.1; NM_001025779.1.
DR RefSeq; NP_035929.1; NM_011799.2.
DR AlphaFoldDB; O89033; -.
DR SMR; O89033; -.
DR BioGRID; 204750; 21.
DR IntAct; O89033; 19.
DR STRING; 10090.ENSMUSP00000091469; -.
DR iPTMnet; O89033; -.
DR PhosphoSitePlus; O89033; -.
DR EPD; O89033; -.
DR MaxQB; O89033; -.
DR PaxDb; O89033; -.
DR PRIDE; O89033; -.
DR ProteomicsDB; 283766; -.
DR Antibodypedia; 16461; 809 antibodies from 42 providers.
DR DNASU; 23834; -.
DR Ensembl; ENSMUST00000092706; ENSMUSP00000090382; ENSMUSG00000017499.
DR GeneID; 23834; -.
DR KEGG; mmu:23834; -.
DR UCSC; uc007lhu.1; mouse.
DR CTD; 990; -.
DR MGI; MGI:1345150; Cdc6.
DR VEuPathDB; HostDB:ENSMUSG00000017499; -.
DR eggNOG; KOG2227; Eukaryota.
DR GeneTree; ENSGT00530000063498; -.
DR HOGENOM; CLU_012774_3_0_1; -.
DR InParanoid; O89033; -.
DR OrthoDB; 935804at2759; -.
DR PhylomeDB; O89033; -.
DR TreeFam; TF101051; -.
DR Reactome; R-MMU-176187; Activation of ATR in response to replication stress.
DR Reactome; R-MMU-68689; CDC6 association with the ORC:origin complex.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-68962; Activation of the pre-replicative complex.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR BioGRID-ORCS; 23834; 22 hits in 77 CRISPR screens.
DR ChiTaRS; Cdc6; mouse.
DR PRO; PR:O89033; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O89033; protein.
DR Bgee; ENSMUSG00000017499; Expressed in fetal liver hematopoietic progenitor cell and 171 other tissues.
DR ExpressionAtlas; O89033; baseline and differential.
DR Genevisible; O89033; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; 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:0005819; C:spindle; IDA:MGI.
DR GO; GO:0051233; C:spindle midzone; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; ISO:MGI.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IBA:GO_Central.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; ISO:MGI.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISO:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; ISO:MGI.
DR CDD; cd08768; Cdc6_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041083; AAA_lid_10.
DR InterPro; IPR016314; Cdc6/18.
DR InterPro; IPR015163; Cdc6_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF13401; AAA_22; 1.
DR Pfam; PF17872; AAA_lid_10; 1.
DR Pfam; PF09079; Cdc6_C; 1.
DR PIRSF; PIRSF001767; Cdc6; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01074; Cdc6_C; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; DNA replication;
KW Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..562
FT /note="Cell division control protein 6 homolog"
FT /id="PRO_0000150980"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 94..101
FT /note="Cy"
FT /evidence="ECO:0000250|UniProtKB:Q99741"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 204..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99741"
FT MOD_RES 68
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99741"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 155
FT /note="E -> K (in Ref. 3; BAB28090)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 562 AA; 62614 MW; CB39D0178FAE4ED7 CRC64;
MPQTRSQTQA TIGFPKKKLS NTLKKPNSRD CEVKLRNVQP VPTTPCVDVK LLPLSPRKRL
GDDNLCNTPR LSPCSPPKLG KKENGPPRSH TWKGCRLVFD DEPTFKASPP KEQDRVRQHQ
IRSSSAQRSP ESKADPEQKC PPEKESVCIR LFKQEGTCYQ QAKLVLNTAV PDRLPAREQE
MGVIRNFLKE HICGKKAGSL YLSGAPGTGK TACLSRILQD FKKEVKGFKS ILLNCMSLRS
AQAVFPAIAQ EIGREELCRP AGKDLMRKLE KHLTAEKGPM IVLVLDEMDQ LDSKGQDVLY
TLFEWPWLSN SRLVLIGIAN TLDLTDRILP RLEARENCKP QLLNFPPYTR NQIAAILQDR
LSQVSKDQVL DSAAIQFCAR KVSAVSGDIR KALDVCRRAI EIVESDVRSQ TVLKPLSECK
SPSESPVPKR VGLAHISQVI SEVDGNRVTL SQENTQDSLP LQQKILVCSL LLLTRRLKIK
EVTLGKLYEA YSSICRKQQV TAVDQSECLS LSGLLESRGL VGLKKNKESR LTKVSLKIEE
KEIEHVLNGK AFTGNILAAG LP
