MCMBP_MOUSE
ID MCMBP_MOUSE Reviewed; 642 AA.
AC Q8R3C0; D3Z3G1;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Mini-chromosome maintenance complex-binding protein;
DE Short=MCM-BP;
DE Short=MCM-binding protein;
GN Name=Mcmbp;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
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: Associated component of the MCM complex that acts as a
CC regulator of DNA replication. Binds to the MCM complex during late S
CC phase and promotes the disassembly of the MCM complex from chromatin,
CC thereby acting as a key regulator of pre-replication complex (pre-RC)
CC unloading from replicated DNA. Can dissociate the MCM complex without
CC addition of ATP; probably acts by destabilizing interactions of each
CC individual subunits of the MCM complex. Required for sister chromatid
CC cohesion (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the MCM complex: associates with the MCM3-7
CC complex which lacks MCM2, while it does not interact with the MCM
CC complex when MCM2 is present (MCM2-7 complex). Interacts with the RPA
CC complex, when composed of all RPA1, RPA2 and RPA3 components, but not
CC with RPA1 or RPA2 alone (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Associates with
CC chromatin. Highly associated with chromatin in G1/S and S phases,
CC reduced binding to chromatin in G2, and further decreased binding in
CC early M phase. It then reassociates with chromatin in late M phase.
CC Dissociates from chromatin later than component of the MCM complex (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MCMBP family. {ECO:0000305}.
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DR EMBL; AC122767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC136741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025641; AAH25641.1; -; mRNA.
DR EMBL; BC038342; AAH38342.1; -; mRNA.
DR CCDS; CCDS40153.1; -.
DR RefSeq; NP_666067.1; NM_145955.3.
DR AlphaFoldDB; Q8R3C0; -.
DR BioGRID; 229174; 8.
DR IntAct; Q8R3C0; 1.
DR MINT; Q8R3C0; -.
DR STRING; 10090.ENSMUSP00000062843; -.
DR iPTMnet; Q8R3C0; -.
DR PhosphoSitePlus; Q8R3C0; -.
DR EPD; Q8R3C0; -.
DR jPOST; Q8R3C0; -.
DR MaxQB; Q8R3C0; -.
DR PaxDb; Q8R3C0; -.
DR PeptideAtlas; Q8R3C0; -.
DR PRIDE; Q8R3C0; -.
DR ProteomicsDB; 295842; -.
DR Antibodypedia; 46307; 157 antibodies from 26 providers.
DR Ensembl; ENSMUST00000057557; ENSMUSP00000062843; ENSMUSG00000048170.
DR GeneID; 210711; -.
DR KEGG; mmu:210711; -.
DR UCSC; uc009jzh.1; mouse.
DR CTD; 79892; -.
DR MGI; MGI:1920977; Mcmbp.
DR VEuPathDB; HostDB:ENSMUSG00000048170; -.
DR eggNOG; KOG2545; Eukaryota.
DR GeneTree; ENSGT00390000017265; -.
DR HOGENOM; CLU_029811_0_0_1; -.
DR InParanoid; Q8R3C0; -.
DR OMA; HTEMIQQ; -.
DR OrthoDB; 1011739at2759; -.
DR PhylomeDB; Q8R3C0; -.
DR TreeFam; TF324793; -.
DR BioGRID-ORCS; 210711; 23 hits in 74 CRISPR screens.
DR ChiTaRS; Mcmbp; mouse.
DR PRO; PR:Q8R3C0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8R3C0; protein.
DR ExpressionAtlas; Q8R3C0; baseline and differential.
DR Genevisible; Q8R3C0; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0042555; C:MCM complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006261; P:DNA-templated DNA replication; ISS:UniProtKB.
DR GO; GO:0007062; P:sister chromatid cohesion; ISS:UniProtKB.
DR InterPro; IPR019140; MCM_complex-bd.
DR PANTHER; PTHR13489; PTHR13489; 1.
DR Pfam; PF09739; MCM_bind; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; DNA replication; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..642
FT /note="Mini-chromosome maintenance complex-binding protein"
FT /id="PRO_0000089828"
FT REGION 151..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTE3"
FT MOD_RES 160
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTE3"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTE3"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 642 AA; 72891 MW; FD5E282DFCC4A5F3 CRC64;
MPCGEDWLSH PLGIVQGFFA QNGVNPDWEK KVIEYFKEKL KENNAPKWVP SLNEVPLHYL
KPNSFVKFRC MIQDMFDPEF YMGIYETVNQ NTKARVLHFG KYRDVAECGP QQELDLSSPR
STTSERQTFY CVPVPGESSW VKEAYVNANQ ARVSPSTSYT PSRHKRSYED DEDMDLQPSK
QKEQHPGSRQ AGGLGGLHWC GEPKRLETEA SSGQQLNTLN LSSPFDLNFP LPGEKGPACL
VKVYEDWDCF KVNDVLELYG VLSVDPVLSV LNSEERDASA LLDPMECTDM AEEQRVHSPP
ASLVPRIHVI LAQKLQHINP LLPTCLNKEE SRSCQFVSNF MSELSPVRAE LLGFLTHALL
GDSLAAEYLI LHLISTVYTR RDVLPLGKFT VNLSGCPQNS TFTEHLYRII QHLVPASFRL
QMTIENMNQL KLIPHKDYTA NRLVSGLLQL PNNTSLVIDE TLLEQGQLDT PGVHNVTALS
NLITWQKVDY DFSYHQMEFP CNINVLITSE GRSLLPADCQ IHLQPQLIPP NMEEYMNGLL
SAVLPSVLNK FRIYLTLLRF LDYNLSDDIT KAVEDDFVEM RKDDPQSITA DDLHQLLVVA
RFLSLSVGQT TLSRERWLRA KQLELSRKAR LQQQKSVNGN EL
