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MCMBP_DANRE
ID   MCMBP_DANRE             Reviewed;         631 AA.
AC   Q803A6; A8E7D0;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Mini-chromosome maintenance complex-binding protein;
DE            Short=MCM-BP;
DE            Short=MCM-binding protein;
GN   Name=mcmbp; ORFNames=si:dkey-192p21.2;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Associates with
CC       chromatin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MCMBP family. {ECO:0000305}.
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DR   EMBL; BX005252; CAP09248.1; -; Genomic_DNA.
DR   EMBL; BC044562; AAH44562.1; -; mRNA.
DR   RefSeq; NP_997743.1; NM_212578.1.
DR   AlphaFoldDB; Q803A6; -.
DR   STRING; 7955.ENSDARP00000120704; -.
DR   PaxDb; Q803A6; -.
DR   Ensembl; ENSDART00000135788; ENSDARP00000120704; ENSDARG00000055314.
DR   Ensembl; ENSDART00000168099; ENSDARP00000130337; ENSDARG00000055314.
DR   GeneID; 321119; -.
DR   KEGG; dre:321119; -.
DR   CTD; 79892; -.
DR   ZFIN; ZDB-GENE-030131-9676; mcmbp.
DR   eggNOG; KOG2545; Eukaryota.
DR   GeneTree; ENSGT00390000017265; -.
DR   HOGENOM; CLU_029811_0_0_1; -.
DR   InParanoid; Q803A6; -.
DR   OrthoDB; 1011739at2759; -.
DR   PhylomeDB; Q803A6; -.
DR   TreeFam; TF324793; -.
DR   PRO; PR:Q803A6; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 13.
DR   Bgee; ENSDARG00000055314; Expressed in blastula and 41 other tissues.
DR   ExpressionAtlas; Q803A6; baseline and differential.
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   2: Evidence at transcript level;
KW   Cell cycle; Cell division; DNA replication; Mitosis; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..631
FT                   /note="Mini-chromosome maintenance complex-binding protein"
FT                   /id="PRO_0000405809"
FT   REGION          148..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        189
FT                   /note="S -> T (in Ref. 2; AAH44562)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        357
FT                   /note="F -> Y (in Ref. 2; AAH44562)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   631 AA;  71062 MW;  8ED47656E40781CC CRC64;
     MPTTHDWINN PLGVVDGLFA QSNSSPDWEK KVVEYFKEKL KLNDAHTWVP SLNDVPLHYL
     KPNSLVKFRC MVQDMFDPEF FMGVYEMNDP TSNSKQVKCG KYKDVTECGQ VDFNSRNTVT
     SERQTFYCVP IPGESNWVKE SYAGTSQARV VPSTSYVPNR HKRSYEEDDE MDTQCQQTKD
     ISQGAQSSSE SHGNTEPKRQ ETEAPSQDSS SSHCTSSLDL NFPLPGEKGP ACLVKVYEDW
     DSFKLNDMLE VFGILSVDPA LSVIADEREA SSLLDPTEGM ETMEEQRVHS PPASLVPRLH
     MLYAQPLAHN NPLLPSSPLE NNADYLSCVL GELASVRAEL LTFFTHILMG DSLAAEFLIL
     HLISNVYSRR DVLPLGKFTL NLSGCPLSSP FTEHLFKVIQ QLVPSSYRLS MSLHNMNTQR
     MVPRKDYTAN RLVSGTLQLA KNTSLFLDET QLEQGQLDST GVRNITALGN LISWQKVDYD
     FNYHQMEFPC NINVLIASEG RSLLPSDCQV HLRASLNPPN LEEYLSAVQV AQVPSQLNKY
     RVYLSVARAL NYTISDEITK AVEEDFVDMR KDDPQSMSAE DLHRLLVVAR LLSLSHGQNT
     LSRDGWMKAK QLEALRISRT QQQKCVNGNE P
 
 
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