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MCMBP_XENLA
ID   MCMBP_XENLA             Reviewed;         626 AA.
AC   Q7ZYP6;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Mini-chromosome maintenance complex-binding protein;
DE            Short=MCM-BP;
DE            Short=MCM-binding protein;
GN   Name=mcmbp;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE MCM COMPLEX.
RX   PubMed=21196493; DOI=10.1101/gad.614411;
RA   Nishiyama A., Frappier L., Mechali M.;
RT   "MCM-BP regulates unloading of the MCM2-7 helicase in late S phase.";
RL   Genes Dev. 25:165-175(2011).
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. May also be required for sister
CC       chromatid cohesion. {ECO:0000269|PubMed:21196493}.
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 mcm7.
CC       {ECO:0000269|PubMed:21196493}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21196493}.
CC       Note=Imported in the nucleus in late S phase when mcm2-7 dissociates
CC       from chromatin.
CC   -!- SIMILARITY: Belongs to the MCMBP family. {ECO:0000305}.
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DR   EMBL; BC042336; AAH42336.1; -; mRNA.
DR   RefSeq; NP_001080558.1; NM_001087089.1.
DR   AlphaFoldDB; Q7ZYP6; -.
DR   BioGRID; 98492; 1.
DR   DNASU; 380250; -.
DR   GeneID; 380250; -.
DR   KEGG; xla:380250; -.
DR   CTD; 380250; -.
DR   Xenbase; XB-GENE-5898075; mcmbp.L.
DR   OrthoDB; 1011739at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 380250; Expressed in oocyte and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IDA: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; IMP: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   Reference proteome.
FT   CHAIN           1..626
FT                   /note="Mini-chromosome maintenance complex-binding protein"
FT                   /id="PRO_0000405811"
FT   REGION          159..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   626 AA;  70356 MW;  2AE9F8B92401C523 CRC64;
     MAGVEDWISA PLAVVQGLFS QRQANGDWEK NVTDYFHDKL QGNRSPASVP CLNDVPLHYL
     KPNSLVRFRC MVQDMFDPEF YMGVYETVDT NTSARVLHFG KYRDLAESLP QQEVDLDSRR
     NVTCERQTFY CVPVPGESPW VKDAYTSSSQ ARACASTSYT PSRQKRSYEE DEDVGPCDTR
     TSHGLGEPKR LETEAAGLQQ NQPSSCSSAP DLNFPLPGEK GPACLIKVYE GWDSFKVNDI
     IEVYGILSVD PALSAVNEDR DAVSALLDPS DNMETLEEQR AHCPPASLVP RIHSVVTWKL
     QHNNPLLPGT LQGTEESKLF VSNLLCEVSA VRAELLGFLS HALLGDSLAA EYLIIHLIST
     VYARRDVLPL GKFTLNLSGC PRNGIFSELL YRILQQIVPA AHYLPMTIEN MNKLRFIPHK
     DYNANRLRSG LLQLSAHTSL LLDETLLEQG QLDTAGVHNV TALGNLITWQ KVDYDFSYHR
     MEFPCNINVL VTSEGRSLLP SDCRVHLQPQ MTPPNLEQYM GALLSASLPS LLNKFRSYIG
     LLRLLDYSIS DEITKAVEDD FVEMRKNDPQ SISADDLHRL LVVSRLLSLS SGQTTLSREM
     WLRAKQLEQQ RKSRFREQKH VNGNEL
 
 
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