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ORC2_MOUSE
ID   ORC2_MOUSE              Reviewed;         576 AA.
AC   Q60862;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Origin recognition complex subunit 2;
GN   Name=Orc2; Synonyms=Orc2l;
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=8808289; DOI=10.1006/geno.1996.0018;
RA   Takahara K., Bong M., Brevard R., Eddy R.L., Haley L.L., Sait S.J.,
RA   Shows T.B., Hoffman G.G., Greenspan D.S.;
RT   "Mouse and human homologues of the yeast origin of replication recognition
RT   complex subunit ORC2 and chromosomal localization of the cognate human gene
RT   ORC2L.";
RL   Genomics 31:119-122(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
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   INTERACTION WITH DBF4.
RX   PubMed=12614612; DOI=10.1016/s0022-2836(03)00079-2;
RA   Kneissl M., Puetter V., Szalay A.A., Grummt F.;
RT   "Interaction and assembly of murine pre-replicative complex proteins in
RT   yeast and mouse cells.";
RL   J. Mol. Biol. 327:111-128(2003).
CC   -!- FUNCTION: Component of the origin recognition complex (ORC) that binds
CC       origins of replication. DNA-binding is ATP-dependent. The specific DNA
CC       sequences that define origins of replication have not been identified
CC       yet. ORC is required to assemble the pre-replication complex necessary
CC       to initiate DNA replication (By similarity). Binds histone H3 and H4
CC       trimethylation marks H3K9me3, H3K20me3 and H4K27me3. Stabilizes LRWD1,
CC       by protecting it from ubiquitin-mediated proteasomal degradation. Also
CC       stabilizes ORC3 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of ORC, a complex composed of at least 6 subunits:
CC       ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a cell-cycle
CC       dependent manner. It is sequentially assembled at the exit from
CC       anaphase of mitosis and disassembled as cells enter S phase (By
CC       similarity). Interacts with DBF4 (PubMed:12614612). Interacts with
CC       MCM10. Interacts with LRWD1 throughout the cell cycle; this
CC       interaction, wich occurs only with non-ubiquitinated form of LRWD1,
CC       prevents LRWD1 ubiquitination and hence stabilizes the protein.
CC       Interacts with POLQ (By similarity). {ECO:0000250|UniProtKB:Q13416,
CC       ECO:0000269|PubMed:12614612}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the ORC2 family. {ECO:0000305}.
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DR   EMBL; U27457; AAB33994.1; -; mRNA.
DR   EMBL; BC015257; AAH15257.1; -; mRNA.
DR   CCDS; CCDS14975.1; -.
DR   RefSeq; NP_001258455.1; NM_001271526.1.
DR   RefSeq; NP_032791.1; NM_008765.3.
DR   AlphaFoldDB; Q60862; -.
DR   SMR; Q60862; -.
DR   BioGRID; 201975; 11.
DR   ComplexPortal; CPX-1915; Nuclear origin of replication recognition complex.
DR   CORUM; Q60862; -.
DR   IntAct; Q60862; 10.
DR   STRING; 10090.ENSMUSP00000027198; -.
DR   iPTMnet; Q60862; -.
DR   PhosphoSitePlus; Q60862; -.
DR   EPD; Q60862; -.
DR   MaxQB; Q60862; -.
DR   PaxDb; Q60862; -.
DR   PRIDE; Q60862; -.
DR   ProteomicsDB; 294106; -.
DR   Antibodypedia; 34131; 226 antibodies from 37 providers.
DR   DNASU; 18393; -.
DR   Ensembl; ENSMUST00000027198; ENSMUSP00000027198; ENSMUSG00000026037.
DR   GeneID; 18393; -.
DR   KEGG; mmu:18393; -.
DR   UCSC; uc007bcd.2; mouse.
DR   CTD; 4999; -.
DR   MGI; MGI:1328306; Orc2.
DR   VEuPathDB; HostDB:ENSMUSG00000026037; -.
DR   eggNOG; KOG2928; Eukaryota.
DR   GeneTree; ENSGT00390000015228; -.
DR   InParanoid; Q60862; -.
DR   OMA; FPQWAFE; -.
DR   OrthoDB; 1404162at2759; -.
DR   PhylomeDB; Q60862; -.
DR   TreeFam; TF101092; -.
DR   Reactome; R-MMU-176187; Activation of ATR in response to replication stress.
DR   Reactome; R-MMU-68616; Assembly of the ORC complex at the origin of replication.
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   BioGRID-ORCS; 18393; 4 hits in 74 CRISPR screens.
DR   ChiTaRS; Orc2; mouse.
DR   PRO; PR:Q60862; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q60862; protein.
DR   Bgee; ENSMUSG00000026037; Expressed in spermatocyte and 251 other tissues.
DR   ExpressionAtlas; Q60862; baseline and differential.
DR   Genevisible; Q60862; MM.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0000785; C:chromatin; IDA:MGI.
DR   GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR   GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR   GO; GO:0000939; C:inner kinetochore; IDA:MGI.
DR   GO; GO:0005664; C:nuclear origin of replication recognition complex; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0000808; C:origin recognition complex; ISO:MGI.
DR   GO; GO:0003688; F:DNA replication origin binding; IDA:MGI.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   InterPro; IPR007220; ORC2.
DR   PANTHER; PTHR14052; PTHR14052; 1.
DR   Pfam; PF04084; ORC2; 1.
PE   1: Evidence at protein level;
KW   DNA replication; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..576
FT                   /note="Origin recognition complex subunit 2"
FT                   /id="PRO_0000127076"
FT   REPEAT          1..100
FT                   /note="Involved in LRWD1-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          112..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..197
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         116
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13416"
FT   MOD_RES         225
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13416"
FT   MOD_RES         247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13416"
SQ   SEQUENCE   576 AA;  65893 MW;  A18BA2D18E72553B CRC64;
     MSTLQLKETK VPSVQFVGDD DVLSHILDRE GGTKLKKEKA QLLVNPQKVI KKADCELEKS
     DLEVLEDQNY VKVLGRNIQE SLGNGSAKDG RNKVYSFQQR KHPEEMTKLA LELAKTSGKK
     DPLDSNDPEI TKNIAQKSKG HSTSEKAPLV NNNKTEFLST QPHNLRKRII ASRSHYDSES
     EYSASSSEDD EEATKDEEED TNVARLSQKS QGQNRLLPAP VSKETLPKKK KRDKASDLVE
     EYFEAHSSSK VLTSDRTLQR LRRARVDQKT LHNLLRKFVP SFSAEIERLN QQHEKLFHKW
     MLQLHLGFNI VLYGLGSKRD LLEKFRTTML QDSIHVVING YFPGVSVKSI LNSITEDVLS
     HVGTFQSVLD QRDWIINRFK EDSSLELFLL IHNLDSQMLR GDNSQQILGQ LSSLHNVYLI
     ASIDHLNAPL MWDHAKQSLY NWLWYETTTY SPYTEETSYE NSLLVKQSGS LPLSSLIHVL
     RSLTPNARGI FRLLMKFQLD NQDSPSYIGL SFQDFYQQCR EAFLVNSDLT LRAQLTEFRD
     HKLIRTKKGT DGVEYLLIPV DSGILADFLE KEEEEA
 
 
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