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ORC2_YEAST
ID   ORC2_YEAST              Reviewed;         620 AA.
AC   P32833; D6VQ60;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   03-AUG-2022, entry version 183.
DE   RecName: Full=Origin recognition complex subunit 2;
DE   AltName: Full=Origin recognition complex 71 kDa subunit;
GN   Name=ORC2; Synonyms=RRR1, SIR5; OrderedLocusNames=YBR060C;
GN   ORFNames=YBR0523;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8266071; DOI=10.1126/science.8266071;
RA   Foss M., McNally F.J., Laurenson P., Rine J.;
RT   "Origin recognition complex (ORC) in transcriptional silencing and DNA
RT   replication in S. cerevisiae.";
RL   Science 262:1838-1844(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8232543; DOI=10.1038/366087a0;
RA   Micklem G., Rowley A., Harwood J., Nasmyth K., Diffley J.F.X.;
RT   "Yeast origin recognition complex is involved in DNA replication and
RT   transcriptional silencing.";
RL   Nature 366:87-89(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX   PubMed=8266072; DOI=10.1126/science.8266072;
RA   Bell S.P., Kobayashi R., Stillman B.;
RT   "Yeast origin recognition complex functions in transcription silencing and
RT   DNA replication.";
RL   Science 262:1844-1849(1993).
RN   [6]
RP   INTERACTION MCM10.
RX   PubMed=11168584; DOI=10.1046/j.1365-2443.2000.00387.x;
RA   Kawasaki Y., Hiraga S., Sugino A.;
RT   "Interactions between Mcm10p and other replication factors are required for
RT   proper initiation and elongation of chromosomal DNA replication in
RT   Saccharomyces cerevisiae.";
RL   Genes Cells 5:975-989(2000).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH TAH11.
RX   PubMed=17825064; DOI=10.1111/j.1567-1364.2007.00299.x;
RA   Asano T., Makise M., Takehara M., Mizushima T.;
RT   "Interaction between ORC and Cdt1p of Saccharomyces cerevisiae.";
RL   FEMS Yeast Res. 7:1256-1262(2007).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60; THR-187 AND SER-188, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Component of the origin recognition complex (ORC) that binds
CC       origins of replication. It has a role in both chromosomal replication
CC       and mating type transcriptional silencing. Binds to the ARS consensus
CC       sequence (ACS) of origins of replication.
CC       {ECO:0000269|PubMed:17825064}.
CC   -!- SUBUNIT: Component of the origin recognition complex (ORC) composed of
CC       at least ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. Interacts with MCM10
CC       and TAH11. {ECO:0000269|PubMed:11168584, ECO:0000269|PubMed:17825064}.
CC   -!- INTERACTION:
CC       P32833; P54790: ORC3; NbExp=6; IntAct=EBI-12572, EBI-12576;
CC       P32833; P50874: ORC5; NbExp=4; IntAct=EBI-12572, EBI-12584;
CC       P32833; P38826: ORC6; NbExp=6; IntAct=EBI-12572, EBI-12588;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 1700 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ORC2 family. {ECO:0000305}.
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DR   EMBL; L23924; AAA16325.1; -; Unassigned_DNA.
DR   EMBL; Z21817; CAA79883.1; -; Genomic_DNA.
DR   EMBL; Z35929; CAA85003.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07180.1; -; Genomic_DNA.
DR   PIR; S38994; S38994.
DR   RefSeq; NP_009616.1; NM_001178408.1.
DR   PDB; 5V8F; EM; 3.90 A; B=1-620.
DR   PDB; 5ZR1; EM; 3.00 A; B=1-620.
DR   PDB; 6RQC; EM; 4.40 A; B=1-620.
DR   PDB; 6WGC; EM; 4.30 A; B=1-620.
DR   PDB; 6WGG; EM; 8.10 A; B=1-620.
DR   PDB; 6WGI; EM; 10.00 A; B=1-620.
DR   PDB; 7MCA; EM; 3.60 A; B=1-620.
DR   PDBsum; 5V8F; -.
DR   PDBsum; 5ZR1; -.
DR   PDBsum; 6RQC; -.
DR   PDBsum; 6WGC; -.
DR   PDBsum; 6WGG; -.
DR   PDBsum; 6WGI; -.
DR   PDBsum; 7MCA; -.
DR   AlphaFoldDB; P32833; -.
DR   SMR; P32833; -.
DR   BioGRID; 32764; 691.
DR   ComplexPortal; CPX-768; Nuclear origin recognition complex.
DR   DIP; DIP-2285N; -.
DR   IntAct; P32833; 17.
DR   MINT; P32833; -.
DR   STRING; 4932.YBR060C; -.
DR   iPTMnet; P32833; -.
DR   MaxQB; P32833; -.
DR   PaxDb; P32833; -.
DR   PRIDE; P32833; -.
DR   TopDownProteomics; P32833; -.
DR   EnsemblFungi; YBR060C_mRNA; YBR060C; YBR060C.
DR   GeneID; 852352; -.
DR   KEGG; sce:YBR060C; -.
DR   SGD; S000000264; ORC2.
DR   VEuPathDB; FungiDB:YBR060C; -.
DR   eggNOG; KOG2928; Eukaryota.
DR   GeneTree; ENSGT00390000015228; -.
DR   HOGENOM; CLU_022671_0_0_1; -.
DR   InParanoid; P32833; -.
DR   OMA; FIEHKMA; -.
DR   BioCyc; YEAST:G3O-29031-MON; -.
DR   Reactome; R-SCE-68616; Assembly of the ORC complex at the origin of replication.
DR   Reactome; R-SCE-68689; CDC6 association with the ORC:origin complex.
DR   Reactome; R-SCE-68949; Orc1 removal from chromatin.
DR   Reactome; R-SCE-68962; Activation of the pre-replicative complex.
DR   PRO; PR:P32833; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P32833; protein.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0031261; C:DNA replication preinitiation complex; IDA:SGD.
DR   GO; GO:0005664; C:nuclear origin of replication recognition complex; IDA:SGD.
DR   GO; GO:0005656; C:nuclear pre-replicative complex; IDA:SGD.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR   GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR   GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR   GO; GO:0006270; P:DNA replication initiation; IMP:SGD.
DR   GO; GO:0051568; P:histone H3-K4 methylation; IMP:SGD.
DR   GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IDA:SGD.
DR   GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IDA:SGD.
DR   GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR   InterPro; IPR007220; ORC2.
DR   PANTHER; PTHR14052; PTHR14052; 1.
DR   Pfam; PF04084; ORC2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; DNA replication; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..620
FT                   /note="Origin recognition complex subunit 2"
FT                   /id="PRO_0000127082"
FT   REGION          1..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         60
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         187
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         188
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   HELIX           243..249
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   TURN            255..257
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   HELIX           271..284
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   HELIX           287..296
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   TURN            297..300
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   HELIX           301..308
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   TURN            309..311
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   STRAND          313..317
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   HELIX           323..331
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   HELIX           334..341
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   STRAND          360..364
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   HELIX           372..383
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   TURN            390..392
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   HELIX           399..411
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   STRAND          420..425
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   TURN            430..432
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   HELIX           435..445
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   STRAND          450..455
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   HELIX           461..464
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   HELIX           467..473
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   STRAND          475..479
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   TURN            487..490
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   STRAND          491..493
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   TURN            495..499
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   HELIX           507..514
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   HELIX           519..539
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   HELIX           550..552
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   STRAND          553..555
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   HELIX           556..565
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   HELIX           572..583
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   TURN            584..586
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   STRAND          587..592
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   STRAND          598..601
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   HELIX           606..615
FT                   /evidence="ECO:0007829|PDB:5ZR1"
FT   TURN            616..619
FT                   /evidence="ECO:0007829|PDB:5ZR1"
SQ   SEQUENCE   620 AA;  71238 MW;  486E3E5CE353807F CRC64;
     MLNGEDFVEH NDILSSPAKS RNVTPKRVDP HGERQLRRIH SSKKNLLERI SLVGNERKNT
     SPDPALKPKT PSKAPRKRGR PRKIQEELTD RIKKDEKDTI SSKKKRKLDK DTSGNVNEES
     KTSNNKQVME KTGIKEKRER EKIQVATTTY EDNVTPQTDD NFVSNSPEPP EPATPSKKSL
     TTNHDFTSPL KQIIMNNLKE YKDSTSPGKL TLSRNFTPTP VPKNKKLYQT SETKSASSFL
     DTFEGYFDQR KIVRTNAKSR HTMSMAPDVT REEFSLVSNF FNENFQKRPR QKLFEIQKKM
     FPQYWFELTQ GFSLLFYGVG SKRNFLEEFA IDYLSPKIAY SQLAYENELQ QNKPVNSIPC
     LILNGYNPSC NYRDVFKEIT DLLVPAELTR SETKYWGNHV ILQIQKMIDF YKNQPLDIKL
     ILVVHNLDGP SIRKNTFQTM LSFLSVIRQI AIVASTDHIY APLLWDNMKA QNYNFVFHDI
     SNFEPSTVES TFQDVMKMGK SDTSSGAEGA KYVLQSLTVN SKKMYKLLIE TQMQNMGNLS
     ANTGPKRGTQ RTGVELKLFN HLCAADFIAS NEIALRSMLR EFIEHKMANI TKNNSGMEII
     WVPYTYAELE KLLKTVLNTL
 
 
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