RAD4_SCHPO
ID RAD4_SCHPO Reviewed; 648 AA.
AC P32372;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=S-M checkpoint control protein rad4;
DE AltName: Full=P74;
DE AltName: Full=Protein cut5;
GN Name=rad4; Synonyms=cut5; ORFNames=SPAC23C4.18c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=8343962; DOI=10.1016/0092-8674(93)90428-s;
RA Saka Y., Yanagida M.;
RT "Fission yeast cut5+, required for S phase onset and M phase restraint, is
RT identical to the radiation-damage repair gene rad4+.";
RL Cell 74:383-393(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-648.
RX PubMed=1762905; DOI=10.1093/nar/19.24.6737;
RA Fenech M., Carr A.M., Murray J., Watts F.Z., Lehmann A.R.;
RT "Cloning and characterization of the rad4 gene of Schizosaccharomyces
RT pombe; a gene showing short regions of sequence similarity to the human
RT XRCC1 gene.";
RL Nucleic Acids Res. 19:6737-6741(1991).
RN [4]
RP SEQUENCE REVISION, AND SIMILARITY.
RX PubMed=8255785; DOI=10.1093/nar/21.22.5274;
RA Lehmann A.R.;
RT "Duplicated region of sequence similarity to the human XRCC1 DNA repair
RT gene in the Schizosaccharomyces pombe rad4/cut5 gene.";
RL Nucleic Acids Res. 21:5274-5274(1993).
RN [5]
RP FUNCTION.
RX PubMed=7957098; DOI=10.1002/j.1460-2075.1994.tb06866.x;
RA Saka Y., Fantes P., Sutani T., McInerny C., Creanor J., Yanagida M.;
RT "Fission yeast cut5 links nuclear chromatin and M phase regulator in the
RT replication checkpoint control.";
RL EMBO J. 13:5319-5329(1994).
RN [6]
RP INTERACTION WITH CRB2.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9407031; DOI=10.1101/gad.11.24.3387;
RA Saka Y., Esashi F., Matsusaka T., Mochida S., Yanagida M.;
RT "Damage and replication checkpoint control in fission yeast is ensured by
RT interactions of Crb2, a protein with BRCT motif, with Cut5 and Chk1.";
RL Genes Dev. 11:3387-3400(1997).
RN [7]
RP INTERACTION WITH DRC1.
RX PubMed=11937031; DOI=10.1016/s0960-9822(02)00739-x;
RA Noguchi E., Shanahan P., Noguchi C., Russell P.;
RT "CDK phosphorylation of Drc1 regulates DNA replication in fission yeast.";
RL Curr. Biol. 12:599-605(2002).
RN [8]
RP INTERACTION WITH CRB2.
RX PubMed=14739927; DOI=10.1038/sj.emboj.7600018;
RA Mochida S., Esashi F., Aono N., Tamai K., O'Connell M.J., Yanagida M.;
RT "Regulation of checkpoint kinases through dynamic interaction with Crb2.";
RL EMBO J. 23:418-428(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-186 AND 291-494, FUNCTION, AND
RP INTERACTION WITH CRB2.
RX PubMed=24074952; DOI=10.1016/j.molcel.2013.08.030;
RA Qu M., Rappas M., Wardlaw C.P., Garcia V., Ren J.Y., Day M., Carr A.M.,
RA Oliver A.W., Du L.L., Pearl L.H.;
RT "Phosphorylation-dependent assembly and coordination of the DNA damage
RT checkpoint apparatus by Rad4(TopBP1).";
RL Mol. Cell 51:723-736(2013).
CC -!- FUNCTION: Essential component for DNA replication and also the
CC checkpoint control system which couples S and M phases. May directly or
CC indirectly interact with chromatin proteins to form the complex
CC required for the initiation and/or progression of DNA synthesis
CC (PubMed:8343962, PubMed:7957098). Interacts simultaneously with both
CC 'Thr-187' phosphorylation sites in a crb2 dimer for establishing the
CC DNA checkpoint (PubMed:24074952). {ECO:0000269|PubMed:24074952,
CC ECO:0000269|PubMed:7957098, ECO:0000269|PubMed:8343962}.
CC -!- SUBUNIT: Interacts with drc1/sld2 (PubMed:11937031). Interacts (via
CC BRCT1,2 domains) with crb2 (PubMed:9407031, PubMed:14739927); a single
CC rad4 molecule interacts simultaneously with both 'Thr-187'
CC phosphorylation sites in a crb2 dimer (PubMed:24074952).
CC {ECO:0000269|PubMed:11937031, ECO:0000269|PubMed:14739927,
CC ECO:0000269|PubMed:24074952, ECO:0000269|PubMed:9407031}.
CC -!- INTERACTION:
CC P32372; P87074: crb2; NbExp=2; IntAct=EBI-768521, EBI-768448;
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; D16627; BAA04048.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB16889.1; -; Genomic_DNA.
DR EMBL; X62676; CAA44548.1; -; Genomic_DNA.
DR PIR; B40727; B40727.
DR RefSeq; NP_593190.1; NM_001018586.2.
DR PDB; 4BMC; X-ray; 1.98 A; A=1-186.
DR PDB; 4BMD; X-ray; 2.50 A; A=291-494.
DR PDB; 4BU0; X-ray; 1.50 A; A=1-186.
DR PDB; 4BU1; X-ray; 2.10 A; A/B=1-186.
DR PDB; 6HM3; X-ray; 1.77 A; A=1-186.
DR PDB; 6HM4; X-ray; 1.77 A; A=1-186.
DR PDBsum; 4BMC; -.
DR PDBsum; 4BMD; -.
DR PDBsum; 4BU0; -.
DR PDBsum; 4BU1; -.
DR PDBsum; 6HM3; -.
DR PDBsum; 6HM4; -.
DR AlphaFoldDB; P32372; -.
DR SMR; P32372; -.
DR BioGRID; 279708; 39.
DR IntAct; P32372; 3.
DR MINT; P32372; -.
DR STRING; 4896.SPAC23C4.18c.1; -.
DR iPTMnet; P32372; -.
DR MaxQB; P32372; -.
DR PaxDb; P32372; -.
DR PRIDE; P32372; -.
DR EnsemblFungi; SPAC23C4.18c.1; SPAC23C4.18c.1:pep; SPAC23C4.18c.
DR GeneID; 2543281; -.
DR KEGG; spo:SPAC23C4.18c; -.
DR PomBase; SPAC23C4.18c; rad4.
DR VEuPathDB; FungiDB:SPAC23C4.18c; -.
DR eggNOG; KOG1929; Eukaryota.
DR HOGENOM; CLU_422818_0_0_1; -.
DR InParanoid; P32372; -.
DR OMA; YTHAKQW; -.
DR PhylomeDB; P32372; -.
DR PRO; PR:P32372; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0043596; C:nuclear replication fork; NAS:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0035591; F:signaling adaptor activity; IDA:PomBase.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; EXP:PomBase.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IMP:PomBase.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:PomBase.
DR Gene3D; 3.40.50.10190; -; 4.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF12738; PTCB-BRCT; 2.
DR SMART; SM00292; BRCT; 4.
DR SUPFAM; SSF52113; SSF52113; 4.
DR PROSITE; PS50172; BRCT; 4.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..648
FT /note="S-M checkpoint control protein rad4"
FT /id="PRO_0000097153"
FT DOMAIN 2..92
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 96..185
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 298..384
FT /note="BRCT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 392..486
FT /note="BRCT 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT MOTIF 242..249
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 643..648
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT TURN 6..9
FT /evidence="ECO:0007829|PDB:4BU0"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:4BU0"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:4BU0"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:4BU0"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:4BU0"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:4BU0"
FT HELIX 55..63
FT /evidence="ECO:0007829|PDB:4BU0"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:4BU0"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:4BU0"
FT TURN 90..96
FT /evidence="ECO:0007829|PDB:4BU0"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:4BU0"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:4BU0"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:4BU0"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:4BU0"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:4BU0"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:4BU0"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4BU0"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:4BU0"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:4BU0"
FT TURN 302..305
FT /evidence="ECO:0007829|PDB:4BMD"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:4BMD"
FT HELIX 315..326
FT /evidence="ECO:0007829|PDB:4BMD"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:4BMD"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:4BMD"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:4BMD"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:4BMD"
FT HELIX 364..372
FT /evidence="ECO:0007829|PDB:4BMD"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:4BMD"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:4BMD"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:4BMD"
FT STRAND 401..406
FT /evidence="ECO:0007829|PDB:4BMD"
FT HELIX 409..421
FT /evidence="ECO:0007829|PDB:4BMD"
FT STRAND 425..429
FT /evidence="ECO:0007829|PDB:4BMD"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:4BMD"
FT HELIX 447..458
FT /evidence="ECO:0007829|PDB:4BMD"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:4BMD"
FT HELIX 467..475
FT /evidence="ECO:0007829|PDB:4BMD"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:4BMD"
SQ SEQUENCE 648 AA; 74168 MW; C14EC1EC26863BEF CRC64;
MGSSKPLKGF VICCTSIDLK QRTEISTKAT KLGAAYRSDF TKDVTHLIAG DFDTPKYKFA
AKSRPDIKIM SSEWIPVLYE SWVQGEDLDD GLLVDKHFLP TLFKCRVCLT NIGQPERSRI
ENYVLKHGGT FCPDLTRDVT HLIAGTSSGR KYEYALKWKI NVVCVEWLWQ SIQRNAVLEP
QYFQLDMPAE KIGLGAYVRL DPNTTEAKSY SENQKISKNK EKSGQSLAAL AEEADLEPVI
MKRGKKRDRS ILWEELNNGK FEFSSRSEEN SVLLDDFTPE TVQPLEENEL DTELNIENEA
KLFKNLTFYL YEFPNTKVSR LHKCLSDNGG QISEFLSSTI DFVVIPHYFP VDELPIFSFP
TVNEWWIERC LYYKKIFGID EHALAKPFFR PSLVPYFNGL SIHLTGFKGE ELSHLKKALT
ILGAVVHEFL GVQRSILLVN TNEPFSMKTR FKIQHATEWN VRVVGVAWLW NIIQSGKFID
QVSPWAIDKK ENQEIKKFTN QNNMVFPTSD RDTRLQNSLA QQPIGHSTPH NSPSLLSVKK
RQNNHIRSNT LIQLNSNSKD STIFPRRSVT VPGDKIDTVW KSSVTKPETP TSPQEHVSYI
DPDAQREKHK LYAQLTSNVD AIPPANDLQN QENGLLLITE SHRKLRRR
