RAD24_SCHPO
ID RAD24_SCHPO Reviewed; 270 AA.
AC P42656; O42704; O42879;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Checkpoint signal transducer rad24;
GN Name=rad24 {ECO:0000312|PomBase:SPAC8E11.02c};
GN ORFNames=SPAC8E11.02c {ECO:0000312|PomBase:SPAC8E11.02c};
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=8036497; DOI=10.1126/science.8036497;
RA Ford J.C., Al-Khodairy F., Fotou E., Sheldrick K.S., Griffiths D.J.F.,
RA Carr A.M.;
RT "14-3-3 protein homologs required for the DNA damage checkpoint in fission
RT yeast.";
RL Science 265:533-535(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH BYR2 AND RAD25, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12242289; DOI=10.1128/mcb.22.20.7105-7119.2002;
RA Ozoe F., Kurokawa R., Kobayashi Y., Jeong H.T., Tanaka K., Sen K.,
RA Nakagawa T., Matsuda H., Kawamukai M.;
RT "The 14-3-3 proteins Rad24 and Rad25 negatively regulate Byr2 by affecting
RT its localization in Schizosaccharomyces pombe.";
RL Mol. Cell. Biol. 22:7105-7119(2002).
RN [3]
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 [4]
RP FUNCTION, AND INTERACTION WITH MEI2.
RX PubMed=11818066; DOI=10.1016/s0960-9822(01)00654-6;
RA Sato M., Watanabe Y., Akiyoshi Y., Yamamoto M.;
RT "14-3-3 protein interferes with the binding of RNA to the phosphorylated
RT form of fission yeast meiotic regulator Mei2p.";
RL Curr. Biol. 12:141-145(2002).
RN [5]
RP FUNCTION, AND INTERACTION WITH CDC25.
RX PubMed=15629716; DOI=10.1016/j.molcel.2004.11.043;
RA Lopez-Aviles S., Grande M., Gonzalez M., Helgesen A.L., Alemany V.,
RA Sanchez-Piris M., Bachs O., Millar J.B., Aligue R.;
RT "Inactivation of the Cdc25 phosphatase by the stress-activated Srk1 kinase
RT in fission yeast.";
RL Mol. Cell 17:49-59(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND SER-66, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Acts in cell cycle and stress checkpoint signaling by
CC sequestering signal transducers regulated by the checkpoints
CC (PubMed:11818066, PubMed:8036497, PubMed:15629716). Required for the
CC DNA damage checkpoint that ensures that DNA damage is repaired before
CC mitosis is attempted (PubMed:8036497). During environmental stress,
CC sequesters srk1-phosphorylated cdc25 in the cytoplasm to delay the G2/M
CC transition (PubMed:15629716). Sequesters byr2 in the cytoplasm to
CC prevent its translocation to the plasma membrane (PubMed:12242289).
CC Sequesters ran1/pat1-phosphorylated mei2 from its non-coding RNA
CC activators (including meiRNA), to prevent meiotic induction in
CC vegetative cells and to regulate meiosis I (PubMed:11818066).
CC {ECO:0000269|PubMed:11818066, ECO:0000269|PubMed:12242289,
CC ECO:0000269|PubMed:15629716, ECO:0000269|PubMed:8036497}.
CC -!- SUBUNIT: Homodimer (PubMed:12242289). Binds preferentially to mei2
CC phosphorylated by ran1/pat1 (PubMed:11818066). Binds preferentially to
CC cdc25 phosphorylated by srk1 during G2; the interaction is increased
CC during osmotic stress (PubMed:15629716). Interacts with byr2
CC (PubMed:12242289). Interacts with rad25 (PubMed:12242289).
CC {ECO:0000269|PubMed:11818066, ECO:0000269|PubMed:12242289,
CC ECO:0000269|PubMed:15629716}.
CC -!- INTERACTION:
CC P42656; Q9P7H1: clp1; NbExp=3; IntAct=EBI-704791, EBI-704737;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:12242289}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; X79206; CAA55795.1; -; Genomic_DNA.
DR EMBL; AB010899; BAA24800.1; -; mRNA.
DR EMBL; AB008545; BAA28672.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA17023.1; -; Genomic_DNA.
DR PIR; T39156; T39156.
DR PIR; T43316; T43316.
DR PIR; T45211; T45211.
DR RefSeq; NP_594167.1; NM_001019591.2.
DR AlphaFoldDB; P42656; -.
DR SMR; P42656; -.
DR BioGRID; 278511; 90.
DR ELM; P42656; -.
DR IntAct; P42656; 3.
DR STRING; 4896.SPAC8E11.02c.1; -.
DR iPTMnet; P42656; -.
DR SwissPalm; P42656; -.
DR MaxQB; P42656; -.
DR PaxDb; P42656; -.
DR PRIDE; P42656; -.
DR EnsemblFungi; SPAC8E11.02c.1; SPAC8E11.02c.1:pep; SPAC8E11.02c.
DR GeneID; 2542029; -.
DR KEGG; spo:SPAC8E11.02c; -.
DR PomBase; SPAC8E11.02c; rad24.
DR VEuPathDB; FungiDB:SPAC8E11.02c; -.
DR eggNOG; KOG0841; Eukaryota.
DR HOGENOM; CLU_058290_0_0_1; -.
DR InParanoid; P42656; -.
DR OMA; IPCATTG; -.
DR PhylomeDB; P42656; -.
DR PRO; PR:P42656; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0120106; C:mitotic actomyosin contractile ring, distal actin filament layer; IDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0050815; F:phosphoserine residue binding; IBA:GO_Central.
DR GO; GO:0140311; F:protein sequestering activity; IMP:PomBase.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; IC:GOC-OWL.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0044878; P:mitotic cytokinesis checkpoint signaling; IMP: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 GO; GO:0010515; P:negative regulation of induction of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0031031; P:positive regulation of septation initiation signaling; IMP:PomBase.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.190.20; -; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; PTHR18860; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; DNA damage; Meiosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..270
FT /note="Checkpoint signal transducer rad24"
FT /id="PRO_0000058717"
FT REGION 242..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 219
FT /note="S -> F (in Ref. 2; BAA24800)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="A -> R (in Ref. 1; CAA55795)"
FT /evidence="ECO:0000305"
FT CONFLICT 269..270
FT /note="DA -> THR (in Ref. 1; CAA55795)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 270 AA; 30082 MW; 1401DD425A1A872F CRC64;
MSTTSREDAV YLAKLAEQAE RYEGMVENMK SVASTDQELT VEERNLLSVA YKNVIGARRA
SWRIVSSIEQ KEESKGNTAQ VELIKEYRQK IEQELDTICQ DILTVLEKHL IPNAASAESK
VFYYKMKGDY YRYLAEFAVG EKRQHSADQS LEGYKAASEI ATAELAPTHP IRLGLALNFS
VFYYEILNSP DRACYLAKQA FDEAISELDS LSEESYKDST LIMQLLRDNL TLWTSDAEYS
AAAAGGNTEG AQENAPSNAP EGEAEPKADA
