RAD25_SCHPO
ID RAD25_SCHPO Reviewed; 270 AA.
AC P42657;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Checkpoint signal transducer rad25;
GN Name=rad25 {ECO:0000303|PubMed:8036497, ECO:0000312|PomBase:SPAC17A2.13c};
GN ORFNames=SPAC17A2.13c {ECO:0000312|PomBase:SPAC17A2.13c};
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 [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 FUNCTION, INTERACTION WITH RAD24 AND BYR2, AND 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-253, 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 (By
CC similarity). Required for the DNA damage checkpoint that ensures that
CC DNA damage is repaired before mitosis is attempted (PubMed:8036497).
CC Sequesters byr2 in the cytoplasm to prevent its translocation to the
CC plasma membrane (PubMed:12242289). {ECO:0000250|UniProtKB:P42656,
CC ECO:0000269|PubMed:12242289, ECO:0000269|PubMed:8036497}.
CC -!- SUBUNIT: Interacts with rad24 (PubMed:12242289). Interacts with byr2
CC (PubMed:12242289). {ECO:0000269|PubMed:12242289}.
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; X79207; CAA55796.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB16570.1; -; Genomic_DNA.
DR PIR; T37814; T37814.
DR RefSeq; NP_594247.1; NM_001019670.2.
DR AlphaFoldDB; P42657; -.
DR SMR; P42657; -.
DR BioGRID; 278722; 60.
DR IntAct; P42657; 1.
DR STRING; 4896.SPAC17A2.13c.1; -.
DR iPTMnet; P42657; -.
DR MaxQB; P42657; -.
DR PaxDb; P42657; -.
DR PRIDE; P42657; -.
DR EnsemblFungi; SPAC17A2.13c.1; SPAC17A2.13c.1:pep; SPAC17A2.13c.
DR GeneID; 2542252; -.
DR KEGG; spo:SPAC17A2.13c; -.
DR PomBase; SPAC17A2.13c; rad25.
DR VEuPathDB; FungiDB:SPAC17A2.13c; -.
DR eggNOG; KOG0841; Eukaryota.
DR HOGENOM; CLU_058290_0_0_1; -.
DR InParanoid; P42657; -.
DR OMA; MVECMKA; -.
DR PhylomeDB; P42657; -.
DR PRO; PR:P42657; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA: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; NAS:PomBase.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint 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; Phosphoprotein; Reference proteome.
FT CHAIN 1..270
FT /note="Checkpoint signal transducer rad25"
FT /id="PRO_0000058718"
FT REGION 240..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 270 AA; 30369 MW; 06CBF55E1A597819 CRC64;
MSNSRENSVY LAKLAEQAER YEEMVENMKK VACSNDKLSV EERNLLSVAY KNIIGARRAS
WRIISSIEQK EESRGNTRQA ALIKEYRKKI EDELSDICHD VLSVLEKHLI PAATTGESKV
FYYKMKGDYY RYLAEFTVGE VCKEAADSSL EAYKAASDIA VAELPPTDPM RLGLALNFSV
FYYEILDSPE SACHLAKQVF DEAISELDSL SEESYKDSTL IMQLLRDNLT LWTSDAEYNQ
SAKEEAPAAA AASENEHPEP KESTTDTVKA
