ID   2ABA_SCHPO              Reviewed;         463 AA.
AC   Q12702; Q9UTD2;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=Protein phosphatase PP2A regulatory subunit B;
DE   AltName: Full=Protein phosphatase 2A 55 kDa regulatory subunit;
DE            Short=PR55;
GN   Name=pab1; ORFNames=SPAC227.07c;
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], FUNCTION, AND SUBUNIT.
RX   PubMed=9078365; DOI=10.1046/j.1365-2443.1996.02002.x;
RA   Kinoshita K., Nemoto T., Nabeshima K., Kondoh H., Niwa H., Yanagida M.;
RT   "The regulatory subunits of fission yeast protein phosphatase 2A (PP2A)
RT   affect cell morphogenesis, cell wall synthesis and cytokinesis.";
RL   Genes Cells 1:29-45(1996).
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, 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).
CC   -!- FUNCTION: Phosphatase 2A affects a variety of biological processes in
CC       the cell such as transcription, cell cycle progression and cellular
CC       morphogenesis, and provides an initial identification of critical
CC       substrates for this phosphatase. The regulatory subunit may direct the
CC       catalytic subunit to distinct, albeit overlapping, subsets of
CC       substrates. {ECO:0000269|PubMed:9078365}.
CC   -!- SUBUNIT: PP2A exists in several trimeric forms, all of which consist of
CC       a core composed of a catalytic subunit associated with a 65 kDa (PR65)
CC       (Subunit A) and a 55 kDa (PR55) (Subunit B) regulatory subunit.
CC       {ECO:0000269|PubMed:9078365}.
CC   -!- INTERACTION:
CC       Q12702; P13681: dis2; NbExp=9; IntAct=EBI-16132256, EBI-4320127;
CC       Q12702; Q9UT08: paa1; NbExp=6; IntAct=EBI-16132256, EBI-16132377;
CC   -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC       {ECO:0000305}.
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DR   EMBL; D63915; BAA09945.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB61456.1; -; Genomic_DNA.
DR   PIR; T50163; T50163.
DR   RefSeq; NP_592961.1; NM_001018361.2.
DR   AlphaFoldDB; Q12702; -.
DR   SMR; Q12702; -.
DR   BioGRID; 278020; 41.
DR   DIP; DIP-61472N; -.
DR   IntAct; Q12702; 2.
DR   STRING; 4896.SPAC227.07c.1; -.
DR   iPTMnet; Q12702; -.
DR   MaxQB; Q12702; -.
DR   PaxDb; Q12702; -.
DR   PRIDE; Q12702; -.
DR   EnsemblFungi; SPAC227.07c.1; SPAC227.07c.1:pep; SPAC227.07c.
DR   GeneID; 2541519; -.
DR   KEGG; spo:SPAC227.07c; -.
DR   PomBase; SPAC227.07c; pab1.
DR   VEuPathDB; FungiDB:SPAC227.07c; -.
DR   eggNOG; KOG1354; Eukaryota.
DR   HOGENOM; CLU_021713_3_3_1; -.
DR   OMA; EFRYKSE; -.
DR   PhylomeDB; Q12702; -.
DR   Reactome; R-SPO-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR   Reactome; R-SPO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   PRO; PR:Q12702; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:PomBase.
DR   GO; GO:0072542; F:protein phosphatase activator activity; EXP:PomBase.
DR   GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR   GO; GO:0010515; P:negative regulation of induction of conjugation with cellular fusion; IMP:PomBase.
DR   GO; GO:0031030; P:negative regulation of septation initiation signaling; IGI:PomBase.
DR   GO; GO:0035307; P:positive regulation of protein dephosphorylation; IDA:PomBase.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR000009; PP2A_PR55.
DR   InterPro; IPR018067; PP2A_PR55_CS.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR11871; PTHR11871; 1.
DR   PIRSF; PIRSF037309; PP2A_PR55; 1.
DR   PRINTS; PR00600; PP2APR55.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS01024; PR55_1; 1.
DR   PROSITE; PS01025; PR55_2; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..463
FT                   /note="Protein phosphatase PP2A regulatory subunit B"
FT                   /id="PRO_0000071441"
FT   REPEAT          27..66
FT                   /note="WD 1"
FT   REPEAT          87..128
FT                   /note="WD 2"
FT   REPEAT          174..212
FT                   /note="WD 3"
FT   REPEAT          223..263
FT                   /note="WD 4"
FT   REPEAT          282..320
FT                   /note="WD 5"
FT   REPEAT          337..378
FT                   /note="WD 6"
FT   MOD_RES         134
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CONFLICT        126
FT                   /note="K -> R (in Ref. 1; BAA09945)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        145
FT                   /note="L -> V (in Ref. 1; BAA09945)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   463 AA;  52795 MW;  43B289222A2D8CC3 CRC64;
     MDDIEDSLDQ WKFAQCFGDK GDVEDITEAD IISAVEFDHT GDYLATGDKG GRVVLFERNH
     SKKGCEYKFF TEFQSHEPEF DYLKSLEIEE KINKIRWCKR TNRAHFLLST NDKTIKLWKL
     YEKNLKVVAE NNLSDSFHSP MQGPLTTPSQ LRLPRLNHHD MIIAAYPRRV YANAHAYHIN
     SISVNSDAET YISADDLRIN LWNLSISDHS FNIVDIKPEN MEELTEVITS AEFHPINCNH
     LMYSSSKGNI KLLDLRQSAL CDNPCKLFED QEDQDSKSFF SEIISSISDV KFSQNGRYIL
     SRDYLTLKIW DVNMEKAPVK TIPLHDVLRS KLCDLYENDC IFDKFECTFS GDDKHVLSGS
     YSNNFGIYPT DSSLPGDRGQ IVLQADKAAF RARKSAANNV PKLNAVKNND WRSQPQAAMG
     SASVGLDPDN LDYNKKILHA SWHPFEDSVA IAATNNLFVF SKL