2ABA_YEAST
ID 2ABA_YEAST Reviewed; 526 AA.
AC Q00362; D6VTW4;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Protein phosphatase PP2A regulatory subunit B;
DE AltName: Full=Cell division control protein 55;
DE AltName: Full=PR55;
GN Name=CDC55; OrderedLocusNames=YGL190C; ORFNames=G1345;
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 [GENOMIC DNA].
RX PubMed=1656238; DOI=10.1128/mcb.11.11.5767-5780.1991;
RA Healy A.M., Zolnierowicz S., Stapleton A.E., Goebl M., Depaoli-Roach A.A.,
RA Pringle J.R.;
RT "CDC55, a Saccharomyces cerevisiae gene involved in cellular morphogenesis:
RT identification, characterization, and homology to the B subunit of
RT mammalian type 2A protein phosphatase.";
RL Mol. Cell. Biol. 11:5767-5780(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046087;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<55::aid-yea48>3.0.co;2-9;
RA Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P., Bruschi C.V.;
RT "Sequencing of a 40.5 kb fragment located on the left arm of chromosome VII
RT from Saccharomyces cerevisiae.";
RL Yeast 13:55-64(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 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 [6]
RP INTERACTION WITH YND1.
RX PubMed=16227198; DOI=10.1074/jbc.m507281200;
RA Maoz T., Koren R., Ben-Ari I., Kleinberger T.;
RT "YND1 interacts with CDC55 and is a novel mediator of E4orf4-induced
RT toxicity.";
RL J. Biol. Chem. 280:41270-41277(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP 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).
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.
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 Interacts with YND1; this interaction mediates adenovirus E4orf4 (early
CC region 4 open reading frame 4) induced toxicity and is disrupted by
CC adenovirus E4orf4, which remains associated with both CDC55 and YND1.
CC {ECO:0000269|PubMed:16227198}.
CC -!- INTERACTION:
CC Q00362; Q03018: ESP1; NbExp=2; IntAct=EBI-1942, EBI-6657;
CC Q00362; Q04439: MYO5; NbExp=4; IntAct=EBI-1942, EBI-11687;
CC -!- MISCELLANEOUS: Present with 8600 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC {ECO:0000305}.
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DR EMBL; M72716; AAA34482.1; -; Genomic_DNA.
DR EMBL; X91837; CAA62954.1; -; Genomic_DNA.
DR EMBL; X91489; CAA62785.1; -; Genomic_DNA.
DR EMBL; Z72712; CAA96902.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07925.1; -; Genomic_DNA.
DR PIR; A41698; A41698.
DR RefSeq; NP_011325.1; NM_001181055.1.
DR AlphaFoldDB; Q00362; -.
DR SMR; Q00362; -.
DR BioGRID; 33066; 391.
DR ComplexPortal; CPX-1856; Serine/threonine-protein phosphatase PP2A variant 1.
DR ComplexPortal; CPX-1859; Serine/threonine-protein phosphatase PP2A variant 3.
DR DIP; DIP-2281N; -.
DR IntAct; Q00362; 82.
DR MINT; Q00362; -.
DR STRING; 4932.YGL190C; -.
DR iPTMnet; Q00362; -.
DR MaxQB; Q00362; -.
DR PaxDb; Q00362; -.
DR PRIDE; Q00362; -.
DR EnsemblFungi; YGL190C_mRNA; YGL190C; YGL190C.
DR GeneID; 852685; -.
DR KEGG; sce:YGL190C; -.
DR SGD; S000003158; CDC55.
DR VEuPathDB; FungiDB:YGL190C; -.
DR eggNOG; KOG1354; Eukaryota.
DR GeneTree; ENSGT00950000182864; -.
DR HOGENOM; CLU_021713_3_3_1; -.
DR InParanoid; Q00362; -.
DR OMA; HPISCNW; -.
DR BioCyc; YEAST:YGL190C-MON; -.
DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:Q00362; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; Q00362; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:SGD.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IGI:SGD.
DR GO; GO:0045143; P:homologous chromosome segregation; IGI:SGD.
DR GO; GO:0016237; P:lysosomal microautophagy; IMP:SGD.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; IGI:SGD.
DR GO; GO:0001100; P:negative regulation of exit from mitosis; IMP:SGD.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IGI:SGD.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:1905477; P:positive regulation of protein localization to membrane; IMP:SGD.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:SGD.
DR GO; GO:0061586; P:positive regulation of transcription by transcription factor localization; IMP:SGD.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:ComplexPortal.
DR GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 2.
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 Pfam; PF00400; WD40; 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 Cell cycle; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..526
FT /note="Protein phosphatase PP2A regulatory subunit B"
FT /id="PRO_0000071442"
FT REPEAT 23..62
FT /note="WD 1"
FT REPEAT 82..123
FT /note="WD 2"
FT REPEAT 182..220
FT /note="WD 3"
FT REPEAT 231..271
FT /note="WD 4"
FT REPEAT 290..328
FT /note="WD 5"
FT REPEAT 345..386
FT /note="WD 6"
FT REPEAT 495..525
FT /note="WD 7"
FT REGION 390..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 500
FT /note="I -> N (in Ref. 1; AAA34482)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 59662 MW; 6DA12C2805FA6A82 CRC64;
MAQNNFDFKF SQCFGDKADI VVTEADLITA VEFDYTGNYL ATGDKGGRVV LFERSNSRHC
EYKFLTEFQS HDAEFDYLKS LEIEEKINEI KWLRPTQRSH FLLSTNDKTI KLWKVYEKNI
KLVSQNNLTE GVTFAKKGKP DNHNSRGGSV RAVLSLQSLK LPQLSQHDKI IAATPKRIYS
NAHTYHINSI SLNSDQETFL SADDLRINLW NLDIPDQSFN IVDIKPTNME ELTEVITSAE
FHPQECNLFM YSSSKGTIKL CDMRQNSLCD NKTKTFEEYL DPINHNFFTE ITSSISDIKF
SPNGRYIASR DYLTVKIWDV NMDNKPLKTI NIHEQLKERL SDTYENDAIF DKFEVNFSGD
SSSVMTGSYN NNFMIYPNVV TSGDNDNGIV KTFDEHNAPN SNSNKNIHNS IQNKDSSSSG
NSHKRRSNGR NTGMVGSSNS SRSSIAGGEG ANSEDSGTEM NEIVLQADKT AFRNKRYGSL
AQRSARNKDW GDDIDFKKNI LHFSWHPREN SIAVAATNNL FIFSAL
