ID   2ABA_RAT                Reviewed;         447 AA.
AC   P36876; A1A5M9; O35512; P36878;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   02-SEP-2026, entry version 175.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform;
DE   AltName: Full=PP2A subunit B isoform B55-alpha;
DE            Short=B55 {ECO:0000250|UniProtKB:P63151};
DE   AltName: Full=PP2A subunit B isoform BRA;
DE   AltName: Full=PP2A subunit B isoform PR55-alpha;
DE   AltName: Full=PP2A subunit B isoform R2-alpha;
DE   AltName: Full=PP2A subunit B isoform alpha;
GN   Name=Ppp2r2a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1370560; DOI=10.1128/jvi.66.2.886-893.1992;
RA   Pallas D.C., Weller W., Jaspers S., Miller T.B. Jr., Lane W.S.,
RA   Roberts T.M.;
RT   "The third subunit of protein phosphatase 2A (PP2A), a 55-kilodalton
RT   protein which is apparently substituted for by T antigens in complexes with
RT   the 36- and 63-kilodalton PP2A subunits, bears little resemblance to T
RT   antigens.";
RL   J. Virol. 66:886-893(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 80-272.
RC   STRAIN=Fischer 344;
RX   PubMed=8389301; DOI=10.1016/0014-5793(93)81535-8;
RA   Hatano Y., Shima H., Haneji T., Miura A.B., Sugimura T., Nagao M.;
RT   "Expression of PP2A B regulatory subunit beta isotype in rat testis.";
RL   FEBS Lett. 324:71-75(1993).
CC   -!- FUNCTION: Substrate-recognition subunit of protein phosphatase 2A
CC       (PP2A) that plays a key role in cell cycle by controlling mitosis entry
CC       and exit. Involved in chromosome clustering during late mitosis by
CC       mediating dephosphorylation of MKI67 (By similarity). Essential for
CC       serine/threonine-protein phosphatase 2A-mediated dephosphorylation of
CC       WEE1, preventing its ubiquitin-mediated proteolysis, increasing WEE1
CC       protein levels, and promoting the G2/M checkpoint (By similarity).
CC       {ECO:0000250|UniProtKB:P63151, ECO:0000250|UniProtKB:Q6P1F6}.
CC   -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed
CC       of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant
CC       regulatory subunit (PR65 or subunit A), that associates with a variety
CC       of regulatory subunits (By similarity). Proteins that associate with
CC       the core dimer include three families of regulatory subunits B (the
CC       R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48
CC       kDa variable regulatory subunit, viral proteins, and cell signaling
CC       molecules (By similarity). Interacts with the PP2A C catalytic subunit
CC       PPP2CA (By similarity). Interacts with the PP2A A subunit PPP2R1A (By
CC       similarity). Found in a complex with at least ARL2, PPP2CB, PPP2R1A,
CC       PPP2R2A, PPP2R5E and TBCD (By similarity). Interacts with MFHAS1; the
CC       interaction is direct (By similarity). Interacts with PABIR1/FAM122A
CC       (via its N-terminus); the interaction is direct and inhibits PP2A
CC       activity (By similarity). Interacts with ARPP19; the interaction is
CC       direct and inhibits PP2A activity (By similarity). Interacts with CRTC3
CC       (By similarity). {ECO:0000250|UniProtKB:P63151,
CC       ECO:0000250|UniProtKB:Q6P1F6}.
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- DOMAIN: Has an extended WD 2 repeat that is important for the
CC       interaction with PPP2R1A. {ECO:0000250|UniProtKB:P63151}.
CC   -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC       {ECO:0000305}.
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DR   EMBL; M83298; AAA41910.1; -; mRNA.
DR   EMBL; M83297; AAA41909.1; -; mRNA.
DR   EMBL; BC128731; AAI28732.1; -; mRNA.
DR   EMBL; D14419; BAA21904.1; -; mRNA.
DR   PIR; A41805; A41805.
DR   RefSeq; NP_446451.1; NM_053999.2.
DR   AlphaFoldDB; P36876; -.
DR   SMR; P36876; -.
DR   BioGRID; 250676; 3.
DR   DIP; DIP-40819N; -.
DR   FunCoup; P36876; 4991.
DR   IntAct; P36876; 5.
DR   MINT; P36876; -.
DR   STRING; 10116.ENSRNOP00000015318; -.
DR   iPTMnet; P36876; -.
DR   PhosphoSitePlus; P36876; -.
DR   jPOST; P36876; -.
DR   PaxDb; 10116-ENSRNOP00000015318; -.
DR   Ensembl; ENSRNOT00000015318.8; ENSRNOP00000015318.5; ENSRNOG00000011158.8.
DR   Ensembl; ENSRNOT00055011291; ENSRNOP00055008862; ENSRNOG00055006816.
DR   Ensembl; ENSRNOT00060020309; ENSRNOP00060015970; ENSRNOG00060011896.
DR   Ensembl; ENSRNOT00065030623; ENSRNOP00065024361; ENSRNOG00065018068.
DR   GeneID; 117104; -.
DR   KEGG; rno:117104; -.
DR   UCSC; RGD:620919; rat.
DR   AGR; RGD:620919; -.
DR   CTD; 5520; -.
DR   RGD; 620919; Ppp2r2a.
DR   eggNOG; KOG1354; Eukaryota.
DR   GeneTree; ENSGT00950000182864; -.
DR   HOGENOM; CLU_021713_3_3_1; -.
DR   InParanoid; P36876; -.
DR   OrthoDB; 15779at9989; -.
DR   PhylomeDB; P36876; -.
DR   Reactome; R-RNO-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR   Reactome; R-RNO-69231; Cyclin D associated events in G1.
DR   Reactome; R-RNO-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR   Reactome; R-RNO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   Reactome; R-RNO-9860927; Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZO1 and integrins in endothelial cells.
DR   PRO; PR:P36876; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000011158; Expressed in ovary and 20 other cell types or tissues.
DR   ExpressionAtlas; P36876; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; ISS:UniProtKB.
DR   GO; GO:0008287; C:protein serine/threonine phosphatase complex; ISO:RGD.
DR   GO; GO:0045202; C:synapse; ISO:RGD.
DR   GO; GO:0140767; F:enzyme-substrate adaptor activity; ISS:UniProtKB.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:Ensembl.
DR   GO; GO:0051721; F:protein phosphatase 2A binding; IPI:RGD.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; ISS:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:0048156; F:tau protein binding; IPI:RGD.
DR   GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR   GO; GO:0051983; P:regulation of chromosome segregation; ISS:UniProtKB.
DR   GO; GO:0043278; P:response to morphine; ISO:RGD.
DR   FunFam; 2.130.10.10:FF:000002; Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR000009; PP2A_PR55.
DR   InterPro; IPR018067; PP2A_PR55_CS.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR11871; PROTEIN PHOSPHATASE PP2A REGULATORY SUBUNIT B; 1.
DR   PIRSF; PIRSF037309; PP2A_PR55; 1.
DR   PRINTS; PR00600; PP2APR55.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS01024; PR55_1; 1.
DR   PROSITE; PS01025; PR55_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Reference proteome; Repeat; WD repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P63151"
FT   CHAIN           2..447
FT                   /note="Serine/threonine-protein phosphatase 2A 55 kDa
FT                   regulatory subunit B alpha isoform"
FT                   /id="PRO_0000071420"
FT   REPEAT          11..80
FT                   /note="WD 1"
FT                   /evidence="ECO:0000250|UniProtKB:P63151"
FT   REPEAT          94..174
FT                   /note="WD 2"
FT                   /evidence="ECO:0000250|UniProtKB:P63151"
FT   REPEAT          175..218
FT                   /note="WD 3"
FT                   /evidence="ECO:0000250|UniProtKB:P63151"
FT   REPEAT          227..270
FT                   /note="WD 4"
FT                   /evidence="ECO:0000250|UniProtKB:P63151"
FT   REPEAT          288..325
FT                   /note="WD 5"
FT                   /evidence="ECO:0000250|UniProtKB:P63151"
FT   REPEAT          347..381
FT                   /note="WD 6"
FT                   /evidence="ECO:0000250|UniProtKB:P63151"
FT   REPEAT          414..446
FT                   /note="WD 7"
FT                   /evidence="ECO:0000250|UniProtKB:P63151"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P63151"
FT   VARIANT         60
FT                   /note="E -> ESFKVHAALREASNLSMQ"
FT   CONFLICT        105
FT                   /note="K -> E (in Ref. 1; AAA41909)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        105
FT                   /note="K -> R (in Ref. 3; BAA21904)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        213
FT                   /note="N -> S (in Ref. 3; BAA21904)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222
FT                   /note="M -> V (in Ref. 3; BAA21904)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   447 AA;  51678 MW;  180AC837D9DA4ECE CRC64;
     MAGAGGGNDI QWCFSQVKGA VDDDVAEADI ISTVEFNHSG ELLATGDKGG RVVIFQQEQE
     NKIQSHSRGE YNVYSTFQSH EPEFDYLKSL EIEEKINKIR WLPQKNAAQF LLSTNDKTIK
     LWKISERDKR PEGYNLKEED GRYRDPTTVT TLRVPVFRPM DLMVEASPRR IFANAHTYHI
     NSISINSDYE TYLSADDLRI NLWHLEITDR SFNIVDIKPA NMEELTEVIT AAEFHPNSCN
     TFVYSSSKGT IRLCDMRASA LCDRHSKLFE EPEDPSNRSF FSEIISSISD VKFSHSGRYM
     MTRDYLSVKV WDLNMENRPV ETYQVHEYLR SKLCSLYEND CIFDKFECCW NGSDSVVMTG
     SYNNFFRMFD RNTKRDITLE ASRENNKPRT VLKPRKVCAS GKRKKDEISV DSLDFNKKIL
     HTAWHPKENI IAVATTNNLY IFQDKVN
//