ID   2A5B_RABIT              Reviewed;         500 AA.
AC   Q28647;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform;
DE   AltName: Full=PP2A B subunit isoform B'-alpha;
DE   AltName: Full=PP2A B subunit isoform B'-beta;
DE   AltName: Full=PP2A B subunit isoform B56-beta;
DE   AltName: Full=PP2A B subunit isoform PR61-beta;
DE   AltName: Full=PP2A B subunit isoform R5-beta;
GN   Name=PPP2R5B;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand;
RX   PubMed=8576224; DOI=10.1074/jbc.271.5.2578;
RA   Csortos C., Zolnierowicz S., Bako E., Durbin S.D., Depaoli-Roach A.A.;
RT   "High complexity in the expression of the B' subunit of protein phosphatase
RT   2A0. Evidence for the existence of at least seven novel isoforms.";
RL   J. Biol. Chem. 271:2578-2588(1996).
CC   -!- FUNCTION: As the regulatory component of the serine/threonine-protein
CC       phosphatase 2A (PP2A) holoenzyme, modulates substrate specificity,
CC       subcellular localization, and responsiveness to phosphorylation. The
CC       phosphorylated form mediates the interaction between PP2A and AKT1,
CC       leading to AKT1 dephosphorylation. {ECO:0000250|UniProtKB:Q15173}.
CC   -!- SUBUNIT: Component of the serine/threonine-protein phosphatase 2A
CC       complex (PP2A). This complex consists of a common heterodimeric core
CC       enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa
CC       constant scaffold subunit (PR65 or subunit A), that associates with a
CC       variety of regulatory subunits. Proteins that associate with the core
CC       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. Interacts with SGO1. Interacts with AKT1.
CC       {ECO:0000250|UniProtKB:Q15173}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain.
CC   -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC       family. {ECO:0000305}.
CC   -!- CAUTION: Nomenclature used in PubMed:8576224 refers to PP2A B subunit
CC       B' alpha isoform, which is cited as PP2A B subunit beta-PR61 isoform in
CC       later publications. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U37769; AAC48527.1; -; mRNA.
DR   RefSeq; NP_001075832.1; NM_001082363.1.
DR   AlphaFoldDB; Q28647; -.
DR   SMR; Q28647; -.
DR   STRING; 9986.ENSOCUP00000021664; -.
DR   PRIDE; Q28647; -.
DR   GeneID; 100009215; -.
DR   KEGG; ocu:100009215; -.
DR   CTD; 5526; -.
DR   eggNOG; KOG2085; Eukaryota.
DR   InParanoid; Q28647; -.
DR   OrthoDB; 890437at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:InterPro.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002554; PP2A_B56.
DR   PANTHER; PTHR10257; PTHR10257; 1.
DR   Pfam; PF01603; B56; 1.
DR   PIRSF; PIRSF028043; PP2A_B56; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   2: Evidence at transcript level;
KW   Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..500
FT                   /note="Serine/threonine-protein phosphatase 2A 56 kDa
FT                   regulatory subunit beta isoform"
FT                   /id="PRO_0000071451"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         32
FT                   /note="Phosphoserine; by CLK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q15173"
FT   MOD_RES         35
FT                   /note="Phosphoserine; by CLK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q15173"
FT   MOD_RES         44
FT                   /note="Phosphoserine; by CLK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q15173"
FT   MOD_RES         46
FT                   /note="Phosphoserine; by CLK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q15173"
FT   MOD_RES         47
FT                   /note="Phosphoserine; by CLK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q15173"
FT   MOD_RES         48
FT                   /note="Phosphoserine; by CLK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q15173"
SQ   SEQUENCE   500 AA;  57709 MW;  001CA9360E4C04B0 CRC64;
     METKLPPAST PTSPSSPGLS PVPPADKVDG FSRRSLRRAR PRRSHSSSQF RYQSNQQELT
     PLPLLKDVPA SELHDLLSRK LAQCGVMFDF LDCVADLKGK EVKRAALNEL VECVGSTRGV
     LIEPVYPDII RMISVNIFRT LPPSENPEFD PEEDEPNLEP SWPHLQLVYE FFLRFLESPD
     FQPSVAKRYV DQKFVLMLLE LFDSEDPRER EYLKTILHRV YGKFLGLRAY IRKQCNHIFL
     RFIYEFEHFN GVAELLEILG SIINGFALPL KTEHKQFLVR VLIPLHSVKS LSVFHAQLAY
     CVVQFLEKDA TLTEHVIRGL LKYWPKTCTQ KEVMFLGEVE EILDVIEPSQ FVKIQEPLFK
     QVARCVSSPH FQVAERALYF WNNEYILSLI EDNCHTVLPA VFGTLYQVSK EHWNQTIVSL
     IYNVLKTFME MNGKLFDELT ASYKLEKQQE QQKARERQEL WQGLEELRLR RLQGTQGTQG
     AREAPLQRFV PQVAATGGQS