2ABA_RAT
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 03-AUG-2022, entry version 161.
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 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: The B regulatory subunit might modulate substrate selectivity
CC and catalytic activity, and also might direct the localization of the
CC catalytic enzyme to a particular subcellular compartment. 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.
CC {ECO:0000250|UniProtKB:P63151}.
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. Proteins that associate with the core dimer
CC include three families of regulatory subunits B (the R2/B/PR55/B55,
CC R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable
CC regulatory subunit, viral proteins, and cell signaling molecules (By
CC similarity). Found in a complex with at least ARL2, PPP2CB, PPP2R1A,
CC PPP2R2A, PPP2R5E and TBCD (By similarity). Interacts with TP53 (By
CC similarity). Interacts with IER5 (By similarity). Interacts with
CC MFHAS1; the interaction is direct (By similarity). Interacts with
CC PABIR1/FAM122A (By similarity). Interacts with CRTC3 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P63151,
CC ECO:0000250|UniProtKB:Q6P1F6}.
CC -!- TISSUE SPECIFICITY: Brain.
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 IntAct; P36876; 5.
DR MINT; P36876; -.
DR STRING; 10116.ENSRNOP00000015318; -.
DR iPTMnet; P36876; -.
DR PhosphoSitePlus; P36876; -.
DR jPOST; P36876; -.
DR PaxDb; P36876; -.
DR PRIDE; P36876; -.
DR Ensembl; ENSRNOT00000015318; ENSRNOP00000015318; ENSRNOG00000011158.
DR GeneID; 117104; -.
DR KEGG; rno:117104; -.
DR UCSC; RGD:620919; rat.
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 OMA; TQQGHHL; -.
DR OrthoDB; 810409at2759; -.
DR PhylomeDB; P36876; -.
DR TreeFam; TF105553; -.
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 PRO; PR:P36876; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000011158; Expressed in ovary and 20 other tissues.
DR Genevisible; P36876; RN.
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; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IPI:RGD.
DR GO; GO:0019888; F:protein phosphatase regulator activity; ISO:RGD.
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:0043278; P:response to morphine; ISO:RGD.
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; 7.
DR SUPFAM; SSF50978; SSF50978; 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 26..65
FT /note="WD 1"
FT REPEAT 91..132
FT /note="WD 2"
FT REPEAT 175..213
FT /note="WD 3"
FT REPEAT 224..264
FT /note="WD 4"
FT REPEAT 283..321
FT /note="WD 5"
FT REPEAT 338..379
FT /note="WD 6"
FT REPEAT 414..446
FT /note="WD 7"
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
