2ABB_MOUSE
ID 2ABB_MOUSE Reviewed; 443 AA.
AC Q6ZWR4; Q3UF60; Q8K413; Q9D3B7; Q9D6I1;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform;
DE AltName: Full=PP2A subunit B isoform B55-beta;
DE AltName: Full=PP2A subunit B isoform PR55-beta;
DE AltName: Full=PP2A subunit B isoform R2-beta;
DE AltName: Full=PP2A subunit B isoform beta;
GN Name=Ppp2r2b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=CD-1, and Czech II; TISSUE=Lung tumor, and Testis;
RX PubMed=12473071; DOI=10.1046/j.1460-9568.2002.02274.x;
RA Schmidt K., Kins S., Schild A., Nitsch R.M., Hemmings B.A., Goetz J.;
RT "Diversity, developmental regulation and distribution of murine PR55/B
RT subunits of protein phosphatase 2A.";
RL Eur. J. Neurosci. 16:2039-2048(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Hippocampus, Medulla oblongata, Spinal cord, and
RC Sympathetic ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary tumor;
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).
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. Within the
CC PP2A holoenzyme complex, isoform 2 is required to promote proapoptotic
CC activity. Isoform 2 regulates neuronal survival through the
CC mitochondrial fission and fusion balance. {ECO:0000250}.
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). Interacts with TOMM22 (By similarity). Interacts with IER5
CC (via N- and C-terminal regions) (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P36877, ECO:0000250|UniProtKB:Q00005}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Cytoplasm, cytoskeleton.
CC Membrane.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000250}.
CC Mitochondrion {ECO:0000250}. Mitochondrion outer membrane
CC {ECO:0000250}. Note=Under basal conditions, localizes to both cytosolic
CC and mitochondrial compartments. Relocalizes from the cytosolic to the
CC mitochondrial compartment during apoptosis. Its targeting to the outer
CC mitochondrial membrane (OMM) involves an association with import
CC receptors of the TOM complex and is required to promote proapoptotic
CC activity (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Bbeta;
CC IsoId=Q6ZWR4-1; Sequence=Displayed;
CC Name=2; Synonyms=Bbeta2;
CC IsoId=Q6ZWR4-2; Sequence=VSP_037983;
CC Name=3; Synonyms=Bbeta1;
CC IsoId=Q6ZWR4-3; Sequence=VSP_037982;
CC -!- TISSUE SPECIFICITY: Expressed in brain, testis, lung and spleen. In the
CC brain, expressed in the cortex, hippocampus and cerebellum (at protein
CC level). {ECO:0000269|PubMed:12473071}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo at 14 and 17 dpc.
CC {ECO:0000269|PubMed:12473071}.
CC -!- DOMAIN: The N-terminal 26 residues of isoform 2 constitute a cryptic
CC mitochondrial matrix import signal with critical basic and hydrophobic
CC residues, that is necessary and sufficient for targeting the PP2A
CC holoenzyme to the outer mitochondrial membrane (OMM) and does not
CC affect holoenzyme formation or catalytic activity. {ECO:0000250}.
CC -!- DOMAIN: The last WD repeat of isoform 2 constitutes a mitochondrial
CC stop-transfer domain that confers resistance to the unfolding step
CC process required for import and therefore prevents PPP2R2B matrix
CC translocation and signal sequence cleavage. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: Contains a cryptic mitochondrial transit
CC peptide at positions 1-26. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB31079.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=EDL10024.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF512670; AAM46987.1; -; mRNA.
DR EMBL; AF536771; AAN05641.1; -; mRNA.
DR EMBL; AK013600; BAB28921.1; -; mRNA.
DR EMBL; AK018119; BAB31079.1; ALT_SEQ; mRNA.
DR EMBL; AK039592; BAC30395.1; -; mRNA.
DR EMBL; AK148956; BAE28701.1; -; mRNA.
DR EMBL; CH466528; EDL10024.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH466528; EDL10025.1; -; Genomic_DNA.
DR EMBL; BC026686; AAH26686.1; -; mRNA.
DR EMBL; BC088979; AAH88979.1; -; mRNA.
DR CCDS; CCDS29216.1; -. [Q6ZWR4-2]
DR RefSeq; NP_082668.1; NM_028392.3. [Q6ZWR4-2]
DR AlphaFoldDB; Q6ZWR4; -.
DR SMR; Q6ZWR4; -.
DR BioGRID; 215651; 2.
DR CORUM; Q6ZWR4; -.
DR IntAct; Q6ZWR4; 1.
DR STRING; 10090.ENSMUSP00000025377; -.
DR iPTMnet; Q6ZWR4; -.
DR PhosphoSitePlus; Q6ZWR4; -.
DR MaxQB; Q6ZWR4; -.
DR PaxDb; Q6ZWR4; -.
DR PeptideAtlas; Q6ZWR4; -.
DR PRIDE; Q6ZWR4; -.
DR ProteomicsDB; 285989; -. [Q6ZWR4-1]
DR ProteomicsDB; 285990; -. [Q6ZWR4-2]
DR ProteomicsDB; 285991; -. [Q6ZWR4-3]
DR Antibodypedia; 27589; 244 antibodies from 32 providers.
DR DNASU; 72930; -.
DR Ensembl; ENSMUST00000025377; ENSMUSP00000025377; ENSMUSG00000024500. [Q6ZWR4-2]
DR Ensembl; ENSMUST00000117687; ENSMUSP00000113731; ENSMUSG00000024500. [Q6ZWR4-1]
DR Ensembl; ENSMUST00000120632; ENSMUSP00000113411; ENSMUSG00000024500. [Q6ZWR4-1]
DR GeneID; 72930; -.
DR KEGG; mmu:72930; -.
DR UCSC; uc008eub.2; mouse. [Q6ZWR4-1]
DR UCSC; uc008euc.2; mouse. [Q6ZWR4-2]
DR CTD; 5521; -.
DR MGI; MGI:1920180; Ppp2r2b.
DR VEuPathDB; HostDB:ENSMUSG00000024500; -.
DR eggNOG; KOG1354; Eukaryota.
DR GeneTree; ENSGT00950000182864; -.
DR HOGENOM; CLU_021713_3_3_1; -.
DR InParanoid; Q6ZWR4; -.
DR OrthoDB; 810409at2759; -.
DR TreeFam; TF105553; -.
DR BioGRID-ORCS; 72930; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Ppp2r2b; mouse.
DR PRO; PR:Q6ZWR4; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q6ZWR4; protein.
DR Bgee; ENSMUSG00000024500; Expressed in cortical plate and 174 other tissues.
DR ExpressionAtlas; Q6ZWR4; baseline and differential.
DR Genevisible; Q6ZWR4; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; ISO:MGI.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000266; P:mitochondrial fission; ISO:MGI.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISO:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISO:MGI.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; ISO:MGI.
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; 6.
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 Alternative splicing; Apoptosis; Cytoplasm; Cytoskeleton; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..443
FT /note="Serine/threonine-protein phosphatase 2A 55 kDa
FT regulatory subunit B beta isoform"
FT /id="PRO_0000071423"
FT REPEAT 22..61
FT /note="WD 1"
FT REPEAT 87..128
FT /note="WD 2"
FT REPEAT 171..209
FT /note="WD 3"
FT REPEAT 220..260
FT /note="WD 4"
FT REPEAT 279..317
FT /note="WD 5"
FT REPEAT 334..375
FT /note="WD 6"
FT REPEAT 410..442
FT /note="WD 7"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36877"
FT MOD_RES 295
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P36877"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P36877"
FT VAR_SEQ 1..24
FT /note="MEEDIDTRKINNSFLRDHSYATEA -> MKPFTA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12473071"
FT /id="VSP_037982"
FT VAR_SEQ 1..21
FT /note="MEEDIDTRKINNSFLRDHSYA -> MKCFSRYLPYIFRPPNTILSSSCH
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12473071,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_037983"
FT CONFLICT 35
FT /note="T -> S (in Ref. 2; BAE28701)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 51710 MW; C383C834B2852B8F CRC64;
MEEDIDTRKI NNSFLRDHSY ATEADIISTV EFNHTGELLA TGDKGGRVVI FQREQESKNQ
VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAYFLLST NDKTVKLWKV
SERDKRPEGY NLKDEEGRLR DPATITTLRV PVLRPMDLMV EATPRRVFAN AHTYHINSIS
VNSDYETYMS ADDLRINLWN FEITNQSFNI VDIKPANMEE LTEVITAAEF HPHHCNTFVY
SSSKGTIRLC DMRASALCDR HTKFFEEPED PSNRSFFSEI ISSISDVKFS HSGRYIMTRD
YLTVKVWDLN MENRPIETYQ VHDYLRSKLC SLYENDCIFD KFECVWNGSD SVIMTGSYNN
FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR KDEISVDSLD FSKKILHTAW
HPSENIIAVA ATNNLYIFQD KVN
