2ABB_HUMAN
ID 2ABB_HUMAN Reviewed; 443 AA.
AC Q00005; A6NEJ2; A8K102; B3KPD0; B7Z2F2; B7Z304; D3DQF7; D3DQF8; G3V149;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 208.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=1849734; DOI=10.1021/bi00229a001;
RA Mayer R.E., Hendrix P., Cron P., Matthies R., Stone S.R., Goris J.,
RA Merlevede W., Hofsteenge J., Hemmings B.A.;
RT "Structure of the 55-kDa regulatory subunit of protein phosphatase 2A:
RT evidence for a neuronal-specific isoform.";
RL Biochemistry 30:3589-3597(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-433 (ISOFORM 7).
RC TISSUE=Brain, and Corpus callosum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-131 (ISOFORM 6).
RC TISSUE=Brain, and Hypothalamus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-197 (ISOFORM 2).
RA Strausberg R.L.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INVOLVEMENT IN SCA12.
RX PubMed=10581021; DOI=10.1038/70493;
RA Holmes S.E., O'Hearn E.E., McInnis M.G., Gorelick-Feldman D.A.,
RA Kleiderlein J.J., Callahan C., Kwak N.G., Ingersoll-Ashworth R.G.,
RA Sherr M., Sumner A.J., Sharp A.H., Ananth U., Seltzer W.K., Boss M.A.,
RA Vieria-Saecker A.-M., Epplen J.T., Riess O., Ross C.A., Margolis R.L.;
RT "Expansion of a novel CAG trinucleotide repeat in the 5' region of PPP2R2B
RT is associated with SCA12.";
RL Nat. Genet. 23:391-392(1999).
RN [8]
RP INTERACTION WITH IER5.
RX PubMed=25816751; DOI=10.1016/j.febslet.2015.03.019;
RA Ishikawa Y., Kawabata S., Sakurai H.;
RT "HSF1 transcriptional activity is modulated by IER5 and PP2A/B55.";
RL FEBS Lett. 589:1150-1155(2015).
RN [9]
RP INTERACTION WITH IER5.
RX PubMed=26496226; DOI=10.1016/j.febslet.2015.10.013;
RA Kawabata S., Ishita Y., Ishikawa Y., Sakurai H.;
RT "Immediate-early response 5 (IER5) interacts with protein phosphatase 2A
RT and regulates the phosphorylation of ribosomal protein S6 kinase and heat
RT shock factor 1.";
RL FEBS Lett. 589:3679-3685(2015).
RN [10]
RP VARIANT PRO-138.
RX PubMed=25356899; DOI=10.1371/journal.pgen.1004772;
RA Hamdan F.F., Srour M., Capo-Chichi J.M., Daoud H., Nassif C., Patry L.,
RA Massicotte C., Ambalavanan A., Spiegelman D., Diallo O., Henrion E.,
RA Dionne-Laporte A., Fougerat A., Pshezhetsky A.V., Venkateswaran S.,
RA Rouleau G.A., Michaud J.L.;
RT "De novo mutations in moderate or severe intellectual disability.";
RL PLoS Genet. 10:E1004772-E1004772(2014).
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 (By similarity). Isoform 2 regulates neuronal survival through
CC the mitochondrial fission and fusion balance (By similarity).
CC {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) (PubMed:25816751, PubMed:26496226).
CC {ECO:0000250, ECO:0000250|UniProtKB:P36877,
CC ECO:0000269|PubMed:25816751, ECO:0000269|PubMed:26496226}.
CC -!- INTERACTION:
CC Q00005; P05067: APP; NbExp=3; IntAct=EBI-1052159, EBI-77613;
CC Q00005; O15530: PDPK1; NbExp=8; IntAct=EBI-1052159, EBI-717097;
CC Q00005; P30153: PPP2R1A; NbExp=10; IntAct=EBI-1052159, EBI-302388;
CC Q00005; P23443: RPS6KB1; NbExp=2; IntAct=EBI-1052159, EBI-1775921;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Membrane {ECO:0000250}.
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=7;
CC Name=1; Synonyms=Bbeta, Bbeta1;
CC IsoId=Q00005-1; Sequence=Displayed;
CC Name=2; Synonyms=Bbeta2;
CC IsoId=Q00005-2; Sequence=VSP_037976;
CC Name=3;
CC IsoId=Q00005-3; Sequence=VSP_037977;
CC Name=4;
CC IsoId=Q00005-4; Sequence=VSP_037978;
CC Name=5;
CC IsoId=Q00005-5; Sequence=VSP_037979;
CC Name=6;
CC IsoId=Q00005-6; Sequence=VSP_044923;
CC Name=7;
CC IsoId=Q00005-7; Sequence=VSP_045748;
CC -!- TISSUE SPECIFICITY: Brain.
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 -!- DISEASE: Spinocerebellar ataxia 12 (SCA12) [MIM:604326]:
CC Spinocerebellar ataxia is a clinically and genetically heterogeneous
CC group of cerebellar disorders. Patients show progressive incoordination
CC of gait and often poor coordination of hands, speech and eye movements,
CC due to degeneration of the cerebellum with variable involvement of the
CC brainstem and spinal cord. SCA12 is an autosomal dominant cerebellar
CC ataxia (ADCA). {ECO:0000269|PubMed:10581021}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 1]: Conserved additional ATG codons are found
CC 5' of the putative initiator codon in transcripts supporting isoform 1.
CC They may initiate the translation of upstream short open reading frames
CC altering the expression of that isoform as described in PubMed:1849734.
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=AAH31790.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG51642.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG51642.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; M64930; AAA36493.1; -; mRNA.
DR EMBL; AK056192; BAG51642.1; ALT_SEQ; mRNA.
DR EMBL; AK289717; BAF82406.1; -; mRNA.
DR EMBL; AK294659; BAH11838.1; -; mRNA.
DR EMBL; AK295347; BAH12040.1; -; mRNA.
DR EMBL; AC008728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61829.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61831.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61832.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61833.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61834.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61835.1; -; Genomic_DNA.
DR EMBL; BC031790; AAH31790.1; ALT_INIT; mRNA.
DR EMBL; BI490027; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BI669304; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS4283.1; -. [Q00005-2]
DR CCDS; CCDS4284.2; -. [Q00005-5]
DR CCDS; CCDS43380.1; -. [Q00005-6]
DR CCDS; CCDS64281.1; -. [Q00005-4]
DR CCDS; CCDS64282.1; -. [Q00005-3]
DR PIR; B38351; B38351.
DR RefSeq; NP_001258828.1; NM_001271899.1. [Q00005-3]
DR RefSeq; NP_001258829.1; NM_001271900.1. [Q00005-4]
DR RefSeq; NP_001258877.1; NM_001271948.1. [Q00005-6]
DR RefSeq; NP_858060.2; NM_181674.2. [Q00005-5]
DR RefSeq; NP_858061.2; NM_181675.3. [Q00005-1]
DR RefSeq; NP_858062.1; NM_181676.2. [Q00005-2]
DR RefSeq; NP_858063.1; NM_181677.2.
DR RefSeq; NP_858064.1; NM_181678.2. [Q00005-6]
DR AlphaFoldDB; Q00005; -.
DR SMR; Q00005; -.
DR BioGRID; 111513; 234.
DR IntAct; Q00005; 181.
DR STRING; 9606.ENSP00000377936; -.
DR iPTMnet; Q00005; -.
DR PhosphoSitePlus; Q00005; -.
DR BioMuta; PPP2R2B; -.
DR DMDM; 231446; -.
DR EPD; Q00005; -.
DR jPOST; Q00005; -.
DR MassIVE; Q00005; -.
DR MaxQB; Q00005; -.
DR PaxDb; Q00005; -.
DR PeptideAtlas; Q00005; -.
DR PRIDE; Q00005; -.
DR ProteomicsDB; 32258; -.
DR ProteomicsDB; 57832; -.
DR ProteomicsDB; 57833; -. [Q00005-2]
DR ProteomicsDB; 57834; -. [Q00005-3]
DR ProteomicsDB; 57835; -. [Q00005-4]
DR ProteomicsDB; 57836; -. [Q00005-5]
DR Antibodypedia; 27589; 244 antibodies from 32 providers.
DR DNASU; 5521; -.
DR Ensembl; ENST00000336640.10; ENSP00000336591.6; ENSG00000156475.19. [Q00005-2]
DR Ensembl; ENST00000394409.7; ENSP00000377931.4; ENSG00000156475.19. [Q00005-1]
DR Ensembl; ENST00000394411.9; ENSP00000377933.3; ENSG00000156475.19. [Q00005-1]
DR Ensembl; ENST00000394413.7; ENSP00000377935.4; ENSG00000156475.19. [Q00005-4]
DR Ensembl; ENST00000394414.5; ENSP00000377936.1; ENSG00000156475.19. [Q00005-5]
DR Ensembl; ENST00000453001.5; ENSP00000398779.2; ENSG00000156475.19. [Q00005-6]
DR Ensembl; ENST00000504198.5; ENSP00000421396.1; ENSG00000156475.19. [Q00005-3]
DR Ensembl; ENST00000508545.6; ENSP00000431320.1; ENSG00000156475.19. [Q00005-6]
DR GeneID; 5521; -.
DR KEGG; hsa:5521; -.
DR MANE-Select; ENST00000394411.9; ENSP00000377933.3; NM_181675.4; NP_858061.3.
DR UCSC; uc003loe.6; human. [Q00005-1]
DR CTD; 5521; -.
DR DisGeNET; 5521; -.
DR GeneCards; PPP2R2B; -.
DR HGNC; HGNC:9305; PPP2R2B.
DR HPA; ENSG00000156475; Tissue enhanced (brain, retina).
DR MalaCards; PPP2R2B; -.
DR MIM; 604325; gene.
DR MIM; 604326; phenotype.
DR neXtProt; NX_Q00005; -.
DR OpenTargets; ENSG00000156475; -.
DR Orphanet; 98762; Spinocerebellar ataxia type 12.
DR PharmGKB; PA33669; -.
DR VEuPathDB; HostDB:ENSG00000156475; -.
DR eggNOG; KOG1354; Eukaryota.
DR GeneTree; ENSGT00950000182864; -.
DR HOGENOM; CLU_021713_3_3_1; -.
DR InParanoid; Q00005; -.
DR OMA; HPISCNW; -.
DR OrthoDB; 810409at2759; -.
DR PhylomeDB; Q00005; -.
DR TreeFam; TF105553; -.
DR PathwayCommons; Q00005; -.
DR SignaLink; Q00005; -.
DR SIGNOR; Q00005; -.
DR BioGRID-ORCS; 5521; 14 hits in 1072 CRISPR screens.
DR ChiTaRS; PPP2R2B; human.
DR GeneWiki; PPP2R2B; -.
DR GenomeRNAi; 5521; -.
DR Pharos; Q00005; Tbio.
DR PRO; PR:Q00005; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q00005; protein.
DR Bgee; ENSG00000156475; Expressed in sperm and 167 other tissues.
DR ExpressionAtlas; Q00005; baseline and differential.
DR Genevisible; Q00005; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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; Disease variant;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Neurodegeneration;
KW Phosphoprotein; Reference proteome; Repeat; Spinocerebellar ataxia;
KW WD repeat.
FT CHAIN 1..443
FT /note="Serine/threonine-protein phosphatase 2A 55 kDa
FT regulatory subunit B beta isoform"
FT /id="PRO_0000071421"
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..23
FT /note="MEEDIDTRKINNSFLRDHSYATE -> MNYPDENTYGNK (in isoform
FT 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044923"
FT VAR_SEQ 1..21
FT /note="MEEDIDTRKINNSFLRDHSYA -> MKCFSRYLPYIFRPPNTILSSSCH
FT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_037976"
FT VAR_SEQ 1..21
FT /note="MEEDIDTRKINNSFLRDHSYA -> MIPGIGTLTQDTLWCFSQVKGTIEIGT
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037977"
FT VAR_SEQ 1
FT /note="M -> MVLQPSERHYRDWNHRRLGPWCSPTGSPAPLSCETGCGEGSWILVCR
FT LLVPTQVSLLSM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037978"
FT VAR_SEQ 1
FT /note="M -> MLLSLPALHLQTSEHHPFFQLPHRRLGPWCSPTGSPAPLSCETGCGE
FT GSWILVCRLLVPTQVSLLSM (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037979"
FT VAR_SEQ 1
FT /note="M -> MHQPPPASCSSSSSSSSSSCECARVGVRVSALAPAAAPCPAPRQLPY
FT PRLPEPPSRGTSTLIPARLGPWCSPTGSPAPLSCETGCGEGSWILVCRLLVPTQVSLLS
FT M (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045748"
FT VARIANT 36
FT /note="G -> V (in dbSNP:rs11547494)"
FT /id="VAR_051738"
FT VARIANT 138
FT /note="R -> P (probable disease-associated variant found in
FT a patient with moderate intellectual disability, authism
FT and intractable epilepsy)"
FT /evidence="ECO:0000269|PubMed:25356899"
FT /id="VAR_078654"
FT CONFLICT 22
FT /note="T -> A (in Ref. 2; BAH11838)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="H -> N (in Ref. 5; BI669304)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="S -> F (in Ref. 2; BAH12040)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="T -> S (in Ref. 6; BI490027)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="P -> S (in Ref. 2; BAF82406)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="S -> R (in Ref. 2; BAH12040)"
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
