ID   2ABA_HUMAN              Reviewed;         447 AA.
AC   P63151; B2RBU8; B4E1T7; P50409; Q00007;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 1.
DT   02-SEP-2026, entry version 195.
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:0000303|PubMed:38123684};
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   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), FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Lung fibroblast;
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 AND 2).
RC   TISSUE=Brain, and Trachea;
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=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
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 1).
RC   TISSUE=Blood;
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   INTERACTION WITH TP53.
RX   PubMed=17245430; DOI=10.1038/sj.emboj.7601519;
RA   Li H.H., Cai X., Shouse G.P., Piluso L.G., Liu X.;
RT   "A specific PP2A regulatory subunit, B56gamma, mediates DNA damage-induced
RT   dephosphorylation of p53 at Thr55.";
RL   EMBO J. 26:402-411(2007).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [11]
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   [12]
RP   INTERACTION WITH PABIR1.
RX   PubMed=27588481; DOI=10.18632/oncotarget.11698;
RA   Fan L., Liu M.H., Guo M., Hu C.X., Yan Z.W., Chen J., Chen G.Q., Huang Y.;
RT   "FAM122A, a new endogenous inhibitor of protein phosphatase 2A.";
RL   Oncotarget 7:63887-63900(2016).
RN   [13]
RP   INTERACTION WITH MFHAS1.
RX   PubMed=28609714; DOI=10.1016/j.molimm.2017.06.017;
RA   Shi Q., Xiong B., Zhong J., Wang H., Ma D., Miao C.;
RT   "MFHAS1 suppresses TLR4 signaling pathway via induction of PP2A C subunit
RT   cytoplasm translocation and inhibition of c-Jun dephosphorylation at
RT   Thr239.";
RL   Mol. Immunol. 88:79-88(2017).
RN   [14]
RP   INTERACTION WITH CRTC3.
RX   PubMed=30611118; DOI=10.1016/j.isci.2018.12.012;
RA   Sonntag T., Ostojic J., Vaughan J.M., Moresco J.J., Yoon Y.S.,
RA   Yates J.R. III, Montminy M.;
RT   "Mitogenic Signals Stimulate the CREB Coactivator CRTC3 through PP2A
RT   Recruitment.";
RL   IScience 11:134-145(2018).
RN   [15]
RP   FUNCTION, AND INTERACTION WITH PABIR1.
RX   PubMed=33108758; DOI=10.1016/j.molcel.2020.10.008;
RA   Li F., Kozono D., Deraska P., Branigan T., Dunn C., Zheng X.F., Parmar K.,
RA   Nguyen H., DeCaprio J., Shapiro G.I., Chowdhury D., D'Andrea A.D.;
RT   "CHK1 Inhibitor Blocks Phosphorylation of FAM122A and Promotes Replication
RT   Stress.";
RL   Mol. Cell 0:0-0(2020).
RN   [16] {ECO:0007744|PDB:8SO0, ECO:0007744|PDB:8TTB, ECO:0007744|PDB:8TWE}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.55 ANGSTROMS) OF 2-447 IN COMPLEXES
RP   WITH PPP2CA; PPP2R1A; ARPP19 AND PABIR1/FAM122A, INTERACTION WITH PPP2CA;
RP   PPP2R1A; ARPP19 AND PABIR1/FAM122A, DOMAIN, AND WD REPEATS.
RX   PubMed=38123684; DOI=10.1038/s41586-023-06870-3;
RA   Padi S.K.R., Vos M.R., Godek R.J., Fuller J.R., Kruse T., Hein J.B.,
RA   Nilsson J., Kelker M.S., Page R., Peti W.;
RT   "Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19.";
RL   Nature 625:195-203(2024).
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 (PubMed:1849734, PubMed:33108758). Involved in chromosome
CC       clustering during late mitosis by mediating dephosphorylation of MKI67
CC       (By similarity). Essential for serine/threonine-protein phosphatase 2A-
CC       mediated dephosphorylation of WEE1, preventing its ubiquitin-mediated
CC       proteolysis, increasing WEE1 protein levels, and promoting the G2/M
CC       checkpoint (PubMed:33108758). {ECO:0000250|UniProtKB:Q6P1F6,
CC       ECO:0000269|PubMed:1849734, ECO:0000269|PubMed:33108758}.
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 (PubMed:38123684). 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 (PubMed:38123684). Interacts with the PP2A C catalytic
CC       subunit PPP2CA (PubMed:38123684). Interacts with the PP2A A subunit
CC       PPP2R1A (PubMed:38123684). Interacts with TP53 (PubMed:17245430).
CC       Interacts with IER5 (PubMed:25816751). Interacts with MFHAS1; the
CC       interaction is direct (PubMed:28609714). Interacts with PABIR1/FAM122A
CC       (via its N-terminus); the interaction is direct and inhibits PP2A
CC       activity (PubMed:27588481, PubMed:33108758, PubMed:38123684). Interacts
CC       with ARPP19; the interaction is direct and inhibits PP2A activity
CC       (PubMed:27588481, PubMed:33108758, PubMed:38123684). Interacts with
CC       CRTC3 (PubMed:30611118). {ECO:0000269|PubMed:17245430,
CC       ECO:0000269|PubMed:25816751, ECO:0000269|PubMed:27588481,
CC       ECO:0000269|PubMed:28609714, ECO:0000269|PubMed:30611118,
CC       ECO:0000269|PubMed:33108758, ECO:0000269|PubMed:38123684}.
CC   -!- INTERACTION:
CC       P63151; P05067: APP; NbExp=3; IntAct=EBI-1048931, EBI-77613;
CC       P63151; P56211: ARPP19; NbExp=8; IntAct=EBI-1048931, EBI-5773880;
CC       P63151; Q8NE08: COL25A1; NbExp=3; IntAct=EBI-1048931, EBI-25836642;
CC       P63151; P53355: DAPK1; NbExp=3; IntAct=EBI-1048931, EBI-358616;
CC       P63151; Q96IG2: FBXL20; NbExp=4; IntAct=EBI-1048931, EBI-8835647;
CC       P63151; Q9NZR2: LRP1B; NbExp=3; IntAct=EBI-1048931, EBI-1642131;
CC       P63151; Q5S007: LRRK2; NbExp=4; IntAct=EBI-1048931, EBI-5323863;
CC       P63151; Q15843: NEDD8; NbExp=3; IntAct=EBI-1048931, EBI-716247;
CC       P63151; Q96E09: PABIR1; NbExp=11; IntAct=EBI-1048931, EBI-9355758;
CC       P63151; P30153: PPP2R1A; NbExp=31; IntAct=EBI-1048931, EBI-302388;
CC       P63151; P30154: PPP2R1B; NbExp=5; IntAct=EBI-1048931, EBI-357094;
CC       P63151; P28749: RBL1; NbExp=2; IntAct=EBI-1048931, EBI-971402;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P63151-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P63151-2; Sequence=VSP_043100;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined.
CC       {ECO:0000269|PubMed:1849734}.
CC   -!- DOMAIN: Has an extended WD 2 repeat that is important for the
CC       interaction with PPP2R1A. {ECO:0000269|PubMed:38123684}.
CC   -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC       {ECO:0000305}.
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DR   EMBL; M64929; AAA36490.1; -; mRNA.
DR   EMBL; AK303981; BAG64899.1; -; mRNA.
DR   EMBL; AK314823; BAG37345.1; -; mRNA.
DR   EMBL; AC022911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471080; EAW63578.1; -; Genomic_DNA.
DR   EMBL; BC041071; AAH41071.1; -; mRNA.
DR   CCDS; CCDS34867.1; -. [P63151-1]
DR   CCDS; CCDS55213.1; -. [P63151-2]
DR   PIR; A38351; A38351.
DR   RefSeq; NP_001171062.1; NM_001177591.2. [P63151-2]
DR   RefSeq; NP_002708.1; NM_002717.4. [P63151-1]
DR   PDB; 3DW8; X-ray; 2.85 A; B/E=1-447.
DR   PDB; 8SO0; EM; 2.80 A; B=2-447.
DR   PDB; 8TTB; EM; 2.77 A; B=2-447.
DR   PDB; 8TWE; EM; 2.55 A; B=2-447.
DR   PDB; 8UO5; EM; 3.27 A; B=1-447.
DR   PDB; 9C6B; EM; 2.60 A; B=2-447.
DR   PDB; 9C7T; EM; 2.70 A; B=2-447.
DR   PDB; 9MZW; EM; 3.16 A; B=2-447.
DR   PDB; 9N0Y; EM; 3.71 A; B=2-447.
DR   PDB; 9N0Z; EM; 3.50 A; B=2-447.
DR   AlphaFoldDB; P63151; -.
DR   EMDB; EMD-40644; -.
DR   EMDB; EMD-41604; -.
DR   EMDB; EMD-41667; -.
DR   EMDB; EMD-42428; -.
DR   EMDB; EMD-45243; -.
DR   EMDB; EMD-45292; -.
DR   EMDB; EMD-48770; -.
DR   EMDB; EMD-48798; -.
DR   EMDB; EMD-48799; -.
DR   SMR; P63151; -.
DR   BioGRID; 111512; 353.
DR   ComplexPortal; CPX-2575; Serine/threonine-protein phosphatase 2A complex, B55 alpha variant.
DR   CORUM; P63151; -.
DR   DIP; DIP-29398N; -.
DR   FunCoup; P63151; 4161.
DR   IntAct; P63151; 160.
DR   MINT; P63151; -.
DR   NDEx; IQUERY-CP-PPP2R2A; 9 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000325074; -.
DR   BindingDB; P63151; -.
DR   ChEMBL; CHEMBL4284; -.
DR   DrugBank; DB02506; 2,6,8-Trimethyl-3-Amino-9-Benzyl-9-Methoxynonanoic Acid.
DR   GlyGen; P63151; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P63151; -.
DR   PhosphoSitePlus; P63151; -.
DR   SwissPalm; P63151; -.
DR   BioMuta; PPP2R2A; -.
DR   DMDM; 52783535; -.
DR   jPOST; P63151; -.
DR   MassIVE; P63151; -.
DR   PaxDb; 9606-ENSP00000325074; -.
DR   PeptideAtlas; P63151; -.
DR   PRIDE; P63151; -.
DR   ProteomicsDB; 57497; -.
DR   ProteomicsDB; 57498; -. [P63151-2]
DR   Pumba; P63151; -.
DR   Antibodypedia; 22918; 221 antibodies from 31 providers.
DR   DNASU; 5520; -.
DR   Ensembl; ENST00000315985.7; ENSP00000325074.7; ENSG00000221914.12. [P63151-2]
DR   Ensembl; ENST00000380737.8; ENSP00000370113.3; ENSG00000221914.12. [P63151-1]
DR   GeneID; 5520; -.
DR   KEGG; hsa:5520; -.
DR   MANE-Select; ENST00000380737.8; ENSP00000370113.3; NM_002717.4; NP_002708.1.
DR   UCSC; uc003xeu.4; human. [P63151-1]
DR   AGR; HGNC:9304; -.
DR   CIViC; 5520; 2 evidence items across 2 molecular profiles.
DR   ClinPGx; PA33668; -.
DR   CTD; 5520; -.
DR   DisGeNET; 5520; -.
DR   GeneCards; PPP2R2A; -.
DR   HGNC; HGNC:9304; PPP2R2A.
DR   HPA; ENSG00000221914; Low tissue specificity.
DR   MalaCards; PPP2R2A; -.
DR   MIM; 604941; gene.
DR   OpenTargets; ENSG00000221914; -.
DR   VEuPathDB; HostDB:ENSG00000221914; -.
DR   eggNOG; KOG1354; Eukaryota.
DR   GeneTree; ENSGT00950000182864; -.
DR   HOGENOM; CLU_021713_3_3_1; -.
DR   InParanoid; P63151; -.
DR   OMA; NQIKWCR; -.
DR   OrthoDB; 6274823at2759; -.
DR   PAN-GO; P63151; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; P63151; -.
DR   PathwayCommons; P63151; -.
DR   Reactome; R-HSA-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR   Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR   Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR   Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   Reactome; R-HSA-9860927; Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZO1 and integrins in endothelial cells.
DR   SignaLink; P63151; -.
DR   SIGNOR; P63151; -.
DR   Agora; ENSG00000221914; -.
DR   BioGRID-ORCS; 5520; 208 hits in 1187 CRISPR screens.
DR   ChiTaRS; PPP2R2A; human.
DR   EvolutionaryTrace; P63151; -.
DR   GeneWiki; PPP2R2A; -.
DR   GenomeRNAi; 5520; -.
DR   Pharos; P63151; Tchem.
DR   PRO; PR:P63151; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; P63151; protein.
DR   Bgee; ENSG00000221914; Expressed in calcaneal tendon and 206 other cell types or tissues.
DR   ExpressionAtlas; P63151; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB.
DR   GO; GO:0008287; C:protein serine/threonine phosphatase complex; IDA:UniProt.
DR   GO; GO:0140767; F:enzyme-substrate adaptor activity; ISS:UniProtKB.
DR   GO; GO:0051721; F:protein phosphatase 2A binding; IEA:Ensembl.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IDA:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0048156; F:tau protein binding; IEA:Ensembl.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR   GO; GO:0051983; P:regulation of chromosome segregation; ISS:UniProtKB.
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.
DR   PDBsum; 3DW8; -.
DR   PDBsum; 8SO0; -.
DR   PDBsum; 8TTB; -.
DR   PDBsum; 8TWE; -.
DR   PDBsum; 8UO5; -.
DR   PDBsum; 9C6B; -.
DR   PDBsum; 9C7T; -.
DR   PDBsum; 9MZW; -.
DR   PDBsum; 9N0Y; -.
DR   PDBsum; 9N0Z; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Proteomics identification;
KW   Reference proteome; Repeat; WD repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895"
FT   CHAIN           2..447
FT                   /note="Serine/threonine-protein phosphatase 2A 55 kDa
FT                   regulatory subunit B alpha isoform"
FT                   /id="PRO_0000071415"
FT   REPEAT          11..80
FT                   /note="WD 1"
FT                   /evidence="ECO:0000269|PubMed:38123684,
FT                   ECO:0007744|PDB:8SO0, ECO:0007744|PDB:8TTB,
FT                   ECO:0007744|PDB:8TWE"
FT   REPEAT          94..174
FT                   /note="WD 2"
FT                   /evidence="ECO:0000269|PubMed:38123684,
FT                   ECO:0007744|PDB:8SO0, ECO:0007744|PDB:8TTB,
FT                   ECO:0007744|PDB:8TWE"
FT   REPEAT          175..218
FT                   /note="WD 3"
FT                   /evidence="ECO:0000269|PubMed:38123684,
FT                   ECO:0007744|PDB:8SO0, ECO:0007744|PDB:8TTB,
FT                   ECO:0007744|PDB:8TWE"
FT   REPEAT          227..270
FT                   /note="WD 4"
FT                   /evidence="ECO:0000269|PubMed:38123684,
FT                   ECO:0007744|PDB:8SO0, ECO:0007744|PDB:8TTB,
FT                   ECO:0007744|PDB:8TWE"
FT   REPEAT          288..325
FT                   /note="WD 5"
FT                   /evidence="ECO:0000269|PubMed:38123684,
FT                   ECO:0007744|PDB:8SO0, ECO:0007744|PDB:8TTB,
FT                   ECO:0007744|PDB:8TWE"
FT   REPEAT          347..381
FT                   /note="WD 6"
FT                   /evidence="ECO:0000269|PubMed:38123684,
FT                   ECO:0007744|PDB:8SO0, ECO:0007744|PDB:8TTB,
FT                   ECO:0007744|PDB:8TWE"
FT   REPEAT          414..446
FT                   /note="WD 7"
FT                   /evidence="ECO:0000269|PubMed:38123684,
FT                   ECO:0007744|PDB:8SO0, ECO:0007744|PDB:8TTB,
FT                   ECO:0007744|PDB:8TWE"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895"
FT   VAR_SEQ         1..2
FT                   /note="MA -> MFPKFSLRSMFH (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_043100"
FT   STRAND          12..18
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          21..23
FT                   /evidence="ECO:0007829|PDB:9C7T"
FT   TURN            26..28
FT                   /evidence="ECO:0007829|PDB:9C7T"
FT   STRAND          31..36
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          38..47
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          50..57
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          71..78
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          83..85
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   TURN            86..89
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          90..92
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          98..101
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   HELIX           102..104
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          106..114
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          119..132
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          135..137
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   HELIX           146..148
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          156..172
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          182..185
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          189..195
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          197..204
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          211..216
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   HELIX           222..224
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          229..234
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          241..246
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          251..255
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   TURN            256..258
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          260..262
FT                   /evidence="ECO:0007829|PDB:3DW8"
FT   STRAND          266..269
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   HELIX           272..274
FT                   /evidence="ECO:0007829|PDB:9C6B"
FT   HELIX           275..277
FT                   /evidence="ECO:0007829|PDB:9C6B"
FT   HELIX           282..285
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          288..293
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          297..312
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          320..325
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   HELIX           327..329
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   TURN            330..332
FT                   /evidence="ECO:0007829|PDB:3DW8"
FT   HELIX           333..338
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   HELIX           341..343
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          348..350
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          354..360
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   TURN            362..364
FT                   /evidence="ECO:0007829|PDB:8UO5"
FT   STRAND          365..370
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   TURN            371..373
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          376..380
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   HELIX           383..385
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   HELIX           392..395
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          396..398
FT                   /evidence="ECO:0007829|PDB:9C6B"
FT   TURN            404..406
FT                   /evidence="ECO:0007829|PDB:9C6B"
FT   STRAND          407..409
FT                   /evidence="ECO:0007829|PDB:9C6B"
FT   HELIX           410..412
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          421..424
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          426..434
FT                   /evidence="ECO:0007829|PDB:8TWE"
FT   STRAND          439..444
FT                   /evidence="ECO:0007829|PDB:8TWE"
SQ   SEQUENCE   447 AA;  51692 MW;  F4D407FF7ADA4ED6 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
     MTRDYLSVKI WDLNMENRPV ETYQVHEYLR SKLCSLYEND CIFDKFECCW NGSDSVVMTG
     SYNNFFRMFD RNTKRDITLE ASRENNKPRT VLKPRKVCAS GKRKKDEISV DSLDFNKKIL
     HTAWHPKENI IAVATTNNLY IFQDKVN
//