PP2AA_MOUSE
ID PP2AA_MOUSE Reviewed; 309 AA.
AC P63330; O88591; P13353; Q5SNY5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;
DE Short=PP2A-alpha;
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:P67775};
GN Name=Ppp2ca;
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].
RC STRAIN=C57BL/6 X DBA/2; TISSUE=Brain;
RA Goetz J.M., Kues W.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9920888; DOI=10.1074/jbc.274.6.3439;
RA Hsu W., Zeng L., Costantini F.;
RT "Identification of a domain of Axin that binds to the serine/threonine
RT protein phosphatase 2A and a self-binding domain.";
RL J. Biol. Chem. 274:3439-3445(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Spleen;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye, and Mammary gland;
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 PHOSPHORYLATION AT TYR-307.
RX PubMed=7510677; DOI=10.1016/s0021-9258(17)37144-2;
RA Chen J., Parsons S., Brautigan D.L.;
RT "Tyrosine phosphorylation of protein phosphatase 2A in response to growth
RT stimulation and v-src transformation of fibroblasts.";
RL J. Biol. Chem. 269:7957-7962(1994).
RN [7]
RP MUTAGENESIS OF TYR-307 AND LEU-309, AND METHYLATION AT LEU-309.
RX PubMed=10441131; DOI=10.1021/bi990902g;
RA Chung H., Nairn A.C., Murata K., Brautigan D.L.;
RT "Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic
RT subunit favors association with the alpha 4 subunit which promotes
RT dephosphorylation of elongation factor-2.";
RL Biochemistry 38:10371-10376(1999).
RN [8]
RP INTERACTION WITH NXN.
RX PubMed=16764867; DOI=10.1016/j.febslet.2006.04.101;
RA Lechward K., Sugajska E., de Baere I., Goris J., Hemmings B.A.,
RA Zolnierowicz S.;
RT "Interaction of nucleoredoxin with protein phosphatase 2A.";
RL FEBS Lett. 580:3631-3637(2006).
RN [9]
RP INTERACTION WITH ADCY8.
RX PubMed=16258073; DOI=10.1124/mol.105.018275;
RA Crossthwaite A.J., Ciruela A., Rayner T.F., Cooper D.M.;
RT "A direct interaction between the N terminus of adenylyl cyclase AC8 and
RT the catalytic subunit of protein phosphatase 2A.";
RL Mol. Pharmacol. 69:608-617(2006).
RN [10]
RP INTERACTION WITH BTBD10.
RX PubMed=18160256; DOI=10.1016/j.cellsig.2007.11.004;
RA Nawa M., Kanekura K., Hashimoto Y., Aiso S., Matsuoka M.;
RT "A novel Akt/PKB-interacting protein promotes cell adhesion and inhibits
RT familial amyotrophic lateral sclerosis-linked mutant SOD1-induced neuronal
RT death via inhibition of PP2A-mediated dephosphorylation of Akt/PKB.";
RL Cell. Signal. 20:493-505(2008).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18084284; DOI=10.1038/ncb1667;
RA Lee J., Kitajima T.S., Tanno Y., Yoshida K., Morita T., Miyano T.,
RA Miyake M., Watanabe Y.;
RT "Unified mode of centromeric protection by shugoshin in mammalian oocytes
RT and somatic cells.";
RL Nat. Cell Biol. 10:42-52(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP INTERACTION WITH KCTD20.
RX PubMed=24156551; DOI=10.1186/1471-2091-14-27;
RA Nawa M., Matsuoka M.;
RT "KCTD20, a relative of BTBD10, is a positive regulator of Akt.";
RL BMC Biochem. 14:27-27(2013).
RN [14]
RP MONUBIQUITINATION BY NOSIP.
RX PubMed=25546391; DOI=10.1371/journal.pone.0116150;
RA Hoffmeister M., Prelle C., Kuechler P., Kovacevic I., Moser M.,
RA Mueller-Esterl W., Oess S.;
RT "The ubiquitin E3 ligase NOSIP modulates protein phosphatase 2A activity in
RT craniofacial development.";
RL PLoS ONE 9:E116150-E116150(2014).
RN [15]
RP FUNCTION, AND INTERACTION WITH AMBRA1.
RX PubMed=25438055; DOI=10.1038/ncb3072;
RA Cianfanelli V., Fuoco C., Lorente M., Salazar M., Quondamatteo F.,
RA Gherardini P.F., De Zio D., Nazio F., Antonioli M., D'Orazio M., Skobo T.,
RA Bordi M., Rohde M., Dalla Valle L., Helmer-Citterich M., Gretzmeier C.,
RA Dengjel J., Fimia G.M., Piacentini M., Di Bartolomeo S., Velasco G.,
RA Cecconi F.;
RT "AMBRA1 links autophagy to cell proliferation and tumorigenesis by
RT promoting c-Myc dephosphorylation and degradation.";
RL Nat. Cell Biol. 17:20-30(2015).
RN [16]
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).
CC -!- FUNCTION: PP2A is the major phosphatase for microtubule-associated
CC proteins (MAPs) (By similarity). PP2A can modulate the activity of
CC phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase,
CC and MAP-2 kinase (By similarity). Cooperates with SGO2 to protect
CC centromeric cohesin from separase-mediated cleavage in oocytes
CC specifically during meiosis I (PubMed:18084284). Can dephosphorylate
CC p53/TP53 (By similarity). Activates RAF1 by dephosphorylating it at
CC 'Ser-259' (By similarity). Mediates dephosphorylation of WEE1,
CC preventing its ubiquitin-mediated proteolysis, increasing WEE1 protein
CC levels, and promoting the G2/M checkpoint (By similarity). Mediates
CC dephosphorylation of MYC; promoting its ubiquitin-mediated proteolysis:
CC interaction with AMBRA1 enhances interaction between PPP2CA and MYC
CC (PubMed:25438055). Mediates dephosphorylation of FOXO3; promoting its
CC stabilization: interaction with AMBRA1 enhances interaction between
CC PPP2CA and FOXO3 (By similarity). {ECO:0000250|UniProtKB:P67775,
CC ECO:0000269|PubMed:18084284, ECO:0000269|PubMed:25438055}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000250|UniProtKB:P67775};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000250|UniProtKB:P67775};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P67775};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:P67775};
CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed
CC of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa
CC constant regulatory subunit (PR65 or subunit A), that associates with a
CC variety of regulatory subunitst (By similarity). Proteins that
CC associate with the core dimer include three families of regulatory
CC subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56
CC families), the 48 kDa variable regulatory subunit, viral proteins, and
CC cell signaling molecules (By similarity). Interacts with NXN; the
CC interaction is direct (By similarity). Interacts with KCTD20
CC (PubMed:24156551). Interacts with BTBD10 (PubMed:18160256). Interacts
CC with SGO1 and SGO2 (By similarity). Interacts with TP53 (By
CC similarity). Interacts with AXIN1; the interaction dephosphorylates
CC AXIN1 (By similarity). Interacts with PIM3; this interaction promotes
CC dephosphorylation, ubiquitination and proteasomal degradation of PIM3
CC (By similarity). Interacts with RAF1 (By similarity). Interaction with
CC IGBP1 protects unassembled PPP2CA from degradative ubiquitination (By
CC similarity). Interacts with GSK3B (via C2 domain) (By similarity).
CC Interacts with MFHAS1; retains PPP2CA into the cytoplasm and excludes
CC it from the nucleus (By similarity). Interacts with PABIR1/FAM122A (By
CC similarity). Interacts with ADCY8; interaction is phosphatase activity-
CC dependent; antagonizes interaction between ADCY8 and calmodulin
CC (PubMed:16258073). Interacts with CRTC3 (when phosphorylated at 'Ser-
CC 391') (PubMed:30611118). Interacts with SPRY2; the interaction is
CC inhibited by TESK1 interaction with SPRY2, possibly by vesicular
CC sequestration of SPRY2 (By similarity). Interacts with TRAF3IP3 (By
CC similarity). Interacts with AMBRA1 (via PxP motifs); enhancing
CC interaction between PPP2CA and MYC or FOXO3 (PubMed:25438055). Forms a
CC complex with AMBRA1 and BECN1; AMBRA1 and BECN1 components of the
CC complex regulate MYC stability via different pathways (By similarity).
CC {ECO:0000250|UniProtKB:P67775, ECO:0000269|PubMed:16258073,
CC ECO:0000269|PubMed:18160256, ECO:0000269|PubMed:24156551,
CC ECO:0000269|PubMed:25438055, ECO:0000269|PubMed:30611118}.
CC -!- INTERACTION:
CC P63330; Q61249: Igbp1; NbExp=2; IntAct=EBI-397144, EBI-7002233;
CC P63330; Q76MZ3: Ppp2r1a; NbExp=3; IntAct=EBI-397144, EBI-400413;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18084284}. Nucleus
CC {ECO:0000250|UniProtKB:P67775}. Chromosome, centromere
CC {ECO:0000269|PubMed:18084284}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:P67775}. Note=In prometaphase cells, but not in
CC anaphase cells, localizes at centromeres (By similarity). During
CC mitosis, also found at spindle poles (By similarity). Centromeric
CC localization requires the presence of SGO2 (PubMed:18084284).
CC {ECO:0000250|UniProtKB:P67775, ECO:0000269|PubMed:18084284}.
CC -!- PTM: Reversibly methyl esterified on Leu-309 by leucine carboxyl
CC methyltransferase 1 (Lcmt1) and protein phosphatase methylesterase 1
CC (Ppme1). Carboxyl methylation influences the affinity of the catalytic
CC subunit for the different regulatory subunits, thereby modulating the
CC PP2A holoenzyme's substrate specificity, enzyme activity and cellular
CC localization. {ECO:0000269|PubMed:10441131}.
CC -!- PTM: Phosphorylation of either threonine (by autophosphorylation-
CC activated protein kinase) or tyrosine results in inactivation of the
CC phosphatase. Auto-dephosphorylation has been suggested as a mechanism
CC for reactivation. {ECO:0000269|PubMed:7510677}.
CC -!- PTM: Polyubiquitinated, leading to its degradation by the proteasome
CC (By similarity). May be monoubiquitinated by NOSIP (PubMed:25546391).
CC {ECO:0000250|UniProtKB:P67775, ECO:0000269|PubMed:25546391}.
CC -!- MISCELLANEOUS: Double mutation Phe-307 and Gln-309 results in
CC association of the PP2A C subunit with alpha-4 protein.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF076192; AAD12587.1; -; mRNA.
DR EMBL; Z67745; CAA91558.1; -; mRNA.
DR EMBL; AK076110; BAC36190.1; -; mRNA.
DR EMBL; AK172644; BAE43111.1; -; mRNA.
DR EMBL; AL935177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003856; AAH03856.1; -; mRNA.
DR EMBL; BC054458; AAH54458.1; -; mRNA.
DR CCDS; CCDS24666.1; -.
DR RefSeq; NP_062284.1; NM_019411.4.
DR AlphaFoldDB; P63330; -.
DR SMR; P63330; -.
DR BioGRID; 202341; 107.
DR CORUM; P63330; -.
DR IntAct; P63330; 66.
DR MINT; P63330; -.
DR STRING; 10090.ENSMUSP00000020608; -.
DR iPTMnet; P63330; -.
DR PhosphoSitePlus; P63330; -.
DR SwissPalm; P63330; -.
DR EPD; P63330; -.
DR jPOST; P63330; -.
DR MaxQB; P63330; -.
DR PaxDb; P63330; -.
DR PeptideAtlas; P63330; -.
DR PRIDE; P63330; -.
DR ProteomicsDB; 289785; -.
DR Antibodypedia; 3550; 674 antibodies from 45 providers.
DR DNASU; 19052; -.
DR Ensembl; ENSMUST00000020608; ENSMUSP00000020608; ENSMUSG00000020349.
DR GeneID; 19052; -.
DR KEGG; mmu:19052; -.
DR UCSC; uc007ivb.1; mouse.
DR CTD; 5515; -.
DR MGI; MGI:1321159; Ppp2ca.
DR VEuPathDB; HostDB:ENSMUSG00000020349; -.
DR eggNOG; KOG0371; Eukaryota.
DR GeneTree; ENSGT00550000074618; -.
DR HOGENOM; CLU_004962_0_5_1; -.
DR InParanoid; P63330; -.
DR OMA; SWSHQES; -.
DR OrthoDB; 808922at2759; -.
DR PhylomeDB; P63330; -.
DR TreeFam; TF105559; -.
DR Reactome; R-MMU-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-MMU-1295596; Spry regulation of FGF signaling.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-180024; DARPP-32 events.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-MMU-198753; ERK/MAPK targets.
DR Reactome; R-MMU-202670; ERKs are inactivated.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-MMU-389513; CTLA4 inhibitory signaling.
DR Reactome; R-MMU-432142; Platelet sensitization by LDL.
DR Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-5673000; RAF activation.
DR Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR Reactome; R-MMU-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 19052; 23 hits in 71 CRISPR screens.
DR ChiTaRS; Ppp2ca; mouse.
DR PRO; PR:P63330; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P63330; protein.
DR Bgee; ENSMUSG00000020349; Expressed in medial ganglionic eminence and 255 other tissues.
DR Genevisible; P63330; MM.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:MGI.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0031698; F:beta-2 adrenergic receptor binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0050811; F:GABA receptor binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:1990405; F:protein antigen binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0043422; F:protein kinase B binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0048156; F:tau protein binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007498; P:mesoderm development; IMP:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:1901020; P:negative regulation of calcium ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; ISO:MGI.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:1904528; P:positive regulation of microtubule binding; ISO:MGI.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:MGI.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; TAS:MGI.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0031952; P:regulation of protein autophosphorylation; ISO:MGI.
DR GO; GO:0042176; P:regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0010469; P:regulation of signaling receptor activity; ISO:MGI.
DR GO; GO:0010288; P:response to lead ion; ISO:MGI.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Centromere; Chromosome; Cytoplasm; Cytoskeleton; Hydrolase; Manganese;
KW Meiosis; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW Protein phosphatase; Reference proteome; Ubl conjugation.
FT CHAIN 1..309
FT /note="Serine/threonine-protein phosphatase 2A catalytic
FT subunit alpha isoform"
FT /id="PRO_0000058840"
FT ACT_SITE 118
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 57
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 59
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 85
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 85
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 117
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 241
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT MOD_RES 307
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:7510677"
FT MOD_RES 309
FT /note="Leucine methyl ester"
FT /evidence="ECO:0000269|PubMed:10441131"
FT MUTAGEN 307
FT /note="Y->Q: Loss of trimeric subunit ABC assembly."
FT /evidence="ECO:0000269|PubMed:10441131"
FT MUTAGEN 309
FT /note="L->A: Loss of binding to PP2A B-alpha regulatory
FT subunit."
FT /evidence="ECO:0000269|PubMed:10441131"
FT CONFLICT 31
FT /note="L -> P (in Ref. 2; AAD12587)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="G -> V (in Ref. 2; AAD12587)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 35608 MW; 8DC11276E6DF9E33 CRC64;
MDEKLFTKEL DQWIEQLNEC KQLSESQVKS LCEKAKEILT KESNVQEVRC PVTVCGDVHG
QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL VALKVRYRER ITILRGNHES
RQITQVYGFY DECLRKYGNA NVWKYFTDLF DYLPLTALVD GQIFCLHGGL SPSIDTLDHI
RALDRLQEVP HEGPMCDLLW SDPDDRGGWG ISPRGAGYTF GQDISETFNH ANGLTLVSRA
HQLVMEGYNW CHDRNVVTIF SAPNYCYRCG NQAAIMELDD TLKYSFLQFD PAPRRGEPHV
TRRTPDYFL
