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Database: UniProt
Entry: 2AAA_HUMAN
LinkDB: 2AAA_HUMAN
Original site: 2AAA_HUMAN 
ID   2AAA_HUMAN              Reviewed;         589 AA.
AC   P30153; Q13773; Q6ICQ3; Q96DH3;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 4.
DT   27-MAR-2024, entry version 230.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;
DE   AltName: Full=Medium tumor antigen-associated 61 kDa protein;
DE   AltName: Full=PP2A subunit A isoform PR65-alpha;
DE   AltName: Full=PP2A subunit A isoform R1-alpha;
GN   Name=PPP2R1A;
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], AND PROTEIN SEQUENCE OF 242-255.
RC   TISSUE=Placenta;
RX   PubMed=2554323; DOI=10.1073/pnas.86.22.8669;
RA   Walter G., Ferre F., Espiritu O., Carbone-Wiley A.;
RT   "Molecular cloning and sequence of cDNA encoding polyoma medium tumor
RT   antigen-associated 61-kDa protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:8669-8672(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2159327; DOI=10.1021/bi00465a002;
RA   Hemmings B.A., Adams-Pearson C., Maurer F., Mueller P., Goris J.,
RA   Merlevede W., Hofsteenge J., Stone S.R.;
RT   "Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have
RT   a similar 39 amino acid repeating structure.";
RL   Biochemistry 29:3166-3173(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
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   [5]
RP   PROTEIN SEQUENCE OF 34-46, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Brain, and Cajal-Retzius cell;
RA   Lubec G., Vishwanath V.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [6]
RP   PROTEIN SEQUENCE OF 204-214; 261-272 AND 521-527.
RX   PubMed=8694763; DOI=10.1042/bj3170187;
RA   Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I.,
RA   Merlevede W., Goris J., Hemmings B.A.;
RT   "The variable subunit associated with protein phosphatase 2A0 defines a
RT   novel multimember family of regulatory subunits.";
RL   Biochem. J. 317:187-194(1996).
RN   [7]
RP   BINDING DOMAINS.
RX   PubMed=8254721; DOI=10.1128/jvi.68.1.123-129.1994;
RA   Ruediger R., Hentz M., Fait J., Mumby M., Walter G.;
RT   "Molecular model of the A subunit of protein phosphatase 2A: interaction
RT   with other subunits and tumor antigens.";
RL   J. Virol. 68:123-129(1994).
RN   [8]
RP   INTERACTION WITH IPO9.
RX   PubMed=12670497; DOI=10.1016/s0006-291x(03)00434-0;
RA   Lubert E.J., Sarge K.D.;
RT   "Interaction between protein phosphatase 2A and members of the importin
RT   beta superfamily.";
RL   Biochem. Biophys. Res. Commun. 303:908-913(2003).
RN   [9]
RP   FUNCTION, INTERACTION WITH GNA12, AND SUBCELLULAR LOCATION.
RX   PubMed=15525651; DOI=10.1074/jbc.c400508200;
RA   Zhu D., Kosik K.S., Meigs T.E., Yanamadala V., Denker B.M.;
RT   "Galpha12 directly interacts with PP2A: evidence for Galpha12-stimulated
RT   PP2A phosphatase activity and dephosphorylation of microtubule-associated
RT   protein, tau.";
RL   J. Biol. Chem. 279:54983-54986(2004).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH SGO1.
RX   PubMed=16580887; DOI=10.1016/j.devcel.2006.03.010;
RA   Tang Z., Shu H., Qi W., Mahmood N.A., Mumby M.C., Yu H.;
RT   "PP2A is required for centromeric localization of Sgo1 and proper
RT   chromosome segregation.";
RL   Dev. Cell 10:575-585(2006).
RN   [11]
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   [12]
RP   INTERACTION WITH PLA2G16.
RX   PubMed=17374643; DOI=10.1242/jcs.000018;
RA   Nazarenko I., Schafer R., Sers C.;
RT   "Mechanisms of the HRSL3 tumor suppressor function in ovarian carcinoma
RT   cells.";
RL   J. Cell Sci. 120:1393-1404(2007).
RN   [13]
RP   INTERACTION WITH SPRY2.
RX   PubMed=17974561; DOI=10.1074/jbc.m705457200;
RA   Chandramouli S., Yu C.Y., Yusoff P., Lao D.H., Leong H.F., Mizuno K.,
RA   Guy G.R.;
RT   "Tesk1 interacts with Spry2 to abrogate its inhibition of ERK
RT   phosphorylation downstream of receptor tyrosine kinase signaling.";
RL   J. Biol. Chem. 283:1679-1691(2008).
RN   [14]
RP   INTERACTION WITH JC VIRUS SMALL T ANTIGEN (MICROBIAL INFECTION).
RX   PubMed=18353419; DOI=10.1016/j.virol.2008.02.020;
RA   Sariyer I.K., Khalili K., Safak M.;
RT   "Dephosphorylation of JC virus agnoprotein by protein phosphatase 2A:
RT   inhibition by small t antigen.";
RL   Virology 375:464-479(2008).
RN   [15]
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   [16]
RP   INTERACTION WITH CTTNBP2NL.
RX   PubMed=18782753; DOI=10.1074/mcp.m800266-mcp200;
RA   Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G.,
RA   Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I.,
RA   Aebersold R., Raught B., Gingras A.C.;
RT   "A PP2A phosphatase high density interaction network identifies a novel
RT   striatin-interacting phosphatase and kinase complex linked to the cerebral
RT   cavernous malformation 3 (CCM3) protein.";
RL   Mol. Cell. Proteomics 8:157-171(2009).
RN   [17]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-280, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [18]
RP   INTERACTION WITH JC VIRUS SMALL T ANTIGEN (MICROBIAL INFECTION).
RX   PubMed=20485545; DOI=10.1371/journal.pone.0010606;
RA   Bollag B., Hofstetter C.A., Reviriego-Mendoza M.M., Frisque R.J.;
RT   "JC virus small T antigen binds phosphatase PP2A and Rb family proteins and
RT   is required for efficient viral DNA replication activity.";
RL   PLoS ONE 5:e10606-e10606(2010).
RN   [19]
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   [20]
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   [21]
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=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [22]
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   [23]
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=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [24]
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   [25]
RP   INTERACTION WITH CIP2A.
RX   PubMed=28174209; DOI=10.15252/embr.201642788;
RA   Wang J., Okkeri J., Pavic K., Wang Z., Kauko O., Halonen T., Sarek G.,
RA   Ojala P.M., Rao Z., Xu W., Westermarck J.;
RT   "Oncoprotein CIP2A is stabilized via interaction with tumor suppressor
RT   PP2A/B56.";
RL   EMBO Rep. 18:437-450(2017).
RN   [26]
RP   INTERACTION WITH CRTC3, AND SUBCELLULAR LOCATION.
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   [27]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   PubMed=9989501; DOI=10.1016/s0092-8674(00)80963-0;
RA   Groves M.R., Hanlon N., Turowski P., Hemmings B.A., Barford D.;
RT   "The structure of the protein phosphatase 2A PR65/A subunit reveals the
RT   conformation of its 15 tandemly repeated HEAT motifs.";
RL   Cell 96:99-110(1999).
RN   [28]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 9-589 IN COMPLEX WITH PPP2CA AND
RP   PPME1.
RX   PubMed=18394995; DOI=10.1016/j.cell.2008.02.041;
RA   Xing Y., Li Z., Chen Y., Stock J.B., Jeffrey P.D., Shi Y.;
RT   "Structural mechanism of demethylation and inactivation of protein
RT   phosphatase 2A.";
RL   Cell 133:154-163(2008).
RN   [29]
RP   VARIANTS HJS2 LEU-179; TRP-182 AND HIS-258, AND CHARACTERIZATION HJS2 OF
RP   VARIANTS LEU-179; TRP-182 AND HIS-258.
RX   PubMed=26168268; DOI=10.1172/jci79860;
RA   Houge G., Haesen D., Vissers L.E., Mehta S., Parker M.J., Wright M.,
RA   Vogt J., McKee S., Tolmie J.L., Cordeiro N., Kleefstra T., Willemsen M.H.,
RA   Reijnders M.R., Berland S., Hayman E., Lahat E., Brilstra E.H.,
RA   van Gassen K.L., Zonneveld-Huijssoon E., de Bie C.I., Hoischen A.,
RA   Eichler E.E., Holdhus R., Steen V.M., Doeskeland S.O., Hurles M.E.,
RA   FitzPatrick D.R., Janssens V.;
RT   "B56delta-related protein phosphatase 2A dysfunction identified in patients
RT   with intellectual disability.";
RL   J. Clin. Invest. 125:3051-3062(2015).
RN   [30]
RP   INVOLVEMENT IN HJS2, AND VARIANT HJS2 LEU-132.
RX   PubMed=25533962; DOI=10.1038/nature14135;
RG   Deciphering Developmental Disorders Study;
RT   "Large-scale discovery of novel genetic causes of developmental
RT   disorders.";
RL   Nature 519:223-228(2015).
RN   [31]
RP   VARIANTS HJS2 VAL-180; THR-180; ALA-470 AND LEU-498, CHARACTERIZATION OF
RP   VARIANTS HJS2 THR-180; ALA-470 AND LEU-498, AND INTERACTION WITH PPP2R5D
RP   AND PPP2CA.
RX   PubMed=37761890; DOI=10.3390/genes14091750;
RA   Qian Y., Jiang Y., Wang J., Li G., Wu B., Zhou Y., Xu X., Wang H.;
RT   "Novel Variants of PPP2R1A in Catalytic Subunit Binding Domain and
RT   Genotype-Phenotype Analysis in Neurodevelopmentally Delayed Patients.";
RL   Genes (Basel) 14:1750-1750(2023).
CC   -!- FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a
CC       scaffolding molecule to coordinate the assembly of the catalytic
CC       subunit and a variable regulatory B subunit. Upon interaction with
CC       GNA12 promotes dephosphorylation of microtubule associated protein
CC       TAU/MAPT (PubMed:15525651). Required for proper chromosome segregation
CC       and for centromeric localization of SGO1 in mitosis (PubMed:16580887).
CC       Together with RACK1 adapter, mediates dephosphorylation of AKT1 at
CC       'Ser-473', preventing AKT1 activation and AKT-mTOR signaling pathway
CC       (By similarity). Dephosphorylation of AKT1 is essential for regulatory
CC       T-cells (Treg) homeostasis and stability (By similarity).
CC       {ECO:0000250|UniProtKB:Q76MZ3, ECO:0000269|PubMed:15525651,
CC       ECO:0000269|PubMed:16580887}.
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 subunits. Proteins that associate with the core
CC       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. Found in a complex with at least ARL2, PPP2CB, PPP2R1A,
CC       PPP2R2A, PPP2R5E and TBCD (By similarity). Interacts with the PP2A C
CC       catalytic subunit PPP2CA (PubMed:37761890). Interacts with the PP2A B
CC       subunit PPP2R5D (PubMed:37761890). Interacts with FOXO1; the
CC       interaction dephosphorylates FOXO1 on AKT-mediated phosphorylation
CC       sites (By similarity). Interacts with IPO9 (PubMed:12670497). Interacts
CC       with TP53 and SGO1 (PubMed:17245430, PubMed:16580887). Interacts with
CC       PLA2G16; this interaction might decrease PP2A activity
CC       (PubMed:17374643). Interacts with CTTNBP2NL (PubMed:18782753).
CC       Interacts with GNA12; the interaction promotes protein phosphatase 2A
CC       activation causing dephosphorylation of MAPT (PubMed:15525651).
CC       Interacts with CIP2A; this interaction stabilizes CIP2A
CC       (PubMed:28174209). Interacts with PABIR1/FAM122A (PubMed:27588481).
CC       Interacts with ADCY8; antagonizes interaction between ADCY8 and
CC       calmodulin (By similarity). Interacts with CRTC3 (when phosphorylated
CC       at 'Ser-391') (PubMed:30611118). Interacts with SPRY2
CC       (PubMed:17974561). {ECO:0000250|UniProtKB:Q32PI5,
CC       ECO:0000250|UniProtKB:Q76MZ3, ECO:0000269|PubMed:12670497,
CC       ECO:0000269|PubMed:15525651, ECO:0000269|PubMed:16580887,
CC       ECO:0000269|PubMed:17245430, ECO:0000269|PubMed:17374643,
CC       ECO:0000269|PubMed:17974561, ECO:0000269|PubMed:18394995,
CC       ECO:0000269|PubMed:18782753, ECO:0000269|PubMed:27588481,
CC       ECO:0000269|PubMed:28174209, ECO:0000269|PubMed:30611118,
CC       ECO:0000269|PubMed:37761890}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with JC virus small t antigen;
CC       this interaction inhibits PPP2R1A activity.
CC       {ECO:0000269|PubMed:18353419, ECO:0000269|PubMed:20485545}.
CC   -!- INTERACTION:
CC       P30153; P31749: AKT1; NbExp=2; IntAct=EBI-302388, EBI-296087;
CC       P30153; Q9C0C7: AMBRA1; NbExp=3; IntAct=EBI-302388, EBI-2512975;
CC       P30153; Q14155: ARHGEF7; NbExp=3; IntAct=EBI-302388, EBI-717515;
CC       P30153; Q96GD4: AURKB; NbExp=3; IntAct=EBI-302388, EBI-624291;
CC       P30153; Q9Y2V2: CARHSP1; NbExp=3; IntAct=EBI-302388, EBI-718719;
CC       P30153; P51959: CCNG1; NbExp=2; IntAct=EBI-302388, EBI-3905829;
CC       P30153; Q8TCG1: CIP2A; NbExp=4; IntAct=EBI-302388, EBI-1379376;
CC       P30153; Q9Y534: CSDC2; NbExp=6; IntAct=EBI-302388, EBI-1763657;
CC       P30153; Q4G163: FBXO43; NbExp=3; IntAct=EBI-302388, EBI-12053217;
CC       P30153; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-302388, EBI-11163335;
CC       P30153; Q08AF8: GOLGA8G; NbExp=3; IntAct=EBI-302388, EBI-10181260;
CC       P30153; P53816: PLAAT3; NbExp=7; IntAct=EBI-302388, EBI-746318;
CC       P30153; P67775: PPP2CA; NbExp=46; IntAct=EBI-302388, EBI-712311;
CC       P30153; P67775-1: PPP2CA; NbExp=5; IntAct=EBI-302388, EBI-16765970;
CC       P30153; P30154: PPP2R1B; NbExp=2; IntAct=EBI-302388, EBI-357094;
CC       P30153; P63151: PPP2R2A; NbExp=17; IntAct=EBI-302388, EBI-1048931;
CC       P30153; Q00005: PPP2R2B; NbExp=10; IntAct=EBI-302388, EBI-1052159;
CC       P30153; Q15172: PPP2R5A; NbExp=6; IntAct=EBI-302388, EBI-641666;
CC       P30153; Q15173: PPP2R5B; NbExp=4; IntAct=EBI-302388, EBI-1369497;
CC       P30153; Q13362: PPP2R5C; NbExp=10; IntAct=EBI-302388, EBI-1266156;
CC       P30153; Q13362-1: PPP2R5C; NbExp=5; IntAct=EBI-302388, EBI-1266170;
CC       P30153; Q13362-2: PPP2R5C; NbExp=4; IntAct=EBI-302388, EBI-1266173;
CC       P30153; Q14738: PPP2R5D; NbExp=12; IntAct=EBI-302388, EBI-396563;
CC       P30153; Q16537: PPP2R5E; NbExp=7; IntAct=EBI-302388, EBI-968374;
CC       P30153; P60510: PPP4C; NbExp=6; IntAct=EBI-302388, EBI-1046072;
CC       P30153; P53041: PPP5C; NbExp=3; IntAct=EBI-302388, EBI-716663;
CC       P30153; Q15257-2: PTPA; NbExp=3; IntAct=EBI-302388, EBI-12164121;
CC       P30153; Q04206: RELA; NbExp=2; IntAct=EBI-302388, EBI-73886;
CC       P30153; O43815: STRN; NbExp=8; IntAct=EBI-302388, EBI-1046642;
CC       P30153; O43815-2: STRN; NbExp=3; IntAct=EBI-302388, EBI-1266294;
CC       P30153; Q13033-2: STRN3; NbExp=9; IntAct=EBI-302388, EBI-1053876;
CC       P30153; P04637: TP53; NbExp=3; IntAct=EBI-302388, EBI-366083;
CC       P30153; P03129: E7; Xeno; NbExp=3; IntAct=EBI-302388, EBI-866453;
CC       P30153; P04020: E7; Xeno; NbExp=2; IntAct=EBI-302388, EBI-7005254;
CC       P30153; P97346: Nxn; Xeno; NbExp=2; IntAct=EBI-302388, EBI-309684;
CC       P30153; Q60996-3: Ppp2r5c; Xeno; NbExp=2; IntAct=EBI-302388, EBI-1369292;
CC       P30153; P03081; Xeno; NbExp=5; IntAct=EBI-302388, EBI-1266256;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q32PI5}. Nucleus
CC       {ECO:0000269|PubMed:30611118}. Chromosome, centromere
CC       {ECO:0000269|PubMed:16580887}. Lateral cell membrane
CC       {ECO:0000269|PubMed:15525651}. Cell projection, dendrite
CC       {ECO:0000269|PubMed:15525651}. Note=Centromeric localization requires
CC       the presence of BUB1. {ECO:0000269|PubMed:16580887}.
CC   -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices joined
CC       by a hydrophilic region, the intrarepeat loop. The repeat units may be
CC       arranged laterally to form a rod-like structure.
CC   -!- DISEASE: Houge-Janssens syndrome 2 (HJS2) [MIM:616362]: An autosomal
CC       dominant disorder characterized by global developmental delay,
CC       hypotonia, variably impaired intellectual development, poor speech, and
CC       dysmorphic facial features. Some patients may develop seizures.
CC       {ECO:0000269|PubMed:25533962, ECO:0000269|PubMed:26168268,
CC       ECO:0000269|PubMed:37761890}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A family.
CC       {ECO:0000305}.
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DR   EMBL; M31786; AAA35531.1; -; mRNA.
DR   EMBL; J02902; AAA36399.1; -; mRNA.
DR   EMBL; CR450340; CAG29336.1; -; mRNA.
DR   EMBL; BC001537; AAH01537.1; -; mRNA.
DR   CCDS; CCDS12849.1; -.
DR   PIR; A34541; A34541.
DR   RefSeq; NP_055040.2; NM_014225.5.
DR   PDB; 1B3U; X-ray; 2.30 A; A/B=2-589.
DR   PDB; 2IE3; X-ray; 2.80 A; A=1-589.
DR   PDB; 2IE4; X-ray; 2.60 A; A=1-589.
DR   PDB; 2NPP; X-ray; 3.30 A; A/D=1-589.
DR   PDB; 2NYL; X-ray; 3.80 A; A/D=8-589.
DR   PDB; 2NYM; X-ray; 3.60 A; A/D=8-589.
DR   PDB; 2PKG; X-ray; 3.30 A; A/B=10-589.
DR   PDB; 3C5W; X-ray; 2.80 A; A=9-46, A=400-589.
DR   PDB; 3DW8; X-ray; 2.85 A; A/D=9-589.
DR   PDB; 3K7V; X-ray; 2.85 A; A=1-589.
DR   PDB; 3K7W; X-ray; 2.96 A; A=1-589.
DR   PDB; 4I5L; X-ray; 2.43 A; A/D=6-589.
DR   PDB; 4I5N; X-ray; 2.80 A; A/D=6-589.
DR   PDB; 4LAC; X-ray; 2.82 A; A=404-589.
DR   PDB; 5W0W; X-ray; 3.80 A; A/D/G/J=9-589.
DR   PDB; 6IUR; X-ray; 3.33 A; A/B/E/F=8-589.
DR   PDB; 6NTS; EM; 3.63 A; A=1-589.
DR   PDB; 7CUN; EM; 3.50 A; P=1-589.
DR   PDB; 7K36; EM; 3.30 A; A=1-589.
DR   PDB; 7PKS; EM; 3.60 A; p=1-589.
DR   PDB; 7SOY; EM; 3.40 A; A=1-589.
DR   PDB; 7YCX; EM; 4.18 A; P=1-589.
DR   PDB; 8SO0; EM; 2.80 A; A=9-589.
DR   PDB; 8TTB; EM; 2.77 A; A=9-589.
DR   PDB; 8TWE; EM; 2.55 A; A=9-589.
DR   PDB; 8TWI; EM; 2.69 A; A=9-589.
DR   PDBsum; 1B3U; -.
DR   PDBsum; 2IE3; -.
DR   PDBsum; 2IE4; -.
DR   PDBsum; 2NPP; -.
DR   PDBsum; 2NYL; -.
DR   PDBsum; 2NYM; -.
DR   PDBsum; 2PKG; -.
DR   PDBsum; 3C5W; -.
DR   PDBsum; 3DW8; -.
DR   PDBsum; 3K7V; -.
DR   PDBsum; 3K7W; -.
DR   PDBsum; 4I5L; -.
DR   PDBsum; 4I5N; -.
DR   PDBsum; 4LAC; -.
DR   PDBsum; 5W0W; -.
DR   PDBsum; 6IUR; -.
DR   PDBsum; 6NTS; -.
DR   PDBsum; 7CUN; -.
DR   PDBsum; 7K36; -.
DR   PDBsum; 7PKS; -.
DR   PDBsum; 7SOY; -.
DR   PDBsum; 7YCX; -.
DR   PDBsum; 8SO0; -.
DR   PDBsum; 8TTB; -.
DR   PDBsum; 8TWE; -.
DR   PDBsum; 8TWI; -.
DR   AlphaFoldDB; P30153; -.
DR   EMDB; EMD-0510; -.
DR   EMDB; EMD-13479; -.
DR   EMDB; EMD-22650; -.
DR   EMDB; EMD-25363; -.
DR   EMDB; EMD-30473; -.
DR   EMDB; EMD-33741; -.
DR   EMDB; EMD-40644; -.
DR   EMDB; EMD-41604; -.
DR   EMDB; EMD-41667; -.
DR   EMDB; EMD-41668; -.
DR   SMR; P30153; -.
DR   BioGRID; 111510; 658.
DR   CORUM; P30153; -.
DR   DIP; DIP-29394N; -.
DR   IntAct; P30153; 270.
DR   MINT; P30153; -.
DR   STRING; 9606.ENSP00000324804; -.
DR   DrugBank; DB06905; (2S,3S,4E,6E,8S,9S)-3-amino-9-methoxy-2,6,8-trimethyl-10-phenyldeca-4,6-dienoic acid.
DR   DrugBank; DB02506; 2,6,8-Trimethyl-3-Amino-9-Benzyl-9-Methoxynonanoic Acid.
DR   GlyCosmos; P30153; 1 site, 1 glycan.
DR   GlyGen; P30153; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P30153; -.
DR   MetOSite; P30153; -.
DR   PhosphoSitePlus; P30153; -.
DR   SwissPalm; P30153; -.
DR   BioMuta; PPP2R1A; -.
DR   DMDM; 143811355; -.
DR   OGP; P30153; -.
DR   REPRODUCTION-2DPAGE; IPI00554737; -.
DR   CPTAC; CPTAC-257; -.
DR   CPTAC; CPTAC-258; -.
DR   EPD; P30153; -.
DR   jPOST; P30153; -.
DR   MassIVE; P30153; -.
DR   MaxQB; P30153; -.
DR   PaxDb; 9606-ENSP00000324804; -.
DR   PeptideAtlas; P30153; -.
DR   ProteomicsDB; 54636; -.
DR   Pumba; P30153; -.
DR   Antibodypedia; 4348; 421 antibodies from 42 providers.
DR   DNASU; 5518; -.
DR   Ensembl; ENST00000322088.11; ENSP00000324804.6; ENSG00000105568.19.
DR   GeneID; 5518; -.
DR   KEGG; hsa:5518; -.
DR   MANE-Select; ENST00000322088.11; ENSP00000324804.6; NM_014225.6; NP_055040.2.
DR   UCSC; uc002pyp.4; human.
DR   AGR; HGNC:9302; -.
DR   CTD; 5518; -.
DR   DisGeNET; 5518; -.
DR   GeneCards; PPP2R1A; -.
DR   GeneReviews; PPP2R1A; -.
DR   HGNC; HGNC:9302; PPP2R1A.
DR   HPA; ENSG00000105568; Low tissue specificity.
DR   MalaCards; PPP2R1A; -.
DR   MIM; 605983; gene.
DR   MIM; 616362; phenotype.
DR   neXtProt; NX_P30153; -.
DR   OpenTargets; ENSG00000105568; -.
DR   Orphanet; 457284; Microcephaly-corpus callosum hypoplasia-intellectual disability-facial dysmorphism syndrome.
DR   PharmGKB; PA33666; -.
DR   VEuPathDB; HostDB:ENSG00000105568; -.
DR   eggNOG; KOG0211; Eukaryota.
DR   GeneTree; ENSGT00950000183066; -.
DR   HOGENOM; CLU_015533_2_1_1; -.
DR   InParanoid; P30153; -.
DR   OMA; FVILAQD; -.
DR   OrthoDB; 759105at2759; -.
DR   PhylomeDB; P30153; -.
DR   TreeFam; TF105552; -.
DR   BioCyc; MetaCyc:ENSG00000105568-MONOMER; -.
DR   PathwayCommons; P30153; -.
DR   Reactome; R-HSA-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR   Reactome; R-HSA-1295596; Spry regulation of FGF signaling.
DR   Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-HSA-163685; Integration of energy metabolism.
DR   Reactome; R-HSA-163767; PP2A-mediated dephosphorylation of key metabolic factors.
DR   Reactome; R-HSA-180024; DARPP-32 events.
DR   Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-HSA-196299; Beta-catenin phosphorylation cascade.
DR   Reactome; R-HSA-198753; ERK/MAPK targets.
DR   Reactome; R-HSA-202670; ERKs are inactivated.
DR   Reactome; R-HSA-2465910; MASTL Facilitates Mitotic Progression.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-HSA-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR   Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR   Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR   Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR   Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR   Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
DR   Reactome; R-HSA-432142; Platelet sensitization by LDL.
DR   Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR   Reactome; R-HSA-5339716; Signaling by GSK3beta mutants.
DR   Reactome; R-HSA-5358747; CTNNB1 S33 mutants aren't phosphorylated.
DR   Reactome; R-HSA-5358749; CTNNB1 S37 mutants aren't phosphorylated.
DR   Reactome; R-HSA-5358751; CTNNB1 S45 mutants aren't phosphorylated.
DR   Reactome; R-HSA-5358752; CTNNB1 T41 mutants aren't phosphorylated.
DR   Reactome; R-HSA-5467337; APC truncation mutants have impaired AXIN binding.
DR   Reactome; R-HSA-5467340; AXIN missense mutants destabilize the destruction complex.
DR   Reactome; R-HSA-5467348; Truncations of AMER1 destabilize the destruction complex.
DR   Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR   Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-HSA-5673000; RAF activation.
DR   Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
DR   Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
DR   Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-HSA-68877; Mitotic Prometaphase.
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-8854518; AURKA Activation by TPX2.
DR   Reactome; R-HSA-9634600; Regulation of glycolysis by fructose 2,6-bisphosphate metabolism.
DR   Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR   Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   Reactome; R-HSA-9833482; PKR-mediated signaling.
DR   SignaLink; P30153; -.
DR   SIGNOR; P30153; -.
DR   BioGRID-ORCS; 5518; 712 hits in 1185 CRISPR screens.
DR   ChiTaRS; PPP2R1A; human.
DR   EvolutionaryTrace; P30153; -.
DR   GeneWiki; PPP2R1A; -.
DR   GenomeRNAi; 5518; -.
DR   Pharos; P30153; Tbio.
DR   PRO; PR:P30153; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P30153; Protein.
DR   Bgee; ENSG00000105568; Expressed in cortical plate and 199 other cell types or tissues.
DR   ExpressionAtlas; P30153; baseline and differential.
DR   Genevisible; P30153; HS.
DR   GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0015630; C:microtubule cytoskeleton; NAS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; NAS:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB.
DR   GO; GO:1990405; F:protein antigen binding; IPI:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:Ensembl.
DR   GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
DR   GO; GO:0006672; P:ceramide metabolic process; NAS:UniProtKB.
DR   GO; GO:0007059; P:chromosome segregation; IDA:UniProtKB.
DR   GO; GO:0007143; P:female meiotic nuclear division; IEA:Ensembl.
DR   GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IEA:Ensembl.
DR   GO; GO:0051232; P:meiotic spindle elongation; IEA:Ensembl.
DR   GO; GO:0051306; P:mitotic sister chromatid separation; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; NAS:UniProtKB.
DR   GO; GO:0043409; P:negative regulation of MAPK cascade; NAS:UniProtKB.
DR   GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB.
DR   GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; NAS:UniProtKB.
DR   GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR   GO; GO:0006470; P:protein dephosphorylation; TAS:UniProtKB.
DR   GO; GO:0065003; P:protein-containing complex assembly; TAS:UniProtKB.
DR   GO; GO:0030155; P:regulation of cell adhesion; NAS:UniProtKB.
DR   GO; GO:0045595; P:regulation of cell differentiation; NAS:UniProtKB.
DR   GO; GO:0006275; P:regulation of DNA replication; NAS:UniProtKB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:UniProtKB.
DR   GO; GO:0040008; P:regulation of growth; NAS:UniProtKB.
DR   GO; GO:1903538; P:regulation of meiotic cell cycle process involved in oocyte maturation; IEA:Ensembl.
DR   GO; GO:0030111; P:regulation of Wnt signaling pathway; NAS:UniProtKB.
DR   GO; GO:0010033; P:response to organic substance; NAS:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; NAS:UniProtKB.
DR   GO; GO:0019932; P:second-messenger-mediated signaling; NAS:UniProtKB.
DR   GO; GO:0043029; P:T cell homeostasis; ISS:UniProtKB.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000357; HEAT.
DR   InterPro; IPR021133; HEAT_type_2.
DR   PANTHER; PTHR10648; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A 65 KDA REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR10648:SF2; SERINE_THREONINE-PROTEIN PHOSPHATASE 2A 65 KDA REGULATORY SUBUNIT A ALPHA ISOFORM; 1.
DR   Pfam; PF02985; HEAT; 5.
DR   Pfam; PF13646; HEAT_2; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 11.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell membrane; Cell projection; Centromere;
KW   Chromosome; Chromosome partition; Cytoplasm; Direct protein sequencing;
KW   Disease variant; Host-virus interaction; Intellectual disability; Membrane;
KW   Nucleus; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT                   ECO:0007744|PubMed:25944712"
FT   CHAIN           2..589
FT                   /note="Serine/threonine-protein phosphatase 2A 65 kDa
FT                   regulatory subunit A alpha isoform"
FT                   /id="PRO_0000071400"
FT   REPEAT          8..46
FT                   /note="HEAT 1"
FT   REPEAT          47..84
FT                   /note="HEAT 2"
FT   REPEAT          85..123
FT                   /note="HEAT 3"
FT   REPEAT          124..161
FT                   /note="HEAT 4"
FT   REPEAT          162..200
FT                   /note="HEAT 5"
FT   REPEAT          201..239
FT                   /note="HEAT 6"
FT   REPEAT          240..278
FT                   /note="HEAT 7"
FT   REPEAT          279..321
FT                   /note="HEAT 8"
FT   REPEAT          322..360
FT                   /note="HEAT 9"
FT   REPEAT          361..399
FT                   /note="HEAT 10"
FT   REPEAT          400..438
FT                   /note="HEAT 11"
FT   REPEAT          439..477
FT                   /note="HEAT 12"
FT   REPEAT          478..516
FT                   /note="HEAT 13"
FT   REPEAT          517..555
FT                   /note="HEAT 14"
FT   REPEAT          556..589
FT                   /note="HEAT 15"
FT   REGION          8..399
FT                   /note="PP2A subunit B binding"
FT   REGION          47..321
FT                   /note="Polyoma small and medium T antigens Binding"
FT   REGION          85..239
FT                   /note="SV40 small T antigen binding"
FT   REGION          400..589
FT                   /note="PP2A subunit C binding"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT                   ECO:0007744|PubMed:25944712"
FT   MOD_RES         280
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VARIANT         132
FT                   /note="V -> L (in HJS2)"
FT                   /evidence="ECO:0000269|PubMed:25533962"
FT                   /id="VAR_073718"
FT   VARIANT         179
FT                   /note="P -> L (in HJS2; reduces PPP2CA binding; reduces
FT                   PPP2R5A binding; reduces PPP2R5C binding; does not affect
FT                   PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B
FT                   binding; does not affect PPP2R3A binding; decreases
FT                   phosphatase activity of PPP2CA; dbSNP:rs786205228)"
FT                   /evidence="ECO:0000269|PubMed:26168268"
FT                   /id="VAR_074488"
FT   VARIANT         180
FT                   /note="M -> T (in HJS2; likely pathogenic; disrupts
FT                   interaction with PPP2R5D and impairs interaction with
FT                   PPP2CA)"
FT                   /evidence="ECO:0000269|PubMed:37761890"
FT                   /id="VAR_088637"
FT   VARIANT         180
FT                   /note="M -> V (in HJS2; likely pathogenic)"
FT                   /evidence="ECO:0000269|PubMed:37761890"
FT                   /id="VAR_088638"
FT   VARIANT         182
FT                   /note="R -> W (in HJS2; reduces PPP2CA binding; reduces
FT                   PPP2R5A binding; reduces PPP2R5C binding; does not affect
FT                   PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B
FT                   binding; reduces PPP2R3A binding; decreases phosphatase
FT                   activity of PPP2CA; dbSNP:rs786205227)"
FT                   /evidence="ECO:0000269|PubMed:26168268"
FT                   /id="VAR_074489"
FT   VARIANT         258
FT                   /note="R -> H (in HJS2; reduces PPP2CA binding; reduces
FT                   PPP2R5A binding; reduces PPP2R5C binding; does not affect
FT                   PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B
FT                   binding; reduces PPP2R3A binding; does not affect
FT                   phosphatase activity of PPP2CA; dbSNP:rs863225094)"
FT                   /evidence="ECO:0000269|PubMed:26168268"
FT                   /id="VAR_074490"
FT   VARIANT         470
FT                   /note="V -> A (in HJS2; uncertain significance; does not
FT                   affect interaction with PPP2R5D and PPP2CA)"
FT                   /evidence="ECO:0000269|PubMed:37761890"
FT                   /id="VAR_088639"
FT   VARIANT         498
FT                   /note="R -> L (in HJS2; likely pathogenic; disrupts
FT                   interaction with PPP2R5D and PPP2CA)"
FT                   /evidence="ECO:0000269|PubMed:37761890"
FT                   /id="VAR_088640"
FT   CONFLICT        130
FT                   /note="P -> A (in Ref. 1; AAA35531)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        258
FT                   /note="R -> A (in Ref. 2; AAA36399)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        272
FT                   /note="K -> R (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        551
FT                   /note="L -> P (in Ref. 3; CAG29336)"
FT                   /evidence="ECO:0000305"
FT   TURN            6..8
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           11..19
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   STRAND          21..23
FT                   /evidence="ECO:0007829|PDB:7CUN"
FT   HELIX           25..33
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           35..41
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           44..49
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           51..57
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           63..73
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   TURN            74..77
FT                   /evidence="ECO:0007829|PDB:6IUR"
FT   HELIX           78..80
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           83..89
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           90..96
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   STRAND          99..101
FT                   /evidence="ECO:0007829|PDB:2IE4"
FT   HELIX           102..116
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   STRAND          117..119
FT                   /evidence="ECO:0007829|PDB:7CUN"
FT   HELIX           121..126
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           128..136
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   STRAND          138..140
FT                   /evidence="ECO:0007829|PDB:2PKG"
FT   HELIX           141..147
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           148..150
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           151..154
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   TURN            155..157
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           160..174
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   STRAND          175..177
FT                   /evidence="ECO:0007829|PDB:7K36"
FT   HELIX           179..194
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           198..203
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           205..213
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           218..221
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           224..234
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           237..239
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           240..243
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           245..252
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           257..265
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           267..274
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           276..281
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           283..291
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   STRAND          292..294
FT                   /evidence="ECO:0007829|PDB:7CUN"
FT   HELIX           296..311
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   TURN            315..317
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           318..324
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           326..334
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           339..346
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           349..352
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           353..356
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           358..364
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           366..373
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           378..385
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           389..394
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           397..412
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   STRAND          413..415
FT                   /evidence="ECO:0007829|PDB:7CUN"
FT   HELIX           417..434
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           436..438
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           441..449
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           450..452
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           456..473
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           475..481
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           483..488
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   TURN            489..491
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   STRAND          492..494
FT                   /evidence="ECO:0007829|PDB:7K36"
FT   HELIX           495..520
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           522..527
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           528..530
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           534..547
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           548..550
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   HELIX           553..567
FT                   /evidence="ECO:0007829|PDB:1B3U"
FT   STRAND          569..571
FT                   /evidence="ECO:0007829|PDB:7SOY"
FT   HELIX           573..585
FT                   /evidence="ECO:0007829|PDB:1B3U"
SQ   SEQUENCE   589 AA;  65309 MW;  5174EBE94D537836 CRC64;
     MAAADGDDSL YPIAVLIDEL RNEDVQLRLN SIKKLSTIAL ALGVERTRSE LLPFLTDTIY
     DEDEVLLALA EQLGTFTTLV GGPEYVHCLL PPLESLATVE ETVVRDKAVE SLRAISHEHS
     PSDLEAHFVP LVKRLAGGDW FTSRTSACGL FSVCYPRVSS AVKAELRQYF RNLCSDDTPM
     VRRAAASKLG EFAKVLELDN VKSEIIPMFS NLASDEQDSV RLLAVEACVN IAQLLPQEDL
     EALVMPTLRQ AAEDKSWRVR YMVADKFTEL QKAVGPEITK TDLVPAFQNL MKDCEAEVRA
     AASHKVKEFC ENLSADCREN VIMSQILPCI KELVSDANQH VKSALASVIM GLSPILGKDN
     TIEHLLPLFL AQLKDECPEV RLNIISNLDC VNEVIGIRQL SQSLLPAIVE LAEDAKWRVR
     LAIIEYMPLL AGQLGVEFFD EKLNSLCMAW LVDHVYAIRE AATSNLKKLV EKFGKEWAHA
     TIIPKVLAMS GDPNYLHRMT TLFCINVLSE VCGQDITTKH MLPTVLRMAG DPVANVRFNV
     AKSLQKIGPI LDNSTLQSEV KPILEKLTQD QDVDVKYFAQ EALTVLSLA
//
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