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 03-AUG-2022, entry version 221.
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 INVOLVEMENT IN MRD36, AND VARIANT MRD36 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 [24]
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 [25]
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 [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 MRD36 LEU-179; TRP-182 AND HIS-258, AND CHARACTERIZATION MRD36 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 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).
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 {ECO:0000269|PubMed:15525651, 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 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 -!- 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: Intellectual developmental disorder, autosomal dominant 36
CC (MRD36) [MIM:616362]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC {ECO:0000269|PubMed:25533962, ECO:0000269|PubMed:26168268}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC 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 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 AlphaFoldDB; P30153; -.
DR SMR; P30153; -.
DR BioGRID; 111510; 535.
DR CORUM; P30153; -.
DR DIP; DIP-29394N; -.
DR IntAct; P30153; 267.
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 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; P30153; -.
DR PeptideAtlas; P30153; -.
DR PRIDE; P30153; -.
DR ProteomicsDB; 54636; -.
DR Antibodypedia; 4348; 392 antibodies from 42 providers.
DR DNASU; 5518; -.
DR Ensembl; ENST00000322088.11; ENSP00000324804.6; ENSG00000105568.18.
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 CTD; 5518; -.
DR DisGeNET; 5518; -.
DR GeneCards; 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; WAQNTVI; -.
DR OrthoDB; 447572at2759; -.
DR PhylomeDB; P30153; -.
DR TreeFam; TF105552; -.
DR BioCyc; MetaCyc:ENSG00000105568-MON; -.
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 SignaLink; P30153; -.
DR SIGNOR; P30153; -.
DR BioGRID-ORCS; 5518; 685 hits in 1097 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 197 other 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:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; NAS:UniProtKB.
DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; IEA:Ensembl.
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; IBA:GO_Central.
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: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:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
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 Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR031090; PP2A_A_meta.
DR PANTHER; PTHR10648:SF2; PTHR10648:SF2; 1.
DR Pfam; PF02985; HEAT; 1.
DR SUPFAM; SSF48371; SSF48371; 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 MRD36)"
FT /evidence="ECO:0000269|PubMed:25533962"
FT /id="VAR_073718"
FT VARIANT 179
FT /note="P -> L (in MRD36; 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 182
FT /note="R -> W (in MRD36; 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 MRD36; 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 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 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
