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Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (Medium tumor antigen-associated 61 kDa protein) (PP2A subunit A isoform PR65-alpha) (PP2A subunit A isoform R1-alpha)

 2AAA_HUMAN              Reviewed;         589 AA.
P30153; Q13773; Q6ICQ3; Q96DH3;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 4.
22-NOV-2017, entry version 187.
RecName: Full=Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;
AltName: Full=Medium tumor antigen-associated 61 kDa protein;
AltName: Full=PP2A subunit A isoform PR65-alpha;
AltName: Full=PP2A subunit A isoform R1-alpha;
Name=PPP2R1A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 242-255.
TISSUE=Placenta;
PubMed=2554323; DOI=10.1073/pnas.86.22.8669;
Walter G., Ferre F., Espiritu O., Carbone-Wiley A.;
"Molecular cloning and sequence of cDNA encoding polyoma medium tumor
antigen-associated 61-kDa protein.";
Proc. Natl. Acad. Sci. U.S.A. 86:8669-8672(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2159327; DOI=10.1021/bi00465a002;
Hemmings B.A., Adams-Pearson C., Maurer F., Mueller P., Goris J.,
Merlevede W., Hofsteenge J., Stone S.R.;
"Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A
have a similar 39 amino acid repeating structure.";
Biochemistry 29:3166-3173(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 34-46, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[6]
PROTEIN SEQUENCE OF 204-214; 261-272 AND 521-527.
PubMed=8694763; DOI=10.1042/bj3170187;
Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I.,
Merlevede W., Goris J., Hemmings B.A.;
"The variable subunit associated with protein phosphatase 2A0 defines
a novel multimember family of regulatory subunits.";
Biochem. J. 317:187-194(1996).
[7]
BINDING DOMAINS.
PubMed=8254721;
Ruediger R., Hentz M., Fait J., Mumby M., Walter G.;
"Molecular model of the A subunit of protein phosphatase 2A:
interaction with other subunits and tumor antigens.";
J. Virol. 68:123-129(1994).
[8]
INTERACTION WITH IPO9.
PubMed=12670497; DOI=10.1016/S0006-291X(03)00434-0;
Lubert E.J., Sarge K.D.;
"Interaction between protein phosphatase 2A and members of the
importin beta superfamily.";
Biochem. Biophys. Res. Commun. 303:908-913(2003).
[9]
FUNCTION, INTERACTION WITH GNA12, AND SUBCELLULAR LOCATION.
PubMed=15525651; DOI=10.1074/jbc.C400508200;
Zhu D., Kosik K.S., Meigs T.E., Yanamadala V., Denker B.M.;
"Galpha12 directly interacts with PP2A: evidence for Galpha12-
stimulated PP2A phosphatase activity and dephosphorylation of
microtubule-associated protein, tau.";
J. Biol. Chem. 279:54983-54986(2004).
[10]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
AND INTERACTION WITH SGO1.
PubMed=16580887; DOI=10.1016/j.devcel.2006.03.010;
Tang Z., Shu H., Qi W., Mahmood N.A., Mumby M.C., Yu H.;
"PP2A is required for centromeric localization of Sgo1 and proper
chromosome segregation.";
Dev. Cell 10:575-585(2006).
[11]
INTERACTION WITH TP53.
PubMed=17245430; DOI=10.1038/sj.emboj.7601519;
Li H.H., Cai X., Shouse G.P., Piluso L.G., Liu X.;
"A specific PP2A regulatory subunit, B56gamma, mediates DNA damage-
induced dephosphorylation of p53 at Thr55.";
EMBO J. 26:402-411(2007).
[12]
INTERACTION WITH PLA2G16.
PubMed=17374643; DOI=10.1242/jcs.000018;
Nazarenko I., Schafer R., Sers C.;
"Mechanisms of the HRSL3 tumor suppressor function in ovarian
carcinoma cells.";
J. Cell Sci. 120:1393-1404(2007).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
INTERACTION WITH CTTNBP2NL.
PubMed=18782753; DOI=10.1074/mcp.M800266-MCP200;
Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G.,
Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I.,
Aebersold R., Raught B., Gingras A.C.;
"A PP2A phosphatase high density interaction network identifies a
novel striatin-interacting phosphatase and kinase complex linked to
the cerebral cavernous malformation 3 (CCM3) protein.";
Mol. Cell. Proteomics 8:157-171(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-280, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
INVOLVEMENT IN MRD36, AND VARIANT MRD36 LEU-132.
PubMed=25533962; DOI=10.1038/nature14135;
Deciphering Developmental Disorders Study;
"Large-scale discovery of novel genetic causes of developmental
disorders.";
Nature 519:223-228(2015).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[22]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=9989501; DOI=10.1016/S0092-8674(00)80963-0;
Groves M.R., Hanlon N., Turowski P., Hemmings B.A., Barford D.;
"The structure of the protein phosphatase 2A PR65/A subunit reveals
the conformation of its 15 tandemly repeated HEAT motifs.";
Cell 96:99-110(1999).
[23]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 9-589 IN COMPLEX WITH WITH
PPP2CA AND PPME1.
PubMed=18394995; DOI=10.1016/j.cell.2008.02.041;
Xing Y., Li Z., Chen Y., Stock J.B., Jeffrey P.D., Shi Y.;
"Structural mechanism of demethylation and inactivation of protein
phosphatase 2A.";
Cell 133:154-163(2008).
[24]
VARIANTS MRD36 LEU-179; TRP-182 AND HIS-258, AND CHARACTERIZATION
MRD36 OF VARIANTS LEU-179; TRP-182 AND HIS-258.
PubMed=26168268; DOI=10.1172/JCI79860;
Houge G., Haesen D., Vissers L.E., Mehta S., Parker M.J., Wright M.,
Vogt J., McKee S., Tolmie J.L., Cordeiro N., Kleefstra T.,
Willemsen M.H., Reijnders M.R., Berland S., Hayman E., Lahat E.,
Brilstra E.H., van Gassen K.L., Zonneveld-Huijssoon E., de Bie C.I.,
Hoischen A., Eichler E.E., Holdhus R., Steen V.M., Doeskeland S.O.,
Hurles M.E., FitzPatrick D.R., Janssens V.;
"B56delta-related protein phosphatase 2A dysfunction identified in
patients with intellectual disability.";
J. Clin. Invest. 125:3051-3062(2015).
-!- FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a
scaffolding molecule to coordinate the assembly of the catalytic
subunit and a variable regulatory B subunit. Upon interaction with
GNA12 promotes dephosphorylation of microtubule associated protein
TAU/MAPT (PubMed:15525651). Required for proper chromosome
segregation and for centromeric localization of SGO1 in mitosis
(PubMed:16580887). {ECO:0000269|PubMed:15525651,
ECO:0000269|PubMed:16580887}.
-!- SUBUNIT: Found in a complex with at least ARL2, PPP2CB, PPP2R1A,
PPP2R2A, PPP2R5E and TBCD (By similarity). Interacts with FOXO1;
the interaction dephosphorylates FOXO1 on AKT-mediated
phosphorylation sites (By similarity). PP2A consists of a common
heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic
subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory
subunit (PR65 or subunit A), that associates with a variety of
regulatory subunits. Proteins that associate with the core dimer
include three families of regulatory subunits B (the
R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the
48 kDa variable regulatory subunit, viral proteins, and cell
signaling molecules. Interacts with IPO9 (PubMed:12670497).
Interacts with TP53 and SGO1 (PubMed:17245430, PubMed:16580887).
Interacts with PLA2G16; this interaction might decrease PP2A
activity (PubMed:17374643). Interacts with CTTNBP2NL
(PubMed:18782753). Interacts with GNA12; the interaction promotes
protein phosphatase 2A activation causing dephosphorylation of
MAPT (PubMed:15525651). {ECO:0000250|UniProtKB:Q32PI5,
ECO:0000250|UniProtKB:Q76MZ3, ECO:0000269|PubMed:12670497,
ECO:0000269|PubMed:15525651, ECO:0000269|PubMed:16580887,
ECO:0000269|PubMed:17245430, ECO:0000269|PubMed:17374643,
ECO:0000269|PubMed:18394995, ECO:0000269|PubMed:18782753}.
-!- INTERACTION:
P03081:- (xeno); NbExp=5; IntAct=EBI-302388, EBI-1266256;
P31749:AKT1; NbExp=2; IntAct=EBI-302388, EBI-296087;
Q9C0C7:AMBRA1; NbExp=3; IntAct=EBI-302388, EBI-2512975;
Q14155:ARHGEF7; NbExp=3; IntAct=EBI-302388, EBI-717515;
Q96GD4:AURKB; NbExp=2; IntAct=EBI-302388, EBI-624291;
P51959:CCNG1; NbExp=2; IntAct=EBI-302388, EBI-3905829;
Q9Y534:CSDC2; NbExp=4; IntAct=EBI-302388, EBI-1763657;
P03129:E7 (xeno); NbExp=3; IntAct=EBI-302388, EBI-866453;
P04020:E7 (xeno); NbExp=2; IntAct=EBI-302388, EBI-7005254;
Q8TCG1:KIAA1524; NbExp=4; IntAct=EBI-302388, EBI-1379376;
P97346:Nxn (xeno); NbExp=2; IntAct=EBI-302388, EBI-309684;
P53816:PLA2G16; NbExp=7; IntAct=EBI-302388, EBI-746318;
P67775:PPP2CA; NbExp=32; IntAct=EBI-302388, EBI-712311;
P30154:PPP2R1B; NbExp=2; IntAct=EBI-302388, EBI-357094;
P63151:PPP2R2A; NbExp=17; IntAct=EBI-302388, EBI-1048931;
Q00005:PPP2R2B; NbExp=6; IntAct=EBI-302388, EBI-1052159;
Q15172:PPP2R5A; NbExp=6; IntAct=EBI-302388, EBI-641666;
Q15173:PPP2R5B; NbExp=3; IntAct=EBI-302388, EBI-1369497;
Q13362:PPP2R5C; NbExp=10; IntAct=EBI-302388, EBI-1266156;
Q13362-1:PPP2R5C; NbExp=5; IntAct=EBI-302388, EBI-1266170;
Q13362-2:PPP2R5C; NbExp=4; IntAct=EBI-302388, EBI-1266173;
Q60996-3:Ppp2r5c (xeno); NbExp=2; IntAct=EBI-302388, EBI-1369292;
Q14738:PPP2R5D; NbExp=11; IntAct=EBI-302388, EBI-396563;
Q16537:PPP2R5E; NbExp=7; IntAct=EBI-302388, EBI-968374;
P60510:PPP4C; NbExp=5; IntAct=EBI-302388, EBI-1046072;
P53041:PPP5C; NbExp=3; IntAct=EBI-302388, EBI-716663;
Q15257-2:PTPA; NbExp=4; IntAct=EBI-302388, EBI-12164121;
Q04206:RELA; NbExp=2; IntAct=EBI-302388, EBI-73886;
O43815:STRN; NbExp=8; IntAct=EBI-302388, EBI-1046642;
Q13033-2:STRN3; NbExp=4; IntAct=EBI-302388, EBI-1053876;
P04637:TP53; NbExp=3; IntAct=EBI-302388, EBI-366083;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q32PI5}.
Chromosome, centromere {ECO:0000269|PubMed:16580887}. Lateral cell
membrane {ECO:0000269|PubMed:15525651}. Cell projection, dendrite
{ECO:0000269|PubMed:15525651}. Note=Centromeric localization
requires the presence of BUB1. {ECO:0000269|PubMed:16580887}.
-!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices
joined by a hydrophilic region, the intrarepeat loop. The repeat
units may be arranged laterally to form a rod-like structure.
-!- DISEASE: Mental retardation, autosomal dominant 36 (MRD36)
[MIM:616362]: A form of mental retardation, a disorder
characterized by significantly below average general intellectual
functioning associated with impairments in adaptive behavior and
manifested during the developmental period.
{ECO:0000269|PubMed:25533962, ECO:0000269|PubMed:26168268}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A
family. {ECO:0000305}.
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EMBL; M31786; AAA35531.1; -; mRNA.
EMBL; J02902; AAA36399.1; -; mRNA.
EMBL; CR450340; CAG29336.1; -; mRNA.
EMBL; BC001537; AAH01537.1; -; mRNA.
CCDS; CCDS12849.1; -.
PIR; A34541; A34541.
RefSeq; NP_055040.2; NM_014225.5.
UniGene; Hs.467192; -.
PDB; 1B3U; X-ray; 2.30 A; A/B=2-589.
PDB; 2IE3; X-ray; 2.80 A; A=1-589.
PDB; 2IE4; X-ray; 2.60 A; A=1-589.
PDB; 2NPP; X-ray; 3.30 A; A/D=1-589.
PDB; 2NYL; X-ray; 3.80 A; A/D=8-589.
PDB; 2NYM; X-ray; 3.60 A; A/D=8-589.
PDB; 2PKG; X-ray; 3.30 A; A/B=10-589.
PDB; 3C5W; X-ray; 2.80 A; A=9-589.
PDB; 3DW8; X-ray; 2.85 A; A/D=9-589.
PDB; 3K7V; X-ray; 2.85 A; A=1-589.
PDB; 3K7W; X-ray; 2.96 A; A=1-589.
PDB; 4I5L; X-ray; 2.43 A; A/D=6-589.
PDB; 4I5N; X-ray; 2.80 A; A/D=6-589.
PDB; 4LAC; X-ray; 2.82 A; A=404-589.
PDBsum; 1B3U; -.
PDBsum; 2IE3; -.
PDBsum; 2IE4; -.
PDBsum; 2NPP; -.
PDBsum; 2NYL; -.
PDBsum; 2NYM; -.
PDBsum; 2PKG; -.
PDBsum; 3C5W; -.
PDBsum; 3DW8; -.
PDBsum; 3K7V; -.
PDBsum; 3K7W; -.
PDBsum; 4I5L; -.
PDBsum; 4I5N; -.
PDBsum; 4LAC; -.
ProteinModelPortal; P30153; -.
SMR; P30153; -.
BioGrid; 111510; 292.
CORUM; P30153; -.
DIP; DIP-29394N; -.
IntAct; P30153; 216.
MINT; MINT-1141071; -.
STRING; 9606.ENSP00000324804; -.
iPTMnet; P30153; -.
PhosphoSitePlus; P30153; -.
SwissPalm; P30153; -.
BioMuta; PPP2R1A; -.
DMDM; 143811355; -.
OGP; P30153; -.
REPRODUCTION-2DPAGE; IPI00554737; -.
EPD; P30153; -.
MaxQB; P30153; -.
PaxDb; P30153; -.
PeptideAtlas; P30153; -.
PRIDE; P30153; -.
DNASU; 5518; -.
Ensembl; ENST00000322088; ENSP00000324804; ENSG00000105568.
GeneID; 5518; -.
KEGG; hsa:5518; -.
UCSC; uc002pyp.4; human.
CTD; 5518; -.
DisGeNET; 5518; -.
EuPathDB; HostDB:ENSG00000105568.17; -.
GeneCards; PPP2R1A; -.
HGNC; HGNC:9302; PPP2R1A.
HPA; CAB018599; -.
MalaCards; PPP2R1A; -.
MIM; 605983; gene.
MIM; 616362; phenotype.
neXtProt; NX_P30153; -.
OpenTargets; ENSG00000105568; -.
PharmGKB; PA33666; -.
eggNOG; KOG0211; Eukaryota.
eggNOG; ENOG410XQVI; LUCA.
GeneTree; ENSGT00730000110944; -.
HOGENOM; HOG000078539; -.
HOVERGEN; HBG000011; -.
InParanoid; P30153; -.
KO; K03456; -.
OMA; WAQNTVI; -.
OrthoDB; EOG091G045V; -.
PhylomeDB; P30153; -.
TreeFam; TF105552; -.
BioCyc; MetaCyc:ENSG00000105568-MONOMER; -.
Reactome; R-HSA-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
Reactome; R-HSA-1295596; Spry regulation of FGF signaling.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-163685; Integration of energy metabolism.
Reactome; R-HSA-163767; PP2A-mediated dephosphorylation of key metabolic factors.
Reactome; R-HSA-180024; DARPP-32 events.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-196299; Beta-catenin phosphorylation cascade.
Reactome; R-HSA-198753; ERK/MAPK targets.
Reactome; R-HSA-202670; ERKs are inactivated.
Reactome; R-HSA-2465910; MASTL Facilitates Mitotic Progression.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-2995383; Initiation of Nuclear Envelope Reformation.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
Reactome; R-HSA-432142; Platelet sensitization by LDL.
Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
Reactome; R-HSA-5339716; Misspliced GSK3beta mutants stabilize beta-catenin.
Reactome; R-HSA-5358747; S33 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358749; S37 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358751; S45 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358752; T41 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5467337; APC truncation mutants have impaired AXIN binding.
Reactome; R-HSA-5467340; AXIN missense mutants destabilize the destruction complex.
Reactome; R-HSA-5467348; Truncations of AMER1 destabilize the destruction complex.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-5673000; RAF activation.
Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-68877; Mitotic Prometaphase.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-HSA-70171; Glycolysis.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SignaLink; P30153; -.
SIGNOR; P30153; -.
ChiTaRS; PPP2R1A; human.
EvolutionaryTrace; P30153; -.
GeneWiki; PPP2R1A; -.
GenomeRNAi; 5518; -.
PMAP-CutDB; P30153; -.
PRO; PR:P30153; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105568; -.
CleanEx; HS_PPP2R1A; -.
ExpressionAtlas; P30153; baseline and differential.
Genevisible; P30153; HS.
GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:UniProtKB.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; NAS:UniProtKB.
GO; GO:0015630; C:microtubule cytoskeleton; NAS:UniProtKB.
GO; GO:0005739; C:mitochondrion; NAS:UniProtKB.
GO; GO:0005634; C:nucleus; NAS:UniProtKB.
GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB.
GO; GO:1990405; F:protein antigen binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0019888; F:protein phosphatase regulator activity; TAS:UniProtKB.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
GO; GO:0006672; P:ceramide metabolic process; NAS:UniProtKB.
GO; GO:0007059; P:chromosome segregation; IDA:UniProtKB.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0007143; P:female meiotic nuclear division; IEA:Ensembl.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0000188; P:inactivation of MAPK activity; NAS:UniProtKB.
GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IEA:Ensembl.
GO; GO:0051232; P:meiotic spindle elongation; IEA:Ensembl.
GO; GO:0007084; P:mitotic nuclear envelope reassembly; TAS:Reactome.
GO; GO:0051306; P:mitotic sister chromatid separation; IEA:Ensembl.
GO; GO:0030308; P:negative regulation of cell growth; NAS:UniProtKB.
GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; NAS:UniProtKB.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
GO; GO:0070262; P:peptidyl-serine dephosphorylation; IEA:Ensembl.
GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0006461; P:protein complex assembly; TAS:UniProtKB.
GO; GO:0006470; P:protein dephosphorylation; TAS:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; NAS:UniProtKB.
GO; GO:0045595; P:regulation of cell differentiation; NAS:UniProtKB.
GO; GO:0006275; P:regulation of DNA replication; NAS:UniProtKB.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0040008; P:regulation of growth; NAS:UniProtKB.
GO; GO:1903538; P:regulation of meiotic cell cycle process involved in oocyte maturation; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0030111; P:regulation of Wnt signaling pathway; NAS:UniProtKB.
GO; GO:0010033; P:response to organic substance; NAS:UniProtKB.
GO; GO:0008380; P:RNA splicing; NAS:UniProtKB.
GO; GO:0019932; P:second-messenger-mediated signaling; NAS:UniProtKB.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000357; HEAT.
InterPro; IPR021133; HEAT_type_2.
InterPro; IPR031090; PP2A_A_meta.
PANTHER; PTHR10648:SF2; PTHR10648:SF2; 1.
Pfam; PF02985; HEAT; 1.
SUPFAM; SSF48371; SSF48371; 1.
PROSITE; PS50077; HEAT_REPEAT; 11.
1: Evidence at protein level;
3D-structure; Acetylation; Cell membrane; Cell projection; Centromere;
Chromosome; Chromosome partition; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Membrane;
Mental retardation; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712}.
CHAIN 2 589 Serine/threonine-protein phosphatase 2A
65 kDa regulatory subunit A alpha
isoform.
/FTId=PRO_0000071400.
REPEAT 8 46 HEAT 1.
REPEAT 47 84 HEAT 2.
REPEAT 85 123 HEAT 3.
REPEAT 124 161 HEAT 4.
REPEAT 162 200 HEAT 5.
REPEAT 201 239 HEAT 6.
REPEAT 240 278 HEAT 7.
REPEAT 279 321 HEAT 8.
REPEAT 322 360 HEAT 9.
REPEAT 361 399 HEAT 10.
REPEAT 400 438 HEAT 11.
REPEAT 439 477 HEAT 12.
REPEAT 478 516 HEAT 13.
REPEAT 517 555 HEAT 14.
REPEAT 556 589 HEAT 15.
REGION 8 399 PP2A subunit B binding.
REGION 47 321 Polyoma small and medium T antigens
Binding.
REGION 85 239 SV40 small T antigen binding.
REGION 400 589 PP2A subunit C binding.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712}.
MOD_RES 280 280 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VARIANT 132 132 V -> L (in MRD36).
{ECO:0000269|PubMed:25533962}.
/FTId=VAR_073718.
VARIANT 179 179 P -> L (in MRD36; reduces PPP2CA binding;
reduces PPP2R5A binding; reduces PPP2R5C
binding; does not affect PPP2R5D binding;
reduces PPP2R2A binding; reduces PPP2R2B
binding; does not affect PPP2R3A binding;
decreases phosphatase activity of PPP2CA;
dbSNP:rs786205228).
{ECO:0000269|PubMed:26168268}.
/FTId=VAR_074488.
VARIANT 182 182 R -> W (in MRD36; reduces PPP2CA binding;
reduces PPP2R5A binding; reduces PPP2R5C
binding; does not affect PPP2R5D binding;
reduces PPP2R2A binding; reduces PPP2R2B
binding; reduces PPP2R3A binding;
decreases phosphatase activity of PPP2CA;
dbSNP:rs786205227).
{ECO:0000269|PubMed:26168268}.
/FTId=VAR_074489.
VARIANT 258 258 R -> H (in MRD36; reduces PPP2CA binding;
reduces PPP2R5A binding; reduces PPP2R5C
binding; does not affect PPP2R5D binding;
reduces PPP2R2A binding; reduces PPP2R2B
binding; reduces PPP2R3A binding; does
not affect phosphatase activity of
PPP2CA; dbSNP:rs863225094).
{ECO:0000269|PubMed:26168268}.
/FTId=VAR_074490.
CONFLICT 130 130 P -> A (in Ref. 1; AAA35531).
{ECO:0000305}.
CONFLICT 258 258 R -> A (in Ref. 2; AAA36399).
{ECO:0000305}.
CONFLICT 272 272 K -> R (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 551 551 L -> P (in Ref. 3; CAG29336).
{ECO:0000305}.
TURN 6 8 {ECO:0000244|PDB:1B3U}.
HELIX 11 19 {ECO:0000244|PDB:1B3U}.
HELIX 25 33 {ECO:0000244|PDB:1B3U}.
HELIX 35 41 {ECO:0000244|PDB:1B3U}.
HELIX 44 49 {ECO:0000244|PDB:1B3U}.
HELIX 51 57 {ECO:0000244|PDB:1B3U}.
HELIX 63 73 {ECO:0000244|PDB:1B3U}.
HELIX 78 80 {ECO:0000244|PDB:1B3U}.
HELIX 83 89 {ECO:0000244|PDB:1B3U}.
HELIX 90 96 {ECO:0000244|PDB:1B3U}.
STRAND 99 101 {ECO:0000244|PDB:2IE4}.
HELIX 102 116 {ECO:0000244|PDB:1B3U}.
HELIX 121 126 {ECO:0000244|PDB:1B3U}.
HELIX 128 136 {ECO:0000244|PDB:1B3U}.
STRAND 138 140 {ECO:0000244|PDB:2PKG}.
HELIX 141 147 {ECO:0000244|PDB:1B3U}.
HELIX 148 150 {ECO:0000244|PDB:1B3U}.
HELIX 151 154 {ECO:0000244|PDB:1B3U}.
TURN 155 157 {ECO:0000244|PDB:1B3U}.
HELIX 160 174 {ECO:0000244|PDB:1B3U}.
HELIX 179 194 {ECO:0000244|PDB:1B3U}.
HELIX 198 203 {ECO:0000244|PDB:1B3U}.
HELIX 205 213 {ECO:0000244|PDB:1B3U}.
HELIX 218 221 {ECO:0000244|PDB:1B3U}.
HELIX 224 234 {ECO:0000244|PDB:1B3U}.
HELIX 237 239 {ECO:0000244|PDB:1B3U}.
HELIX 240 243 {ECO:0000244|PDB:1B3U}.
HELIX 245 252 {ECO:0000244|PDB:1B3U}.
HELIX 257 265 {ECO:0000244|PDB:1B3U}.
HELIX 267 274 {ECO:0000244|PDB:1B3U}.
HELIX 276 281 {ECO:0000244|PDB:1B3U}.
HELIX 283 291 {ECO:0000244|PDB:1B3U}.
HELIX 296 311 {ECO:0000244|PDB:1B3U}.
TURN 315 317 {ECO:0000244|PDB:1B3U}.
HELIX 318 324 {ECO:0000244|PDB:1B3U}.
HELIX 326 334 {ECO:0000244|PDB:1B3U}.
HELIX 339 346 {ECO:0000244|PDB:1B3U}.
HELIX 349 352 {ECO:0000244|PDB:1B3U}.
HELIX 353 356 {ECO:0000244|PDB:1B3U}.
HELIX 358 364 {ECO:0000244|PDB:1B3U}.
HELIX 366 373 {ECO:0000244|PDB:1B3U}.
HELIX 378 385 {ECO:0000244|PDB:1B3U}.
HELIX 389 394 {ECO:0000244|PDB:1B3U}.
HELIX 397 412 {ECO:0000244|PDB:1B3U}.
HELIX 417 434 {ECO:0000244|PDB:1B3U}.
HELIX 436 438 {ECO:0000244|PDB:1B3U}.
HELIX 441 449 {ECO:0000244|PDB:1B3U}.
HELIX 450 452 {ECO:0000244|PDB:1B3U}.
HELIX 456 473 {ECO:0000244|PDB:1B3U}.
HELIX 475 481 {ECO:0000244|PDB:1B3U}.
HELIX 483 488 {ECO:0000244|PDB:1B3U}.
TURN 489 491 {ECO:0000244|PDB:1B3U}.
HELIX 495 520 {ECO:0000244|PDB:1B3U}.
HELIX 522 527 {ECO:0000244|PDB:1B3U}.
HELIX 528 530 {ECO:0000244|PDB:1B3U}.
HELIX 534 547 {ECO:0000244|PDB:1B3U}.
HELIX 548 550 {ECO:0000244|PDB:1B3U}.
HELIX 553 567 {ECO:0000244|PDB:1B3U}.
HELIX 573 585 {ECO:0000244|PDB:1B3U}.
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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