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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.
07-APR-2021, entry version 216.
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; DOI=10.1128/jvi.68.1.123-129.1994;
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]
INTERACTION WITH SPRY2.
PubMed=17974561; DOI=10.1074/jbc.m705457200;
Chandramouli S., Yu C.Y., Yusoff P., Lao D.H., Leong H.F., Mizuno K.,
Guy G.R.;
"Tesk1 interacts with Spry2 to abrogate its inhibition of ERK
phosphorylation downstream of receptor tyrosine kinase signaling.";
J. Biol. Chem. 283:1679-1691(2008).
[14]
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).
[15]
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).
[16]
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).
[17]
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).
[18]
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).
[19]
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).
[20]
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).
[21]
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).
[22]
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).
[23]
INTERACTION WITH PABIR1.
PubMed=27588481; DOI=10.18632/oncotarget.11698;
Fan L., Liu M.H., Guo M., Hu C.X., Yan Z.W., Chen J., Chen G.Q., Huang Y.;
"FAM122A, a new endogenous inhibitor of protein phosphatase 2A.";
Oncotarget 7:63887-63900(2016).
[24]
INTERACTION WITH CRTC3, AND SUBCELLULAR LOCATION.
PubMed=30611118; DOI=10.1016/j.isci.2018.12.012;
Sonntag T., Ostojic J., Vaughan J.M., Moresco J.J., Yoon Y.S.,
Yates J.R. III, Montminy M.;
"Mitogenic Signals Stimulate the CREB Coactivator CRTC3 through PP2A
Recruitment.";
IScience 11:134-145(2018).
[25]
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).
[26]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 9-589 IN COMPLEX 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).
[27]
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).
[28]
INTERACTION WITH CIP2A.
PubMed=28174209; DOI=10.15252/embr.201642788;
Wang J., Okkeri J., Pavic K., Wang Z., Kauko O., Halonen T., Sarek G.,
Ojala P.M., Rao Z., Xu W., Westermarck J.;
"Oncoprotein CIP2A is stabilized via interaction with tumor suppressor
PP2A/B56.";
EMBO Rep. 18:437-450(2017).
-!- 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: 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. 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). 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).
Interacts with CIP2A; this interaction stabilizes CIP2A
(PubMed:28174209). Interacts with PABIR1/FAM122A (PubMed:27588481).
Interacts with ADCY8; antagonizes interaction between ADCY8 and
calmodulin (By similarity). Interacts with CRTC3 (when phosphorylated
at 'Ser-391') (PubMed:30611118). Interacts with SPRY2
(PubMed:17974561). {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:17974561, ECO:0000269|PubMed:18394995,
ECO:0000269|PubMed:18782753, ECO:0000269|PubMed:27588481,
ECO:0000269|PubMed:28174209, ECO:0000269|PubMed:30611118}.
-!- INTERACTION:
P30153; P31749: AKT1; NbExp=2; IntAct=EBI-302388, EBI-296087;
P30153; Q9C0C7: AMBRA1; NbExp=3; IntAct=EBI-302388, EBI-2512975;
P30153; Q14155: ARHGEF7; NbExp=3; IntAct=EBI-302388, EBI-717515;
P30153; Q96GD4: AURKB; NbExp=2; IntAct=EBI-302388, EBI-624291;
P30153; Q9Y2V2: CARHSP1; NbExp=3; IntAct=EBI-302388, EBI-718719;
P30153; P51959: CCNG1; NbExp=2; IntAct=EBI-302388, EBI-3905829;
P30153; Q8TCG1: CIP2A; NbExp=4; IntAct=EBI-302388, EBI-1379376;
P30153; Q9Y534: CSDC2; NbExp=6; IntAct=EBI-302388, EBI-1763657;
P30153; Q4G163: FBXO43; NbExp=3; IntAct=EBI-302388, EBI-12053217;
P30153; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-302388, EBI-11163335;
P30153; Q08AF8: GOLGA8G; NbExp=3; IntAct=EBI-302388, EBI-10181260;
P30153; P53816: PLAAT3; NbExp=7; IntAct=EBI-302388, EBI-746318;
P30153; P67775: PPP2CA; NbExp=43; IntAct=EBI-302388, EBI-712311;
P30153; P30154: PPP2R1B; NbExp=2; IntAct=EBI-302388, EBI-357094;
P30153; P63151: PPP2R2A; NbExp=17; IntAct=EBI-302388, EBI-1048931;
P30153; Q00005: PPP2R2B; NbExp=10; IntAct=EBI-302388, EBI-1052159;
P30153; Q15172: PPP2R5A; NbExp=6; IntAct=EBI-302388, EBI-641666;
P30153; Q15173: PPP2R5B; NbExp=4; IntAct=EBI-302388, EBI-1369497;
P30153; Q13362: PPP2R5C; NbExp=10; IntAct=EBI-302388, EBI-1266156;
P30153; Q13362-1: PPP2R5C; NbExp=5; IntAct=EBI-302388, EBI-1266170;
P30153; Q13362-2: PPP2R5C; NbExp=4; IntAct=EBI-302388, EBI-1266173;
P30153; Q14738: PPP2R5D; NbExp=12; IntAct=EBI-302388, EBI-396563;
P30153; Q16537: PPP2R5E; NbExp=7; IntAct=EBI-302388, EBI-968374;
P30153; P60510: PPP4C; NbExp=5; IntAct=EBI-302388, EBI-1046072;
P30153; P53041: PPP5C; NbExp=3; IntAct=EBI-302388, EBI-716663;
P30153; Q15257-2: PTPA; NbExp=3; IntAct=EBI-302388, EBI-12164121;
P30153; Q04206: RELA; NbExp=2; IntAct=EBI-302388, EBI-73886;
P30153; O43815: STRN; NbExp=8; IntAct=EBI-302388, EBI-1046642;
P30153; O43815-2: STRN; NbExp=3; IntAct=EBI-302388, EBI-1266294;
P30153; Q13033-2: STRN3; NbExp=5; IntAct=EBI-302388, EBI-1053876;
P30153; P04637: TP53; NbExp=3; IntAct=EBI-302388, EBI-366083;
P30153; P03129: E7; Xeno; NbExp=3; IntAct=EBI-302388, EBI-866453;
P30153; P04020: E7; Xeno; NbExp=2; IntAct=EBI-302388, EBI-7005254;
P30153; P97346: Nxn; Xeno; NbExp=2; IntAct=EBI-302388, EBI-309684;
P30153; Q60996-3: Ppp2r5c; Xeno; NbExp=2; IntAct=EBI-302388, EBI-1369292;
P30153; P03081; Xeno; NbExp=5; IntAct=EBI-302388, EBI-1266256;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q32PI5}. Nucleus
{ECO:0000269|PubMed:30611118}. 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 variants
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.
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=9-46, A=400-589.
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.
PDB; 5W0W; X-ray; 3.80 A; A/D/G/J=9-589.
PDB; 6IUR; X-ray; 3.33 A; A/B/E/F=8-589.
PDB; 6NTS; EM; 3.63 A; A=1-589.
PDB; 7CUN; EM; 3.50 A; P=1-589.
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; -.
PDBsum; 5W0W; -.
PDBsum; 6IUR; -.
PDBsum; 6NTS; -.
PDBsum; 7CUN; -.
SMR; P30153; -.
BioGRID; 111510; 471.
CORUM; P30153; -.
DIP; DIP-29394N; -.
IntAct; P30153; 252.
MINT; P30153; -.
STRING; 9606.ENSP00000324804; -.
DrugBank; DB06905; (2S,3S,4E,6E,8S,9S)-3-amino-9-methoxy-2,6,8-trimethyl-10-phenyldeca-4,6-dienoic acid.
DrugBank; DB02506; 2,6,8-Trimethyl-3-Amino-9-Benzyl-9-Methoxynonanoic Acid.
iPTMnet; P30153; -.
MetOSite; P30153; -.
PhosphoSitePlus; P30153; -.
SwissPalm; P30153; -.
BioMuta; PPP2R1A; -.
DMDM; 143811355; -.
OGP; P30153; -.
REPRODUCTION-2DPAGE; IPI00554737; -.
CPTAC; CPTAC-257; -.
CPTAC; CPTAC-258; -.
EPD; P30153; -.
jPOST; P30153; -.
MassIVE; P30153; -.
MaxQB; P30153; -.
PaxDb; P30153; -.
PeptideAtlas; P30153; -.
PRIDE; P30153; -.
ProteomicsDB; 54636; -.
Antibodypedia; 4348; 381 antibodies.
DNASU; 5518; -.
Ensembl; ENST00000322088; ENSP00000324804; ENSG00000105568.
GeneID; 5518; -.
KEGG; hsa:5518; -.
UCSC; uc002pyp.4; human.
CTD; 5518; -.
DisGeNET; 5518; -.
GeneCards; PPP2R1A; -.
HGNC; HGNC:9302; PPP2R1A.
HPA; ENSG00000105568; Low tissue specificity.
MalaCards; PPP2R1A; -.
MIM; 605983; gene.
MIM; 616362; phenotype.
neXtProt; NX_P30153; -.
OpenTargets; ENSG00000105568; -.
Orphanet; 457284; Microcephaly-corpus callosum hypoplasia-intellectual disability-facial dysmorphism syndrome.
PharmGKB; PA33666; -.
VEuPathDB; HostDB:ENSG00000105568.17; -.
eggNOG; KOG0211; Eukaryota.
GeneTree; ENSGT00950000183066; -.
HOGENOM; CLU_015533_2_1_1; -.
InParanoid; P30153; -.
OMA; VKFFATR; -.
OrthoDB; 447572at2759; -.
PhylomeDB; P30153; -.
TreeFam; TF105552; -.
BioCyc; MetaCyc:ENSG00000105568-MONOMER; -.
PathwayCommons; P30153; -.
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 (NE) 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; Signaling by GSK3beta mutants.
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-8854518; AURKA Activation by TPX2.
Reactome; R-HSA-9634600; Regulation of glycolysis by fructose 2,6-bisphosphate metabolism.
Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SignaLink; P30153; -.
SIGNOR; P30153; -.
BioGRID-ORCS; 5518; 674 hits in 1007 CRISPR screens.
ChiTaRS; PPP2R1A; human.
EvolutionaryTrace; P30153; -.
GeneWiki; PPP2R1A; -.
GenomeRNAi; 5518; -.
Pharos; P30153; Tbio.
PRO; PR:P30153; -.
Proteomes; UP000005640; Chromosome 19.
RNAct; P30153; protein.
Bgee; ENSG00000105568; Expressed in anterior cingulate cortex and 242 other tissues.
ExpressionAtlas; P30153; baseline and differential.
Genevisible; P30153; HS.
GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:UniProtKB.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; HDA: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; IDA:UniProtKB.
GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB.
GO; GO:0008287; C:protein serine/threonine phosphatase complex; IBA:GO_Central.
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; IBA:GO_Central.
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:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0000188; P:inactivation of MAPK activity; NAS:UniProtKB.
GO; GO:0007084; P:mitotic nuclear envelope reassembly; TAS:Reactome.
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:0006470; P:protein dephosphorylation; TAS:UniProtKB.
GO; GO:0065003; P:protein-containing complex assembly; 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: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; 3.
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; Cytoplasm; Direct protein sequencing;
Disease variant; Membrane; Mental retardation; Nucleus; Reference proteome;
Repeat.
INIT_MET 1
/note="Removed"
/evidence="ECO:0007744|PubMed:19413330,
ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
ECO:0007744|PubMed:25944712"
CHAIN 2..589
/note="Serine/threonine-protein phosphatase 2A 65 kDa
regulatory subunit A alpha isoform"
/id="PRO_0000071400"
REPEAT 8..46
/note="HEAT 1"
REPEAT 47..84
/note="HEAT 2"
REPEAT 85..123
/note="HEAT 3"
REPEAT 124..161
/note="HEAT 4"
REPEAT 162..200
/note="HEAT 5"
REPEAT 201..239
/note="HEAT 6"
REPEAT 240..278
/note="HEAT 7"
REPEAT 279..321
/note="HEAT 8"
REPEAT 322..360
/note="HEAT 9"
REPEAT 361..399
/note="HEAT 10"
REPEAT 400..438
/note="HEAT 11"
REPEAT 439..477
/note="HEAT 12"
REPEAT 478..516
/note="HEAT 13"
REPEAT 517..555
/note="HEAT 14"
REPEAT 556..589
/note="HEAT 15"
REGION 8..399
/note="PP2A subunit B binding"
REGION 47..321
/note="Polyoma small and medium T antigens Binding"
REGION 85..239
/note="SV40 small T antigen binding"
REGION 400..589
/note="PP2A subunit C binding"
MOD_RES 2
/note="N-acetylalanine"
/evidence="ECO:0007744|PubMed:19413330,
ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
ECO:0007744|PubMed:25944712"
MOD_RES 280
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:19608861"
VARIANT 132
/note="V -> L (in MRD36)"
/evidence="ECO:0000269|PubMed:25533962"
/id="VAR_073718"
VARIANT 179
/note="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)"
/evidence="ECO:0000269|PubMed:26168268"
/id="VAR_074488"
VARIANT 182
/note="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)"
/evidence="ECO:0000269|PubMed:26168268"
/id="VAR_074489"
VARIANT 258
/note="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)"
/evidence="ECO:0000269|PubMed:26168268"
/id="VAR_074490"
CONFLICT 130
/note="P -> A (in Ref. 1; AAA35531)"
/evidence="ECO:0000305"
CONFLICT 258
/note="R -> A (in Ref. 2; AAA36399)"
/evidence="ECO:0000305"
CONFLICT 272
/note="K -> R (in Ref. 6; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 551
/note="L -> P (in Ref. 3; CAG29336)"
/evidence="ECO:0000305"
TURN 6..8
/evidence="ECO:0007744|PDB:1B3U"
HELIX 11..19
/evidence="ECO:0007744|PDB:1B3U"
HELIX 25..33
/evidence="ECO:0007744|PDB:1B3U"
HELIX 35..41
/evidence="ECO:0007744|PDB:1B3U"
HELIX 44..49
/evidence="ECO:0007744|PDB:1B3U"
HELIX 51..57
/evidence="ECO:0007744|PDB:1B3U"
HELIX 63..73
/evidence="ECO:0007744|PDB:1B3U"
TURN 74..77
/evidence="ECO:0007744|PDB:6IUR"
HELIX 78..80
/evidence="ECO:0007744|PDB:1B3U"
HELIX 83..89
/evidence="ECO:0007744|PDB:1B3U"
HELIX 90..96
/evidence="ECO:0007744|PDB:1B3U"
STRAND 99..101
/evidence="ECO:0007744|PDB:2IE4"
HELIX 102..116
/evidence="ECO:0007744|PDB:1B3U"
HELIX 121..126
/evidence="ECO:0007744|PDB:1B3U"
HELIX 128..136
/evidence="ECO:0007744|PDB:1B3U"
STRAND 138..140
/evidence="ECO:0007744|PDB:2PKG"
HELIX 141..147
/evidence="ECO:0007744|PDB:1B3U"
HELIX 148..150
/evidence="ECO:0007744|PDB:1B3U"
HELIX 151..154
/evidence="ECO:0007744|PDB:1B3U"
TURN 155..157
/evidence="ECO:0007744|PDB:1B3U"
HELIX 160..174
/evidence="ECO:0007744|PDB:1B3U"
HELIX 179..194
/evidence="ECO:0007744|PDB:1B3U"
HELIX 198..203
/evidence="ECO:0007744|PDB:1B3U"
HELIX 205..213
/evidence="ECO:0007744|PDB:1B3U"
HELIX 218..221
/evidence="ECO:0007744|PDB:1B3U"
HELIX 224..234
/evidence="ECO:0007744|PDB:1B3U"
HELIX 237..239
/evidence="ECO:0007744|PDB:1B3U"
HELIX 240..243
/evidence="ECO:0007744|PDB:1B3U"
HELIX 245..252
/evidence="ECO:0007744|PDB:1B3U"
HELIX 257..265
/evidence="ECO:0007744|PDB:1B3U"
HELIX 267..274
/evidence="ECO:0007744|PDB:1B3U"
HELIX 276..281
/evidence="ECO:0007744|PDB:1B3U"
HELIX 283..291
/evidence="ECO:0007744|PDB:1B3U"
HELIX 296..311
/evidence="ECO:0007744|PDB:1B3U"
TURN 315..317
/evidence="ECO:0007744|PDB:1B3U"
HELIX 318..324
/evidence="ECO:0007744|PDB:1B3U"
HELIX 326..334
/evidence="ECO:0007744|PDB:1B3U"
HELIX 339..346
/evidence="ECO:0007744|PDB:1B3U"
HELIX 349..352
/evidence="ECO:0007744|PDB:1B3U"
HELIX 353..356
/evidence="ECO:0007744|PDB:1B3U"
HELIX 358..364
/evidence="ECO:0007744|PDB:1B3U"
HELIX 366..373
/evidence="ECO:0007744|PDB:1B3U"
HELIX 378..385
/evidence="ECO:0007744|PDB:1B3U"
HELIX 389..394
/evidence="ECO:0007744|PDB:1B3U"
HELIX 397..412
/evidence="ECO:0007744|PDB:1B3U"
HELIX 417..434
/evidence="ECO:0007744|PDB:1B3U"
HELIX 436..438
/evidence="ECO:0007744|PDB:1B3U"
HELIX 441..449
/evidence="ECO:0007744|PDB:1B3U"
HELIX 450..452
/evidence="ECO:0007744|PDB:1B3U"
HELIX 456..473
/evidence="ECO:0007744|PDB:1B3U"
HELIX 475..481
/evidence="ECO:0007744|PDB:1B3U"
HELIX 483..488
/evidence="ECO:0007744|PDB:1B3U"
TURN 489..491
/evidence="ECO:0007744|PDB:1B3U"
HELIX 495..520
/evidence="ECO:0007744|PDB:1B3U"
HELIX 522..527
/evidence="ECO:0007744|PDB:1B3U"
HELIX 528..530
/evidence="ECO:0007744|PDB:1B3U"
HELIX 534..547
/evidence="ECO:0007744|PDB:1B3U"
HELIX 548..550
/evidence="ECO:0007744|PDB:1B3U"
HELIX 553..567
/evidence="ECO:0007744|PDB:1B3U"
HELIX 573..585
/evidence="ECO:0007744|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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Pathways :
WP1566: Citrate cycle (TCA cycle)
WP2199: Seed Development
WP1614: 1- and 2-Methylnaphthalene degradation
WP1655: Geraniol degradation
WP1644: DNA replication
WP1694: Pyrimidine metabolism
WP210: Cytoplasmic Ribosomal Proteins
WP1693: Purine metabolism
WP2292: Chemokine signaling pathway
WP1663: Homologous recombination
WP1672: Mismatch repair
WP1531: Vitamin D synthesis
WP2272: Pathogenic Escherichia coli infection
WP1659: Glycine, serine and threonine metabolism
WP1711: Trinitrotoluene degradation
WP1671: Methane metabolism
WP244: Alpha 6 Beta 4 signaling pathway
WP1487: TNF-alpha and mucus production in lung epythelium
WP1680: Oxidative phosphorylation
WP1003: Ovarian Infertility Genes
WP566: canonical wnt - zebrafish
WP1120: Ovarian Infertility Genes
WP1654: gamma-Hexachlorocyclohexane degradation
WP1904: RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways
WP263: Ovarian Infertility Genes

Related Genes :
[PPP2R1A] 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)
[Ppp2r1a] Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (PP2A subunit A isoform PR65-alpha) (PP2A subunit A isoform R1-alpha)
[PPP2R1B] Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform (PP2A subunit A isoform PR65-beta) (PP2A subunit A isoform R1-beta)
[PP2AA1 EER1 RCN1 REGA At1g25490 F2J7.19] Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (AtA alpha) (PP2A, subunit A, alpha isoform) (PR-65 A) (Protein ROOTS CURL IN NAPHTHYLPHTHALAMIC ACID 1) (Protein enhancer of ethylene-response 1)
[PPP2R5A] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform (PP2A B subunit isoform B'-alpha) (PP2A B subunit isoform B56-alpha) (PP2A B subunit isoform PR61-alpha) (PR61alpha) (PP2A B subunit isoform R5-alpha)
[PPP2R5C KIAA0044] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform (PP2A B subunit isoform B'-gamma) (PP2A B subunit isoform B56-gamma) (PP2A B subunit isoform PR61-gamma) (PP2A B subunit isoform R5-gamma) (Renal carcinoma antigen NY-REN-29)
[PPP2R2A] Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform (PP2A subunit B isoform B55-alpha) (PP2A subunit B isoform PR55-alpha) (PP2A subunit B isoform R2-alpha) (PP2A subunit B isoform alpha)
[PPP2R5D] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (PP2A B subunit isoform B'-delta) (PP2A B subunit isoform B56-delta) (PP2A B subunit isoform PR61-delta) (PP2A B subunit isoform R5-delta)
[PPP2R5B] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform (PP2A B subunit isoform B'-beta) (PP2A B subunit isoform B56-beta) (PP2A B subunit isoform PR61-beta) (PP2A B subunit isoform R5-beta)
[PPP2R5E] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform (PP2A B subunit isoform B'-epsilon) (PP2A B subunit isoform B56-epsilon) (PP2A B subunit isoform PR61-epsilon) (PP2A B subunit isoform R5-epsilon)
[PPP2R2B] Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform (PP2A subunit B isoform B55-beta) (PP2A subunit B isoform PR55-beta) (PP2A subunit B isoform R2-beta) (PP2A subunit B isoform beta)
[Ppp2r5a] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform (PP2A B subunit isoform B'-alpha) (PP2A B subunit isoform B56-alpha) (PP2A B subunit isoform PR61-alpha) (PR61alpha) (PP2A B subunit isoform R5-alpha)
[Ppp2r5b LOC100909468 rCG_47223] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform (PP2A B subunit isoform B'-beta) (PP2A B subunit isoform B56-beta) (PP2A B subunit isoform PR61-beta) (PP2A B subunit isoform R5-beta)
[Ppp2r2b] Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform (PP2A subunit B isoform B55-beta) (PP2A subunit B isoform BRB) (PP2A subunit B isoform PR55-beta) (PP2A subunit B isoform R2-beta) (PP2A subunit B isoform beta)
[PPP2R1A] 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)
[Ppp2r2b] Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform (PP2A subunit B isoform B55-beta) (PP2A subunit B isoform PR55-beta) (PP2A subunit B isoform R2-beta) (PP2A subunit B isoform beta)
[PPP2R3A PPP2R3] Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit alpha (PP2A subunit B isoform PR72/PR130) (PP2A subunit B isoform R3 isoform) (PP2A subunit B isoforms B''-PR72/PR130) (PP2A subunit B isoforms B72/B130) (Serine/threonine-protein phosphatase 2A 72/130 kDa regulatory subunit B)
[RTS1 SCS1 YOR014W OR26.04] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (PP2A, B subunit, B' delta isoform) (Protein RTS1) (Protein SCS1)
[PPP2CA] Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (PP2A-alpha) (EC 3.1.3.16) (Replication protein C) (RP-C)
[PTPA PPP2R4] Serine/threonine-protein phosphatase 2A activator (EC 5.2.1.8) (PP2A, subunit B', PR53 isoform) (Phosphotyrosyl phosphatase activator) (PTPA) (Serine/threonine-protein phosphatase 2A regulatory subunit 4) (Serine/threonine-protein phosphatase 2A regulatory subunit B')
[par1 pbp1 SPCC188.02] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta 1 isoform (PP2A, B subunit, B' delta 1 isoform)
[Ppp2ca] Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (PP2A-alpha) (EC 3.1.3.16)
[Ppp2ca] Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (PP2A-alpha) (EC 3.1.3.16)
[PP2AA3 DF2 At1g13320 T6J4.8] Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A gamma isoform (AtA gamma) (PP2A, subunit A, gamma isoform)
[PPP2CA] Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (PP2A-alpha) (EC 3.1.3.16)
[Ppp2r5c] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform (PP2A B subunit isoform B'-alpha-3) (PP2A B subunit isoform B'-gamma) (PP2A B subunit isoform B56-gamma) (PP2A B subunit isoform PR61-gamma) (PP2A B subunit isoform R5-gamma)
[PPP2R3B PPP2R3L] Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta (PP2A subunit B isoform PR48) (Protein phosphatase 2A 48 kDa regulatory subunit)
[tws aar Pp2A-85F CG6235] Protein phosphatase PP2A 55 kDa regulatory subunit (PR55) (Protein phosphatase PP2A regulatory subunit B) (Protein twins)
[Ptpa Ppp2r4] Serine/threonine-protein phosphatase 2A activator (EC 5.2.1.8) (PP2A, subunit B', PR53 isoform) (Phosphotyrosyl phosphatase activator) (PTPA) (Serine/threonine-protein phosphatase 2A regulatory subunit 4) (Serine/threonine-protein phosphatase 2A regulatory subunit B')
[PPP2CB] Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform (PP2A-beta) (EC 3.1.3.16)

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