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Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (PP2A-alpha) (EC 3.1.3.16) (Replication protein C) (RP-C)

 PP2AA_HUMAN             Reviewed;         309 AA.
P67775; P05323; P13197;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
05-DEC-2018, entry version 155.
RecName: Full=Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;
Short=PP2A-alpha;
EC=3.1.3.16;
AltName: Full=Replication protein C;
Short=RP-C;
Name=PPP2CA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fibroblast;
PubMed=2849764; DOI=10.1093/nar/16.23.11365;
Stone S.R., Mayer R., Wernet W., Maurer F., Hofsteenge J.,
Hemmings B.A.;
"The nucleotide sequence of the cDNA encoding the human lung protein
phosphatase 2A alpha catalytic subunit.";
Nucleic Acids Res. 16:11365-11365(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=2837763; DOI=10.1073/pnas.85.12.4252;
Arino J., Woon C.W., Brautigan D.L., Miller T.B. Jr., Johnson G.L.;
"Human liver phosphatase 2A: cDNA and amino acid sequence of two
catalytic subunit isotypes.";
Proc. Natl. Acad. Sci. U.S.A. 85:4252-4256(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1846293; DOI=10.1021/bi00215a014;
Khew-Goodall Y., Mayer R.E., Maurer F., Stone S.R., Hemmings B.A.;
"Structure and transcriptional regulation of protein phosphatase 2A
catalytic subunit genes.";
Biochemistry 30:89-97(1991).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, Placenta, and Uterus;
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]
DEPHOSPHORYLATION OF SV40 LARGE-T ANTIGEN AND P53 PROTEIN.
PubMed=1848668; DOI=10.1128/MCB.11.4.1996;
Scheidtmann K.H., Mumby M.C., Rundell K., Walter G.;
"Dephosphorylation of simian virus 40 large-T antigen and p53 protein
by protein phosphatase 2A: inhibition by small-t antigen.";
Mol. Cell. Biol. 11:1996-2003(1991).
[6]
METHYLATION AT LEU-309.
PubMed=8206937;
Favre B., Zolnierowicz S., Turowski P., Hemmings B.A.;
"The catalytic subunit of protein phosphatase 2A is carboxyl-
methylated in vivo.";
J. Biol. Chem. 269:16311-16317(1994).
[7]
INTERACTION WITH IGBP1.
PubMed=9647778; DOI=10.1006/bbrc.1998.8792;
Chen J., Peterson R.T., Schreiber S.L.;
"Alpha 4 associates with protein phosphatases 2A, 4, and 6.";
Biochem. Biophys. Res. Commun. 247:827-832(1998).
[8]
MUTAGENESIS OF LEU-309.
PubMed=10191253; DOI=10.1042/bj3390241;
Bryant J.C., Westphal R.S., Wadzinski B.E.;
"Methylated C-terminal leucine residue of PP2A catalytic subunit is
important for binding of regulatory Balpha subunit.";
Biochem. J. 339:241-246(1999).
[9]
PARTIAL PROTEIN SEQUENCE, AND ACTIVATION OF SV40 REPLICATION.
PubMed=2555176;
Virshup D.M., Kauffman M.G., Kelly T.J.;
"Activation of SV40 DNA replication in vitro by cellular protein
phosphatase 2A.";
EMBO J. 8:3891-3898(1989).
[10]
INTERACTION WITH AXIN1, AND FUNCTION.
PubMed=9920888; DOI=10.1074/jbc.274.6.3439;
Hsu W., Zeng L., Costantini F.;
"Identification of a domain of Axin that binds to the serine/threonine
protein phosphatase 2A and a self-binding domain.";
J. Biol. Chem. 274:3439-3445(1999).
[11]
FUNCTION, AND INTERACTION WITH RAF1.
PubMed=10801873; DOI=10.1074/jbc.M003259200;
Abraham D., Podar K., Pacher M., Kubicek M., Welzel N., Hemmings B.A.,
Dilworth S.M., Mischak H., Kolch W., Baccarini M.;
"Raf-1-associated protein phosphatase 2A as a positive regulator of
kinase activation.";
J. Biol. Chem. 275:22300-22304(2000).
[12]
IDENTIFICATION BY MASS SPECTROMETRY, 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).
[13]
INTERACTION WITH ADCY8.
PubMed=16258073; DOI=10.1124/mol.105.018275;
Crossthwaite A.J., Ciruela A., Rayner T.F., Cooper D.M.;
"A direct interaction between the N terminus of adenylyl cyclase AC8
and the catalytic subunit of protein phosphatase 2A.";
Mol. Pharmacol. 69:608-617(2006).
[14]
SUBCELLULAR LOCATION, AND INTERACTION WITH SGO1.
PubMed=16541025; DOI=10.1038/nature04663;
Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T.,
Kawashima S.A., Watanabe Y.;
"Shugoshin collaborates with protein phosphatase 2A to protect
cohesin.";
Nature 441:46-52(2006).
[15]
INTERACTION WITH PIM3.
PubMed=12473674; DOI=10.1074/jbc.M208246200;
Losman J.A., Chen X.P., Vuong B.Q., Fay S., Rothman P.B.;
"Protein phosphatase 2A regulates the stability of Pim protein
kinases.";
J. Biol. Chem. 278:4800-4805(2003).
[16]
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).
[17]
INTERACTION WITH SGO2.
PubMed=17485487; DOI=10.1083/jcb.200701122;
Huang H., Feng J., Famulski J., Rattner J.B., Liu S.T., Kao G.D.,
Muschel R., Chan G.K., Yen T.J.;
"Tripin/hSgo2 recruits MCAK to the inner centromere to correct
defective kinetochore attachments.";
J. Cell Biol. 177:413-424(2007).
[18]
INTERACTION WITH IGBP1.
PubMed=19818709; DOI=10.1016/j.molcel.2009.09.025;
Kong M., Ditsworth D., Lindsten T., Thompson C.B.;
"Alpha4 is an essential regulator of PP2A phosphatase activity.";
Mol. Cell 36:51-60(2009).
[19]
INTERACTION WITH IGBP1.
PubMed=20092282; DOI=10.1021/bi901837h;
McConnell J.L., Watkins G.R., Soss S.E., Franz H.S., McCorvey L.R.,
Spiller B.W., Chazin W.J., Wadzinski B.E.;
"Alpha4 is a ubiquitin-binding protein that regulates protein
serine/threonine phosphatase 2A ubiquitination.";
Biochemistry 49:1713-1718(2010).
[20]
INTERACTION WITH GSK3B.
PubMed=20080667; DOI=10.1073/pnas.0908133107;
Xie D., Gore C., Liu J., Pong R.C., Mason R., Hao G., Long M.,
Kabbani W., Yu L., Zhang H., Chen H., Sun X., Boothman D.A., Min W.,
Hsieh J.T.;
"Role of DAB2IP in modulating epithelial-to-mesenchymal transition and
prostate cancer metastasis.";
Proc. Natl. Acad. Sci. U.S.A. 107:2485-2490(2010).
[21]
ALTERNATIVE SPLICING (ISOFORM 2).
PubMed=22167190; DOI=10.1074/jbc.M111.283341;
Migueleti D.L., Smetana J.H., Nunes H.F., Kobarg J., Zanchin N.I.;
"Identification and characterization of an alternatively spliced
isoform of the human protein phosphatase 2Aalpha catalytic subunit.";
J. Biol. Chem. 287:4853-4862(2012).
[22]
FUNCTION.
PubMed=22613722; DOI=10.1074/jbc.M112.368613;
Watkins G.R., Wang N., Mazalouskas M.D., Gomez R.J., Guthrie C.R.,
Kraemer B.C., Schweiger S., Spiller B.W., Wadzinski B.E.;
"Monoubiquitination promotes calpain cleavage of the protein
phosphatase 2A (PP2A) regulatory subunit alpha4, altering PP2A
stability and microtubule-associated protein phosphorylation.";
J. Biol. Chem. 287:24207-24215(2012).
[23]
INTERACTION WITH FAM122A, UBIQUITINATION, AND PROTEASOMAL DEGRADATION.
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 MFHAS1.
PubMed=28609714; DOI=10.1016/j.molimm.2017.06.017;
Shi Q., Xiong B., Zhong J., Wang H., Ma D., Miao C.;
"MFHAS1 suppresses TLR4 signaling pathway via induction of PP2A C
subunit cytoplasm translocation and inhibition of c-Jun
dephosphorylation at Thr239.";
Mol. Immunol. 88:79-88(2017).
[25]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS,
AND COFACTOR.
PubMed=17055435; DOI=10.1016/j.cell.2006.09.025;
Xing Y., Xu Y., Chen Y., Jeffrey P.D., Chao Y., Lin Z., Li Z.,
Strack S., Stock J.B., Shi Y.;
"Structure of protein phosphatase 2A core enzyme bound to tumor-
inducing toxins.";
Cell 127:341-353(2006).
[26]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH PPP2R1A 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).
-!- FUNCTION: PP2A is the major phosphatase for microtubule-associated
proteins (MAPs). PP2A can modulate the activity of phosphorylase B
kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2
kinase. Cooperates with SGO2 to protect centromeric cohesin from
separase-mediated cleavage in oocytes specifically during meiosis
I (By similarity). Can dephosphorylate SV40 large T antigen and
p53/TP53. Activates RAF1 by dephosphorylating it at 'Ser-259'.
{ECO:0000250, ECO:0000269|PubMed:10801873,
ECO:0000269|PubMed:22613722, ECO:0000269|PubMed:9920888}.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999,
ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16;
-!- CATALYTIC ACTIVITY:
Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-
[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-
COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377,
ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977;
EC=3.1.3.16;
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:17055435};
Note=Binds 2 manganese ions per subunit.
{ECO:0000269|PubMed:17055435};
-!- 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. Interacts with NXN;
the interaction is direct (By similarity). Interacts with KCTD20
(By similarity). Interacts with BTBD10 (By similarity). Interacts
with TP53, SGO1 and SGO2. Interacts with AXIN1; the interaction
dephosphorylates AXIN1. Interacts with PIM3; this interaction
promotes dephosphorylation, ubiquitination and proteasomal
degradation of PIM3. Interacts with RAF1. Interaction with IGBP1
protects unassembled PPP2CA from degradative ubiquitination.
Interacts with GSK3B (via C2 domain). Interacts with MFHAS1;
retains PPP2CA into the cytoplasm and excludes it from the nucleus
(PubMed:28609714). Interacts with FAM122A (PubMed:27588481).
Interacts with ADCY8; interaction is phosphatase activity-
dependent; antagonizes interaction between ADCY8 and calmodulin
(PubMed:16258073). {ECO:0000250, ECO:0000250|UniProtKB:P63330,
ECO:0000269|PubMed:10801873, ECO:0000269|PubMed:12473674,
ECO:0000269|PubMed:16258073, ECO:0000269|PubMed:16541025,
ECO:0000269|PubMed:16580887, ECO:0000269|PubMed:17055435,
ECO:0000269|PubMed:17245430, ECO:0000269|PubMed:17485487,
ECO:0000269|PubMed:18394995, ECO:0000269|PubMed:19818709,
ECO:0000269|PubMed:20080667, ECO:0000269|PubMed:20092282,
ECO:0000269|PubMed:27588481, ECO:0000269|PubMed:28609714,
ECO:0000269|PubMed:9647778, ECO:0000269|PubMed:9920888}.
-!- INTERACTION:
P31749:AKT1; NbExp=4; IntAct=EBI-712311, EBI-296087;
P39687:ANP32A; NbExp=2; IntAct=EBI-712311, EBI-359234;
P03129:E7 (xeno); NbExp=3; IntAct=EBI-712311, EBI-866453;
P04020:E7 (xeno); NbExp=2; IntAct=EBI-712311, EBI-7005254;
P06730:EIF4E; NbExp=2; IntAct=EBI-712311, EBI-73440;
P46695:IER3; NbExp=2; IntAct=EBI-712311, EBI-1748945;
P78318:IGBP1; NbExp=16; IntAct=EBI-712311, EBI-1055954;
Q61249:Igbp1 (xeno); NbExp=3; IntAct=EBI-712311, EBI-7002233;
O14920:IKBKB; NbExp=3; IntAct=EBI-712311, EBI-81266;
Q9Y6K9:IKBKG; NbExp=4; IntAct=EBI-712311, EBI-81279;
Q969F8:KISS1R; NbExp=3; IntAct=EBI-712311, EBI-8481408;
P97346:Nxn (xeno); NbExp=2; IntAct=EBI-712311, EBI-309684;
Q9Y570:PPME1; NbExp=2; IntAct=EBI-16765970, EBI-1772895;
P30153:PPP2R1A; NbExp=43; IntAct=EBI-712311, EBI-302388;
P30154:PPP2R1B; NbExp=8; IntAct=EBI-712311, EBI-357094;
Q9Y2T4:PPP2R2C; NbExp=3; IntAct=EBI-712311, EBI-1774058;
Q15172:PPP2R5A; NbExp=5; IntAct=EBI-712311, EBI-641666;
Q15173:PPP2R5B; NbExp=5; IntAct=EBI-712311, EBI-1369497;
Q13362:PPP2R5C; NbExp=9; IntAct=EBI-712311, EBI-1266156;
P04049:RAF1; NbExp=2; IntAct=EBI-712311, EBI-365996;
P28749:RBL1; NbExp=2; IntAct=EBI-712311, EBI-971402;
Q08999:RBL2; NbExp=2; IntAct=EBI-712311, EBI-971439;
Q04206:RELA; NbExp=6; IntAct=EBI-712311, EBI-73886;
Q5FBB7:SGO1; NbExp=3; IntAct=EBI-712311, EBI-989069;
Q5VSL9:STRIP1; NbExp=7; IntAct=EBI-712311, EBI-1773588;
O43815:STRN; NbExp=5; IntAct=EBI-712311, EBI-1046642;
O75663:TIPRL; NbExp=3; IntAct=EBI-16766021, EBI-1054735;
Q15645:TRIP13; NbExp=5; IntAct=EBI-712311, EBI-358993;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16541025}.
Nucleus {ECO:0000269|PubMed:16541025}. Chromosome, centromere
{ECO:0000269|PubMed:16541025}. Cytoplasm, cytoskeleton, spindle
pole {ECO:0000269|PubMed:16541025}. Note=In prometaphase cells,
but not in anaphase cells, localizes at centromeres. During
mitosis, also found at spindle poles. Centromeric localization
requires the presence of SGO2 (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=PP2Acalpha1;
IsoId=P67775-1; Sequence=Displayed;
Name=2; Synonyms=PP2Acalpha2;
IsoId=P67775-2; Sequence=VSP_044320;
Note=Catalytically inactive, shows enhanced binding to IGBP1,
and does not interact with the scaffolding subunit PPP2R1A.;
-!- PTM: Reversibly methyl esterified on Leu-309 by leucine carboxyl
methyltransferase 1 (LCMT1) and protein phosphatase methylesterase
1 (PPME1). Carboxyl methylation influences the affinity of the
catalytic subunit for the different regulatory subunits, thereby
modulating the PP2A holoenzyme's substrate specificity, enzyme
activity and cellular localization. {ECO:0000269|PubMed:8206937}.
-!- PTM: Phosphorylation of either threonine (by autophosphorylation-
activated protein kinase) or tyrosine results in inactivation of
the phosphatase. Auto-dephosphorylation has been suggested as a
mechanism for reactivation.
-!- PTM: Polyubiquitinated, leading to its degradation by the
proteasome. {ECO:0000269|PubMed:27588481}.
-!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
{ECO:0000305}.
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EMBL; X12646; CAA31176.1; -; mRNA.
EMBL; J03804; AAB38019.1; -; mRNA.
EMBL; M60483; AAA36466.1; -; Genomic_DNA.
EMBL; BC000400; AAH00400.1; -; mRNA.
EMBL; BC002657; AAH02657.1; -; mRNA.
EMBL; BC019275; AAH19275.1; -; mRNA.
EMBL; BC031696; AAH31696.1; -; mRNA.
CCDS; CCDS4173.1; -. [P67775-1]
PIR; S01986; PAHU2A.
RefSeq; NP_002706.1; NM_002715.2. [P67775-1]
UniGene; Hs.105818; -.
PDB; 2IAE; X-ray; 3.50 A; C/F=1-309.
PDB; 2IE3; X-ray; 2.80 A; C=1-309.
PDB; 2IE4; X-ray; 2.60 A; C=1-309.
PDB; 2NPP; X-ray; 3.30 A; C/F=1-309.
PDB; 2NYL; X-ray; 3.80 A; C/F=2-294.
PDB; 2NYM; X-ray; 3.60 A; C/F=2-294.
PDB; 3C5W; X-ray; 2.80 A; C=1-309.
PDB; 3DW8; X-ray; 2.85 A; C/F=1-309.
PDB; 3FGA; X-ray; 2.70 A; C=1-309.
PDB; 3K7V; X-ray; 2.85 A; C=1-309.
PDB; 3K7W; X-ray; 2.96 A; C=1-309.
PDB; 3P71; X-ray; 2.70 A; C=1-309.
PDB; 4I5L; X-ray; 2.43 A; C/F=1-309.
PDB; 4I5N; X-ray; 2.80 A; C/F=1-309.
PDB; 4IYP; X-ray; 2.80 A; C=6-153.
PDB; 4LAC; X-ray; 2.82 A; C=1-309.
PDB; 5W0W; X-ray; 3.80 A; C/F/I/L=1-309.
PDBsum; 2IAE; -.
PDBsum; 2IE3; -.
PDBsum; 2IE4; -.
PDBsum; 2NPP; -.
PDBsum; 2NYL; -.
PDBsum; 2NYM; -.
PDBsum; 3C5W; -.
PDBsum; 3DW8; -.
PDBsum; 3FGA; -.
PDBsum; 3K7V; -.
PDBsum; 3K7W; -.
PDBsum; 3P71; -.
PDBsum; 4I5L; -.
PDBsum; 4I5N; -.
PDBsum; 4IYP; -.
PDBsum; 4LAC; -.
PDBsum; 5W0W; -.
ProteinModelPortal; P67775; -.
SMR; P67775; -.
BioGrid; 111507; 288.
CORUM; P67775; -.
DIP; DIP-29395N; -.
IntAct; P67775; 166.
MINT; P67775; -.
STRING; 9606.ENSP00000418447; -.
BindingDB; P67775; -.
ChEMBL; CHEMBL4703; -.
DrugBank; DB00163; Vitamin E.
DEPOD; P67775; -.
iPTMnet; P67775; -.
PhosphoSitePlus; P67775; -.
BioMuta; PPP2CA; -.
DMDM; 54038809; -.
EPD; P67775; -.
MaxQB; P67775; -.
PaxDb; P67775; -.
PeptideAtlas; P67775; -.
PRIDE; P67775; -.
ProteomicsDB; 57521; -.
DNASU; 5515; -.
Ensembl; ENST00000481195; ENSP00000418447; ENSG00000113575. [P67775-1]
GeneID; 5515; -.
KEGG; hsa:5515; -.
UCSC; uc003kze.4; human. [P67775-1]
CTD; 5515; -.
DisGeNET; 5515; -.
EuPathDB; HostDB:ENSG00000113575.9; -.
GeneCards; PPP2CA; -.
HGNC; HGNC:9299; PPP2CA.
HPA; CAB003848; -.
HPA; HPA043236; -.
MIM; 176915; gene.
neXtProt; NX_P67775; -.
OpenTargets; ENSG00000113575; -.
PharmGKB; PA33663; -.
eggNOG; KOG0371; Eukaryota.
eggNOG; COG0639; LUCA.
GeneTree; ENSGT00550000074618; -.
HOGENOM; HOG000172696; -.
HOVERGEN; HBG000216; -.
InParanoid; P67775; -.
KO; K04382; -.
OMA; QILWNDP; -.
OrthoDB; EOG091G0B6S; -.
PhylomeDB; P67775; -.
TreeFam; TF105559; -.
BioCyc; MetaCyc:HS03696-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-2995383; Initiation of Nuclear Envelope Reformation.
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-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-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SignaLink; P67775; -.
SIGNOR; P67775; -.
ChiTaRS; PPP2CA; human.
EvolutionaryTrace; P67775; -.
GeneWiki; PPP2CA; -.
GenomeRNAi; 5515; -.
PRO; PR:P67775; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113575; Expressed in 233 organ(s), highest expression level in adrenal tissue.
CleanEx; HS_PPP2CA; -.
ExpressionAtlas; P67775; baseline and differential.
Genevisible; P67775; HS.
GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016020; C:membrane; NAS:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA: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:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0045202; C:synapse; IEA:Ensembl.
GO; GO:0050811; F:GABA receptor binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004721; F:phosphoprotein phosphatase activity; TAS:ARUK-UCL.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:ARUK-UCL.
GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
GO; GO:0006672; P:ceramide metabolic process; NAS:UniProtKB.
GO; GO:0000188; P:inactivation of MAPK activity; NAS:UniProtKB.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
GO; GO:0007498; P:mesoderm development; IEA:Ensembl.
GO; GO:0030308; P:negative regulation of cell growth; NAS:UniProtKB.
GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
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; TAS:ARUK-UCL.
GO; GO:0035970; P:peptidyl-threonine dephosphorylation; TAS:ARUK-UCL.
GO; GO:1904528; P:positive regulation of microtubule binding; ISS:ARUK-UCL.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:BHF-UCL.
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:0040008; P:regulation of growth; NAS:UniProtKB.
GO; GO:1904526; P:regulation of microtubule binding; NAS:ARUK-UCL.
GO; GO:0001932; P:regulation of protein phosphorylation; NAS:ARUK-UCL.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0030111; P:regulation of Wnt signaling pathway; NAS:UniProtKB.
GO; GO:0010288; P:response to lead ion; ISS:ARUK-UCL.
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; 3.60.21.10; -; 1.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
Pfam; PF00149; Metallophos; 1.
PRINTS; PR00114; STPHPHTASE.
SMART; SM00156; PP2Ac; 1.
PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Centromere; Chromosome;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Hydrolase; Manganese; Meiosis; Metal-binding; Methylation; Nucleus;
Phosphoprotein; Polymorphism; Protein phosphatase; Reference proteome;
Ubl conjugation.
CHAIN 1 309 Serine/threonine-protein phosphatase 2A
catalytic subunit alpha isoform.
/FTId=PRO_0000058839.
ACT_SITE 118 118 Proton donor. {ECO:0000250}.
METAL 57 57 Manganese 1.
{ECO:0000269|PubMed:17055435}.
METAL 59 59 Manganese 1.
{ECO:0000269|PubMed:17055435}.
METAL 85 85 Manganese 1.
{ECO:0000269|PubMed:17055435}.
METAL 85 85 Manganese 2.
{ECO:0000269|PubMed:17055435}.
METAL 117 117 Manganese 2.
{ECO:0000269|PubMed:17055435}.
METAL 167 167 Manganese 2.
{ECO:0000269|PubMed:17055435}.
METAL 241 241 Manganese 2.
{ECO:0000269|PubMed:17055435}.
MOD_RES 307 307 Phosphotyrosine.
{ECO:0000250|UniProtKB:P67774}.
MOD_RES 309 309 Leucine methyl ester.
{ECO:0000269|PubMed:8206937}.
VAR_SEQ 193 246 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_044320.
VARIANT 52 52 V -> A (in dbSNP:rs11552681).
/FTId=VAR_051735.
MUTAGEN 309 309 L->A: Loss of binding to PP2A B-alpha
regulatory subunit.
{ECO:0000269|PubMed:10191253}.
HELIX 3 18 {ECO:0000244|PDB:4I5L}.
HELIX 25 39 {ECO:0000244|PDB:4I5L}.
STRAND 44 48 {ECO:0000244|PDB:4I5L}.
STRAND 50 55 {ECO:0000244|PDB:4I5L}.
HELIX 62 72 {ECO:0000244|PDB:4I5L}.
TURN 75 77 {ECO:0000244|PDB:4I5L}.
STRAND 80 82 {ECO:0000244|PDB:4I5L}.
STRAND 87 91 {ECO:0000244|PDB:4I5L}.
HELIX 93 106 {ECO:0000244|PDB:4I5L}.
TURN 108 110 {ECO:0000244|PDB:4I5L}.
STRAND 111 113 {ECO:0000244|PDB:4I5L}.
HELIX 121 127 {ECO:0000244|PDB:4I5L}.
HELIX 129 137 {ECO:0000244|PDB:4I5L}.
STRAND 138 140 {ECO:0000244|PDB:4I5L}.
HELIX 141 150 {ECO:0000244|PDB:4I5L}.
STRAND 155 159 {ECO:0000244|PDB:4I5L}.
TURN 160 162 {ECO:0000244|PDB:4I5L}.
STRAND 163 168 {ECO:0000244|PDB:4I5L}.
HELIX 177 182 {ECO:0000244|PDB:4I5L}.
STRAND 186 188 {ECO:0000244|PDB:3C5W}.
STRAND 191 193 {ECO:0000244|PDB:4I5L}.
HELIX 194 200 {ECO:0000244|PDB:4I5L}.
STRAND 205 211 {ECO:0000244|PDB:4I5L}.
STRAND 215 220 {ECO:0000244|PDB:4I5L}.
HELIX 222 232 {ECO:0000244|PDB:4I5L}.
STRAND 235 239 {ECO:0000244|PDB:4I5L}.
STRAND 247 251 {ECO:0000244|PDB:4I5L}.
TURN 252 255 {ECO:0000244|PDB:4I5L}.
STRAND 256 259 {ECO:0000244|PDB:4I5L}.
HELIX 265 267 {ECO:0000244|PDB:4I5L}.
STRAND 273 278 {ECO:0000244|PDB:4I5L}.
STRAND 284 289 {ECO:0000244|PDB:4I5L}.
SEQUENCE 309 AA; 35594 MW; C602291F78F34555 CRC64;
MDEKVFTKEL DQWIEQLNEC KQLSESQVKS LCEKAKEILT KESNVQEVRC PVTVCGDVHG
QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL VALKVRYRER ITILRGNHES
RQITQVYGFY DECLRKYGNA NVWKYFTDLF DYLPLTALVD GQIFCLHGGL SPSIDTLDHI
RALDRLQEVP HEGPMCDLLW SDPDDRGGWG ISPRGAGYTF GQDISETFNH ANGLTLVSRA
HQLVMEGYNW CHDRNVVTIF SAPNYCYRCG NQAAIMELDD TLKYSFLQFD PAPRRGEPHV
TRRTPDYFL


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