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

 PP2AA_MOUSE             Reviewed;         309 AA.
P63330; O88591; P13353; Q5SNY5;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
05-DEC-2018, entry version 138.
RecName: Full=Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;
Short=PP2A-alpha;
EC=3.1.3.16;
Name=Ppp2ca;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6 X DBA/2; TISSUE=Brain;
Goetz J.M., Kues W.;
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD; TISSUE=Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Eye, and Mammary gland;
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).
[6]
PHOSPHORYLATION AT TYR-307.
PubMed=7510677;
Chen J., Parsons S., Brautigan D.L.;
"Tyrosine phosphorylation of protein phosphatase 2A in response to
growth stimulation and v-src transformation of fibroblasts.";
J. Biol. Chem. 269:7957-7962(1994).
[7]
MUTAGENESIS OF TYR-307 AND LEU-309, AND METHYLATION AT LEU-309.
PubMed=10441131; DOI=10.1021/bi990902g;
Chung H., Nairn A.C., Murata K., Brautigan D.L.;
"Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic
subunit favors association with the alpha 4 subunit which promotes
dephosphorylation of elongation factor-2.";
Biochemistry 38:10371-10376(1999).
[8]
INTERACTION WITH NXN.
PubMed=16764867; DOI=10.1016/j.febslet.2006.04.101;
Lechward K., Sugajska E., de Baere I., Goris J., Hemmings B.A.,
Zolnierowicz S.;
"Interaction of nucleoredoxin with protein phosphatase 2A.";
FEBS Lett. 580:3631-3637(2006).
[9]
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).
[10]
INTERACTION WITH BTBD10.
PubMed=18160256; DOI=10.1016/j.cellsig.2007.11.004;
Nawa M., Kanekura K., Hashimoto Y., Aiso S., Matsuoka M.;
"A novel Akt/PKB-interacting protein promotes cell adhesion and
inhibits familial amyotrophic lateral sclerosis-linked mutant SOD1-
induced neuronal death via inhibition of PP2A-mediated
dephosphorylation of Akt/PKB.";
Cell. Signal. 20:493-505(2008).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18084284; DOI=10.1038/ncb1667;
Lee J., Kitajima T.S., Tanno Y., Yoshida K., Morita T., Miyano T.,
Miyake M., Watanabe Y.;
"Unified mode of centromeric protection by shugoshin in mammalian
oocytes and somatic cells.";
Nat. Cell Biol. 10:42-52(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
INTERACTION WITH KCTD20.
PubMed=24156551; DOI=10.1186/1471-2091-14-27;
Nawa M., Matsuoka M.;
"KCTD20, a relative of BTBD10, is a positive regulator of Akt.";
BMC Biochem. 14:27-27(2013).
[14]
MONUBIQUITINATION BY NOSIP.
PubMed=25546391; DOI=10.1371/journal.pone.0116150;
Hoffmeister M., Prelle C., Kuechler P., Kovacevic I., Moser M.,
Mueller-Esterl W., Oess S.;
"The ubiquitin E3 ligase NOSIP modulates protein phosphatase 2A
activity in craniofacial development.";
PLoS ONE 9:E116150-E116150(2014).
-!- 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. Activates RAF1 by dephosphorylating it at 'Ser-259' (By
similarity). {ECO:0000250, ECO:0000269|PubMed:18084284}.
-!- 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:0000250};
Note=Binds 2 manganese ions per subunit. {ECO:0000250};
-!- 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. Interacts with TP53, SGO1 and SGO2.
Interacts with AXIN1; the interaction dephosphorylates AXIN1 (By
similarity). Interacts with PIM3; this interaction promotes
dephosphorylation, ubiquitination and proteasomal degradation of
PIM3 (By similarity). Interacts with RAF1. Interacts with GSK3B
(via C2 domain) (By similarity). Interaction with IGBP1 protects
unassembled PPP2CA from degradative ubiquitination (By
similarity). Interacts with KCTD20 (PubMed:24156551). Interacts
with BTBD10 (PubMed:18160256). Interacts with MFHAS1; retains
PPP2CA into the cytoplasm and excludes it from the nucleus (By
similarity). Interacts with FAM122A (By similarity). Interacts
with ADCY8; interaction is phosphatase activity-dependent;
antagonizes interaction between ADCY8 and calmodulin
(PubMed:16258073). {ECO:0000250|UniProtKB:P67775,
ECO:0000269|PubMed:16258073, ECO:0000269|PubMed:18160256,
ECO:0000269|PubMed:24156551}.
-!- INTERACTION:
Q61249:Igbp1; NbExp=2; IntAct=EBI-397144, EBI-7002233;
Q76MZ3:Ppp2r1a; NbExp=3; IntAct=EBI-397144, EBI-400413;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18084284}.
Nucleus {ECO:0000250}. Chromosome, centromere
{ECO:0000269|PubMed:18084284}. Cytoplasm, cytoskeleton, spindle
pole {ECO:0000250}. Note=In prometaphase cells, but not in
anaphase cells, localizes at centromeres. During mitosis, also
found at spindle poles (By similarity). Centromeric localization
requires the presence of SGO2. {ECO:0000250}.
-!- 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:10441131}.
-!- 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. {ECO:0000269|PubMed:7510677}.
-!- PTM: Polyubiquitinated, leading to its degradation by the
proteasome (By similarity). May be monoubiquitinated by NOSIP.
{ECO:0000250|UniProtKB:P67775, ECO:0000269|PubMed:25546391}.
-!- MISCELLANEOUS: Double mutation Phe-307 and Gln-309 results in
association of the PP2A C subunit with alpha-4 protein.
-!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
{ECO:0000305}.
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EMBL; AF076192; AAD12587.1; -; mRNA.
EMBL; Z67745; CAA91558.1; -; mRNA.
EMBL; AK076110; BAC36190.1; -; mRNA.
EMBL; AK172644; BAE43111.1; -; mRNA.
EMBL; AL935177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC003856; AAH03856.1; -; mRNA.
EMBL; BC054458; AAH54458.1; -; mRNA.
CCDS; CCDS24666.1; -.
RefSeq; NP_062284.1; NM_019411.4.
UniGene; Mm.260288; -.
ProteinModelPortal; P63330; -.
SMR; P63330; -.
BioGrid; 202341; 78.
CORUM; P63330; -.
IntAct; P63330; 67.
MINT; P63330; -.
STRING; 10090.ENSMUSP00000020608; -.
iPTMnet; P63330; -.
PhosphoSitePlus; P63330; -.
EPD; P63330; -.
MaxQB; P63330; -.
PaxDb; P63330; -.
PeptideAtlas; P63330; -.
PRIDE; P63330; -.
Ensembl; ENSMUST00000020608; ENSMUSP00000020608; ENSMUSG00000020349.
GeneID; 19052; -.
KEGG; mmu:19052; -.
UCSC; uc007ivb.1; mouse.
CTD; 5515; -.
MGI; MGI:1321159; Ppp2ca.
eggNOG; KOG0371; Eukaryota.
eggNOG; COG0639; LUCA.
GeneTree; ENSGT00550000074618; -.
HOGENOM; HOG000172696; -.
HOVERGEN; HBG000216; -.
InParanoid; P63330; -.
KO; K04382; -.
OMA; QILWNDP; -.
OrthoDB; EOG091G0B6S; -.
PhylomeDB; P63330; -.
TreeFam; TF105559; -.
Reactome; R-MMU-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
Reactome; R-MMU-1295596; Spry regulation of FGF signaling.
Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-MMU-180024; DARPP-32 events.
Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-MMU-196299; Beta-catenin phosphorylation cascade.
Reactome; R-MMU-198753; ERK/MAPK targets.
Reactome; R-MMU-202670; ERKs are inactivated.
Reactome; R-MMU-2467813; Separation of Sister Chromatids.
Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-MMU-389513; CTLA4 inhibitory signaling.
Reactome; R-MMU-432142; Platelet sensitization by LDL.
Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
Reactome; R-MMU-5673000; RAF activation.
Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-68877; Mitotic Prometaphase.
Reactome; R-MMU-69231; Cyclin D associated events in G1.
Reactome; R-MMU-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
ChiTaRS; Ppp2ca; mouse.
PRO; PR:P63330; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020349; Expressed in 307 organ(s), highest expression level in cerebellum.
Genevisible; P63330; MM.
GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0014069; C:postsynaptic density; ISO:MGI.
GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:MGI.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0045202; C:synapse; IDA:SynGO.
GO; GO:0043195; C:terminal bouton; ISO:MGI.
GO; GO:0031698; F:beta-2 adrenergic receptor binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0050811; F:GABA receptor binding; IDA:MGI.
GO; GO:0044325; F:ion channel binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:1990405; F:protein antigen binding; ISO:MGI.
GO; GO:0008022; F:protein C-terminus binding; IPI:MGI.
GO; GO:0046983; F:protein dimerization activity; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0043422; F:protein kinase B binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0051721; F:protein phosphatase 2A binding; ISO:MGI.
GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0048156; F:tau protein binding; ISO:MGI.
GO; GO:0071333; P:cellular response to glucose stimulus; ISO:MGI.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
GO; GO:0007498; P:mesoderm development; IMP:MGI.
GO; GO:1901020; P:negative regulation of calcium ion transmembrane transporter activity; ISO:MGI.
GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISO:MGI.
GO; GO:0042308; P:negative regulation of protein import into nucleus; ISO:MGI.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:1904528; P:positive regulation of microtubule binding; ISO:MGI.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:MGI.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:MGI.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0006470; P:protein dephosphorylation; ISO:MGI.
GO; GO:0070208; P:protein heterotrimerization; ISO:MGI.
GO; GO:0051726; P:regulation of cell cycle; TAS:MGI.
GO; GO:0031952; P:regulation of protein autophosphorylation; ISO:MGI.
GO; GO:0042176; P:regulation of protein catabolic process; ISO:MGI.
GO; GO:0001932; P:regulation of protein phosphorylation; ISO:MGI.
GO; GO:0010469; P:regulation of signaling receptor activity; ISO:MGI.
GO; GO:0010288; P:response to lead ion; ISO:MGI.
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;
Centromere; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton;
Hydrolase; Manganese; Meiosis; Metal-binding; Methylation; Nucleus;
Phosphoprotein; Protein phosphatase; Reference proteome;
Ubl conjugation.
CHAIN 1 309 Serine/threonine-protein phosphatase 2A
catalytic subunit alpha isoform.
/FTId=PRO_0000058840.
ACT_SITE 118 118 Proton donor. {ECO:0000250}.
METAL 57 57 Manganese 1. {ECO:0000250}.
METAL 59 59 Manganese 1. {ECO:0000250}.
METAL 85 85 Manganese 1. {ECO:0000250}.
METAL 85 85 Manganese 2. {ECO:0000250}.
METAL 117 117 Manganese 2. {ECO:0000250}.
METAL 167 167 Manganese 2. {ECO:0000250}.
METAL 241 241 Manganese 2. {ECO:0000250}.
MOD_RES 307 307 Phosphotyrosine.
{ECO:0000269|PubMed:7510677}.
MOD_RES 309 309 Leucine methyl ester.
{ECO:0000269|PubMed:10441131}.
MUTAGEN 307 307 Y->Q: Loss of trimeric subunit ABC
assembly. {ECO:0000269|PubMed:10441131}.
MUTAGEN 309 309 L->A: Loss of binding to PP2A B-alpha
regulatory subunit.
{ECO:0000269|PubMed:10441131}.
CONFLICT 31 31 L -> P (in Ref. 2; AAD12587).
{ECO:0000305}.
CONFLICT 73 73 G -> V (in Ref. 2; AAD12587).
{ECO:0000305}.
SEQUENCE 309 AA; 35608 MW; 8DC11276E6DF9E33 CRC64;
MDEKLFTKEL 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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H0445 Serine threonine-protein phosphatase 2A catalytic subunit alpha isoform (PPP2CA), Rabbit, ELISA Kit 96T
H0441 Serine threonine-protein phosphatase 2A catalytic subunit alpha isoform (PPP2CA), Chicken, ELISA Kit 96T
H0443 Serine threonine-protein phosphatase 2A catalytic subunit alpha isoform (PPP2CA), Mouse, ELISA Kit 96T
H0440 Serine threonine-protein phosphatase 2A catalytic subunit alpha isoform (PPP2CA), Bovine, ELISA Kit 96T
H0442 Serine threonine-protein phosphatase 2A catalytic subunit alpha isoform (PPP2CA), Human, ELISA Kit 96T
PP2BA_RAT ELISA Kit FOR Serine per threonine-protein phosphatase 2B catalytic subunit alpha isoform; organism: Rat; gene name: Ppp3ca 96T
PP2AA_RAT ELISA Kit FOR Serine per threonine-protein phosphatase 2A catalytic subunit alpha isoform; organism: Rat; gene name: Ppp2ca 96T
PP2AA_MOUSE ELISA Kit FOR Serine per threonine-protein phosphatase 2A catalytic subunit alpha isoform; organism: Mouse; gene name: Ppp2ca 96T
PP2BA_MOUSE ELISA Kit FOR Serine per threonine-protein phosphatase 2B catalytic subunit alpha isoform; organism: Mouse; gene name: Ppp3ca 96T
EIAAB31909 Pig,PP2A-alpha,PPP2CA,Serine_threonine-protein phosphatase 2A catalytic subunit alpha isoform,Sus scrofa
EIAAB31907 PP2A-alpha,Ppp2ca,Rat,Rattus norvegicus,Serine_threonine-protein phosphatase 2A catalytic subunit alpha isoform
EIAAB31911 Bos taurus,Bovine,PP2A-alpha,PPP2CA,Serine_threonine-protein phosphatase 2A catalytic subunit alpha isoform
EIAAB31910 Mouse,Mus musculus,PP2A-alpha,Ppp2ca,Serine_threonine-protein phosphatase 2A catalytic subunit alpha isoform
EIAAB31912 Oryctolagus cuniculus,PP2A-alpha,PPP2CA,Rabbit,Serine_threonine-protein phosphatase 2A catalytic subunit alpha isoform
EIAAB31906 Homo sapiens,Human,PP2A-alpha,PPP2CA,Replication protein C,RP-C,Serine_threonine-protein phosphatase 2A catalytic subunit alpha isoform
EIAAB31922 Calmodulin-dependent calcineurin A subunit alpha isoform,CALNA,CAM-PRP catalytic subunit,CNA,Homo sapiens,Human,PPP3CA,Serine_threonine-protein phosphatase 2B catalytic subunit alpha isoform


 

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