Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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')

 PTPA_HUMAN              Reviewed;         358 AA.
Q15257; A2A347; A9IZU4; B4DXM4; Q15258; Q53GZ3; Q5TZQ2; Q9BUK1;
Q9NNZ7; Q9NNZ8; Q9NNZ9;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
05-DEC-2018, entry version 170.
RecName: Full=Serine/threonine-protein phosphatase 2A activator;
EC=5.2.1.8;
AltName: Full=PP2A, subunit B', PR53 isoform;
AltName: Full=Phosphotyrosyl phosphatase activator;
Short=PTPA;
AltName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit 4;
AltName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit B';
Name=PTPA {ECO:0000312|HGNC:HGNC:9308}; Synonyms=PPP2R4;
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), AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Heart;
PubMed=8195217;
Cayla X., Van Hoof C., Bosch M., Waelkens E., Peeters B.,
Merlevede W., Goris J.;
"Molecular cloning, expression, and characterization of PTPA, a
protein that activates the tyrosyl phosphatase activity of protein
phosphatase 2A.";
J. Biol. Chem. 269:15668-15675(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
TISSUE=Blood;
PubMed=8530035; DOI=10.1006/geno.1995.1140;
Van Hoof C., Aly M., Garcia A., Cayla X., Cassiman J.-J.,
Merlevede W., Goris J.;
"Structure and chromosomal localization of the human gene of the
phosphotyrosyl phosphatase activator (PTPA) of protein phosphatase
2A.";
Genomics 28:261-272(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2; 3 AND 4).
PubMed=10880964; DOI=10.1046/j.1432-1327.2000.01486.x;
Janssens V., van Hoof C., Martens E., de Baere I., Merlevede W.,
Goris J.;
"Identification and characterization of alternative splice products
encoded by the human phosphotyrosyl phosphatase activator gene.";
Eur. J. Biochem. 267:4406-4413(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
LEU-357.
TISSUE=Liver;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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).
[10]
FUNCTION IN APOPTOSIS, AND SUBCELLULAR LOCATION.
PubMed=17333320; DOI=10.1007/s10495-006-0050-8;
Azam S., Drobetsky E., Ramotar D.;
"Overexpression of the cis/trans isomerase PTPA triggers caspase 3-
dependent apoptosis.";
Apoptosis 12:1243-1255(2007).
[11]
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).
[12]
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).
[13]
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).
[14]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 22-358.
PubMed=16782712; DOI=10.1074/jbc.C600100200;
Magnusdottir A., Stenmark P., Flodin S., Nyman T., Hammarstroem M.,
Ehn M., Bakali H M.A., Berglund H., Nordlund P.;
"The crystal structure of a human PP2A phosphatase activator reveals a
novel fold and highly conserved cleft implicated in protein-protein
interactions.";
J. Biol. Chem. 281:22434-22438(2006).
[15]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 20-357.
PubMed=16885030; DOI=10.1016/j.molcel.2006.07.008;
Leulliot N., Vicentini G., Jordens J., Quevillon-Cheruel S.,
Schiltz M., Barford D., van Tilbeurgh H., Goris J.;
"Crystal structure of the PP2A phosphatase activator: implications for
its PP2A-specific PPIase activity.";
Mol. Cell 23:413-424(2006).
[16]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), FUNCTION IN MODULATION OF PP2A
SUBSTRATE SPECIFICITY, ATP-BINDING, MUTAGENESIS OF ASP-185; ALA-239;
GLY-240; VAL-244; GLU-305; GLY-325; MET-329 AND LYS-337, AND
INTERACTION WITH THE PP2A(D) COMPLEX.
PubMed=16916641; DOI=10.1016/j.molcel.2006.07.027;
Chao Y., Xing Y., Chen Y., Xu Y., Lin Z., Li Z., Jeffrey P.D.,
Stock J.B., Shi Y.;
"Structure and mechanism of the phosphotyrosyl phosphatase
activator.";
Mol. Cell 23:535-546(2006).
-!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
the cis-trans isomerization of proline imidic peptide bonds in
oligopeptides. Acts as a regulatory subunit for serine/threonine-
protein phosphatase 2A (PP2A) modulating its activity or substrate
specificity, probably by inducing a conformational change in the
catalytic subunit, a proposed direct target of the PPIase. Can
reactivate inactive phosphatase PP2A-phosphatase methylesterase
complexes (PP2A(i)) in presence of ATP and Mg(2+) (By similarity).
Reversibly stimulates the variable phosphotyrosyl phosphatase
activity of PP2A core heterodimer PP2A(D) in presence of ATP and
Mg(2+) (in vitro). The phosphotyrosyl phosphatase activity is
dependent of an ATPase activity of the PP2A(D):PPP2R4 complex. Is
involved in apoptosis; the function appears to be independent from
PP2A. {ECO:0000250, ECO:0000269|PubMed:16916641,
ECO:0000269|PubMed:17333320}.
-!- CATALYTIC ACTIVITY:
Reaction=[protein]-peptidylproline (omega=180) = [protein]-
peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
ChEBI:CHEBI:83834; EC=5.2.1.8;
-!- SUBUNIT: Associates with PP2A heterodimeric core enzyme PP2A(D),
composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa
constant regulatory subunit (PR65 or subunit A) (PubMed:16916641).
Interacts with PPP2CB (By similarity).
{ECO:0000250|UniProtKB:P58389, ECO:0000269|PubMed:16916641}.
-!- INTERACTION:
Q4VCS5-2:AMOT; NbExp=3; IntAct=EBI-1774121, EBI-3891843;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17333320}.
Nucleus {ECO:0000269|PubMed:17333320}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=2; Synonyms=Beta;
IsoId=Q15257-1; Sequence=Displayed;
Name=1; Synonyms=Alpha;
IsoId=Q15257-2; Sequence=VSP_005123;
Name=3; Synonyms=Delta;
IsoId=Q15257-3; Sequence=VSP_005122;
Name=4; Synonyms=Epsilon;
IsoId=Q15257-4; Sequence=VSP_005124;
-!- TISSUE SPECIFICITY: Widely expressed.
-!- SIMILARITY: Belongs to the PTPA-type PPIase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PPP2R4ID41817ch9q34.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X73478; CAA51873.1; -; mRNA.
EMBL; X86428; CAA60163.1; -; Genomic_DNA.
EMBL; X86429; CAA60163.1; JOINED; Genomic_DNA.
EMBL; X86430; CAA60163.1; JOINED; Genomic_DNA.
EMBL; X86432; CAA60163.1; JOINED; Genomic_DNA.
EMBL; X86434; CAA60163.1; JOINED; Genomic_DNA.
EMBL; X86435; CAA60163.1; JOINED; Genomic_DNA.
EMBL; X86436; CAA60163.1; JOINED; Genomic_DNA.
EMBL; X86437; CAA60163.1; JOINED; Genomic_DNA.
EMBL; X86438; CAA60163.1; JOINED; Genomic_DNA.
EMBL; X86439; CAA60163.1; JOINED; Genomic_DNA.
EMBL; X86428; CAB77601.1; -; Genomic_DNA.
EMBL; X86429; CAB77601.1; JOINED; Genomic_DNA.
EMBL; X86430; CAB77601.1; JOINED; Genomic_DNA.
EMBL; X86431; CAB77601.1; JOINED; Genomic_DNA.
EMBL; X86432; CAB77601.1; JOINED; Genomic_DNA.
EMBL; X86434; CAB77601.1; JOINED; Genomic_DNA.
EMBL; X86435; CAB77601.1; JOINED; Genomic_DNA.
EMBL; X86436; CAB77601.1; JOINED; Genomic_DNA.
EMBL; X86437; CAB77601.1; JOINED; Genomic_DNA.
EMBL; X86438; CAB77601.1; JOINED; Genomic_DNA.
EMBL; X86439; CAB77601.1; JOINED; Genomic_DNA.
EMBL; X86428; CAB77602.1; -; Genomic_DNA.
EMBL; X86429; CAB77602.1; JOINED; Genomic_DNA.
EMBL; X86432; CAB77602.1; JOINED; Genomic_DNA.
EMBL; X86434; CAB77602.1; JOINED; Genomic_DNA.
EMBL; X86435; CAB77602.1; JOINED; Genomic_DNA.
EMBL; X86436; CAB77602.1; JOINED; Genomic_DNA.
EMBL; X86437; CAB77602.1; JOINED; Genomic_DNA.
EMBL; X86438; CAB77602.1; JOINED; Genomic_DNA.
EMBL; X86439; CAB77602.1; JOINED; Genomic_DNA.
EMBL; X86428; CAB77603.1; -; Genomic_DNA.
EMBL; X86429; CAB77603.1; JOINED; Genomic_DNA.
EMBL; X86430; CAB77603.1; JOINED; Genomic_DNA.
EMBL; X86434; CAB77603.1; JOINED; Genomic_DNA.
EMBL; X86435; CAB77603.1; JOINED; Genomic_DNA.
EMBL; X86436; CAB77603.1; JOINED; Genomic_DNA.
EMBL; X86437; CAB77603.1; JOINED; Genomic_DNA.
EMBL; X86438; CAB77603.1; JOINED; Genomic_DNA.
EMBL; X86439; CAB77603.1; JOINED; Genomic_DNA.
EMBL; AK302043; BAG63436.1; -; mRNA.
EMBL; BT020119; AAV38922.1; -; mRNA.
EMBL; AK222788; BAD96508.1; -; mRNA.
EMBL; AL158151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471090; EAW87876.1; -; Genomic_DNA.
EMBL; CH471090; EAW87882.1; -; Genomic_DNA.
EMBL; BC002545; AAH02545.1; -; mRNA.
EMBL; BC011605; AAH11605.1; -; mRNA.
CCDS; CCDS65156.1; -. [Q15257-3]
CCDS; CCDS6920.1; -. [Q15257-2]
PIR; A54021; A54021.
RefSeq; NP_001180326.1; NM_001193397.1.
RefSeq; NP_001258761.1; NM_001271832.1. [Q15257-3]
RefSeq; NP_066954.2; NM_021131.4. [Q15257-2]
RefSeq; NP_821067.1; NM_178000.2. [Q15257-2]
RefSeq; NP_821068.1; NM_178001.2. [Q15257-1]
RefSeq; NP_821070.1; NM_178003.2. [Q15257-4]
UniGene; Hs.400740; -.
PDB; 2G62; X-ray; 1.60 A; A=22-358.
PDB; 2HV6; X-ray; 1.90 A; A/B=1-358.
PDB; 2HV7; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-358.
PDB; 2IXM; X-ray; 1.50 A; A=20-357.
PDB; 4LAC; X-ray; 2.82 A; B=19-358.
PDB; 4NY3; X-ray; 1.80 A; A/B=22-358.
PDBsum; 2G62; -.
PDBsum; 2HV6; -.
PDBsum; 2HV7; -.
PDBsum; 2IXM; -.
PDBsum; 4LAC; -.
PDBsum; 4NY3; -.
ProteinModelPortal; Q15257; -.
SMR; Q15257; -.
BioGrid; 111516; 67.
IntAct; Q15257; 18.
BindingDB; Q15257; -.
ChEMBL; CHEMBL2505; -.
iPTMnet; Q15257; -.
PhosphoSitePlus; Q15257; -.
SwissPalm; Q15257; -.
BioMuta; PPP2R4; -.
DMDM; 116242737; -.
OGP; Q15257; -.
EPD; Q15257; -.
MaxQB; Q15257; -.
PeptideAtlas; Q15257; -.
PRIDE; Q15257; -.
ProteomicsDB; 60499; -.
ProteomicsDB; 60500; -. [Q15257-2]
ProteomicsDB; 60501; -. [Q15257-3]
ProteomicsDB; 60502; -. [Q15257-4]
DNASU; 5524; -.
Ensembl; ENST00000337738; ENSP00000337448; ENSG00000119383. [Q15257-1]
Ensembl; ENST00000355007; ENSP00000347109; ENSG00000119383. [Q15257-4]
Ensembl; ENST00000357197; ENSP00000349726; ENSG00000119383. [Q15257-3]
Ensembl; ENST00000358994; ENSP00000351885; ENSG00000119383. [Q15257-2]
Ensembl; ENST00000393370; ENSP00000377036; ENSG00000119383. [Q15257-2]
GeneID; 5524; -.
KEGG; hsa:5524; -.
UCSC; uc004bxl.3; human. [Q15257-1]
CTD; 5524; -.
DisGeNET; 5524; -.
EuPathDB; HostDB:ENSG00000119383.19; -.
GeneCards; PTPA; -.
HGNC; HGNC:9308; PTPA.
HPA; CAB022068; -.
HPA; CAB035999; -.
HPA; HPA005695; -.
MIM; 600756; gene.
neXtProt; NX_Q15257; -.
OpenTargets; ENSG00000119383; -.
PharmGKB; PA33671; -.
GeneTree; ENSGT00390000011500; -.
HOVERGEN; HBG019168; -.
InParanoid; Q15257; -.
KO; K17605; -.
OMA; TGWGDCC; -.
OrthoDB; EOG091G0ITS; -.
PhylomeDB; Q15257; -.
TreeFam; TF105555; -.
SIGNOR; Q15257; -.
ChiTaRS; PTPA; human.
EvolutionaryTrace; Q15257; -.
GeneWiki; PPP2R4; -.
GenomeRNAi; 5524; -.
PRO; PR:Q15257; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000119383; Expressed in 235 organ(s), highest expression level in endometrium epithelium.
CleanEx; HS_PPP2R4; -.
ExpressionAtlas; Q15257; baseline and differential.
Genevisible; Q15257; HS.
GO; GO:0034704; C:calcium channel complex; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IDA:HGNC.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; TAS:HGNC.
GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC.
GO; GO:0051721; F:protein phosphatase 2A binding; IDA:HGNC.
GO; GO:0019888; F:protein phosphatase regulator activity; IDA:HGNC.
GO; GO:0008160; F:protein tyrosine phosphatase activator activity; IDA:HGNC.
GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IDA:HGNC.
GO; GO:0035308; P:negative regulation of protein dephosphorylation; IDA:HGNC.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:HGNC.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; IDA:HGNC.
GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IDA:HGNC.
CDD; cd04087; PTPA; 1.
InterPro; IPR004327; Phstyr_phstse_ac.
InterPro; IPR037218; PTPA_sf.
PANTHER; PTHR10012; PTHR10012; 1.
Pfam; PF03095; PTPA; 1.
PIRSF; PIRSF016325; Phstyr_phstse_ac; 1.
SUPFAM; SSF140984; SSF140984; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Complete proteome; Cytoplasm; Direct protein sequencing; Isomerase;
Nucleotide-binding; Nucleus; Polymorphism; Reference proteome;
Rotamase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 358 Serine/threonine-protein phosphatase 2A
activator.
/FTId=PRO_0000071524.
NP_BIND 183 189 ATP.
NP_BIND 240 242 ATP.
NP_BIND 342 343 ATP.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
VAR_SEQ 45 108 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_005122.
VAR_SEQ 73 149 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_005124.
VAR_SEQ 73 107 Missing (in isoform 1).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8195217,
ECO:0000303|Ref.5, ECO:0000303|Ref.6}.
/FTId=VSP_005123.
VARIANT 28 28 K -> R (in dbSNP:rs17481693).
/FTId=VAR_028101.
VARIANT 208 208 R -> Q (in dbSNP:rs4836639).
/FTId=VAR_028102.
VARIANT 357 357 S -> L (in dbSNP:rs2480452).
{ECO:0000269|Ref.6}.
/FTId=VAR_028103.
MUTAGEN 185 185 D->A: Impairs ATPase activity of the
PP2A(D):PPP2R4 complex; no effect on
interaction with the PP2A(D) complex.
{ECO:0000269|PubMed:16916641}.
MUTAGEN 239 239 A->D: Impairs ATPase activity of the
PP2A(D):PPP2R4 complex; no effect on
interaction with the PP2A(D) complex.
{ECO:0000269|PubMed:16916641}.
MUTAGEN 240 240 G->D: Impairs ATPase activity of the
PP2A(D):PPP2R4 complex; no effect on
interaction with the PP2A(D) complex.
{ECO:0000269|PubMed:16916641}.
MUTAGEN 244 244 V->D: Impairs interaction with the
PP2A(D) complex.
{ECO:0000269|PubMed:16916641}.
MUTAGEN 305 305 E->A: Abolishes interaction with the
PP2A(D) complex.
{ECO:0000269|PubMed:16916641}.
MUTAGEN 316 316 V->D: Impairs interaction with the
PP2A(D) complex.
MUTAGEN 325 325 G->D: Abolishes interaction with the
PP2A(D) complex.
{ECO:0000269|PubMed:16916641}.
MUTAGEN 329 329 M->D: Abolishes interaction with the
PP2A(D) complex.
{ECO:0000269|PubMed:16916641}.
MUTAGEN 337 337 K->G: Impairs interaction with the
PP2A(D) complex.
{ECO:0000269|PubMed:16916641}.
CONFLICT 113 113 V -> L (in Ref. 1; CAA51873, 2; CAA60163
and 3; CAB77601/CAB77602). {ECO:0000305}.
CONFLICT 297 297 Missing (in Ref. 2; CAA60163 and 3;
CAB77601/CAB77602/CAB77603).
{ECO:0000305}.
CONFLICT 357 357 S -> V (in Ref. 1; AA sequence).
{ECO:0000305}.
HELIX 34 40 {ECO:0000244|PDB:2IXM}.
HELIX 43 58 {ECO:0000244|PDB:2IXM}.
TURN 59 61 {ECO:0000244|PDB:2IXM}.
HELIX 108 124 {ECO:0000244|PDB:2IXM}.
STRAND 134 136 {ECO:0000244|PDB:2IXM}.
HELIX 139 156 {ECO:0000244|PDB:2IXM}.
HELIX 161 166 {ECO:0000244|PDB:2IXM}.
HELIX 167 175 {ECO:0000244|PDB:2IXM}.
TURN 181 184 {ECO:0000244|PDB:2IXM}.
HELIX 188 203 {ECO:0000244|PDB:2IXM}.
HELIX 209 211 {ECO:0000244|PDB:2IXM}.
HELIX 212 217 {ECO:0000244|PDB:2IXM}.
HELIX 219 233 {ECO:0000244|PDB:2IXM}.
STRAND 237 240 {ECO:0000244|PDB:2IXM}.
HELIX 243 245 {ECO:0000244|PDB:2IXM}.
STRAND 247 250 {ECO:0000244|PDB:2IXM}.
HELIX 253 261 {ECO:0000244|PDB:2IXM}.
TURN 262 264 {ECO:0000244|PDB:2IXM}.
HELIX 270 274 {ECO:0000244|PDB:2IXM}.
HELIX 276 282 {ECO:0000244|PDB:2IXM}.
HELIX 283 285 {ECO:0000244|PDB:2IXM}.
HELIX 287 298 {ECO:0000244|PDB:2IXM}.
HELIX 303 306 {ECO:0000244|PDB:2IXM}.
HELIX 308 313 {ECO:0000244|PDB:2IXM}.
HELIX 319 333 {ECO:0000244|PDB:2IXM}.
TURN 334 336 {ECO:0000244|PDB:2IXM}.
HELIX 338 341 {ECO:0000244|PDB:2IXM}.
STRAND 348 350 {ECO:0000244|PDB:2IXM}.
STRAND 352 354 {ECO:0000244|PDB:2IXM}.
SEQUENCE 358 AA; 40668 MW; 2A962521AF5B4CF7 CRC64;
MAEGERQPPP DSSEEAPPAT QNFIIPKKEI HTVPDMGKWK RSQAYADYIG FILTLNEGVK
GKKLTFEYRV SEMWNEVHEE KEQAAKQSVS CDECIPLPRA GHCAPSEAIE KLVALLNTLD
RWIDETPPVD QPSRFGNKAY RTWYAKLDEE AENLVATVVP THLAAAVPEV AVYLKESVGN
STRIDYGTGH EAAFAAFLCC LCKIGVLRVD DQIAIVFKVF NRYLEVMRKL QKTYRMEPAG
SQGVWGLDDF QFLPFIWGSS QLIDHPYLEP RHFVDEKAVN ENHKDYMFLE CILFITEMKT
GPFAEHSNQL WNISAVPSWS KVNQGLIRMY KAECLEKFPV IQHFKFGSLL PIHPVTSG


Related products :

Catalog number Product name Quantity
EIAAB33066 Bos taurus,Bovine,Phosphotyrosyl phosphatase activator,PP2A, subunit B', PR53 isoform,PPP2R4,PTPA,Serine_threonine-protein phosphatase 2A activator,Serine_threonine-protein phosphatase 2A regulatory s
EIAAB33064 Homo sapiens,Human,Phosphotyrosyl phosphatase activator,PP2A, subunit B', PR53 isoform,PPP2R4,PTPA,PTPA,Serine_threonine-protein phosphatase 2A activator,Serine_threonine-protein phosphatase 2A regula
EIAAB33065 Oryctolagus cuniculus,Phosphotyrosyl phosphatase activator,PP2A, subunit B', PR53 isoform,PPP2R4,PTPA,PTPA,Rabbit,Serine_threonine-protein phosphatase 2A activator,Serine_threonine-protein phosphatase
EIAAB33063 Mouse,Mus musculus,Phosphotyrosyl phosphatase activator,PP2A, subunit B', PR53 isoform,Ppp2r4,PTPA,Ptpa,Serine_threonine-protein phosphatase 2A activator,Serine_threonine-protein phosphatase 2A regula
2ABA_RAT Rat ELISA Kit FOR Serine per threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform 96T
E1056r Pig ELISA Kit FOR Serine per threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform 96T
E14916h Mouse ELISA Kit FOR Serine per threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform 96T
2A5D_RABIT Rabbit ELISA Kit FOR Serine per threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform 96T
2ABB_HUMAN Human ELISA Kit FOR Serine per threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform 96T
E14891b Mouse ELISA Kit FOR Serine per threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform 96T
E14498r Human ELISA Kit FOR Serine per threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform 96T
H0421 Serine threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform (PPP2R2B), Pig, ELISA Kit 96T
H0427 Serine threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform (PPP2R2D), Rat, ELISA Kit 96T
H0435 Serine threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (PPP2R1A), Pig, ELISA Kit 96T
H0415 Serine threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform (PPP2R2A), Pig, ELISA Kit 96T
E13952b Mouse ELISA Kit FOR Serine per threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform 96T
E1436r Rabbit ELISA Kit FOR Serine per threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform 96T
2ABD_MOUSE Mouse ELISA Kit FOR Serine per threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform 96T
H0417 Serine threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform (PPP2R2A), Rat, ELISA Kit 96T
E1416h Human ELISA Kit FOR Serine per threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform 96T
H0423 Serine threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform (PPP2R2B), Rat, ELISA Kit 96T
E2016b Bovine ELISA Kit FOR Serine per threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform 96T
H0439 Serine threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform (PPP2R1B), Rat, ELISA Kit 96T
H0438 Serine threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform (PPP2R1B), Pig, ELISA Kit 96T
H0431 Serine threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform (PPP2R2C), Rat, ELISA Kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur