PTPA_HUMAN
ID PTPA_HUMAN Reviewed; 358 AA.
AC Q15257; A2A347; A9IZU4; B4DXM4; Q15258; Q53GZ3; Q5TZQ2; Q9BUK1; Q9NNZ7;
AC Q9NNZ8; Q9NNZ9;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Serine/threonine-protein phosphatase 2A activator;
DE EC=5.2.1.8;
DE AltName: Full=PP2A, subunit B', PR53 isoform;
DE AltName: Full=Phosphotyrosyl phosphatase activator;
DE Short=PTPA;
DE AltName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit 4;
DE AltName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit B';
GN Name=PTPA {ECO:0000312|HGNC:HGNC:9308}; Synonyms=PPP2R4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Heart;
RX PubMed=8195217; DOI=10.1016/s0021-9258(17)40733-2;
RA Cayla X., Van Hoof C., Bosch M., Waelkens E., Peeters B., Merlevede W.,
RA Goris J.;
RT "Molecular cloning, expression, and characterization of PTPA, a protein
RT that activates the tyrosyl phosphatase activity of protein phosphatase
RT 2A.";
RL J. Biol. Chem. 269:15668-15675(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC TISSUE=Blood;
RX PubMed=8530035; DOI=10.1006/geno.1995.1140;
RA Van Hoof C., Aly M., Garcia A., Cayla X., Cassiman J.-J., Merlevede W.,
RA Goris J.;
RT "Structure and chromosomal localization of the human gene of the
RT phosphotyrosyl phosphatase activator (PTPA) of protein phosphatase 2A.";
RL Genomics 28:261-272(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2; 3 AND 4).
RX PubMed=10880964; DOI=10.1046/j.1432-1327.2000.01486.x;
RA Janssens V., van Hoof C., Martens E., de Baere I., Merlevede W., Goris J.;
RT "Identification and characterization of alternative splice products encoded
RT by the human phosphotyrosyl phosphatase activator gene.";
RL Eur. J. Biochem. 267:4406-4413(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-357.
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP FUNCTION IN APOPTOSIS, AND SUBCELLULAR LOCATION.
RX PubMed=17333320; DOI=10.1007/s10495-006-0050-8;
RA Azam S., Drobetsky E., Ramotar D.;
RT "Overexpression of the cis/trans isomerase PTPA triggers caspase 3-
RT dependent apoptosis.";
RL Apoptosis 12:1243-1255(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 22-358.
RX PubMed=16782712; DOI=10.1074/jbc.c600100200;
RA Magnusdottir A., Stenmark P., Flodin S., Nyman T., Hammarstroem M., Ehn M.,
RA Bakali H M.A., Berglund H., Nordlund P.;
RT "The crystal structure of a human PP2A phosphatase activator reveals a
RT novel fold and highly conserved cleft implicated in protein-protein
RT interactions.";
RL J. Biol. Chem. 281:22434-22438(2006).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 20-357.
RX PubMed=16885030; DOI=10.1016/j.molcel.2006.07.008;
RA Leulliot N., Vicentini G., Jordens J., Quevillon-Cheruel S., Schiltz M.,
RA Barford D., van Tilbeurgh H., Goris J.;
RT "Crystal structure of the PP2A phosphatase activator: implications for its
RT PP2A-specific PPIase activity.";
RL Mol. Cell 23:413-424(2006).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), FUNCTION IN MODULATION OF PP2A
RP SUBSTRATE SPECIFICITY, ATP-BINDING, MUTAGENESIS OF ASP-185; ALA-239;
RP GLY-240; VAL-244; GLU-305; GLY-325; MET-329 AND LYS-337, AND INTERACTION
RP WITH THE PP2A(D) COMPLEX.
RX PubMed=16916641; DOI=10.1016/j.molcel.2006.07.027;
RA Chao Y., Xing Y., Chen Y., Xu Y., Lin Z., Li Z., Jeffrey P.D., Stock J.B.,
RA Shi Y.;
RT "Structure and mechanism of the phosphotyrosyl phosphatase activator.";
RL Mol. Cell 23:535-546(2006).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. Acts as a regulatory subunit for serine/threonine-
CC protein phosphatase 2A (PP2A) modulating its activity or substrate
CC specificity, probably by inducing a conformational change in the
CC catalytic subunit, a proposed direct target of the PPIase. Can
CC reactivate inactive phosphatase PP2A-phosphatase methylesterase
CC complexes (PP2A(i)) in presence of ATP and Mg(2+) (By similarity).
CC Reversibly stimulates the variable phosphotyrosyl phosphatase activity
CC of PP2A core heterodimer PP2A(D) in presence of ATP and Mg(2+) (in
CC vitro). The phosphotyrosyl phosphatase activity is dependent of an
CC ATPase activity of the PP2A(D):PPP2R4 complex. Is involved in
CC apoptosis; the function appears to be independent from PP2A.
CC {ECO:0000250, ECO:0000269|PubMed:16916641,
CC ECO:0000269|PubMed:17333320}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- SUBUNIT: Associates with PP2A heterodimeric core enzyme PP2A(D),
CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa
CC constant regulatory subunit (PR65 or subunit A) (PubMed:16916641).
CC Interacts with PPP2CB (By similarity). {ECO:0000250|UniProtKB:P58389,
CC ECO:0000269|PubMed:16916641}.
CC -!- INTERACTION:
CC Q15257; Q4VCS5-2: AMOT; NbExp=3; IntAct=EBI-1774121, EBI-3891843;
CC Q15257-2; Q5JTZ9: AARS2; NbExp=3; IntAct=EBI-12164121, EBI-308736;
CC Q15257-2; A2BDD9: AMOT; NbExp=3; IntAct=EBI-12164121, EBI-17286414;
CC Q15257-2; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-12164121, EBI-11977221;
CC Q15257-2; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-12164121, EBI-740897;
CC Q15257-2; P30153: PPP2R1A; NbExp=3; IntAct=EBI-12164121, EBI-302388;
CC Q15257-2; Q9NZD8: SPG21; NbExp=5; IntAct=EBI-12164121, EBI-742688;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17333320}. Nucleus
CC {ECO:0000269|PubMed:17333320}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=2; Synonyms=Beta;
CC IsoId=Q15257-1; Sequence=Displayed;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q15257-2; Sequence=VSP_005123;
CC Name=3; Synonyms=Delta;
CC IsoId=Q15257-3; Sequence=VSP_005122;
CC Name=4; Synonyms=Epsilon;
CC IsoId=Q15257-4; Sequence=VSP_005124;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the PTPA-type PPIase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PPP2R4ID41817ch9q34.html";
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DR EMBL; X73478; CAA51873.1; -; mRNA.
DR EMBL; X86428; CAA60163.1; -; Genomic_DNA.
DR EMBL; X86429; CAA60163.1; JOINED; Genomic_DNA.
DR EMBL; X86430; CAA60163.1; JOINED; Genomic_DNA.
DR EMBL; X86432; CAA60163.1; JOINED; Genomic_DNA.
DR EMBL; X86434; CAA60163.1; JOINED; Genomic_DNA.
DR EMBL; X86435; CAA60163.1; JOINED; Genomic_DNA.
DR EMBL; X86436; CAA60163.1; JOINED; Genomic_DNA.
DR EMBL; X86437; CAA60163.1; JOINED; Genomic_DNA.
DR EMBL; X86438; CAA60163.1; JOINED; Genomic_DNA.
DR EMBL; X86439; CAA60163.1; JOINED; Genomic_DNA.
DR EMBL; X86428; CAB77601.1; -; Genomic_DNA.
DR EMBL; X86429; CAB77601.1; JOINED; Genomic_DNA.
DR EMBL; X86430; CAB77601.1; JOINED; Genomic_DNA.
DR EMBL; X86431; CAB77601.1; JOINED; Genomic_DNA.
DR EMBL; X86432; CAB77601.1; JOINED; Genomic_DNA.
DR EMBL; X86434; CAB77601.1; JOINED; Genomic_DNA.
DR EMBL; X86435; CAB77601.1; JOINED; Genomic_DNA.
DR EMBL; X86436; CAB77601.1; JOINED; Genomic_DNA.
DR EMBL; X86437; CAB77601.1; JOINED; Genomic_DNA.
DR EMBL; X86438; CAB77601.1; JOINED; Genomic_DNA.
DR EMBL; X86439; CAB77601.1; JOINED; Genomic_DNA.
DR EMBL; X86428; CAB77602.1; -; Genomic_DNA.
DR EMBL; X86429; CAB77602.1; JOINED; Genomic_DNA.
DR EMBL; X86432; CAB77602.1; JOINED; Genomic_DNA.
DR EMBL; X86434; CAB77602.1; JOINED; Genomic_DNA.
DR EMBL; X86435; CAB77602.1; JOINED; Genomic_DNA.
DR EMBL; X86436; CAB77602.1; JOINED; Genomic_DNA.
DR EMBL; X86437; CAB77602.1; JOINED; Genomic_DNA.
DR EMBL; X86438; CAB77602.1; JOINED; Genomic_DNA.
DR EMBL; X86439; CAB77602.1; JOINED; Genomic_DNA.
DR EMBL; X86428; CAB77603.1; -; Genomic_DNA.
DR EMBL; X86429; CAB77603.1; JOINED; Genomic_DNA.
DR EMBL; X86430; CAB77603.1; JOINED; Genomic_DNA.
DR EMBL; X86434; CAB77603.1; JOINED; Genomic_DNA.
DR EMBL; X86435; CAB77603.1; JOINED; Genomic_DNA.
DR EMBL; X86436; CAB77603.1; JOINED; Genomic_DNA.
DR EMBL; X86437; CAB77603.1; JOINED; Genomic_DNA.
DR EMBL; X86438; CAB77603.1; JOINED; Genomic_DNA.
DR EMBL; X86439; CAB77603.1; JOINED; Genomic_DNA.
DR EMBL; AK302043; BAG63436.1; -; mRNA.
DR EMBL; BT020119; AAV38922.1; -; mRNA.
DR EMBL; AK222788; BAD96508.1; -; mRNA.
DR EMBL; AL158151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87876.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87882.1; -; Genomic_DNA.
DR EMBL; BC002545; AAH02545.1; -; mRNA.
DR EMBL; BC011605; AAH11605.1; -; mRNA.
DR CCDS; CCDS65156.1; -. [Q15257-3]
DR CCDS; CCDS6920.1; -. [Q15257-2]
DR PIR; A54021; A54021.
DR RefSeq; NP_001180326.1; NM_001193397.1.
DR RefSeq; NP_001258761.1; NM_001271832.1. [Q15257-3]
DR RefSeq; NP_066954.2; NM_021131.4. [Q15257-2]
DR RefSeq; NP_821067.1; NM_178000.2. [Q15257-2]
DR RefSeq; NP_821068.1; NM_178001.2. [Q15257-1]
DR RefSeq; NP_821070.1; NM_178003.2. [Q15257-4]
DR PDB; 2G62; X-ray; 1.60 A; A=22-358.
DR PDB; 2HV6; X-ray; 1.90 A; A/B=1-358.
DR PDB; 2HV7; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-358.
DR PDB; 2IXM; X-ray; 1.50 A; A=20-357.
DR PDB; 4LAC; X-ray; 2.82 A; B=19-358.
DR PDB; 4NY3; X-ray; 1.80 A; A/B=22-358.
DR PDBsum; 2G62; -.
DR PDBsum; 2HV6; -.
DR PDBsum; 2HV7; -.
DR PDBsum; 2IXM; -.
DR PDBsum; 4LAC; -.
DR PDBsum; 4NY3; -.
DR AlphaFoldDB; Q15257; -.
DR SMR; Q15257; -.
DR BioGRID; 111516; 95.
DR IntAct; Q15257; 23.
DR MINT; Q15257; -.
DR STRING; 9606.ENSP00000377036; -.
DR BindingDB; Q15257; -.
DR ChEMBL; CHEMBL2505; -.
DR GlyGen; Q15257; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15257; -.
DR MetOSite; Q15257; -.
DR PhosphoSitePlus; Q15257; -.
DR SwissPalm; Q15257; -.
DR BioMuta; PTPA; -.
DR DMDM; 116242737; -.
DR OGP; Q15257; -.
DR CPTAC; CPTAC-259; -.
DR CPTAC; CPTAC-260; -.
DR EPD; Q15257; -.
DR jPOST; Q15257; -.
DR MassIVE; Q15257; -.
DR MaxQB; Q15257; -.
DR PeptideAtlas; Q15257; -.
DR PRIDE; Q15257; -.
DR ProteomicsDB; 60499; -. [Q15257-1]
DR ProteomicsDB; 60500; -. [Q15257-2]
DR ProteomicsDB; 60501; -. [Q15257-3]
DR ProteomicsDB; 60502; -. [Q15257-4]
DR Antibodypedia; 1074; 377 antibodies from 40 providers.
DR CPTC; Q15257; 4 antibodies.
DR DNASU; 5524; -.
DR Ensembl; ENST00000337738.6; ENSP00000337448.1; ENSG00000119383.21. [Q15257-1]
DR Ensembl; ENST00000355007.7; ENSP00000347109.3; ENSG00000119383.21. [Q15257-4]
DR Ensembl; ENST00000357197.8; ENSP00000349726.4; ENSG00000119383.21. [Q15257-3]
DR Ensembl; ENST00000393370.7; ENSP00000377036.2; ENSG00000119383.21. [Q15257-2]
DR GeneID; 5524; -.
DR KEGG; hsa:5524; -.
DR MANE-Select; ENST00000393370.7; ENSP00000377036.2; NM_178000.3; NP_821067.1. [Q15257-2]
DR UCSC; uc004bxl.3; human. [Q15257-1]
DR CTD; 5524; -.
DR DisGeNET; 5524; -.
DR GeneCards; PTPA; -.
DR HGNC; HGNC:9308; PTPA.
DR HPA; ENSG00000119383; Low tissue specificity.
DR MIM; 600756; gene.
DR neXtProt; NX_Q15257; -.
DR OpenTargets; ENSG00000119383; -.
DR PharmGKB; PA33671; -.
DR VEuPathDB; HostDB:ENSG00000119383; -.
DR eggNOG; KOG2867; Eukaryota.
DR GeneTree; ENSGT00390000011500; -.
DR InParanoid; Q15257; -.
DR OMA; YMFLGCI; -.
DR OrthoDB; 1165705at2759; -.
DR PhylomeDB; Q15257; -.
DR TreeFam; TF105555; -.
DR PathwayCommons; Q15257; -.
DR SignaLink; Q15257; -.
DR SIGNOR; Q15257; -.
DR BioGRID-ORCS; 5524; 544 hits in 1103 CRISPR screens.
DR ChiTaRS; PTPA; human.
DR EvolutionaryTrace; Q15257; -.
DR GeneWiki; PPP2R4; -.
DR GenomeRNAi; 5524; -.
DR Pharos; Q15257; Tchem.
DR PRO; PR:Q15257; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q15257; protein.
DR Bgee; ENSG00000119383; Expressed in endometrium epithelium and 208 other tissues.
DR ExpressionAtlas; Q15257; baseline and differential.
DR Genevisible; Q15257; HS.
DR GO; GO:1904949; C:ATPase complex; IDA:HGNC-UCL.
DR GO; GO:0034704; C:calcium channel complex; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IDA:HGNC-UCL.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC-UCL.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IDA:HGNC-UCL.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IDA:HGNC-UCL.
DR GO; GO:0008160; F:protein tyrosine phosphatase activator activity; IDA:HGNC-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IDA:HGNC-UCL.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; IDA:HGNC-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:HGNC-UCL.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IDA:HGNC-UCL.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IDA:HGNC-UCL.
DR CDD; cd04087; PTPA; 1.
DR Gene3D; 1.20.120.1150; -; 1.
DR InterPro; IPR004327; Phstyr_phstse_ac.
DR InterPro; IPR043170; PTPA_C_lid.
DR InterPro; IPR037218; PTPA_sf.
DR PANTHER; PTHR10012; PTHR10012; 1.
DR Pfam; PF03095; PTPA; 1.
DR PIRSF; PIRSF016325; Phstyr_phstse_ac; 1.
DR SUPFAM; SSF140984; SSF140984; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Isomerase; Nucleotide-binding; Nucleus;
KW Reference proteome; Rotamase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..358
FT /note="Serine/threonine-protein phosphatase 2A activator"
FT /id="PRO_0000071524"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 183..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 240..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 342..343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VAR_SEQ 45..108
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_005122"
FT VAR_SEQ 73..149
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_005124"
FT VAR_SEQ 73..107
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8195217, ECO:0000303|Ref.5,
FT ECO:0000303|Ref.6"
FT /id="VSP_005123"
FT VARIANT 28
FT /note="K -> R (in dbSNP:rs17481693)"
FT /id="VAR_028101"
FT VARIANT 208
FT /note="R -> Q (in dbSNP:rs4836639)"
FT /id="VAR_028102"
FT VARIANT 357
FT /note="S -> L (in dbSNP:rs2480452)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_028103"
FT MUTAGEN 185
FT /note="D->A: Impairs ATPase activity of the PP2A(D):PPP2R4
FT complex; no effect on interaction with the PP2A(D)
FT complex."
FT /evidence="ECO:0000269|PubMed:16916641"
FT MUTAGEN 239
FT /note="A->D: Impairs ATPase activity of the PP2A(D):PPP2R4
FT complex; no effect on interaction with the PP2A(D)
FT complex."
FT /evidence="ECO:0000269|PubMed:16916641"
FT MUTAGEN 240
FT /note="G->D: Impairs ATPase activity of the PP2A(D):PPP2R4
FT complex; no effect on interaction with the PP2A(D)
FT complex."
FT /evidence="ECO:0000269|PubMed:16916641"
FT MUTAGEN 244
FT /note="V->D: Impairs interaction with the PP2A(D) complex."
FT /evidence="ECO:0000269|PubMed:16916641"
FT MUTAGEN 305
FT /note="E->A: Abolishes interaction with the PP2A(D)
FT complex."
FT /evidence="ECO:0000269|PubMed:16916641"
FT MUTAGEN 316
FT /note="V->D: Impairs interaction with the PP2A(D) complex."
FT MUTAGEN 325
FT /note="G->D: Abolishes interaction with the PP2A(D)
FT complex."
FT /evidence="ECO:0000269|PubMed:16916641"
FT MUTAGEN 329
FT /note="M->D: Abolishes interaction with the PP2A(D)
FT complex."
FT /evidence="ECO:0000269|PubMed:16916641"
FT MUTAGEN 337
FT /note="K->G: Impairs interaction with the PP2A(D) complex."
FT /evidence="ECO:0000269|PubMed:16916641"
FT CONFLICT 113
FT /note="V -> L (in Ref. 1; CAA51873, 2; CAA60163 and 3;
FT CAB77601/CAB77602)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="Missing (in Ref. 2; CAA60163 and 3; CAB77601/
FT CAB77602/CAB77603)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="S -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:2IXM"
FT HELIX 43..58
FT /evidence="ECO:0007829|PDB:2IXM"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:2IXM"
FT HELIX 108..124
FT /evidence="ECO:0007829|PDB:2IXM"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2IXM"
FT HELIX 139..156
FT /evidence="ECO:0007829|PDB:2IXM"
FT HELIX 161..166
FT /evidence="ECO:0007829|PDB:2IXM"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:2IXM"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:2IXM"
FT HELIX 188..203
FT /evidence="ECO:0007829|PDB:2IXM"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:2IXM"
FT HELIX 212..217
FT /evidence="ECO:0007829|PDB:2IXM"
FT HELIX 219..233
FT /evidence="ECO:0007829|PDB:2IXM"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:2IXM"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:2IXM"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:2IXM"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:2IXM"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:2IXM"
FT HELIX 270..274
FT /evidence="ECO:0007829|PDB:2IXM"
FT HELIX 276..282
FT /evidence="ECO:0007829|PDB:2IXM"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:2IXM"
FT HELIX 287..298
FT /evidence="ECO:0007829|PDB:2IXM"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:2IXM"
FT HELIX 308..313
FT /evidence="ECO:0007829|PDB:2IXM"
FT HELIX 319..333
FT /evidence="ECO:0007829|PDB:2IXM"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:2IXM"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:2IXM"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:2IXM"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:2IXM"
SQ 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
