PTPA | OmnibusX

Name	Number of supported studies	Average coverage
endothelial cell	7 studies	23% ± 7%	Explore
glutamatergic neuron	6 studies	31% ± 17%	Explore
epithelial cell	6 studies	31% ± 12%	Explore
neuron	4 studies	27% ± 6%	Explore
fibroblast	4 studies	21% ± 8%	Explore
myofibroblast cell	4 studies	20% ± 3%	Explore
ciliated cell	4 studies	26% ± 9%	Explore
abnormal cell	4 studies	28% ± 12%	Explore
oligodendrocyte precursor cell	4 studies	24% ± 4%	Explore
astrocyte	3 studies	23% ± 3%	Explore
GABAergic neuron	3 studies	34% ± 10%	Explore
dendritic cell	3 studies	26% ± 1%	Explore
goblet cell	3 studies	19% ± 3%	Explore

II. Expression across tissues

Name	Number of supported studies	Average coverage
brain	6 studies	25% ± 7%	Explore
liver	3 studies	18% ± 2%	Explore

Tissue	GTEx Coverage	GTEx Average TPM	GTEx Number of samples	TCGA Coverage	TCGA Average TPM	TCGA Number of samples
esophagus	100%	9171.98	1445 / 1445	100%	54.49	183 / 183
ovary	100%	5238.02	180 / 180	100%	65.13	430 / 430
thymus	100%	7668.09	653 / 653	100%	106.49	605 / 605
uterus	100%	7738.44	170 / 170	100%	97.01	459 / 459
brain	100%	10812.43	2641 / 2642	100%	103.77	705 / 705
kidney	100%	9402.79	89 / 89	100%	104.70	899 / 901
prostate	100%	11544.05	245 / 245	100%	165.24	500 / 502
skin	100%	6980.10	1805 / 1809	100%	111.71	471 / 472
adrenal gland	100%	10769.03	258 / 258	100%	87.80	229 / 230
breast	100%	5251.45	459 / 459	100%	134.23	1113 / 1118
pancreas	99%	3844.44	326 / 328	100%	94.36	178 / 178
stomach	100%	6138.72	359 / 359	99%	64.36	284 / 286
intestine	100%	7584.26	966 / 966	99%	79.15	522 / 527
lung	100%	6765.47	576 / 578	99%	73.87	1146 / 1155
liver	100%	7255.88	226 / 226	99%	58.20	401 / 406
bladder	100%	6633.38	21 / 21	99%	84.79	497 / 504
eye	0%	0	0 / 0	100%	115.75	80 / 80
lymph node	0%	0	0 / 0	100%	93.71	29 / 29
spleen	100%	7582.43	241 / 241	0%	0	0 / 0
tonsil	0%	0	0 / 0	100%	91.64	45 / 45
ureter	0%	0	0 / 0	100%	84.96	1 / 1
muscle	100%	6792.12	802 / 803	0%	0	0 / 0
adipose	100%	4239.35	1201 / 1204	0%	0	0 / 0
heart	100%	8001.63	858 / 861	0%	0	0 / 0
blood vessel	100%	5726.94	1330 / 1335	0%	0	0 / 0
peripheral blood	89%	3705.38	829 / 929	0%	0	0 / 0
abdomen	0%	0	0 / 0	0%	0	0 / 0
bone marrow	0%	0	0 / 0	0%	0	0 / 0
diaphragm	0%	0	0 / 0	0%	0	0 / 0
gingiva	0%	0	0 / 0	0%	0	0 / 0
nasal cavity	0%	0	0 / 0	0%	0	0 / 0
nasopharynx	0%	0	0 / 0	0%	0	0 / 0
nose	0%	0	0 / 0	0%	0	0 / 0
placenta	0%	0	0 / 0	0%	0	0 / 0
spinal column	0%	0	0 / 0	0%	0	0 / 0

III. Associated gene sets

GO_0032515	Biological process	negative regulation of phosphoprotein phosphatase activity
GO_0007052	Biological process	mitotic spindle organization
GO_0032516	Biological process	positive regulation of phosphoprotein phosphatase activity
GO_0043065	Biological process	positive regulation of apoptotic process
GO_0035308	Biological process	negative regulation of protein dephosphorylation
GO_0035307	Biological process	positive regulation of protein dephosphorylation
GO_0043666	Biological process	regulation of phosphoprotein phosphatase activity
GO_0070062	Cellular component	extracellular exosome
GO_0005634	Cellular component	nucleus
GO_0005654	Cellular component	nucleoplasm
GO_0034704	Cellular component	calcium channel complex
GO_0005737	Cellular component	cytoplasm
GO_1904949	Cellular component	ATPase complex
GO_0000159	Cellular component	protein phosphatase type 2A complex
GO_0042803	Molecular function	protein homodimerization activity
GO_0051721	Molecular function	protein phosphatase 2A binding
GO_0004721	Molecular function	phosphoprotein phosphatase activity
GO_0003755	Molecular function	peptidyl-prolyl cis-trans isomerase activity
GO_0005102	Molecular function	signaling receptor binding
GO_0008160	Molecular function	protein tyrosine phosphatase activator activity
GO_0046872	Molecular function	metal ion binding
GO_0005524	Molecular function	ATP binding
GO_0019888	Molecular function	protein phosphatase regulator activity
GO_0005515	Molecular function	protein binding

IV. Literature review

[source]

Gene name	PTPA
Protein name	Serine/threonine-protein phosphatase 2A activator (EC 5.2.1.8) (Phosphotyrosyl phosphatase activator) 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')
Synonyms	hCG_30599 PPP2R4 DKFZp781M17165
Description	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. . FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. . FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. . FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. . FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. . FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. . FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. . FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. . FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. . FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. . FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. . FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. . FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. . FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. . FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. . FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. .
Accessions	Q68CR8 ENST00000414510.5 ENST00000411917.1 A6PVN6 ENST00000435132.5 ENST00000434095.2 B4DDQ6 ENST00000455240.1 H0Y6E5 B7ZBP7 ENST00000435305.1 F6WIT2 B7ZBP9 ENST00000432651.5 ENST00000423100.5 ENST00000432124.5 ENST00000436883.5 C9IZ76 ENST00000357197.8 [Q15257-3] A6PVN5 ENST00000337738.6 [Q15257-1] A0A804CD06 ENST00000419582.5 ENST00000393370.7 [Q15257-2] ENST00000452489.6 A6PVN7 H0Y562 Q5T949 ENST00000440346.1 ENST00000355007.7 [Q15257-4] ENST00000347048.8 ENST00000414331.5 ENST00000348141.9 ENST00000455292.6 A6PVN8 ENST00000453358.5 ENST00000417504.5 Q15257 ENST00000358994.9 B7ZBQ0

PTPA report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

IV. Literature review