Q15257 (PTPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase 2A activator
EC=5.2.1.8

Alternative name(s):
PP2A, subunit B', PR53 isoform
Phosphotyrosyl phosphatase activator
Short name=PTPA
Serine/threonine-protein phosphatase 2A regulatory subunit 4
Serine/threonine-protein phosphatase 2A regulatory subunit B'

Gene names

Name:	PPP2R4
Synonyms:	PTPA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	358 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 Mg2+ By similarity. Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence of ATP and Mg2+ (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. Ref.10 Ref.15
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subunit structure	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). Interacts with PPP2CB By similarity. Ref.15
Subcellular location	Cytoplasm. Nucleus Ref.10.
Tissue specificity	Widely expressed.
Sequence similarities	Belongs to the PTPA-type PPIase family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Isomerase Rotamase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from direct assay Ref.15. Source: GOC mitotic spindle organization in nucleus Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of phosphoprotein phosphatase activity Inferred from direct assay Ref.15. Source: HGNC negative regulation of protein dephosphorylation Inferred from direct assay Ref.15. Source: HGNC positive regulation of apoptotic process Inferred from direct assay Ref.10. Source: UniProtKB positive regulation of phosphoprotein phosphatase activity Inferred from direct assay Ref.15. Source: HGNC positive regulation of protein dephosphorylation Inferred from direct assay Ref.15. Source: HGNC protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	calcium channel complex Inferred from direct assay PubMed 10830164. Source: BHF-UCL cytoplasm Inferred from direct assay Ref.10. Source: UniProtKB nucleus Inferred from direct assay Ref.10. Source: UniProtKB protein phosphatase type 2A complex Traceable author statement PubMed 10318862. Source: HGNC
Molecular_function	ATP binding Inferred from direct assay Ref.15. Source: HGNC peptidyl-prolyl cis-trans isomerase activity Inferred from Biological aspect of Ancestor. Source: RefGenome protein heterodimerization activity Traceable author statement PubMed 10318862. Source: HGNC protein homodimerization activity Inferred from direct assay Ref.15. Source: HGNC protein phosphatase 2A binding Inferred from direct assay Ref.15. Source: HGNC protein phosphatase type 2A regulator activity Inferred from direct assay Ref.15. Source: HGNC protein tyrosine phosphatase activator activity Inferred from direct assay Ref.15. Source: HGNC
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 2 (identifier: Q15257-1)

Also known as: Beta;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 1 (identifier: Q15257-2)

Also known as: Alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     73-107: Missing.

Isoform 3 (identifier: Q15257-3)

Also known as: Delta;

The sequence of this isoform differs from the canonical sequence as follows:
     45-108: Missing.

Isoform 4 (identifier: Q15257-4)

Also known as: Epsilon;

The sequence of this isoform differs from the canonical sequence as follows:
     73-149: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 358

358

Serine/threonine-protein phosphatase 2A activator

PRO_0000071524

Regions

Nucleotide binding

183 – 189

7

ATP

Nucleotide binding

240 – 242

3

ATP

Nucleotide binding

342 – 343

2

ATP

Natural variations

Alternative sequence

45 – 108

64

Missing in isoform 3.

VSP_005122

Alternative sequence

73 – 149

77

Missing in isoform 4.

VSP_005124

Alternative sequence

73 – 107

35

Missing in isoform 1.

VSP_005123

Natural variant

28

1

K → R.
Corresponds to variant rs17481693 [ dbSNP | Ensembl ].

VAR_028101

Natural variant

208

1

R → Q.
Corresponds to variant rs4836639 [ dbSNP | Ensembl ].

VAR_028102

Natural variant

357

1

S → L. Ref.6
Corresponds to variant rs2480452 [ dbSNP | Ensembl ].

VAR_028103

Experimental info

Mutagenesis

185

1

D → A: Impairs ATPase activity of the PP2A(D):PPP2R4 complex; no effect on interaction with the PP2A(D) complex. Ref.15

Mutagenesis

239

1

A → D: Impairs ATPase activity of the PP2A(D):PPP2R4 complex; no effect on interaction with the PP2A(D) complex. Ref.15

Mutagenesis

240

1

G → D: Impairs ATPase activity of the PP2A(D):PPP2R4 complex; no effect on interaction with the PP2A(D) complex. Ref.15

Mutagenesis

244

1

V → D: Impairs interaction with the PP2A(D) complex. Ref.15

Mutagenesis

305

1

E → A: Abolishes interaction with the PP2A(D) complex. Ref.15

Mutagenesis

316

1

V → D: Impairs interaction with the PP2A(D) complex.

Mutagenesis

325

1

G → D: Abolishes interaction with the PP2A(D) complex. Ref.15

Mutagenesis

329

1

M → D: Abolishes interaction with the PP2A(D) complex. Ref.15

Mutagenesis

337

1

K → G: Impairs interaction with the PP2A(D) complex. Ref.15

Sequence conflict

113

1

V → L in CAA51873. Ref.1

Sequence conflict

113

1

V → L in CAA60163. Ref.2

Sequence conflict

113

1

V → L in CAB77601. Ref.3

Sequence conflict

113

1

V → L in CAB77602. Ref.3

Sequence conflict

297

1

Missing in CAA60163. Ref.2

Sequence conflict

297

1

Missing in CAB77601. Ref.3

Sequence conflict

297

1

Missing in CAB77602. Ref.3

Sequence conflict

297

1

Missing in CAB77603. Ref.3

Sequence conflict

357

1

S → V AA sequence Ref.1

Secondary structure

1

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358

Helix Strand Turn

Details...

Helix

34 – 40

7

Helix

43 – 58

16

Turn

59 – 61

3

Helix

107 – 124

18

Beta strand

134 – 136

3

Helix

139 – 156

18

Helix

161 – 166

6

Helix

167 – 175

9

Turn

181 – 184

4

Helix

188 – 203

16

Helix

209 – 211

3

Helix

212 – 217

6

Helix

219 – 233

15

Beta strand

237 – 240

4

Helix

243 – 245

3

Beta strand

247 – 250

4

Helix

253 – 261

9

Turn

262 – 264

3

Helix

270 – 274

5

Helix

276 – 282

7

Helix

283 – 285

3

Helix

287 – 298

12

Helix

303 – 306

4

Helix

308 – 313

6

Helix

319 – 333

15

Turn

334 – 336

3

Helix

338 – 341

4

Beta strand

348 – 350

3

Beta strand

352 – 354

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 (Beta) [UniParc]. Last modified October 17, 2006. Version 3. Checksum: 2A962521AF5B4CF7	FASTA	358	40,668
	10 20 30 40 50 60 MAEGERQPPP DSSEEAPPAT QNFIIPKKEI HTVPDMGKWK RSQAYADYIG FILTLNEGVK 70 80 90 100 110 120 GKKLTFEYRV SEMWNEVHEE KEQAAKQSVS CDECIPLPRA GHCAPSEAIE KLVALLNTLD 130 140 150 160 170 180 RWIDETPPVD QPSRFGNKAY RTWYAKLDEE AENLVATVVP THLAAAVPEV AVYLKESVGN 190 200 210 220 230 240 STRIDYGTGH EAAFAAFLCC LCKIGVLRVD DQIAIVFKVF NRYLEVMRKL QKTYRMEPAG 250 260 270 280 290 300 SQGVWGLDDF QFLPFIWGSS QLIDHPYLEP RHFVDEKAVN ENHKDYMFLE CILFITEMKT 310 320 330 340 350 GPFAEHSNQL WNISAVPSWS KVNQGLIRMY KAECLEKFPV IQHFKFGSLL PIHPVTSG
	Isoform 1 (Alpha) [UniParc]. Checksum: EA0D7B96FB88CC01	FASTA	323	36,775
	10 20 30 40 50 60 MAEGERQPPP DSSEEAPPAT QNFIIPKKEI HTVPDMGKWK RSQAYADYIG FILTLNEGVK 70 80 90 100 110 120 GKKLTFEYRV SEAIEKLVAL LNTLDRWIDE TPPVDQPSRF GNKAYRTWYA KLDEEAENLV 130 140 150 160 170 180 ATVVPTHLAA AVPEVAVYLK ESVGNSTRID YGTGHEAAFA AFLCCLCKIG VLRVDDQIAI 190 200 210 220 230 240 VFKVFNRYLE VMRKLQKTYR MEPAGSQGVW GLDDFQFLPF IWGSSQLIDH PYLEPRHFVD 250 260 270 280 290 300 EKAVNENHKD YMFLECILFI TEMKTGPFAE HSNQLWNISA VPSWSKVNQG LIRMYKAECL 310 320 EKFPVIQHFK FGSLLPIHPV TSG
	Isoform 3 (Delta) [UniParc]. Checksum: 12C8B0D3D96A490B	FASTA	294	33,467
	10 20 30 40 50 60 MAEGERQPPP DSSEEAPPAT QNFIIPKKEI HTVPDMGKWK RSQAIEKLVA LLNTLDRWID 70 80 90 100 110 120 ETPPVDQPSR FGNKAYRTWY AKLDEEAENL VATVVPTHLA AAVPEVAVYL KESVGNSTRI 130 140 150 160 170 180 DYGTGHEAAF AAFLCCLCKI GVLRVDDQIA IVFKVFNRYL EVMRKLQKTY RMEPAGSQGV 190 200 210 220 230 240 WGLDDFQFLP FIWGSSQLID HPYLEPRHFV DEKAVNENHK DYMFLECILF ITEMKTGPFA 250 260 270 280 290 EHSNQLWNIS AVPSWSKVNQ GLIRMYKAEC LEKFPVIQHF KFGSLLPIHP VTSG
	Isoform 4 (Epsilon) [UniParc]. Checksum: 9C554DF39A3436B1	FASTA	281	31,859
	10 20 30 40 50 60 MAEGERQPPP DSSEEAPPAT QNFIIPKKEI HTVPDMGKWK RSQAYADYIG FILTLNEGVK 70 80 90 100 110 120 GKKLTFEYRV SEEAENLVAT VVPTHLAAAV PEVAVYLKES VGNSTRIDYG TGHEAAFAAF 130 140 150 160 170 180 LCCLCKIGVL RVDDQIAIVF KVFNRYLEVM RKLQKTYRME PAGSQGVWGL DDFQFLPFIW 190 200 210 220 230 240 GSSQLIDHPY LEPRHFVDEK AVNENHKDYM FLECILFITE MKTGPFAEHS NQLWNISAVP 250 260 270 280 SWSKVNQGLI RMYKAECLEK FPVIQHFKFG SLLPIHPVTS G

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, expression, and characterization of PTPA, a protein that activates the tyrosyl phosphatase activity of protein phosphatase 2A." Cayla X., Van Hoof C., Bosch M., Waelkens E., Peeters B., Merlevede W., Goris J. J. Biol. Chem. 269:15668-15675(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE. Tissue: Heart.
[2]	"Structure and chromosomal localization of the human gene of the phosphotyrosyl phosphatase activator (PTPA) of protein phosphatase 2A." Van Hoof C., Aly M., Garcia A., Cayla X., Cassiman J.-J., Merlevede W., Goris J. Genomics 28:261-272(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). Tissue: Blood.
[3]	"Identification and characterization of alternative splice products encoded by the human phosphotyrosyl phosphatase activator gene." Janssens V., van Hoof C., Martens E., de Baere I., Merlevede W., Goris J. Eur. J. Biochem. 267:4406-4413(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2; 3 AND 4).
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Testis.
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-357. Tissue: Liver.
[7]	"DNA sequence and analysis of human chromosome 9." 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. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Placenta.
[10]	"Overexpression of the cis/trans isomerase PTPA triggers caspase 3-dependent apoptosis." Azam S., Drobetsky E., Ramotar D. Apoptosis 12:1243-1255(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN APOPTOSIS, SUBCELLULAR LOCATION.
[11]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"The crystal structure of a human PP2A phosphatase activator reveals a novel fold and highly conserved cleft implicated in protein-protein interactions." Magnusdottir A., Stenmark P., Flodin S., Nyman T., Hammarstroem M., Ehn M., Bakali H M.A., Berglund H., Nordlund P. J. Biol. Chem. 281:22434-22438(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 22-358.
[14]	"Crystal structure of the PP2A phosphatase activator: implications for its PP2A-specific PPIase activity." Leulliot N., Vicentini G., Jordens J., Quevillon-Cheruel S., Schiltz M., Barford D., van Tilbeurgh H., Goris J. Mol. Cell 23:413-424(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 20-357.
[15]	"Structure and mechanism of the phosphotyrosyl phosphatase activator." Chao Y., Xing Y., Chen Y., Xu Y., Lin Z., Li Z., Jeffrey P.D., Stock J.B., Shi Y. Mol. Cell 23:535-546(2006) [PubMed] [Europe PMC] [Abstract] Cited for: 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, INTERACTION WITH THE PP2A(D) COMPLEX.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X73478 mRNA. Translation: CAA51873.1.
X86428 , X86429, X86430, X86432, X86434, X86435, X86436, X86437, X86438, X86439 Genomic DNA. Translation: CAA60163.1.
X86428 , X86429, X86430, X86431, X86432, X86434, X86435, X86436, X86437, X86438, X86439 Genomic DNA. Translation: CAB77601.1.
X86428 , X86429, X86432, X86434, X86435, X86436, X86437, X86438, X86439 Genomic DNA. Translation: CAB77602.1.
X86428 , X86429, X86430, X86434, X86435, X86436, X86437, X86438, X86439 Genomic DNA. Translation: CAB77603.1.
AK302043 mRNA. Translation: BAG63436.1.
BT020119 mRNA. Translation: AAV38922.1.
AK222788 mRNA. Translation: BAD96508.1.
AL158151 Genomic DNA. Translation: CAM14695.1.
AL158151 Genomic DNA. Translation: CAP58847.2.
CH471090 Genomic DNA. Translation: EAW87876.1.
CH471090 Genomic DNA. Translation: EAW87882.1.
BC002545 mRNA. Translation: AAH02545.1.
BC011605 mRNA. Translation: AAH11605.1.

IPI

IPI00217296.
IPI00217297.
IPI00293102.
IPI00893197.

PIR

A54021.

RefSeq

NP_001180326.1. NM_001193397.1.
NP_001258761.1. NM_001271832.1.
NP_066954.2. NM_021131.4.
NP_821067.1. NM_178000.2.
NP_821068.1. NM_178001.2.
NP_821070.1. NM_178003.2.

UniGene

Hs.400740.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2G62	X-ray	1.60	A	22-358	[»]
2HV6	X-ray	1.90	A/B	1-358	[»]
2HV7	X-ray	2.50	A/B/C/D/E/F/G/H	1-358	[»]
2IXM	X-ray	1.50	A	20-357	[»]

ProteinModelPortal

Q15257.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15257. 9 interactions.

MINT

MINT-3031079.

PTM databases

PhosphoSite

Q15257.

Polymorphism databases

DMDM

116242737.

2D gel databases

OGP

Q15257.

Proteomic databases

PaxDb

Q15257.

PRIDE

Q15257.

Protocols and materials databases

DNASU

5524.

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000337738; ENSP00000337448; ENSG00000119383.
ENST00000355007; ENSP00000347109; ENSG00000119383.
ENST00000357197; ENSP00000349726; ENSG00000119383.
ENST00000358994; ENSP00000351885; ENSG00000119383.
ENST00000393370; ENSP00000377036; ENSG00000119383.

GeneID

5524.

KEGG

hsa:5524.

UCSC

uc004bxl.2. human.
uc004bxm.2. human.
uc004bxo.2. human.
uc011mbp.2. human.

Organism-specific databases

CTD

5524.

GeneCards

GC09P131873.

HGNC

HGNC:9308. PPP2R4.

HPA

CAB022068.
CAB035999.
HPA005695.

MIM

600756. gene.

neXtProt

NX_Q15257.

PharmGKB

PA33671.

GenAtlas

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Phylogenomic databases

eggNOG

COG5057.

HOVERGEN

HBG019168.

PhylomeDB

Q15257.

Gene expression databases

ArrayExpress

Q15257.

Bgee

Q15257.

CleanEx

HS_PPP2R4.

Genevestigator

Q15257.

GermOnline

ENSG00000119383. Homo sapiens.

Family and domain databases

InterPro

IPR004327. Phstyr_phstse_ac.
[Graphical view]

PANTHER

PTHR10012. PTHR10012. 1 hit.

Pfam

PF03095. PTPA. 1 hit.
[Graphical view]

PIRSF

PIRSF016325. Phstyr_phstse_ac. 1 hit.

ProtoNet

Search...

Other

BindingDB

Q15257.

ChEMBL

CHEMBL2505.

ChiTaRS

PPP2R4. human.

EvolutionaryTrace

Q15257.

GenomeRNAi

5524.

NextBio

21382.

SOURCE

Search...

Entry information

Entry name

PTPA_HUMAN

Accession

Primary (citable) accession number: Q15257
Secondary accession number(s): A2A347 , A9IZU4, B4DXM4, Q15258, Q53GZ3, Q5TZQ2, Q9BUK1, Q9NNZ7, Q9NNZ8, Q9NNZ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2001
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 116 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.