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Q15257 (PTPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.16

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.16

Subcellular location

Cytoplasm. Nucleus Ref.10.

Tissue specificity

Widely expressed.

Sequence similarities

Belongs to the PTPA-type PPIase family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionIsomerase
Rotamase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.16. 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.16. Source: HGNC

negative regulation of protein dephosphorylation

Inferred from direct assay Ref.16. 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.16. Source: HGNC

positive regulation of protein dephosphorylation

Inferred from direct assay Ref.16. Source: HGNC

protein folding

Inferred from electronic annotation. Source: UniProtKB-KW

protein peptidyl-prolyl isomerization

Inferred from Biological aspect of Ancestor. Source: GOC

regulation of phosphoprotein phosphatase activity

Inferred from direct assay Ref.16. Source: HGNC

   Cellular_componentcalcium 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_functionATP binding

Inferred from direct assay Ref.16. 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.16. Source: HGNC

protein phosphatase 2A binding

Inferred from direct assay Ref.16. Source: HGNC

protein phosphatase type 2A regulator activity

Inferred from direct assay Ref.16. Source: HGNC

protein tyrosine phosphatase activator activity

Inferred from direct assay Ref.16. Source: HGNC

receptor binding

Inferred from physical interaction PubMed 10830164. Source: BHF-UCL

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 358357Serine/threonine-protein phosphatase 2A activator
PRO_0000071524

Regions

Nucleotide binding183 – 1897ATP
Nucleotide binding240 – 2423ATP
Nucleotide binding342 – 3432ATP

Amino acid modifications

Modified residue21N-acetylalanine Ref.11

Natural variations

Alternative sequence45 – 10864Missing in isoform 3.
VSP_005122
Alternative sequence73 – 14977Missing in isoform 4.
VSP_005124
Alternative sequence73 – 10735Missing in isoform 1.
VSP_005123
Natural variant281K → R.
Corresponds to variant rs17481693 [ dbSNP | Ensembl ].
VAR_028101
Natural variant2081R → Q.
Corresponds to variant rs4836639 [ dbSNP | Ensembl ].
VAR_028102
Natural variant3571S → L. Ref.6
Corresponds to variant rs2480452 [ dbSNP | Ensembl ].
VAR_028103

Experimental info

Mutagenesis1851D → A: Impairs ATPase activity of the PP2A(D):PPP2R4 complex; no effect on interaction with the PP2A(D) complex. Ref.16
Mutagenesis2391A → D: Impairs ATPase activity of the PP2A(D):PPP2R4 complex; no effect on interaction with the PP2A(D) complex. Ref.16
Mutagenesis2401G → D: Impairs ATPase activity of the PP2A(D):PPP2R4 complex; no effect on interaction with the PP2A(D) complex. Ref.16
Mutagenesis2441V → D: Impairs interaction with the PP2A(D) complex. Ref.16
Mutagenesis3051E → A: Abolishes interaction with the PP2A(D) complex. Ref.16
Mutagenesis3161V → D: Impairs interaction with the PP2A(D) complex.
Mutagenesis3251G → D: Abolishes interaction with the PP2A(D) complex. Ref.16
Mutagenesis3291M → D: Abolishes interaction with the PP2A(D) complex. Ref.16
Mutagenesis3371K → G: Impairs interaction with the PP2A(D) complex. Ref.16
Sequence conflict1131V → L in CAA51873. Ref.1
Sequence conflict1131V → L in CAA60163. Ref.2
Sequence conflict1131V → L in CAB77601. Ref.3
Sequence conflict1131V → L in CAB77602. Ref.3
Sequence conflict2971Missing in CAA60163. Ref.2
Sequence conflict2971Missing in CAB77601. Ref.3
Sequence conflict2971Missing in CAB77602. Ref.3
Sequence conflict2971Missing in CAB77603. Ref.3
Sequence conflict3571S → V AA sequence Ref.1

Secondary structure

..................................................... 358
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (Beta) [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 2A962521AF5B4CF7

FASTA35840,668
        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 

« Hide

Isoform 1 (Alpha) [UniParc].

Checksum: EA0D7B96FB88CC01
Show »

FASTA32336,775
Isoform 3 (Delta) [UniParc].

Checksum: 12C8B0D3D96A490B
Show »

FASTA29433,467
Isoform 4 (Epsilon) [UniParc].

Checksum: 9C554DF39A3436B1
Show »

FASTA28131,859

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[12]"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].
[13]"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].
[14]"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.
[15]"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.
[16]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X73478 mRNA. Translation: CAA51873.1.
X86428 expand/collapse EMBL AC list , X86429, X86430, X86432, X86434, X86435, X86436, X86437, X86438, X86439 Genomic DNA. Translation: CAA60163.1.
X86428 expand/collapse EMBL AC list , X86429, X86430, X86431, X86432, X86434, X86435, X86436, X86437, X86438, X86439 Genomic DNA. Translation: CAB77601.1.
X86428 expand/collapse EMBL AC list , X86429, X86432, X86434, X86435, X86436, X86437, X86438, X86439 Genomic DNA. Translation: CAB77602.1.
X86428 expand/collapse EMBL AC list , 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.
PIRA54021.
RefSeqNP_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.
UniGeneHs.400740.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2G62X-ray1.60A22-358[»]
2HV6X-ray1.90A/B1-358[»]
2HV7X-ray2.50A/B/C/D/E/F/G/H1-358[»]
2IXMX-ray1.50A20-357[»]
4LACX-ray2.82B19-358[»]
ProteinModelPortalQ15257.
SMRQ15257. Positions 23-357.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111516. 54 interactions.
IntActQ15257. 10 interactions.
MINTMINT-3031079.

Chemistry

BindingDBQ15257.
ChEMBLCHEMBL2505.

PTM databases

PhosphoSiteQ15257.

Polymorphism databases

DMDM116242737.

2D gel databases

OGPQ15257.

Proteomic databases

PaxDbQ15257.
PRIDEQ15257.

Protocols and materials databases

DNASU5524.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337738; ENSP00000337448; ENSG00000119383. [Q15257-1]
ENST00000355007; ENSP00000347109; ENSG00000119383. [Q15257-4]
ENST00000357197; ENSP00000349726; ENSG00000119383. [Q15257-3]
ENST00000358994; ENSP00000351885; ENSG00000119383. [Q15257-2]
ENST00000393370; ENSP00000377036; ENSG00000119383. [Q15257-2]
GeneID5524.
KEGGhsa:5524.
UCSCuc004bxl.2. human. [Q15257-2]
uc004bxm.2. human. [Q15257-1]
uc004bxo.2. human. [Q15257-4]
uc011mbp.2. human. [Q15257-3]

Organism-specific databases

CTD5524.
GeneCardsGC09P131873.
HGNCHGNC:9308. PPP2R4.
HPACAB022068.
CAB035999.
HPA005695.
MIM600756. gene.
neXtProtNX_Q15257.
PharmGKBPA33671.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5057.
HOVERGENHBG019168.
KOK17605.
OrthoDBEOG7KQ21W.
PhylomeDBQ15257.
TreeFamTF105555.

Gene expression databases

ArrayExpressQ15257.
BgeeQ15257.
CleanExHS_PPP2R4.
GenevestigatorQ15257.

Family and domain databases

InterProIPR004327. Phstyr_phstse_ac.
[Graphical view]
PANTHERPTHR10012. PTHR10012. 1 hit.
PfamPF03095. PTPA. 1 hit.
[Graphical view]
PIRSFPIRSF016325. Phstyr_phstse_ac. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPPP2R4. human.
EvolutionaryTraceQ15257.
GeneWikiPPP2R4.
GenomeRNAi5524.
NextBio21382.
PROQ15257.
SOURCESearch...

Entry information

Entry namePTPA_HUMAN
AccessionPrimary (citable) accession number: Q15257
Secondary accession number(s): A2A347 expand/collapse secondary AC list , 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: April 16, 2014
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM