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P58389 (PTPA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length323 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+. 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 By similarity. Ref.3

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) By similarity. Interacts with PPP2CB. Ref.3

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the PTPA-type PPIase family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionIsomerase
Rotamase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmitotic spindle organization in nucleus

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of phosphoprotein phosphatase activity

Inferred from sequence or structural similarity. Source: HGNC

negative regulation of protein dephosphorylation

Inferred from sequence or structural similarity. Source: HGNC

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphoprotein phosphatase activity

Inferred from sequence or structural similarity. Source: HGNC

positive regulation of protein dephosphorylation

Inferred from sequence or structural similarity. 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 sequence or structural similarity. Source: HGNC

   Cellular_componentcalcium channel complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleus

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein phosphatase type 2A complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: HGNC

ATPase activity

Inferred from electronic annotation. Source: Ensembl

peptidyl-prolyl cis-trans isomerase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein homodimerization activity

Inferred from sequence or structural similarity. Source: HGNC

protein phosphatase 2A binding

Inferred from sequence or structural similarity. Source: HGNC

protein phosphatase type 2A regulator activity

Inferred from sequence or structural similarity. Source: HGNC

protein tyrosine phosphatase activator activity

Inferred from sequence or structural similarity. Source: HGNC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 323322Serine/threonine-protein phosphatase 2A activator
PRO_0000071525

Regions

Nucleotide binding148 – 1547ATP By similarity
Nucleotide binding205 – 2073ATP By similarity
Nucleotide binding307 – 3082ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Experimental info

Sequence conflict101Missing in AAK62028. Ref.1
Sequence conflict1961Q → L in AAK62028. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P58389 [UniParc].

Last modified November 16, 2001. Version 1.
Checksum: 1C7FA6C357A35F24

FASTA32336,710
        10         20         30         40         50         60 
MAEGERQPPP DSSEETPPTT QNFIIPKKEI HTVPDMGKWK RSQAYADYIG FILTLNEGVK 

        70         80         90        100        110        120 
GKKLTFDYKV SEAIEKLVAL LDTLDRWIDE TPPVDQPSRF GNKAYRTWYA KLDQEAENLV 

       130        140        150        160        170        180 
ATVVPTHLAA AVPEVAVYLK EAVGNSTRID YGTGHEAAFA AFLCCLCKIG VLRVDDQVAI 

       190        200        210        220        230        240 
VFKVFDRYLE VMRKLQKTYR MEPAGSQGVW GLDDFQFLPF IWGSSQLIDH PHLEPRHFVD 

       250        260        270        280        290        300 
EKAVSENHKD YMFLQCILFI TEMKTGPFAE HSNQLWNISA VPSWSKVNQG LIRMYKAECL 

       310        320 
EKFPVIQHFK FGSLLPIHPV TSG 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the mouse homolog of the human phosphotyrosyl phosphatase activator, PTPA."
David J., Yang X., Hashimoto K., Ramotar D.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Brain.
[2]"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].
Strain: C3H/He and FVB/N.
Tissue: Mammary gland and Osteoblast.
[3]"A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo."
Fellner T., Lackner D.H., Hombauer H., Piribauer P., Mudrak I., Zaragoza K., Juno C., Ogris E.
Genes Dev. 17:2138-2150(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PPP2CB.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY035997 mRNA. Translation: AAK62028.1.
BC006626 mRNA. Translation: AAH06626.1.
BC052852 mRNA. Translation: AAH52852.1.
CCDSCCDS15883.1.
RefSeqNP_620087.3. NM_138748.5.
UniGeneMm.275393.

3D structure databases

ProteinModelPortalP58389.
SMRP58389. Positions 23-322.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid225960. 1 interaction.

PTM databases

PhosphoSiteP58389.

Proteomic databases

MaxQBP58389.
PaxDbP58389.
PRIDEP58389.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000042055; ENSMUSP00000046837; ENSMUSG00000039515.
GeneID110854.
KEGGmmu:110854.
UCSCuc008jcn.2. mouse.

Organism-specific databases

CTD5524.
MGIMGI:1346006. Ppp2r4.

Phylogenomic databases

eggNOGCOG5057.
HOGENOMHOG000205736.
HOVERGENHBG019168.
InParanoidP58389.
KOK17605.
OMAGSHGVWS.
OrthoDBEOG7KQ21W.
PhylomeDBP58389.
TreeFamTF105555.

Gene expression databases

ArrayExpressP58389.
BgeeP58389.
GenevestigatorP58389.

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

NextBio364789.
PROP58389.
SOURCESearch...

Entry information

Entry namePTPA_MOUSE
AccessionPrimary (citable) accession number: P58389
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 16, 2001
Last modified: July 9, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot