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P58389

- PTPA_MOUSE

UniProt

P58389 - PTPA_MOUSE

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Protein

Serine/threonine-protein phosphatase 2A activator

Gene

Ppp2r4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi148 – 1547ATPBy similarity
Nucleotide bindingi205 – 2073ATPBy similarity
Nucleotide bindingi307 – 3082ATPBy similarity

GO - Molecular functioni

  1. ATPase activity Source: Ensembl
  2. ATP binding Source: HGNC
  3. peptidyl-prolyl cis-trans isomerase activity Source: RefGenome
  4. protein homodimerization activity Source: HGNC
  5. protein phosphatase 2A binding Source: HGNC
  6. protein phosphatase type 2A regulator activity Source: HGNC
  7. protein tyrosine phosphatase activator activity Source: HGNC

GO - Biological processi

  1. mitotic spindle organization in nucleus Source: RefGenome
  2. negative regulation of phosphoprotein phosphatase activity Source: HGNC
  3. negative regulation of protein dephosphorylation Source: HGNC
  4. positive regulation of apoptotic process Source: Ensembl
  5. positive regulation of phosphoprotein phosphatase activity Source: HGNC
  6. positive regulation of protein dephosphorylation Source: HGNC
  7. protein folding Source: UniProtKB-KW
  8. protein peptidyl-prolyl isomerization Source: GOC
  9. regulation of phosphoprotein phosphatase activity Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:Ppp2r4
Synonyms:Ptpa
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1346006. Ppp2r4.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. calcium channel complex Source: Ensembl
  2. cytoplasm Source: RefGenome
  3. extracellular vesicular exosome Source: Ensembl
  4. nucleus Source: RefGenome
  5. protein phosphatase type 2A complex Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 323322Serine/threonine-protein phosphatase 2A activatorPRO_0000071525Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP58389.
PaxDbiP58389.
PRIDEiP58389.

PTM databases

PhosphoSiteiP58389.

Expressioni

Gene expression databases

BgeeiP58389.
ExpressionAtlasiP58389. baseline and differential.
GenevestigatoriP58389.

Interactioni

Subunit structurei

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.By similarity1 Publication

Protein-protein interaction databases

BioGridi225960. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP58389.
SMRiP58389. Positions 23-322.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PTPA-type PPIase family.Curated

Phylogenomic databases

eggNOGiCOG5057.
HOGENOMiHOG000205736.
HOVERGENiHBG019168.
InParanoidiP58389.
KOiK17605.
OMAiGSHGVWS.
OrthoDBiEOG7KQ21W.
PhylomeDBiP58389.
TreeFamiTF105555.

Family and domain databases

InterProiIPR004327. Phstyr_phstse_ac.
[Graphical view]
PANTHERiPTHR10012. PTHR10012. 1 hit.
PfamiPF03095. PTPA. 1 hit.
[Graphical view]
PIRSFiPIRSF016325. Phstyr_phstse_ac. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P58389-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEGERQPPP DSSEETPPTT QNFIIPKKEI HTVPDMGKWK RSQAYADYIG
60 70 80 90 100
FILTLNEGVK GKKLTFDYKV SEAIEKLVAL LDTLDRWIDE TPPVDQPSRF
110 120 130 140 150
GNKAYRTWYA KLDQEAENLV ATVVPTHLAA AVPEVAVYLK EAVGNSTRID
160 170 180 190 200
YGTGHEAAFA AFLCCLCKIG VLRVDDQVAI VFKVFDRYLE VMRKLQKTYR
210 220 230 240 250
MEPAGSQGVW GLDDFQFLPF IWGSSQLIDH PHLEPRHFVD EKAVSENHKD
260 270 280 290 300
YMFLQCILFI TEMKTGPFAE HSNQLWNISA VPSWSKVNQG LIRMYKAECL
310 320
EKFPVIQHFK FGSLLPIHPV TSG
Length:323
Mass (Da):36,710
Last modified:November 16, 2001 - v1
Checksum:i1C7FA6C357A35F24
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101Missing in AAK62028. 1 PublicationCurated
Sequence conflicti196 – 1961Q → L in AAK62028. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY035997 mRNA. Translation: AAK62028.1.
BC006626 mRNA. Translation: AAH06626.1.
BC052852 mRNA. Translation: AAH52852.1.
CCDSiCCDS15883.1.
RefSeqiNP_620087.3. NM_138748.5.
UniGeneiMm.275393.

Genome annotation databases

EnsembliENSMUST00000042055; ENSMUSP00000046837; ENSMUSG00000039515.
GeneIDi110854.
KEGGimmu:110854.
UCSCiuc008jcn.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY035997 mRNA. Translation: AAK62028.1 .
BC006626 mRNA. Translation: AAH06626.1 .
BC052852 mRNA. Translation: AAH52852.1 .
CCDSi CCDS15883.1.
RefSeqi NP_620087.3. NM_138748.5.
UniGenei Mm.275393.

3D structure databases

ProteinModelPortali P58389.
SMRi P58389. Positions 23-322.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 225960. 1 interaction.

PTM databases

PhosphoSitei P58389.

Proteomic databases

MaxQBi P58389.
PaxDbi P58389.
PRIDEi P58389.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000042055 ; ENSMUSP00000046837 ; ENSMUSG00000039515 .
GeneIDi 110854.
KEGGi mmu:110854.
UCSCi uc008jcn.2. mouse.

Organism-specific databases

CTDi 5524.
MGIi MGI:1346006. Ppp2r4.

Phylogenomic databases

eggNOGi COG5057.
HOGENOMi HOG000205736.
HOVERGENi HBG019168.
InParanoidi P58389.
KOi K17605.
OMAi GSHGVWS.
OrthoDBi EOG7KQ21W.
PhylomeDBi P58389.
TreeFami TF105555.

Miscellaneous databases

NextBioi 364789.
PROi P58389.
SOURCEi Search...

Gene expression databases

Bgeei P58389.
ExpressionAtlasi P58389. baseline and differential.
Genevestigatori P58389.

Family and domain databases

InterProi IPR004327. Phstyr_phstse_ac.
[Graphical view ]
PANTHERi PTHR10012. PTHR10012. 1 hit.
Pfami PF03095. PTPA. 1 hit.
[Graphical view ]
PIRSFi PIRSF016325. Phstyr_phstse_ac. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiPTPA_MOUSE
AccessioniPrimary (citable) accession number: P58389
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 16, 2001
Last modified: October 29, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3