Ppm1a protein phosphatase 1A, magnesium dependent, alpha isoform [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Ppm1aprovided by MGI
Official Full Name: protein phosphatase 1A, magnesium dependent, alpha isoformprovided by MGI
Primary source: MGI:MGI:99878
See related: Ensembl:ENSMUSG00000021096 AllianceGenome:MGI:99878
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: MMPa-2; MPPa-1; 2310003C21Rik; 2900017D14Rik
Summary: Enables phosphoprotein phosphatase activity. Involved in N-terminal protein myristoylation. Acts upstream of or within several processes, including cellular response to transforming growth factor beta stimulus; negative regulation of BMP signaling pathway; and positive regulation of protein export from nucleus. Located in cytosol; membrane; and nucleus. Is expressed in several structures, including Peyer's patch; brain; ganglia; male reproductive gland or organ; and white fat. Orthologous to human PPM1A (protein phosphatase, Mg2+/Mn2+ dependent 1A). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Ubiquitous expression in testis adult (RPKM 16.2), cortex adult (RPKM 14.0) and 28 other tissues See more
Orthologs: human all
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Genomic context

Location:: 12 C3; 12 30.26 cM

Exon count:: 9

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	12	NC_000078.7 (72804231..72846593)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	12	NC_000078.6 (72761211..72799819)

Chromosome 12 - NC_000078.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

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Expression

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See details

Project title: Mouse ENCODE transcriptome data Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Protein phosphatase PPM1A inhibition attenuates osteoarthritis via regulating TGF-beta/Smad2 signaling in chondrocytes.
Title: Protein phosphatase PPM1A inhibition attenuates osteoarthritis via regulating TGF-β/Smad2 signaling in chondrocytes.
PPM1A Controls Diabetic Gene Programming through Directly Dephosphorylating PPARgamma at Ser273.
Title: PPM1A Controls Diabetic Gene Programming through Directly Dephosphorylating PPARγ at Ser273.
Protein phosphatase magnesium-dependent 1A induces inflammation in rheumatoid arthritis.
Title: Protein phosphatase magnesium-dependent 1A induces inflammation in rheumatoid arthritis.
VRK1 self-represses its activity to phosphorylate PXR through cyclin-dependent kinase 2 (CDK2) in high glucose conditions, resulting in the repression of the PCK1 gene. This PXR phosphorylation was also observed in fasting mouse livers. Thus, the VRK1-CDK2-PXR-PP2Calpha-SGK2 pathway can be a novel physiological cell signaling that regulates gluconeogenesis in response to glucose.
Title: Glucose elicits serine/threonine kinase VRK1 to phosphorylate nuclear pregnane X receptor as a novel hepatic gluconeogenic signal.
findings demonstrate a novel regulatory circuit in which STING and TBK1 reciprocally regulate each other to enable efficient antiviral signaling activation, and PPM1A dephosphorylates STING and TBK1
Title: PPM1A regulates antiviral signaling by antagonizing TBK1-mediated STING phosphorylation and aggregation.
the studies presented here position PPM1A as a new player in the wound healing-inflammation-angiogenesis axis in mouse, reveal its crucial role in homeostasis on injury, and highlight its potential as a therapeutic mediator in pathologic conditions
Title: Protein phosphatase magnesium dependent 1A governs the wound healing-inflammation-angiogenesis cross talk on injury.
a nuclear envelope-localized mechanism of inactivating TGF-beta signaling in which MAN1 competes with transcription factors for binding to Smad2 and Smad3 and facilitates their dephosphorylation by PPM1A.
Title: Inhibition of TGF-β signaling at the nuclear envelope: characterization of interactions between MAN1, Smad2 and Smad3, and PPM1A.
Although a non-myristoylated mutation (G2A) of PPM1A and PPM1B prevented membrane association, this relocalization did not likely cause the decreased activity towards AMPKalpha.
Title: N-Myristoylation is essential for protein phosphatases PPM1A and PPM1B to dephosphorylate their physiological substrates in cells.
we found that PPM1A mRNA is synthesized at the beginning of the maturation process and remains elevated in the mature oocytes, promoting the accumulation of PPM1A protein
Title: De novo synthesis of protein phosphatase 1A, magnesium dependent, alpha isoform (PPM1A) during oocyte maturation.
Protein phosphatase PPM1A regulates the nuclear export of Smad2/3 through targeting nuclear exporter RanBP3.
Title: PPM1A dephosphorylates RanBP3 to enable efficient nuclear export of Smad2 and Smad3.

Submit: New GeneRIF Correction See all GeneRIFs (14)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (3)
Targeted (9) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

D6Arb18 (e-PCR)
- UniSTS:239417

AI427932 (e-PCR)
- UniSTS:180397

AU017636 (e-PCR)
- UniSTS:180398

RH124449 (e-PCR)
- UniSTS:161271

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables R-SMAD binding	ISO Inferred from Sequence Orthology more info
enables R-SMAD binding	ISS Inferred from Sequence or Structural Similarity more info
enables calmodulin-dependent protein phosphatase activity	IEA Inferred from Electronic Annotation more info
enables calmodulin-dependent protein phosphatase activity	ISO Inferred from Sequence Orthology more info
enables magnesium ion binding	IEA Inferred from Electronic Annotation more info
enables manganese ion binding	IEA Inferred from Electronic Annotation more info
enables myosin phosphatase activity	IEA Inferred from Electronic Annotation more info
enables phosphoprotein phosphatase activity	IDA Inferred from Direct Assay more info	PubMed
enables phosphoprotein phosphatase activity	ISO Inferred from Sequence Orthology more info
enables protein serine/threonine phosphatase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein serine/threonine phosphatase activity	ISO Inferred from Sequence Orthology more info
enables transmembrane transporter binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in N-terminal protein myristoylation	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within cellular response to transforming growth factor beta stimulus	IDA Inferred from Direct Assay more info	PubMed
involved_in dephosphorylation	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within negative regulation of BMP signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of canonical NF-kappaB signal transduction	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of canonical NF-kappaB signal transduction	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of non-canonical NF-kappaB signal transduction	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of non-canonical NF-kappaB signal transduction	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of transforming growth factor beta receptor signaling pathway	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of transforming growth factor beta receptor signaling pathway	ISO Inferred from Sequence Orthology more info
involved_in peptidyl-threonine dephosphorylation	IEA Inferred from Electronic Annotation more info
involved_in peptidyl-threonine dephosphorylation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of DNA-templated transcription	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of DNA-templated transcription	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of canonical Wnt signaling pathway	IBA Inferred from Biological aspect of Ancestor more info
involved_in positive regulation of canonical Wnt signaling pathway	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of canonical Wnt signaling pathway	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within positive regulation of protein export from nucleus	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within protein dephosphorylation	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within protein dephosphorylation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein dephosphorylation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein dephosphorylation	ISO Inferred from Sequence Orthology more info
acts_upstream_of protein export from nucleus	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of canonical NF-kappaB signal transduction	IBA Inferred from Biological aspect of Ancestor more info

Component	Evidence Code	Pubs
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	ISO Inferred from Sequence Orthology more info
located_in membrane	IDA Inferred from Direct Assay more info	PubMed
located_in neuron projection	ISO Inferred from Sequence Orthology more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: protein phosphatase 1A

Names: Mpp alpha; PP2C-alpha; protein phosphatase IA

NP_032936.1

EC 3.1.3.16

XP_036013148.1

EC 3.1.3.16

XP_036013149.1

EC 3.1.3.16

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_008910.3 → NP_032936.1 protein phosphatase 1A

See identical proteins and their annotated locations for NP_032936.1

Status: VALIDATED

Source sequence(s)

AK076054, AV307012, BE861326, BM932496, BY739448, D28117

Consensus CDS

CCDS25970.1

UniProtKB/Swiss-Prot

P49443

UniProtKB/TrEMBL

Q9EQE2

Related

ENSMUSP00000021514.9, ENSMUST00000021514.10

Conserved Domains (2) summary

cd00143
Location:23 → 291

PP2Cc; Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence ...

pfam07830
Location:285 → 363

PP2C_C; Protein serine/threonine phosphatase 2C, C-terminal domain

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

NC_000078.7 Reference GRCm39 C57BL/6J

Range

72804231..72846593

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_036157255.1 → XP_036013148.1 protein phosphatase 1A isoform X1

Conserved Domains (2) summary

cd00143
Location:95 → 363

PP2Cc; Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence ...

pfam07830
Location:357 → 435

PP2C_C; Protein serine/threonine phosphatase 2C, C-terminal domain
XM_036157256.1 → XP_036013149.1 protein phosphatase 1A isoform X2

UniProtKB/Swiss-Prot

P49443

UniProtKB/TrEMBL

Q9EQE2

Conserved Domains (2) summary

cd00143
Location:23 → 291

PP2Cc; Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence ...

pfam07830
Location:285 → 363

PP2C_C; Protein serine/threonine phosphatase 2C, C-terminal domain