Gene

ppm1f

ID

ZDB-GENE-051128-2

Name

protein phosphatase, Mg2+/Mn2+ dependent, 1F

Symbol

ppm1f Nomenclature History

Previous Names

CaMKP (1)

Type

protein_coding_gene

Location

Chr: 5 Mapping Details/Browsers

Description

Enables phosphoprotein phosphatase activity. Acts upstream of or within protein dephosphorylation. Predicted to be active in cytosol and nucleus. Is expressed in several structures, including eye; fin; heart; skeletal muscle; and testis. Orthologous to human PPM1F (protein phosphatase, Mg2+/Mn2+ dependent 1F).

Genome Resources

Note

None

Comparative Information

Expression

All Expression Data

1 figure from Sueyoshi et al., 2009

Cross-Species Comparison

High Throughput Data

Expression Atlas

UO scRNA-seq (UCSC browser)

Single Cell Expression Atlas

Daniocell

Thisse Expression Data

No data available

Wild Type Expression Summary

Phenotype

All Phenotype Data: 2 figures from Sueyoshi et al., 2009
Cross-Species Comparison: Alliance

Phenotype Summary

Mutations

Mutants

Allele	Type	Localization	Consequence	Mutagen	Supplier
sa10555	Allele with one point mutation	Unknown	Premature Stop	ENU	European Zebrafish Resource Center (EZRC) (order this) Zebrafish International Resource Center (ZIRC) (order this)
sa15162	Allele with one point mutation	Unknown	Premature Stop	ENU	European Zebrafish Resource Center (EZRC) (order this) Zebrafish International Resource Center (ZIRC) (order this)
sa15839	Allele with one point mutation	Unknown	Premature Stop	ENU	European Zebrafish Resource Center (EZRC) (order this) Zebrafish International Resource Center (ZIRC) (order this)
sa40367	Allele with one point mutation	Unknown	Premature Stop	ENU	Zebrafish International Resource Center (ZIRC) (order this) European Zebrafish Resource Center (EZRC) (order this)

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Sequence Targeting Reagents

Targeting Reagent	Created Alleles	Citations
MO1-ppm1f	N/A	Sueyoshi et al., 2009

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Human Disease

Associated With ppm1f Human Ortholog

No data available

Associated With ppm1f Via Experimental Models

No data available

Gene Ontology

Protein Domains

Domain, Family, and Site Summary

Type	InterPro ID	Name
Binding_site	IPR000222	PPM-type phosphatase, divalent cation binding
Domain	IPR001932	PPM-type phosphatase-like domain
Family	IPR015655	Protein phosphatase 2C
Homologous_superfamily	IPR036457	PPM-type phosphatase-like domain superfamily

Domain Details Per Protein

Protein	Additional Resources	Length	PPM-type phosphatase, divalent cation binding	PPM-type phosphatase-like domain	PPM-type phosphatase-like domain superfamily	Protein phosphatase 2C
UniProtKB:A2BE49	InterPro	424

Transcripts

Genome Browsers

Genome Build: GRCz11Chromosome: 5

Type	Name	Annotation Method	Has Havana Data	Length (nt)	Analysis
mRNA	ppm1f-201 (1) Ensembl	Ensembl		1,924 nt	Select Tool ZFIN BLAST

Interactions and Pathways

No data available

Antibodies

No data available

Plasmids

No data available

Constructs

No data available

Marker Relationships

Relationship	Marker Type	Marker	Accession Numbers	Citations
Contained in	BAC	DKEY-72G15	BX005237	ZFIN Curated Data

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Sequences

Type	Accession #	Length (nt/aa)	Analysis
RNA	RefSeq:NM_001018155 (1)	2198 nt	Select Tool ZFIN BLAST NCBI BLAST Ensembl UCSC BLAT
Genomic	GenBank:BX005237 (2)	213290 nt	Select Tool MegaBLAST
Polypeptide	UniProtKB:A2BE49 (1)	424 aa	Select Tool ZFIN BLAST SIB BLAST Ensembl Protein Blast

Orthology

Comparative Orthology: Alliance
Gene Tree: Ensembl

Species	Symbol	Chromosome	Accession #	Evidence
Human	PPM1F	22	Ensembl:ENSG00000100034 Gene:9647 HGNC:19388 OMIM:619309	Conserved genome location (synteny) (1) Amino acid sequence comparison (1)
Mouse	Ppm1f	16	Ensembl:ENSMUSG00000026181 Gene:68606 MGI:1918464	Conserved genome location (synteny) (1) Amino acid sequence comparison (1)

Citations

Include unpublished citations

Sueyoshi, N., Nimura, T., Ishida, A., Taniguchi, T., Yoshimura, Y., Ito, M., Shigeri, Y., and Kameshita, I. (2009) Ca(2+)/calmodulin-dependent protein kinase phosphatase (CaMKP) is indispensable for normal embryogenesis in zebrafish, Danio rerio. Archives of biochemistry and biophysics. 488(1):48-59

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