PPEF1

PPEF1
Identifiers
Aliases	PPEF1 , PP7, PPEF, PPP7C, PPP7CA, protein phosphatase with EF-hand domain 1
External IDs	OMIM: 300109 MGI: 1097157 HomoloGene: 55960 GeneCards: PPEF1
Gene location (Human)
Chr.	X chromosome (human)
End	18,827,921 bp
Gene location (Mouse)
Chr.	X chromosome (mouse)
End	159,518,761 bp
RNA expression pattern
	Top expressed in
	sperm; ; secondary oocyte; ; endothelial cell; ; spinal ganglia; ; prefrontal cortex; ; orbitofrontal cortex; ; trigeminal ganglion; ; Brodmann area 10; ; Brodmann area 46; ; dorsolateral prefrontal cortex;
	Top expressed in
	spermatid; ; secondary oocyte; ; testicle; ; spermatocyte; ; spinal ganglia; ; neural tube; ; trigeminal ganglion; ; ear; ; superior ganglion of vagus nerve; ; peripheral nervous system;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	iron ion binding ; calcium ion binding ; protein serine/threonine phosphatase activity ; phosphoprotein phosphatase activity ; manganese ion binding ; hydrolase activity ; metal ion binding ; protein binding ;
Cellular component	cytosol ; nucleus ;
Biological process	protein dephosphorylation ; detection of stimulus involved in sensory perception ; regulation of rhodopsin mediated signaling pathway ;
	Sources:Amigo / QuickGO
Orthologs
	5475
	237178
	ENSG00000086717
	ENSMUSG00000062168
	O14829
	O35655
NM_006240 ; NM_152223 ; NM_152224 ; NM_152225 ; NM_152226 ;
	NM_001377986 ; NM_001377993 ; NM_001377994 ; NM_001377995 ; NM_001377996 ; NM_001378381 ; NM_001378382 ; NM_001389620 ; NM_001389621 ; NM_001389623 ; NM_001389624 Contents Function ; Interactions ; References ; Further reading ;
	NM_011147
NP_006231 ; NP_689410 ; NP_689412 ; NP_001364915 ; NP_001364922 ;
	NP_001364923 ; NP_001364924 ; NP_001364925 ; NP_001365310 ; NP_001365311
	NP_035277
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated December 03, 2023

Serine/threonine-protein phosphatase with EF-hands 1 is an enzyme that in humans is encoded by the PPEF1 gene.^[5]^[6]^[7]

Function

This gene encodes a member of the serine/threonine protein phosphatase with EF-hand motif family. The protein contains a protein phosphatase catalytic domain, and at least two EF-hand calcium-binding motifs in its C terminus. Although its substrate(s) is unknown, the encoded protein has been suggested to play a role in specific sensory neuron function and/or development. This gene shares high sequence similarity with the Drosophila retinal degeneration C (rdgC) gene. Several alternatively spliced transcript variants, each encoding a distinct isoform, have been described.^[7]

Interactions

PPEF1 has been shown to interact with Calmodulin 1.^[8]

Related Research Articles

Calmodulin 1 is a protein that in humans is encoded by the CALM1 gene.

Calcium/calmodulin-dependent protein kinase type II subunit alpha (CAMKIIα), a.k.a.Ca²⁺/calmodulin-dependent protein kinase II alpha, is one subunit of CamKII, a protein kinase (i.e., an enzyme which phosphorylates proteins) that in humans is encoded by the CAMK2A gene.

Calcium/calmodulin-dependent protein kinase type IV is an enzyme that in humans is encoded by the CAMK4 gene.

Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform is an enzyme that in humans is encoded by the PPP2CB gene.

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform is an enzyme that in humans is encoded by the PPP2R5A gene.

Calcium/calmodulin-dependent protein kinase type II gamma chain is an enzyme that in humans is encoded by the CAMK2G gene.

Polo-like kinase 3 (Drosophila), also known as PLK3, is an enzyme which in humans is encoded by the PLK3 gene.

Calcium/calmodulin-dependent protein kinase type II delta chain is an enzyme that in humans is encoded by the CAMK2D gene.

Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform (PP2BB) is an enzyme that in humans is encoded by the PPP3CB gene.

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform is an enzyme that in humans is encoded by the PPP2R5B gene.

Proline-serine-threonine phosphatase-interacting protein 1 is an enzyme that in humans is encoded by the PSTPIP1 gene.

Membrane-associated phosphatidylinositol transfer protein 1 is a protein that in humans is encoded by the PITPNM1 gene.

Serine/threonine-protein kinase PLK2 is an enzyme that in humans is encoded by the PLK2 gene.

Death-associated protein kinase 2 is an enzyme that in humans is encoded by the DAPK2 gene.

Protein phosphatase 1G is an enzyme that in humans is encoded by the PPM1G gene.

Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform (PP2BC) is an enzyme that in humans is encoded by the PPP3CC gene.

Integrin-linked kinase-associated serine/threonine phosphatase 2C is an enzyme that in humans is encoded by the ILKAP gene.

Protein phosphatase 1F is an enzyme that in humans is encoded by the PPM1F gene.

Shewanella-like phosphatases, abbreviated as Shelphs, are a group of enzymes structurally related to protein serine/threonine phosphatases. Unlike the canonical subfamilies found in eukaryotes, Shelphs span the eukaryote-prokaryote boundary and are found in several genera of Pseudomonadota, in plants, red algae, fungi and some unicellular parasites, including a causative agent of malaria Plasmodium, Cryptosporidium and kinetoplastids.

Protein phosphatase with EF-hand domain 2 is a protein that in humans is encoded by the PPEF2 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000086717 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000062168 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Montini E, Rugarli EI, Van de Vosse E, Andolfi G, Mariani M, Puca AA, Consalez GG, den Dunnen JT, Ballabio A, Franco B (Jul 1997). "A novel human serine-threonine phosphatase related to the Drosophila retinal degeneration C (rdgC) gene is selectively expressed in sensory neurons of neural crest origin". Human Molecular Genetics. 6 (7): 1137–45. doi: 10.1093/hmg/6.7.1137 . PMID 9215685.
↑ Sherman PM, Sun H, Macke JP, Williams J, Smallwood PM, Nathans J (Oct 1997). "Identification and characterization of a conserved family of protein serine/threonine phosphatases homologous to Drosophila retinal degeneration C". Proceedings of the National Academy of Sciences of the United States of America. 94 (21): 11639–44. doi: 10.1073/pnas.94.21.11639 . PMC 23563 . PMID 9326663.
1 2 "Entrez Gene: PPEF1 protein phosphatase, EF-hand calcium binding domain 1".
↑ Kutuzov MA, Solov'eva OV, Andreeva AV, Bennett N (May 2002). "Protein Ser/Thr phosphatases PPEF interact with calmodulin". Biochemical and Biophysical Research Communications. 293 (3): 1047–52. doi:10.1016/S0006-291X(02)00338-8. PMID 12051765.

Herzig S, Neumann J (Jan 2000). "Effects of serine/threonine protein phosphatases on ion channels in excitable membranes". Physiological Reviews. 80 (1): 173–210. doi:10.1152/physrev.2000.80.1.173. PMID 10617768. S2CID 17770945.
Huang X, Honkanen RE (Jan 1998). "Molecular cloning, expression, and characterization of a novel human serine/threonine protein phosphatase, PP7, that is homologous to Drosophila retinal degeneration C gene product (rdgC)". The Journal of Biological Chemistry. 273 (3): 1462–8. doi: 10.1074/jbc.273.3.1462 . PMID 9430683.
Ramulu P, Kennedy M, Xiong WH, Williams J, Cowan M, Blesh D, Yau KW, Hurley JB, Nathans J (Dec 2001). "Normal light response, photoreceptor integrity, and rhodopsin dephosphorylation in mice lacking both protein phosphatases with EF hands (PPEF-1 and PPEF-2)". Molecular and Cellular Biology. 21 (24): 8605–14. doi:10.1128/MCB.21.24.8605-8614.2001. PMC 100021 . PMID 11713293.
Kutuzov MA, Solov'eva OV, Andreeva AV, Bennett N (May 2002). "Protein Ser/Thr phosphatases PPEF interact with calmodulin". Biochemical and Biophysical Research Communications. 293 (3): 1047–52. doi:10.1016/S0006-291X(02)00338-8. PMID 12051765.
Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
Hillman RT, Green RE, Brenner SE (2005). "An unappreciated role for RNA surveillance". Genome Biology. 5 (2): R8. doi: 10.1186/gb-2004-5-2-r8 . PMC 395752 . PMID 14759258.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000086717 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000062168 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9215685-5] Montini E, Rugarli EI, Van de Vosse E, Andolfi G, Mariani M, Puca AA, Consalez GG, den Dunnen JT, Ballabio A, Franco B (Jul 1997). "A novel human serine-threonine phosphatase related to the Drosophila retinal degeneration C (rdgC) gene is selectively expressed in sensory neurons of neural crest origin". Human Molecular Genetics. 6 (7): 1137–45. doi: 10.1093/hmg/6.7.1137 . PMID 9215685.

[pmid9326663-6] Sherman PM, Sun H, Macke JP, Williams J, Smallwood PM, Nathans J (Oct 1997). "Identification and characterization of a conserved family of protein serine/threonine phosphatases homologous to Drosophila retinal degeneration C". Proceedings of the National Academy of Sciences of the United States of America. 94 (21): 11639–44. doi: 10.1073/pnas.94.21.11639 . PMC 23563 . PMID 9326663.

[entrez-7] 1 2 "Entrez Gene: PPEF1 protein phosphatase, EF-hand calcium binding domain 1".

[pmid12051765-8] Kutuzov MA, Solov'eva OV, Andreeva AV, Bennett N (May 2002). "Protein Ser/Thr phosphatases PPEF interact with calmodulin". Biochemical and Biophysical Research Communications. 293 (3): 1047–52. doi:10.1016/S0006-291X(02)00338-8. PMID 12051765.

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PPEF1

Contents

Function

Interactions

Related Research Articles

References

Further reading