PPP1CA

Enzyme

PPP1CA

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
3E7A, 3E7B, 3EGG, 3EGH, 3HVQ, 3N5U, 3V4Y, 4G9J, 4MOV, 4MOY, 4MP0, 4XPN, 1FJM

Identifiers

Aliases

PPP1CA, PP-1A, PP1A, PP1alpha, PPP1A, protein phosphatase 1 catalytic subunit alpha

External IDs

OMIM: 176875; MGI: 103016; HomoloGene: 105262; GeneCards: PPP1CA; OMA:PPP1CA - orthologs

Gene location (Human)

Chr.	Chromosome 11 (human)^[1]

Band	11q13.2	Start	67,398,181 bp^[1]
Band	11q13.2	End	67,421,183 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 19 (mouse)^[2]

Band	19\|19 A	Start	4,242,064 bp^[2]
Band	19\|19 A	End	4,245,419 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

granulocyte

mucosa of transverse colon

monocyte

spleen

thymus

apex of heart

blood

lymph node

mucosa of pharynx

human penis

Top expressed in

striatum of neuraxis

tail of embryo

granulocyte

yolk sac

neural tube

thymus

mesencephalon

white adipose tissue

epiblast

olfactory bulb

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	phosphoprotein phosphatase activity metal ion binding protein binding hydrolase activity cadherin binding involved in cell-cell adhesion protein serine/threonine phosphatase activity phosphatase activity protein phosphatase 1 binding ribonucleoprotein complex binding protein-containing complex binding
Cellular component	cytoplasm plasma membrane nucleoplasm PTW/PP1 phosphatase complex nucleolus extracellular exosome nucleus cytosol protein phosphatase type 1 complex glycogen granule neuron projection neuronal cell body dendritic spine perikaryon presynapse postsynapse glutamatergic synapse
Biological process	regulation of canonical Wnt signaling pathway negative regulation of protein binding cell division glycogen metabolic process cell cycle regulation of translational initiation by eIF2 alpha dephosphorylation beta-catenin destruction complex disassembly dephosphorylation cell-cell adhesion protein dephosphorylation circadian regulation of gene expression regulation of circadian rhythm entrainment of circadian clock by photoperiod carbohydrate metabolic process regulation of glycogen biosynthetic process regulation of glycogen catabolic process response to lead ion lung development peptidyl-threonine dephosphorylation branching morphogenesis of an epithelial tube peptidyl-serine dephosphorylation positive regulation of extrinsic apoptotic signaling pathway in absence of ligand viral process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


5499


19045

Ensembl


ENSG00000172531


ENSMUSG00000040385

UniProt


P62136


P62137

RefSeq (mRNA)


NM_206873 NM_001008709 NM_002708


NM_031868

RefSeq (protein)


NP_001008709 NP_002699 NP_996756


NP_114074

Location (UCSC)

Chr 11: 67.4 – 67.42 Mb

Chr 19: 4.24 – 4.25 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Serine/threonine-protein phosphatase PP1-alpha catalytic subunit is an enzyme that in humans is encoded by the PPP1CA gene.

Function

The protein encoded by this gene is one of the three catalytic subunits of protein phosphatase 1 (PP1). PP1 is a serine/threonine specific protein phosphatase known to be involved in the regulation of a variety of cellular processes, such as cell division, glycogen metabolism, muscle contractility, protein synthesis, and HIV-1 viral transcription. Increased PP1 activity has been observed in the end stage of heart failure. Studies in both human and mice suggest that PP1 is an important regulator of cardiac function. Three alternatively spliced transcript variants encoding different isoforms have been found for this gene.^[5]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles.^{[§ 1]}

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|alt=Nicotine Activity on Dopaminergic Neurons edit]]

Nicotine Activity on Dopaminergic Neurons edit

^ The interactive pathway map can be edited at WikiPathways: "NicotineDopaminergic_WP1602".

Interactions

PPP1CA has been shown to interact with:

AKAP11,^[6]^[7]
BCL2-like 1,^[8]
BCL2L2,^[8]
BRCA1,^[9]
CDC5L,^[10]
Host cell factor C1,^[11]
KvLQT1,^[12]
LMTK2,^[13]
PHACTR3,^[14]
PPP1R15A,^[15]^[16]^[17]
PPP1R8,^[11]^[18]
PPP1R9B,^[19]
Protein kinase R,^[20] and
SMARCB1.^[16]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000172531 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000040385 – 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.
^ "Entrez Gene: PPP1CA protein phosphatase 1, catalytic subunit, alpha isoform".
^ Tanji C, Yamamoto H, Yorioka N, Kohno N, Kikuchi K, Kikuchi A (October 2002). "A-kinase anchoring protein AKAP220 binds to glycogen synthase kinase-3beta (GSK-3beta ) and mediates protein kinase A-dependent inhibition of GSK-3beta". J. Biol. Chem. 277 (40): 36955–61. doi:10.1074/jbc.M206210200. PMID 12147701.
^ Schillace RV, Scott JD (March 1999). "Association of the type 1 protein phosphatase PP1 with the A-kinase anchoring protein AKAP220". Curr. Biol. 9 (6): 321–4. Bibcode:1999CBio....9..321S. doi:10.1016/s0960-9822(99)80141-9. PMID 10209101. S2CID 9188320.
^ ^a ^b Ayllón V, Cayla X, García A, Fleischer A, Rebollo A (July 2002). "The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1alpha to Bad". Eur. J. Immunol. 32 (7): 1847–55. doi:10.1002/1521-4141(200207)32:7<1847::AID-IMMU1847>3.0.CO;2-7. PMID 12115603.
^ Liu Y, Virshup DM, White RL, Hsu LC (November 2002). "Regulation of BRCA1 phosphorylation by interaction with protein phosphatase 1alpha". Cancer Res. 62 (22): 6357–61. PMID 12438214.
^ Ajuh P, Kuster B, Panov K, Zomerdijk JC, Mann M, Lamond AI (December 2000). "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry". EMBO J. 19 (23): 6569–81. doi:10.1093/emboj/19.23.6569. PMC 305846. PMID 11101529.
^ ^a ^b Ajuh PM, Browne GJ, Hawkes NA, Cohen PT, Roberts SG, Lamond AI (February 2000). "Association of a protein phosphatase 1 activity with the human factor C1 (HCF) complex". Nucleic Acids Res. 28 (3): 678–86. doi:10.1093/nar/28.3.678. PMC 102561. PMID 10637318.
^ Marx SO, Kurokawa J, Reiken S, Motoike H, D'Armiento J, Marks AR, Kass RS (January 2002). "Requirement of a macromolecular signaling complex for beta adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel". Science. 295 (5554): 496–9. Bibcode:2002Sci...295..496M. doi:10.1126/science.1066843. PMID 11799244. S2CID 6153394.
^ Wang H, Brautigan DL (December 2002). "A novel transmembrane Ser/Thr kinase complexes with protein phosphatase-1 and inhibitor-2". J. Biol. Chem. 277 (51): 49605–12. doi:10.1074/jbc.M209335200. PMID 12393858.
^ Sagara J, Higuchi T, Hattori Y, Moriya M, Sarvotham H, Shima H, Shirato H, Kikuchi K, Taniguchi S (November 2003). "Scapinin, a putative protein phosphatase-1 regulatory subunit associated with the nuclear nonchromatin structure". J. Biol. Chem. 278 (46): 45611–9. doi:10.1074/jbc.M305227200. PMID 12925532.
^ Hung WJ, Roberson RS, Taft J, Wu DY (May 2003). "Human BAG-1 proteins bind to the cellular stress response protein GADD34 and interfere with GADD34 functions". Mol. Cell. Biol. 23 (10): 3477–86. doi:10.1128/mcb.23.10.3477-3486.2003. PMC 164759. PMID 12724406.
^ ^a ^b Wu DY, Tkachuck DC, Roberson RS, Schubach WH (August 2002). "The human SNF5/INI1 protein facilitates the function of the growth arrest and DNA damage-inducible protein (GADD34) and modulates GADD34-bound protein phosphatase-1 activity". J. Biol. Chem. 277 (31): 27706–15. doi:10.1074/jbc.M200955200. PMID 12016208.
^ Connor JH, Weiser DC, Li S, Hallenbeck JM, Shenolikar S (October 2001). "Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1". Mol. Cell. Biol. 21 (20): 6841–50. doi:10.1128/MCB.21.20.6841-6850.2001. PMC 99861. PMID 11564868.
^ Jin Q, van Eynde A, Beullens M, Roy N, Thiel G, Stalmans W, Bollen M (August 2003). "The protein phosphatase-1 (PP1) regulator, nuclear inhibitor of PP1 (NIPP1), interacts with the polycomb group protein, embryonic ectoderm development (EED), and functions as a transcriptional repressor". J. Biol. Chem. 278 (33): 30677–85. doi:10.1074/jbc.M302273200. PMID 12788942.
^ Hsieh-Wilson LC, Allen PB, Watanabe T, Nairn AC, Greengard P (April 1999). "Characterization of the neuronal targeting protein spinophilin and its interactions with protein phosphatase-1". Biochemistry. 38 (14): 4365–73. doi:10.1021/bi982900m. PMID 10194355.
^ Tan SL, Tareen SU, Melville MW, Blakely CM, Katze MG (September 2002). "The direct binding of the catalytic subunit of protein phosphatase 1 to the PKR protein kinase is necessary but not sufficient for inactivation and disruption of enzyme dimer formation". J. Biol. Chem. 277 (39): 36109–17. doi:10.1074/jbc.M205109200. PMID 12138106.