PPP1CA
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Also known as: PP-1A, PP1A, PP1A_HUMAN, PP1alpha, PPP1A
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P62136
- Gene
- PPP1CA
- Ensembl
- ENSG00000172531
- Chromosome
- 11
- Canonical length
- 330 aa
- Protein class
- Enzymes, Metabolic proteins, Plasma proteins, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm,Plasma membrane,Cytosol,Flagellar centriole,Mid piece,End piece
OverviewNCBI Gene
The protein encoded by this gene is one of the three catalytic subunits of protein phosphatase 1 (PP1). This broadly expressed gene encodes the alpha subunit of the PP1 complex that associates with over 200 regulatory proteins to form holoenzymes which dephosphorylate their biological targets with high specificity. 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 suggest that PP1 is an important regulator of cardiac function and that PP1 deregulation is implicated in diabetes and multiple types of cancer. Three alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2020]
Canonical amino-acid sequenceUniProt
330 residues, UniProt reviewed canonical sequence.
>P62136|PPP1CA
1 MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP ILLELEAPLK
61 ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL
121 LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL
181 QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVQGWGEND RGVSFTFGAE VVAKFLHKHD
241 LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAD
301 KNKGKYGQFS GLNPGGRPIT PPRNSAKAKKLocalizationUniProt · AlphaFold · HPA
Whether an antibody against PPP1CA can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Intracellular
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.24
- Highest tissue expression
- 181 nTPM
Expression across tissuesHPA
Tissue
- esophagus: 181 nTPM
- tonsil: 146 nTPM
- spleen: 141 nTPM
- lymph node: 138 nTPM
- liver: 125 nTPM
- skeletal muscle: 124 nTPM
Single-cell type
- esophageal apical cells: 821 nCPM
- extravillous trophoblasts: 647 nCPM
- syncytiotrophoblasts: 475 nCPM
- esophageal suprabasal cells: 458 nCPM
- cytotrophoblasts: 416 nCPM
- esophageal basal cells: 412 nCPM
Immune cell
- total PBMC: 2,042 nTPM
- eosinophil: 1,237 nTPM
- non-classical monocyte: 1,191 nTPM
- T-reg: 1,102 nTPM
- intermediate monocyte: 964 nTPM
- basophil: 925 nTPM
Brain region
- basal ganglia: 64 nTPM
- medulla oblongata: 60 nTPM
- white matter: 60 nTPM
- thalamus: 57 nTPM
- spinal cord: 51 nTPM
- pons: 51 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.27
- gnomAD pLI
- 0.99
- gnomAD missense Z
- 3.26
- DepMap mean gene effect
- -0.64
- DepMap dependency class
- common
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 8% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- branching morphogenesis of an epithelial tube
- cell division
- circadian regulation of gene expression
- entrainment of circadian clock by photoperiod
- glycogen metabolic process
- lung development
- negative regulation of transcription elongation by RNA polymerase II
- positive regulation of extrinsic apoptotic signaling pathway in absence of ligand
- positive regulation of glycogen biosynthetic process
- positive regulation of termination of RNA polymerase II transcription, poly(A)-coupled
- positive regulation of transcription elongation by RNA polymerase II
- protein dephosphorylation
- protein stabilization
- regulation of canonical Wnt signaling pathway
- regulation of circadian rhythm
- regulation of glycogen catabolic process
- regulation of translational initiation in response to stress
- response to lead ion
- RNA polymerase II promoter clearance
- telomere maintenance in response to DNA damage
Molecular functions
- cadherin binding involved in cell-cell adhesion
- iron ion binding
- phosphatase activity
- phosphoprotein phosphatase activity
- protein phosphatase 1 binding
- protein serine/threonine phosphatase activity
- ribonucleoprotein complex binding
- RNA polymerase II CTD heptapeptide repeat S5 phosphatase activity
- transition metal ion binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Calcineurin-like, phosphoesterase domain
- Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase
- Metallo-dependent phosphatase-like
- Serine-threonine protein phosphatase, N-terminal
- Serine/threonine-protein phosphatase PP1 catalytic subunit
- Calcineurin-like phosphoesterase
- Serine-threonine protein phosphatase N-terminal domain
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of PPP1CA in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads PPP1CA as an antibody target. Whether an autoantibody or antibody against PPP1CA could matter depends on whether native PPP1CA is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
PPP1CA is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label PPP1CA as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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