{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P62136","secondaryAccessions":["A6NNR3","B2R908","P08129","P20653","P22802","Q07161"],"uniProtkbId":"PP1A_HUMAN","entryAudit":{"firstPublicDate":"1988-08-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2004-06-21","entryVersion":208,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Serine/threonine-protein phosphatase PP1-alpha catalytic subunit"},"shortNames":[{"value":"PP-1A"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26083323"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35768504"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35830882"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35831509"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36175670"}],"value":"3.1.3.16"}]}},"genes":[{"geneName":{"value":"PPP1CA"},"synonyms":[{"value":"PPP1A"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P62137"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17283141"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20516061"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21712997"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23396208"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23499489"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25556658"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26083323"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28216226"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30158517"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31677974"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33264625"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35768504"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35830882"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35831509"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36175670"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39603239"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39603240"}],"value":"Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets (PubMed:28216226, PubMed:30158517, PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670, PubMed:39603239, PubMed:39603240). Protein phosphatase 1 (PP1) is essential for cell division, transcription elongation, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670, PubMed:39603239, PubMed:39603240). Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Catalytic component of the PNUTS-PP1 protein phosphatase complex, a protein phosphatase 1 (PP1) complex that promotes RNA polymerase II transcription pause-release, allowing transcription elongation: the PNUTS-PP1 complex mediates the release of RNA polymerase II from promoter-proximal region of genes by catalyzing dephosphorylation of proteins involved in transcription, such as AFF4, CDK9, MEPCE, INTS12, NCBP1, POLR2M/GDOWN1 and SUPT6H (PubMed:39603239, PubMed:39603240). The PNUTS-PP1 complex also regulates transcription termination by mediating dephosphorylation of SUPT5H in termination zones downstream of poly(A) sites, thereby promoting deceleration of RNA polymerase II transcription (PubMed:31677974). PNUTS-PP1 complex is also involved in the response to replication stress by mediating dephosphorylation of POLR2A at 'Ser-5' of the CTD, promoting RNA polymerase II degradation (PubMed:33264625). PNUTS-PP1 also plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase (PubMed:20516061). Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage (PubMed:17283141). Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development (By similarity). In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation (PubMed:21712997). May dephosphorylate CSNK1D and CSNK1E (PubMed:21712997). Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). Dephosphorylates CENPA (PubMed:25556658). Dephosphorylates the 'Ser-139' residue of ATG16L1 causing dissociation of ATG12-ATG5-ATG16L1 complex, thereby inhibiting autophagy (PubMed:26083323). Together with PPP1CC (PP1-gamma subunit), dephosphorylates IFIH1/MDA5 and RIG-I leading to their activation and a functional innate immune response (PubMed:23499489). Core component of the SHOC2-MRAS-PP1c (SMP) holophosphatase complex that regulates the MAPK pathway activation (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). The SMP complex specifically dephosphorylates the inhibitory phosphorylation at 'Ser-259' of RAF1 kinase, 'Ser-365' of BRAF kinase and 'Ser-214' of ARAF kinase, stimulating their kinase activities (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). The SMP complex enhances the dephosphorylation activity and substrate specificity of PP1c (PubMed:35768504, PubMed:36175670)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29769351"}],"value":"(Microbial infection) Necessary for alphaviruses replication"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20629"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:11604"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:83421"}],"ecNumber":"3.1.3.16","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26083323"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28216226"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31677974"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33264625"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35768504"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35830882"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35831509"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36175670"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39603239"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39603240"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47004"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:61977"}],"ecNumber":"3.1.3.16","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26083323"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31677974"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39603239"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39603240"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe cation","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q08209"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:24875"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q08209"}],"value":"Binds 1 Fe cation per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18992256"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30100357"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35830882"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35831509"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36175670"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18992256"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30100357"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35830882"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35831509"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36175670"}],"value":"Binds 2 manganese ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15705855"}],"value":"The phosphatase activity of the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug that protects cells from endoplasmic reticulum stress"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P62137"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P62139"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11564868"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11739654"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12226088"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16263087"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16732323"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17283141"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17626005"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17890166"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17965019"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18992256"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19389623"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19581931"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19826001"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20305656"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20424263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20516061"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23213405"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23396208"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23846654"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25556658"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26083323"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26981768"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30100357"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31677974"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33264625"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35768504"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35830882"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35831509"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36175670"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39256359"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39446389"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39603239"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39603240"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9023344"}],"value":"PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting or regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. Interacts with PPP1R39 (By similarity). Interacts with BTBD10 (By similarity). Interacts with KCTD20 (By similarity). Interacts with PPP1R9A and PPP1R9B. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts with PHACTR4; which acts as an activator of PP1 activity (By similarity). Interacts with PPP1R15A and PPP1R15B; the interactions mediate binding to EIF2S1 (PubMed:26095357). Interacts with PPP1R7. Interacts with YLPM1. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and NCOA5. Interacts with NOM1 and PPP1R8. Interacts with PPP1R16B. Interacts with RPSA only in the presence of PPP1R16B. Component of the PNUTS-PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC (PubMed:20516061, PubMed:31677974, PubMed:33264625, PubMed:39603240, PubMed:39603239, PubMed:39446389). Interacts with PPP1R10/PNUTS and PPP1R8. Interacts with WDR82 in the presence of PPP1R10/PNUTS. Interacts with TRIM28; the interaction dephosphorylates TRIM28 on 'Ser-824' and forms a complex at the p21 promoter site. Interacts with isoform 1 and isoform 4 of NEK2. Interacts with FER; this promotes phosphorylation at Thr-320. Interacts with DAB2; the interaction is mutually exclusive with the AXIN1:PPP1CA interaction. Interacts with FOXP3 (PubMed:23396208). Interacts with CENPA (PubMed:25556658). Interacts with ATG16L1 (PubMed:26083323). Found in a complex with PPP1CA, PPP1CC, SHC1 and PEAK1 (PubMed:23846654). Interacts with tensin TNS1 (PubMed:19826001). Interacts with SAXO4, PPP1R21, PPP1R26, PPP1R27, PPP1R35, PPP1R36, PPP1R37, SH3RF2, ELFN1 and ELFN2 (PubMed:19389623). Interacts with TPRN; the interaction results in inhibition of PPC1A phosphatase activity (PubMed:23213405). Interacts with SKA1 (via C-terminus); the interaction is direct and required for the recruitment of PP1 to the kinetochore (PubMed:26981768). Interacts with the KNL1 complex subunit KNL1; the interaction is direct and mutually exclusive with KNL1 binding to microtubules (PubMed:30100357). Component of the SHOC2-MRAS-PP1c (SMP) complex consisting of SHOC2, GTP-bound M-Ras/MRAS and the catalytic subunit of protein phosphatase 1 (either PPP1CA, PPP1CB or PPP1CC) (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). SHOC2 and PP1c preferably bind M-Ras/MRAS, but they also bind K-Ras/KRAS, N-Ras/NRAS and H-Ras/HRAS; these interactions are GTP-dependent and both SHOC2 and PP1c are required to form a stable complex (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). Interacts with SHOC2 in the absence of Ras GTPases (PubMed:35768504, PubMed:35831509). Interacts with LRRC7 (PubMed:39256359)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9023344"}],"value":"(Microbial infection) Interacts with HHV-1 ICP34.5"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29769351"}],"value":"(Microbial infection) Interacts with Venezuelan equine encephalitis virus (VEEV) capsid protein; this interaction dephosphorylates the capsid protein, which increases its ability to bind to the viral 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