ID PP1A_HUMAN Reviewed; 330 AA. AC P62136; A6NNR3; B2R908; P08129; P20653; P22802; Q07161; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2004, sequence version 1. DT 27-MAR-2024, entry version 198. DE RecName: Full=Serine/threonine-protein phosphatase PP1-alpha catalytic subunit; DE Short=PP-1A; DE EC=3.1.3.16 {ECO:0000269|PubMed:26083323}; GN Name=PPP1CA; Synonyms=PPP1A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Lung; RX PubMed=8392016; DOI=10.1016/0378-1119(93)90282-8; RA Song Q., Khanna K.K., Lu H., Lavin M.F.; RT "Cloning and characterization of a human protein phosphatase 1-encoding RT cDNA."; RL Gene 129:291-295(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=8384581; DOI=10.1101/gad.7.4.555; RA Durfee T., Becherer K., Chen P.L., Yeh S.H., Yang Y., Kilburn A.E., RA Lee W.H., Elledge S.J.; RT "The retinoblastoma protein associates with the protein phosphatase type 1 RT catalytic subunit."; RL Genes Dev. 7:555-569(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RA Tung L.; RL Submitted (APR-1991) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Synovial cell; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Muscle, Pancreas, and Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PROTEIN SEQUENCE OF 2-15 AND 247-261, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Colon carcinoma; RA Bienvenut W.V., Heiserich L., Gottlieb E.; RL Submitted (OCT-2008) to UniProtKB. RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 23-330 (ISOFORM 1). RX PubMed=2161401; DOI=10.1016/0888-7543(90)90536-4; RA Barker H.M., Jones T.A., da Cruz e Silva E.F., Spurr N.K., Sheer D., RA Cohen P.T.W.; RT "Localization of the gene encoding a type I protein phosphatase catalytic RT subunit to human chromosome band 11q13."; RL Genomics 7:159-166(1990). RN [10] RP INTERACTION WITH PPP1R15A, AND INTERACTION WITH HHV-1 ICP34.5 (MICROBIAL RP INFECTION). RX PubMed=9023344; DOI=10.1073/pnas.94.3.843; RA He B., Gross M., Roizman B.; RT "The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein RT phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic RT translation initiation factor 2 and preclude the shutoff of protein RT synthesis by double-stranded RNA-activated protein kinase."; RL Proc. Natl. Acad. Sci. U.S.A. 94:843-848(1997). RN [11] RP SUBCELLULAR LOCATION, AND INTERACTION WITH PPP1R8. RX PubMed=11739654; DOI=10.1242/jcs.114.23.4219; RA Trinkle-Mulcahy L., Sleeman J.E., Lamond A.I.; RT "Dynamic targeting of protein phosphatase 1 within the nuclei of living RT mammalian cells."; RL J. Cell Sci. 114:4219-4228(2001). RN [12] RP INTERACTION WITH PPP1R15A. RX PubMed=11564868; DOI=10.1128/mcb.21.20.6841-6850.2001; RA Connor J.H., Weiser D.C., Li S., Hallenbeck J.M., Shenolikar S.; RT "Growth arrest and DNA damage-inducible protein GADD34 assembles a novel RT signaling complex containing protein phosphatase 1 and inhibitor 1."; RL Mol. Cell. Biol. 21:6841-6850(2001). RN [13] RP INTERACTION WITH PPP1R7. RX PubMed=12226088; DOI=10.1074/jbc.m206838200; RA Ceulemans H., Vulsteke V., De Maeyer M., Tatchell K., Stalmans W., RA Bollen M.; RT "Binding of the concave surface of the Sds22 superhelix to the alpha RT 4/alpha 5/alpha 6-triangle of protein phosphatase-1."; RL J. Biol. Chem. 277:47331-47337(2002). RN [14] RP REVIEW. RX PubMed=11839776; DOI=10.1242/jcs.115.2.241; RA Cohen P.T.W.; RT "Protein phosphatase 1 -- targeted in many directions."; RL J. Cell Sci. 115:241-256(2002). RN [15] RP INTERACTION WITH PPP1R16B AND RPSA. RX PubMed=16263087; DOI=10.1016/j.bbrc.2005.10.089; RA Kim K., Li L., Kozlowski K., Suh H.S., Cao W., Ballermann B.J.; RT "The protein phosphatase-1 targeting subunit TIMAP regulates LAMR1 RT phosphorylation."; RL Biochem. Biophys. Res. Commun. 338:1327-1334(2005). RN [16] RP ACTIVITY REGULATION. RX PubMed=15705855; DOI=10.1126/science.1101902; RA Boyce M., Bryant K.F., Jousse C., Long K., Harding H.P., Scheuner D., RA Kaufman R.J., Ma D., Coen D.M., Ron D., Yuan J.; RT "A selective inhibitor of eIF2alpha dephosphorylation protects cells from RT ER stress."; RL Science 307:935-939(2005). RN [17] RP INTERACTION WITH FER, AND PHOSPHORYLATION AT THR-320. RX PubMed=16732323; DOI=10.1038/sj.onc.1209695; RA Pasder O., Shpungin S., Salem Y., Makovsky A., Vilchick S., Michaeli S., RA Malovani H., Nir U.; RT "Downregulation of Fer induces PP1 activation and cell-cycle arrest in RT malignant cells."; RL Oncogene 25:4194-4206(2006). RN [18] RP IDENTIFICATION IN A COMPLEX WITH ILF2; ILF3; YLPM1; KHDRBS1; RBMX AND RP NCOA5, AND INTERACTION WITH YLPM1. RX PubMed=17890166; DOI=10.1016/j.bbapap.2007.07.015; RA Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N., RA Glover M., Lamond A.I., Moorhead G.B.G.; RT "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside RT kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G."; RL Biochim. Biophys. Acta 1774:1339-1350(2007). RN [19] RP FUNCTION, INTERACTION WITH NEK2, AND DEPHOSPHORYLATION. RX PubMed=17283141; DOI=10.1158/0008-5472.can-06-3071; RA Mi J., Guo C., Brautigan D.L., Larner J.M.; RT "Protein phosphatase-1alpha regulates centrosome splitting through Nek2."; RL Cancer Res. 67:1082-1089(2007). RN [20] RP INTERACTION WITH NEK2. RX PubMed=17626005; DOI=10.1074/jbc.m704969200; RA Wu W., Baxter J.E., Wattam S.L., Hayward D.G., Fardilha M., Knebel A., RA Ford E.M., da Cruz e Silva E.F., Fry A.M.; RT "Alternative splicing controls nuclear translocation of the cell cycle- RT regulated Nek2 kinase."; RL J. Biol. Chem. 282:26431-26440(2007). RN [21] RP SUBCELLULAR LOCATION, AND INTERACTION WITH NOM1. RX PubMed=17965019; DOI=10.1074/jbc.m706708200; RA Gunawardena S.R., Ruis B.L., Meyer J.A., Kapoor M., Conklin K.F.; RT "NOM1 targets protein phosphatase I to the nucleolus."; RL J. Biol. Chem. 283:398-404(2008). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [24] RP INTERACTION WITH TNS1. RX PubMed=19826001; DOI=10.1074/jbc.m109.059592; RA Hall E.H., Daugherty A.E., Choi C.K., Horwitz A.F., Brautigan D.L.; RT "Tensin1 requires protein phosphatase-1alpha in addition to RhoGAP DLC-1 to RT control cell polarization, migration, and invasion."; RL J. Biol. Chem. 284:34713-34722(2009). RN [25] RP INTERACTION WITH SAXO4; PPP1R21; PPP1R26; PPP1R27; PPP1R35; PPP1R36; RP PPP1R37; SH3RF2; ELFN1 AND ELFN2. RX PubMed=19389623; DOI=10.1016/j.chembiol.2009.02.012; RA Hendrickx A., Beullens M., Ceulemans H., Den Abt T., Van Eynde A., RA Nicolaescu E., Lesage B., Bollen M.; RT "Docking motif-guided mapping of the interactome of protein RT phosphatase-1."; RL Chem. Biol. 16:365-371(2009). RN [26] RP RETRACTED PAPER. RX PubMed=19377461; DOI=10.1038/nature07954; RA Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., RA Kitagawa H., Kato S.; RT "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced RT granulopoiesis."; RL Nature 459:455-459(2009). RN [27] RP CAUTION, AND RETRACTION NOTICE OF PUBMED:19377461. RX PubMed=24336203; DOI=10.1038/nature12896; RA Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., RA Kitagawa H., Kato S.; RT "Retraction: GlcNAcylation of a histone methyltransferase in retinoic-acid- RT induced granulopoiesis."; RL Nature 505:574-574(2014). RN [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [29] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [30] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-22; THR-320 AND RP SER-325, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [32] RP INTERACTION WITH DAB2. RX PubMed=19581931; DOI=10.1038/onc.2009.157; RA Jiang Y., Luo W., Howe P.H.; RT "Dab2 stabilizes Axin and attenuates Wnt/beta-catenin signaling by RT preventing protein phosphatase 1 (PP1)-Axin interactions."; RL Oncogene 28:2999-3007(2009). RN [33] RP IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, AND INTERACTION WITH RP WDR82; PPP1R8 AND PPP1R10/PNUTS. RX PubMed=20516061; DOI=10.1074/jbc.m110.109801; RA Lee J.H., You J., Dobrota E., Skalnik D.G.; RT "Identification and characterization of a novel human PP1 phosphatase RT complex."; RL J. Biol. Chem. 285:24466-24476(2010). RN [34] RP INTERACTION WITH TRIM28. RX PubMed=20424263; DOI=10.1126/scisignal.2000781; RA Li X., Lin H.H., Chen H., Xu X., Shih H.M., Ann D.K.; RT "SUMOylation of the transcriptional co-repressor KAP1 is regulated by the RT serine and threonine phosphatase PP1."; RL Sci. Signal. 3:RA32-RA32(2010). RN [35] RP FUNCTION IN CIRCADIAN CLOCK. RX PubMed=21712997; DOI=10.1371/journal.pone.0021325; RA Schmutz I., Wendt S., Schnell A., Kramer A., Mansuy I.M., Albrecht U.; RT "Protein phosphatase 1 (PP1) is a post-translational regulator of the RT mammalian circadian clock."; RL PLoS ONE 6:E21325-E21325(2011). RN [36] RP INTERACTION WITH PEAK1, PPP1CC AND SHC1, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=23846654; DOI=10.1038/nature12308; RA Zheng Y., Zhang C., Croucher D.R., Soliman M.A., St-Denis N., RA Pasculescu A., Taylor L., Tate S.A., Hardy W.R., Colwill K., Dai A.Y., RA Bagshaw R., Dennis J.W., Gingras A.C., Daly R.J., Pawson T.; RT "Temporal regulation of EGF signalling networks by the scaffold protein RT Shc1."; RL Nature 499:166-171(2013). RN [37] RP FUNCTION, INTERACTION WITH FOXP3, AND INDUCTION. RX PubMed=23396208; DOI=10.1038/nm.3085; RA Nie H., Zheng Y., Li R., Guo T.B., He D., Fang L., Liu X., Xiao L., RA Chen X., Wan B., Chin Y.E., Zhang J.Z.; RT "Phosphorylation of FOXP3 controls regulatory T cell function and is RT inhibited by TNF-alpha in rheumatoid arthritis."; RL Nat. Med. 19:322-328(2013). RN [38] RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH ATG16L1. RX PubMed=26083323; DOI=10.1080/15548627.2015.1060386; RA Song H., Pu J., Wang L., Wu L., Xiao J., Liu Q., Chen J., Zhang M., Liu Y., RA Ni M., Mo J., Zheng Y., Wan D., Cai X., Cao Y., Xiao W., Ye L., Tu E., RA Lin Z., Wen J., Lu X., He J., Peng Y., Su J., Zhang H., Zhao Y., Lin M., RA Zhang Z.; RT "ATG16L1 phosphorylation is oppositely regulated by CSNK2/casein kinase 2 RT and PPP1/protein phosphatase 1 which determines the fate of cardiomyocytes RT during hypoxia/reoxygenation."; RL Autophagy 11:1308-1325(2015). RN [39] RP FUNCTION, AND INTERACTION WITH CENPA. RX PubMed=25556658; DOI=10.1016/j.devcel.2014.11.030; RA Yu Z., Zhou X., Wang W., Deng W., Fang J., Hu H., Wang Z., Li S., Cui L., RA Shen J., Zhai L., Peng S., Wong J., Dong S., Yuan Z., Ou G., Zhang X., RA Xu P., Lou J., Yang N., Chen P., Xu R.M., Li G.; RT "Dynamic phosphorylation of CENP-A at Ser68 orchestrates its cell-cycle- RT dependent deposition at centromeres."; RL Dev. Cell 32:68-81(2015). RN [40] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [41] RP INTERACTION WITH VENEZUELAN EQUINE ENCEPHALITIS VIRUS CAPSID PROTEIN RP (MICROBIAL INFECTION), SUBCELLULAR LOCATION (MICROBIAL INFECTION), AND RP FUNCTION (MICROBIAL INFECTION). RX PubMed=29769351; DOI=10.1128/jvi.02068-17; RA Carey B.D., Ammosova T., Pinkham C., Lin X., Zhou W., Liotta L.A., RA Nekhai S., Kehn-Hall K.; RT "Protein phosphatase 1alpha interacts with Venezuelan equine encephalitis RT virus capsid protein and regulates viral replication through modulation of RT capsid phosphorylation."; RL J. Virol. 92:0-0(2018). RN [42] RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 7-300 IN COMPLEX WITH INHIBITORS, RP COFACTOR, MANGANESE-BINDING SITES, AND SUBUNIT. RX PubMed=18992256; DOI=10.1016/j.jmb.2008.10.053; RA Kelker M.S., Page R., Peti W.; RT "Crystal structures of protein phosphatase-1 bound to nodularin-R and RT tautomycin: a novel scaffold for structure-based drug design of RT serine/threonine phosphatase inhibitors."; RL J. Mol. Biol. 385:11-21(2009). RN [43] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 7-330 IN COMPLEX WITH RAT PPP1R9A RP AND PPP1R9B. RX PubMed=20305656; DOI=10.1038/nsmb.1786; RA Ragusa M.J., Dancheck B., Critton D.A., Nairn A.C., Page R., Peti W.; RT "Spinophilin directs protein phosphatase 1 specificity by blocking RT substrate binding sites."; RL Nat. Struct. Mol. Biol. 17:459-464(2010). RN [44] {ECO:0007744|PDB:4XPN} RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 552-591, AND INTERACTION WITH RP PPP1R15A. RX PubMed=26095357; DOI=10.1016/j.celrep.2015.05.043; RA Choy M.S., Yusoff P., Lee I.C., Newton J.C., Goh C.W., Page R., RA Shenolikar S., Peti W.; RT "Structural and Functional Analysis of the GADD34:PP1 eIF2alpha RT Phosphatase."; RL Cell Rep. 11:1885-1891(2015). CC -!- FUNCTION: Protein phosphatase that associates with over 200 regulatory CC proteins to form highly specific holoenzymes which dephosphorylate CC hundreds of biological targets. Protein phosphatase 1 (PP1) is CC essential for cell division, and participates in the regulation of CC glycogen metabolism, muscle contractility and protein synthesis. CC Involved in regulation of ionic conductances and long-term synaptic CC plasticity. May play an important role in dephosphorylating substrates CC such as the postsynaptic density-associated Ca(2+)/calmodulin dependent CC protein kinase II. Component of the PTW/PP1 phosphatase complex, which CC plays a role in the control of chromatin structure and cell cycle CC progression during the transition from mitosis into interphase. CC Regulates NEK2 function in terms of kinase activity and centrosome CC number and splitting, both in the presence and absence of radiation- CC induced DNA damage. Regulator of neural tube and optic fissure closure, CC and enteric neural crest cell (ENCCs) migration during development. In CC balance with CSNK1D and CSNK1E, determines the circadian period length, CC through the regulation of the speed and rhythmicity of PER1 and PER2 CC phosphorylation. May dephosphorylate CSNK1D and CSNK1E. CC Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells CC (Treg) from patients with rheumatoid arthritis, thereby inactivating CC FOXP3 and rendering Treg cells functionally defective CC (PubMed:23396208). Dephosphorylates CENPA (PubMed:25556658). CC Dephosphorylates the 'Ser-139' residue of ATG16L1 causing dissociation CC of ATG12-ATG5-ATG16L1 complex, thereby inhibiting autophagy CC (PubMed:26083323). {ECO:0000269|PubMed:17283141, CC ECO:0000269|PubMed:21712997, ECO:0000269|PubMed:23396208, CC ECO:0000269|PubMed:25556658, ECO:0000269|PubMed:26083323}. CC -!- FUNCTION: (Microbial infection) Necessary for alphaviruses replication. CC {ECO:0000269|PubMed:29769351}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC Evidence={ECO:0000269|PubMed:26083323}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC Evidence={ECO:0000269|PubMed:26083323}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; CC Note=Binds 1 Fe cation per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:18992256}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:18992256}; CC -!- ACTIVITY REGULATION: The phosphatase activity of the PPP1R15A-PP1 CC complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug CC that protects cells from endoplasmic reticulum stress. CC {ECO:0000269|PubMed:15705855}. CC -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, CC which is folded into its native form by inhibitor 2 and glycogen CC synthetase kinase 3, and then complexed to one or several targeting or CC regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to CC myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, CC PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. Interacts CC with PPP1R39 (By similarity). Interacts with BTBD10 (By similarity). CC Interacts with KCTD20 (By similarity). Interacts with PPP1R9A and CC PPP1R9B. Part of a complex containing PPP1R15B, PP1 and NCK1/2. CC Interacts with PHACTR4; which acts as an activator of PP1 activity (By CC similarity). Interacts with PPP1R15A and PPP1R15B; the interactions CC mediate binding to EIF2S1 (PubMed:26095357). Interacts with PPP1R7. CC Interacts with YLPM1. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, CC RBMX and NCOA5. Interacts with NOM1 and PPP1R8. Interacts with CC PPP1R16B. Interacts with RPSA only in the presence of PPP1R16B. CC Component of the PTW/PP1 phosphatase complex, composed of CC PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts CC with PPP1R10/PNUTS and PPP1R8. Interacts with WDR82 in the presence of CC PPP1R10/PNUTS. Interacts with TRIM28; the interaction dephosphorylates CC TRIM28 on 'Ser-824' and forms a complex at the p21 promoter site. CC Interacts with isoform 1 and isoform 4 of NEK2. Interacts with FER; CC this promotes phosphorylation at Thr-320. Interacts with DAB2; the CC interaction is mutually exclusive with the AXIN1:PPP1CA interaction. CC Interacts with FOXP3 (PubMed:23396208). Interacts with CENPA CC (PubMed:25556658). Interacts with ATG16L1 (PubMed:26083323). Found in a CC complex with PPP1CA, PPP1CC, SHC1 and PEAK1 (PubMed:23846654). CC Interacts with tensin TNS1 (PubMed:19826001). Interacts with SAXO4, CC PPP1R21, PPP1R26, PPP1R27, PPP1R35, PPP1R36, PPP1R37, SH3RF2, ELFN1 and CC ELFN2 (PubMed:19389623). {ECO:0000250|UniProtKB:P62137, CC ECO:0000250|UniProtKB:P62139, ECO:0000269|PubMed:11564868, CC ECO:0000269|PubMed:11739654, ECO:0000269|PubMed:12226088, CC ECO:0000269|PubMed:16263087, ECO:0000269|PubMed:16732323, CC ECO:0000269|PubMed:17283141, ECO:0000269|PubMed:17626005, CC ECO:0000269|PubMed:17890166, ECO:0000269|PubMed:17965019, CC ECO:0000269|PubMed:18992256, ECO:0000269|PubMed:19389623, CC ECO:0000269|PubMed:19581931, ECO:0000269|PubMed:19826001, CC ECO:0000269|PubMed:20305656, ECO:0000269|PubMed:20424263, CC ECO:0000269|PubMed:20516061, ECO:0000269|PubMed:23396208, CC ECO:0000269|PubMed:23846654, ECO:0000269|PubMed:25556658, CC ECO:0000269|PubMed:26083323, ECO:0000269|PubMed:9023344}. CC -!- SUBUNIT: (Microbial infection) Interacts with HHV-1 ICP34.5. CC {ECO:0000269|PubMed:9023344}. CC -!- SUBUNIT: (Microbial infection) Interacts with Venezuelan equine CC encephalitis virus (VEEV) capsid protein; this interaction CC dephosphorylates the capsid protein, which increases its ability to CC bind to the viral genome. {ECO:0000269|PubMed:29769351}. CC -!- INTERACTION: CC P62136; Q6ZMQ8: AATK; NbExp=3; IntAct=EBI-357253, EBI-2008380; CC P62136; P31749: AKT1; NbExp=4; IntAct=EBI-357253, EBI-296087; CC P62136; O14727: APAF1; NbExp=2; IntAct=EBI-357253, EBI-446492; CC P62136; P05067: APP; NbExp=3; IntAct=EBI-357253, EBI-77613; CC P62136; O15169: AXIN1; NbExp=4; IntAct=EBI-357253, EBI-710484; CC P62136; P38398: BRCA1; NbExp=2; IntAct=EBI-357253, EBI-349905; CC P62136; O95400: CD2BP2; NbExp=2; IntAct=EBI-357253, EBI-768015; CC P62136; Q99459: CDC5L; NbExp=2; IntAct=EBI-357253, EBI-374880; CC P62136; P12830: CDH1; NbExp=2; IntAct=EBI-357253, EBI-727477; CC P62136; Q8TEP8: CEP192; NbExp=2; IntAct=EBI-357253, EBI-2339778; CC P62136; Q9NX63: CHCHD3; NbExp=2; IntAct=EBI-357253, EBI-743375; CC P62136; Q6PJW8: CNST; NbExp=4; IntAct=EBI-357253, EBI-750390; CC P62136; Q96S65: CSRNP1; NbExp=8; IntAct=EBI-357253, EBI-4311573; CC P62136; Q9H175: CSRNP2; NbExp=10; IntAct=EBI-357253, EBI-5235958; CC P62136; Q92796: DLG3; NbExp=2; IntAct=EBI-357253, EBI-80440; CC P62136; P05198: EIF2S1; NbExp=2; IntAct=EBI-357253, EBI-1056162; CC P62136; P55199: ELL; NbExp=2; IntAct=EBI-357253, EBI-1245868; CC P62136; Q9BZS1: FOXP3; NbExp=2; IntAct=EBI-357253, EBI-983719; CC P62136; P42858: HTT; NbExp=10; IntAct=EBI-357253, EBI-466029; CC P62136; Q8NI77: KIF18A; NbExp=3; IntAct=EBI-357253, EBI-355426; CC P62136; Q8NG31: KNL1; NbExp=2; IntAct=EBI-357253, EBI-1001161; CC P62136; Q5S007: LRRK2; NbExp=6; IntAct=EBI-357253, EBI-5323863; CC P62136; O00566: MPHOSPH10; NbExp=2; IntAct=EBI-357253, EBI-5235884; CC P62136; Q96QC0: PPP1R10; NbExp=4; IntAct=EBI-357253, EBI-1210346; CC P62136; Q96KQ4: PPP1R13B; NbExp=11; IntAct=EBI-357253, EBI-1105153; CC P62136; Q8WUF5: PPP1R13L; NbExp=8; IntAct=EBI-357253, EBI-5550163; CC P62136; O75807: PPP1R15A; NbExp=12; IntAct=EBI-357253, EBI-714746; CC P62136; Q5SWA1: PPP1R15B; NbExp=5; IntAct=EBI-357253, EBI-2815482; CC P62136; Q96T49: PPP1R16B; NbExp=4; IntAct=EBI-357253, EBI-10293968; CC P62136; Q6NYC8: PPP1R18; NbExp=5; IntAct=EBI-357253, EBI-2557469; CC P62136; P41236: PPP1R2; NbExp=11; IntAct=EBI-357253, EBI-1056517; CC P62136; Q5T8A7: PPP1R26; NbExp=2; IntAct=EBI-357253, EBI-308500; CC P62136; Q86WC6: PPP1R27; NbExp=5; IntAct=EBI-357253, EBI-5235602; CC P62136; Q6NXS1: PPP1R2B; NbExp=3; IntAct=EBI-357253, EBI-10251630; CC P62136; O14990: PPP1R2C; NbExp=3; IntAct=EBI-357253, EBI-12404293; CC P62136; O75864: PPP1R37; NbExp=5; IntAct=EBI-357253, EBI-5235692; CC P62136; Q86XI6: PPP1R3B; NbExp=4; IntAct=EBI-357253, EBI-3918864; CC P62136; Q9UQK1: PPP1R3C; NbExp=5; IntAct=EBI-357253, EBI-2506727; CC P62136; O95685: PPP1R3D; NbExp=3; IntAct=EBI-357253, EBI-1045661; CC P62136; Q15435: PPP1R7; NbExp=7; IntAct=EBI-357253, EBI-1024281; CC P62136; Q12972: PPP1R8; NbExp=7; IntAct=EBI-357253, EBI-716633; CC P62136; Q12972-1: PPP1R8; NbExp=6; IntAct=EBI-357253, EBI-16012257; CC P62136; Q12972-2: PPP1R8; NbExp=7; IntAct=EBI-357253, EBI-12252736; CC P62136; Q96SB3: PPP1R9B; NbExp=6; IntAct=EBI-357253, EBI-351275; CC P62136; P60484: PTEN; NbExp=2; IntAct=EBI-357253, EBI-696162; CC P62136; P06400: RB1; NbExp=2; IntAct=EBI-357253, EBI-491274; CC P62136; Q5UIP0: RIF1; NbExp=4; IntAct=EBI-357253, EBI-711331; CC P62136; Q14684: RRP1B; NbExp=3; IntAct=EBI-357253, EBI-372051; CC P62136; P04271: S100B; NbExp=3; IntAct=EBI-357253, EBI-458391; CC P62136; Q7Z5V6: SAXO4; NbExp=3; IntAct=EBI-357253, EBI-4311771; CC P62136; A8K8P3: SFI1; NbExp=2; IntAct=EBI-357253, EBI-743371; CC P62136; Q562F6: SGO2; NbExp=4; IntAct=EBI-357253, EBI-989213; CC P62136; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-357253, EBI-747035; CC P62136; Q8TEC5: SH3RF2; NbExp=3; IntAct=EBI-357253, EBI-2130111; CC P62136; P63208: SKP1; NbExp=3; IntAct=EBI-357253, EBI-307486; CC P62136; Q7Z699: SPRED1; NbExp=4; IntAct=EBI-357253, EBI-5235340; CC P62136; P43405-2: SYK; NbExp=3; IntAct=EBI-357253, EBI-25892332; CC P62136; Q9HCH5: SYTL2; NbExp=2; IntAct=EBI-357253, EBI-2690103; CC P62136; Q14C87: TMEM132D; NbExp=2; IntAct=EBI-357253, EBI-5235567; CC P62136; Q5JTV8: TOR1AIP1; NbExp=2; IntAct=EBI-357253, EBI-2559665; CC P62136; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-357253, EBI-11952721; CC P62136; Q13625: TP53BP2; NbExp=9; IntAct=EBI-357253, EBI-77642; CC P62136; Q4KMQ1: TPRN; NbExp=3; IntAct=EBI-357253, EBI-3942777; CC P62136; Q4KMQ1-2: TPRN; NbExp=6; IntAct=EBI-357253, EBI-11978969; CC P62136; Q8TEL6: TRPC4AP; NbExp=2; IntAct=EBI-357253, EBI-2559060; CC P62136; P49815: TSC2; NbExp=2; IntAct=EBI-357253, EBI-396587; CC P62136; P55072: VCP; NbExp=2; IntAct=EBI-357253, EBI-355164; CC P62136; Q9Y2W2: WBP11; NbExp=4; IntAct=EBI-357253, EBI-714455; CC P62136; Q9H4A3: WNK1; NbExp=2; IntAct=EBI-357253, EBI-457907; CC P62136; P16989: YBX3; NbExp=3; IntAct=EBI-357253, EBI-358193; CC P62136; P49750: YLPM1; NbExp=3; IntAct=EBI-357253, EBI-712871; CC P62136; Q9HBF4: ZFYVE1; NbExp=2; IntAct=EBI-357253, EBI-4401611; CC P62136; O95405: ZFYVE9; NbExp=3; IntAct=EBI-357253, EBI-296817; CC P62136; O08785: Clock; Xeno; NbExp=2; IntAct=EBI-357253, EBI-79859; CC P62136; P36313: ICP34.5; Xeno; NbExp=4; IntAct=EBI-357253, EBI-6149234; CC P62136; K9N4V7: N; Xeno; NbExp=3; IntAct=EBI-357253, EBI-25592177; CC P62136; Q76TK5: ORF23; Xeno; NbExp=2; IntAct=EBI-357253, EBI-14033469; CC P62136; O35867: Ppp1r9a; Xeno; NbExp=3; IntAct=EBI-357253, EBI-7092421; CC P62136; O35274: Ppp1r9b; Xeno; NbExp=8; IntAct=EBI-357253, EBI-80022; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11739654, CC ECO:0000269|PubMed:29769351}. Nucleus {ECO:0000269|PubMed:11739654, CC ECO:0000269|PubMed:17965019}. Nucleus, nucleoplasm CC {ECO:0000269|PubMed:11739654, ECO:0000269|PubMed:17965019}. Nucleus, CC nucleolus {ECO:0000269|PubMed:11739654, ECO:0000269|PubMed:17965019}. CC Note=Primarily nuclear and largely excluded from the nucleolus. Highly CC mobile in cells and can be relocalized through interaction with CC targeting subunits. NOM1 plays a role in targeting this protein to the CC nucleolus. In the presence of PPP1R8 relocalizes from the nucleus to CC nuclear speckles. Shuttles toward the cytosol during infection with CC VEEV (PubMed:29769351). {ECO:0000269|PubMed:29769351}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P62136-1; Sequence=Displayed; CC Name=2; CC IsoId=P62136-2; Sequence=VSP_043377; CC Name=3; CC IsoId=P62136-3; Sequence=VSP_046754; CC -!- INDUCTION: Up-regulated in synovial fluid mononuclear cells and CC peripheral blood mononuclear cells from patients with rheumatoid CC arthritis. {ECO:0000269|PubMed:23396208}. CC -!- PTM: Phosphorylated. Dephosphorylated at Thr-320 in the presence of CC ionizing radiation. {ECO:0000269|PubMed:16732323}. CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily. CC {ECO:0000305}. CC -!- CAUTION: Was originally thought to be part of the MLL5-L complex, at CC least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and CC OGT (PubMed:19377461). However, the corresponding article has been CC retracted (PubMed:24336203). {ECO:0000269|PubMed:19377461, CC ECO:0000269|PubMed:24336203}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The things we forget - Issue CC 32 of March 2003; CC URL="https://web.expasy.org/spotlight/back_issues/032"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X70848; CAA50197.1; -; mRNA. DR EMBL; S57501; AAB26015.1; -; mRNA. DR EMBL; M63960; AAA36508.1; -; mRNA. DR EMBL; AK313586; BAG36355.1; -; mRNA. DR EMBL; BT006629; AAP35275.1; -; mRNA. DR EMBL; AP003419; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001888; AAH01888.1; -; mRNA. DR EMBL; BC004482; AAH04482.1; -; mRNA. DR EMBL; BC008010; AAH08010.1; -; mRNA. DR EMBL; J04759; AAA36475.1; -; mRNA. DR CCDS; CCDS31618.1; -. [P62136-2] DR CCDS; CCDS8160.1; -. [P62136-1] DR CCDS; CCDS8161.1; -. [P62136-3] DR RefSeq; NP_001008709.1; NM_001008709.1. [P62136-2] DR RefSeq; NP_002699.1; NM_002708.3. [P62136-1] DR RefSeq; NP_996756.1; NM_206873.1. [P62136-3] DR PDB; 3E7A; X-ray; 1.63 A; A/B=7-300. DR PDB; 3E7B; X-ray; 1.70 A; A/B=7-300. DR PDB; 3EGG; X-ray; 1.85 A; A/B=7-330. DR PDB; 3EGH; X-ray; 2.00 A; A/B=7-330. DR PDB; 3HVQ; X-ray; 2.20 A; A/B=7-330. DR PDB; 3N5U; X-ray; 3.20 A; A/B=1-300. DR PDB; 3V4Y; X-ray; 2.10 A; A/C/E/G=7-307. DR PDB; 4G9J; X-ray; 3.10 A; A/B=1-330. DR PDB; 4MOV; X-ray; 1.45 A; A/B=7-300. DR PDB; 4MOY; X-ray; 2.20 A; A=7-300. DR PDB; 4MP0; X-ray; 2.10 A; A/C=7-300. DR PDB; 4XPN; X-ray; 2.29 A; A/C=7-300. DR PDB; 5IOH; X-ray; 2.57 A; A/C=7-300. DR PDB; 6ALZ; X-ray; 2.21 A; A/B=7-300. DR PDB; 6CZO; X-ray; 2.95 A; A/C=7-300. DR PDB; 6DCX; X-ray; 3.41 A; A/B=1-330. DR PDB; 6DNO; X-ray; 1.45 A; A=7-300. DR PDB; 6G0I; X-ray; 2.00 A; A=1-330. DR PDB; 6G0J; X-ray; 2.10 A; A=1-330. DR PDB; 6GHM; X-ray; 2.15 A; A/B=7-330. DR PDB; 6OBN; X-ray; 2.70 A; A/B=1-300. DR PDB; 6OBP; X-ray; 2.70 A; A=1-300. DR PDB; 6OBQ; X-ray; 1.84 A; A/B=7-300. DR PDB; 6OBR; X-ray; 1.50 A; A/B=7-300. DR PDB; 6OBS; X-ray; 1.80 A; A/B=7-300. DR PDB; 6OBU; X-ray; 1.95 A; A/B=7-300. DR PDB; 6ZEE; X-ray; 1.90 A; A/B/I/K/P/Q=7-300. DR PDB; 6ZEF; X-ray; 1.94 A; A/B=7-300. DR PDB; 6ZEG; X-ray; 1.09 A; A/B=7-304. DR PDB; 6ZEH; X-ray; 1.30 A; A/B=7-304. DR PDB; 6ZEI; X-ray; 1.39 A; A/B=7-304. DR PDB; 6ZEJ; X-ray; 1.78 A; A/D/F/I/L/O=7-304. DR PDB; 6ZK6; X-ray; 1.90 A; A=1-330. DR PDB; 7QFB; X-ray; 2.05 A; A=7-300. DR PDB; 7QM2; X-ray; 2.69 A; A/C=7-300. DR PDB; 7T0Y; X-ray; 1.80 A; A/C=7-300. DR PDB; 7TVF; X-ray; 2.17 A; C/F=2-330. DR PDB; 7TXH; X-ray; 1.95 A; C/F=7-300. DR PDB; 7UPI; EM; 2.89 A; B=1-330. DR PDB; 8DWK; X-ray; 2.50 A; A/B=7-300. DR PDB; 8DWL; X-ray; 2.00 A; A/C=7-300. DR PDB; 8U5G; X-ray; 3.20 A; A=7-300. DR PDBsum; 3E7A; -. DR PDBsum; 3E7B; -. DR PDBsum; 3EGG; -. DR PDBsum; 3EGH; -. DR PDBsum; 3HVQ; -. DR PDBsum; 3N5U; -. DR PDBsum; 3V4Y; -. DR PDBsum; 4G9J; -. DR PDBsum; 4MOV; -. DR PDBsum; 4MOY; -. DR PDBsum; 4MP0; -. DR PDBsum; 4XPN; -. DR PDBsum; 5IOH; -. DR PDBsum; 6ALZ; -. DR PDBsum; 6CZO; -. DR PDBsum; 6DCX; -. DR PDBsum; 6DNO; -. DR PDBsum; 6G0I; -. DR PDBsum; 6G0J; -. DR PDBsum; 6GHM; -. DR PDBsum; 6OBN; -. DR PDBsum; 6OBP; -. DR PDBsum; 6OBQ; -. DR PDBsum; 6OBR; -. DR PDBsum; 6OBS; -. DR PDBsum; 6OBU; -. DR PDBsum; 6ZEE; -. DR PDBsum; 6ZEF; -. DR PDBsum; 6ZEG; -. DR PDBsum; 6ZEH; -. DR PDBsum; 6ZEI; -. DR PDBsum; 6ZEJ; -. DR PDBsum; 6ZK6; -. DR PDBsum; 7QFB; -. DR PDBsum; 7QM2; -. DR PDBsum; 7T0Y; -. DR PDBsum; 7TVF; -. DR PDBsum; 7TXH; -. DR PDBsum; 7UPI; -. DR PDBsum; 8DWK; -. DR PDBsum; 8DWL; -. DR PDBsum; 8U5G; -. DR AlphaFoldDB; P62136; -. DR EMDB; EMD-26667; -. DR SASBDB; P62136; -. DR SMR; P62136; -. DR BioGRID; 111493; 627. DR CORUM; P62136; -. DR DIP; DIP-221N; -. DR DIP; DIP-38195N; -. DR ELM; P62136; -. DR IntAct; P62136; 444. DR MINT; P62136; -. DR STRING; 9606.ENSP00000326031; -. DR BindingDB; P62136; -. DR ChEMBL; CHEMBL2164; -. DR DrugBank; DB02506; 2,6,8-Trimethyl-3-Amino-9-Benzyl-9-Methoxynonanoic Acid. DR MoonDB; P62136; Predicted. DR DEPOD; PPP1CA; -. DR GlyGen; P62136; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P62136; -. DR PhosphoSitePlus; P62136; -. DR SwissPalm; P62136; -. DR BioMuta; PPP1CA; -. DR DMDM; 49065811; -. DR OGP; P08129; -. DR EPD; P62136; -. DR jPOST; P62136; -. DR MassIVE; P62136; -. DR MaxQB; P62136; -. DR PaxDb; 9606-ENSP00000326031; -. DR PeptideAtlas; P62136; -. DR PRIDE; P62136; -. DR ProteomicsDB; 1632; -. DR ProteomicsDB; 57365; -. [P62136-1] DR ProteomicsDB; 57366; -. [P62136-2] DR Pumba; P62136; -. DR TopDownProteomics; P62136-1; -. [P62136-1] DR Antibodypedia; 3872; 682 antibodies from 40 providers. DR DNASU; 5499; -. DR Ensembl; ENST00000312989.11; ENSP00000326031.7; ENSG00000172531.16. [P62136-2] DR Ensembl; ENST00000358239.8; ENSP00000350974.4; ENSG00000172531.16. [P62136-3] DR Ensembl; ENST00000376745.9; ENSP00000365936.4; ENSG00000172531.16. [P62136-1] DR GeneID; 5499; -. DR KEGG; hsa:5499; -. DR MANE-Select; ENST00000376745.9; ENSP00000365936.4; NM_002708.4; NP_002699.1. DR UCSC; uc001oku.2; human. [P62136-1] DR AGR; HGNC:9281; -. DR CTD; 5499; -. DR DisGeNET; 5499; -. DR GeneCards; PPP1CA; -. DR HGNC; HGNC:9281; PPP1CA. DR HPA; ENSG00000172531; Low tissue specificity. DR MIM; 176875; gene. DR neXtProt; NX_P62136; -. DR OpenTargets; ENSG00000172531; -. DR PharmGKB; PA33609; -. DR VEuPathDB; HostDB:ENSG00000172531; -. DR eggNOG; KOG0374; Eukaryota. DR GeneTree; ENSGT00940000153472; -. DR HOGENOM; CLU_004962_8_1_1; -. DR InParanoid; P62136; -. DR OMA; YLVMESR; -. DR OrthoDB; 19833at2759; -. DR PhylomeDB; P62136; -. DR TreeFam; TF354243; -. DR BRENDA; 3.1.3.16; 2681. DR PathwayCommons; P62136; -. DR Reactome; R-HSA-163560; Triglyceride catabolism. DR Reactome; R-HSA-180024; DARPP-32 events. DR Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling. DR Reactome; R-HSA-400253; Circadian Clock. DR SignaLink; P62136; -. DR SIGNOR; P62136; -. DR BioGRID-ORCS; 5499; 435 hits in 1183 CRISPR screens. DR ChiTaRS; PPP1CA; human. DR EvolutionaryTrace; P62136; -. DR GeneWiki; PPP1CA; -. DR GenomeRNAi; 5499; -. DR Pharos; P62136; Tchem. DR PRO; PR:P62136; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P62136; Protein. DR Bgee; ENSG00000172531; Expressed in endometrium epithelium and 203 other cell types or tissues. DR ExpressionAtlas; P62136; baseline and differential. DR GO; GO:0005912; C:adherens junction; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0042587; C:glycogen granule; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0043204; C:perikaryon; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0098793; C:presynapse; IEA:Ensembl. DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; IDA:UniProtKB. DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; IDA:BHF-UCL. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB. DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:ParkinsonsUK-UCL. DR GO; GO:0008157; F:protein phosphatase 1 binding; IEA:Ensembl. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central. DR GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:Ensembl. DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Ensembl. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB. DR GO; GO:0016311; P:dephosphorylation; IDA:CACAO. DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB. DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW. DR GO; GO:0030324; P:lung development; IEA:Ensembl. DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl. DR GO; GO:0006470; P:protein dephosphorylation; IMP:CACAO. DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IC:ParkinsonsUK-UCL. DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB. DR GO; GO:0005979; P:regulation of glycogen biosynthetic process; IEA:Ensembl. DR GO; GO:0005981; P:regulation of glycogen catabolic process; IEA:Ensembl. DR GO; GO:0006446; P:regulation of translational initiation; ISS:ParkinsonsUK-UCL. DR GO; GO:0010288; P:response to lead ion; ISS:ARUK-UCL. DR CDD; cd07414; MPP_PP1_PPKL; 1. DR Gene3D; 3.60.21.10; -; 1. DR IDEAL; IID00311; -. DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase. DR InterPro; IPR031675; STPPase_N. DR PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR11668:SF377; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1-ALPHA CATALYTIC SUBUNIT; 1. DR Pfam; PF00149; Metallophos; 1. DR Pfam; PF16891; STPPase_N; 1. DR PRINTS; PR00114; STPHPHTASE. DR SMART; SM00156; PP2Ac; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. DR Genevisible; P62136; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Carbohydrate metabolism; KW Cell cycle; Cell division; Cytoplasm; Direct protein sequencing; KW Glycogen metabolism; Host-virus interaction; Hydrolase; Manganese; KW Metal-binding; Nucleus; Phosphoprotein; Protein phosphatase; KW Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:22814378" FT CHAIN 2..330 FT /note="Serine/threonine-protein phosphatase PP1-alpha FT catalytic subunit" FT /id="PRO_0000058774" FT REGION 306..330 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 125 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 64 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 66 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 92 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 92 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 92 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT BINDING 124 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 124 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT BINDING 173 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 173 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT BINDING 248 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 248 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:22814378" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 22 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 305 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62137" FT MOD_RES 306 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P62137" FT MOD_RES 320 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:16732323, FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 325 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 18 FT /note="E -> EGSRVLTPHCAP (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8384581" FT /id="VSP_043377" FT VAR_SEQ 19..62 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_046754" FT HELIX 9..18 FT /evidence="ECO:0007829|PDB:6ZEG" FT HELIX 19..21 FT /evidence="ECO:0007829|PDB:6ZEG" FT HELIX 32..48 FT /evidence="ECO:0007829|PDB:6ZEG" FT STRAND 51..55 FT /evidence="ECO:0007829|PDB:6ZEG" FT STRAND 57..62 FT /evidence="ECO:0007829|PDB:6ZEG" FT HELIX 69..79 FT /evidence="ECO:0007829|PDB:6ZEG" FT STRAND 87..89 FT /evidence="ECO:0007829|PDB:6ZEG" FT STRAND 94..98 FT /evidence="ECO:0007829|PDB:6ZEG" FT HELIX 100..113 FT /evidence="ECO:0007829|PDB:6ZEG" FT TURN 115..117 FT /evidence="ECO:0007829|PDB:6ZEG" FT STRAND 118..120 FT /evidence="ECO:0007829|PDB:6ZEG" FT HELIX 124..126 FT /evidence="ECO:0007829|PDB:6ALZ" FT HELIX 128..131 FT /evidence="ECO:0007829|PDB:6ZEG" FT TURN 132..135 FT /evidence="ECO:0007829|PDB:4G9J" FT HELIX 136..143 FT /evidence="ECO:0007829|PDB:6ZEG" FT HELIX 146..156 FT /evidence="ECO:0007829|PDB:6ZEG" FT STRAND 162..165 FT /evidence="ECO:0007829|PDB:6ZEG" FT TURN 166..168 FT /evidence="ECO:0007829|PDB:6ZEG" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:6ZEG" FT HELIX 183..187 FT /evidence="ECO:0007829|PDB:6ZEG" FT STRAND 197..199 FT /evidence="ECO:0007829|PDB:6ZEG" FT HELIX 200..206 FT /evidence="ECO:0007829|PDB:6ZEG" FT STRAND 214..218 FT /evidence="ECO:0007829|PDB:6ZEG" FT STRAND 222..227 FT /evidence="ECO:0007829|PDB:6ZEG" FT HELIX 229..239 FT /evidence="ECO:0007829|PDB:6ZEG" FT STRAND 242..246 FT /evidence="ECO:0007829|PDB:6ZEG" FT STRAND 248..251 FT /evidence="ECO:0007829|PDB:8DWL" FT STRAND 254..258 FT /evidence="ECO:0007829|PDB:6ZEG" FT TURN 259..262 FT /evidence="ECO:0007829|PDB:6ZEG" FT STRAND 263..267 FT /evidence="ECO:0007829|PDB:6ZEG" FT HELIX 272..274 FT /evidence="ECO:0007829|PDB:6ZEG" FT STRAND 280..285 FT /evidence="ECO:0007829|PDB:6ZEG" FT STRAND 290..297 FT /evidence="ECO:0007829|PDB:6ZEG" SQ SEQUENCE 330 AA; 37512 MW; 60C37E1AD9831DAC CRC64; MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVQGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAD KNKGKYGQFS GLNPGGRPIT PPRNSAKAKK //