GenomeNet

Database: UniProt
Entry: PP1A_HUMAN
LinkDB: PP1A_HUMAN
Original site: PP1A_HUMAN 
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   13-NOV-2019, entry version 175.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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-
RT   encoding 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
RT   type 1 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT   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.,
RA   Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA   FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA   Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA   Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA   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
RT   project: 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
RP   METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
RP   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
RT   catalytic 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
RP   (MICROBIAL 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
RT   protein phosphatase 1alpha to dephosphorylate the alpha subunit of the
RT   eukaryotic translation initiation factor 2 and preclude the shutoff of
RT   protein 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;
RA   Trinkle-Mulcahy L., Sleeman J.E., Lamond A.I.;
RT   "Dynamic targeting of protein phosphatase 1 within the nuclei of
RT   living 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
RT   novel signaling complex containing protein phosphatase 1 and inhibitor
RT   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;
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
RT   from 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.,
RA   Michaeli S., 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.,
RA   Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.;
RT   "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative
RT   nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-
RT   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
RT   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
RT   cycle-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
RP   BY 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
RP   BY 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   CAUTION.
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   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320, AND IDENTIFICATION
RP   BY 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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [26]
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.,
RA   Buerckstuemmer T., 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   [27]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [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.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-22; THR-320 AND
RP   SER-325, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [29]
RP   CAUTION, AND RETRACTION.
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-
RT   acid-induced granulopoiesis.";
RL   Nature 505:574-574(2014).
RN   [30]
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   [31]
RP   IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, AND INTERACTION
RP   WITH 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   [32]
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
RT   the serine and threonine phosphatase PP1.";
RL   Sci. Signal. 3:RA32-RA32(2010).
RN   [33]
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   [34]
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
RT   protein Shc1.";
RL   Nature 499:166-171(2013).
RN   [35]
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   [36]
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.,
RA   Liu Y., Ni M., Mo J., Zheng Y., Wan D., Cai X., Cao Y., Xiao W.,
RA   Ye L., Tu E., Lin Z., Wen J., Lu X., He J., Peng Y., Su J., Zhang H.,
RA   Zhao Y., Lin M., Zhang Z.;
RT   "ATG16L1 phosphorylation is oppositely regulated by CSNK2/casein
RT   kinase 2 and PPP1/protein phosphatase 1 which determines the fate of
RT   cardiomyocytes during hypoxia/reoxygenation.";
RL   Autophagy 11:1308-1325(2015).
RN   [37]
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.,
RA   Cui L., Shen J., Zhai L., Peng S., Wong J., Dong S., Yuan Z., Ou G.,
RA   Zhang X., Xu P., Lou J., Yang N., Chen P., Xu R.M., Li G.;
RT   "Dynamic phosphorylation of CENP-A at Ser68 orchestrates its cell-
RT   cycle-dependent deposition at centromeres.";
RL   Dev. Cell 32:68-81(2015).
RN   [38]
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.,
RA   Ayoub D., 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   [39]
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
RT   encephalitis virus capsid protein and regulates viral replication
RT   through modulation of capsid phosphorylation.";
RL   J. Virol. 92:0-0(2018).
RN   [40]
RP   X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 7-300 IN COMPLEX WITH
RP   INHIBITORS, 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   [41]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 7-330 IN COMPLEX WITH RAT
RP   PPP1R9A 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).
CC   -!- FUNCTION: Protein phosphatase that associates with over 200
CC       regulatory proteins to form highly specific holoenzymes which
CC       dephosphorylate hundreds of biological targets. Protein
CC       phosphatase 1 (PP1) is essential for cell division, and
CC       participates in the regulation of glycogen metabolism, muscle
CC       contractility and protein synthesis. Involved in regulation of
CC       ionic conductances and long-term synaptic plasticity. May play an
CC       important role in dephosphorylating substrates such as the
CC       postsynaptic density-associated Ca(2+)/calmodulin dependent
CC       protein kinase II. Component of the PTW/PP1 phosphatase complex,
CC       which plays a role in the control of chromatin structure and cell
CC       cycle progression during the transition from mitosis into
CC       interphase. Regulates NEK2 function in terms of kinase activity
CC       and centrosome number and splitting, both in the presence and
CC       absence of radiation-induced DNA damage. Regulator of neural tube
CC       and optic fissure closure, and enteric neural crest cell (ENCCs)
CC       migration during development. In balance with CSNK1D and CSNK1E,
CC       determines the circadian period length, through the regulation of
CC       the speed and rhythmicity of PER1 and PER2 phosphorylation. May
CC       dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418'
CC       residue of FOXP3 in regulatory T-cells (Treg) from patients with
CC       rheumatoid arthritis, thereby inactivating FOXP3 and rendering
CC       Treg cells functionally defective (PubMed:23396208).
CC       Dephosphorylates CENPA (PubMed:25556658). Dephosphorylates the
CC       'Ser-139' residue of ATG16L1 causing dissociation of ATG12-ATG5-
CC       ATG16L1 complex, thereby inhibiting autophagy (PubMed:26083323).
CC       {ECO:0000269|PubMed:17283141, ECO:0000269|PubMed:21712997,
CC       ECO:0000269|PubMed:23396208, ECO:0000269|PubMed:25556658,
CC       ECO:0000269|PubMed:26083323}.
CC   -!- FUNCTION: (Microbial infection) Necessary for alphaviruses
CC       replication. {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,
CC         ChEBI:CHEBI:43474, 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-
CC         [protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-
CC         COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977;
CC         EC=3.1.3.16; 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.
CC       {ECO:0000269|PubMed:18992256};
CC   -!- ACTIVITY REGULATION: The phosphatase activity of the PPP1R15A-PP1
CC       complex toward EIF2S1 is specifically inhibited by Salubrinal, a
CC       drug that protects cells from endoplasmic reticulum stress.
CC       {ECO:0000269|PubMed:15705855}.
CC   -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or
CC       PPP1CC, which is folded into its native form by inhibitor 2 and
CC       glycogen synthetase kinase 3, and then complexed to one or several
CC       targeting or regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C
CC       mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B
CC       (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate
CC       binding to glycogen. Interacts with PPP1R39 (By similarity).
CC       Interacts with BTBD10 (By similarity). Interacts with KCTD20 (By
CC       similarity). Interacts with PPP1R9A and PPP1R9B. Part of a complex
CC       containing PPP1R15B, PP1 and NCK1/2. Interacts with PHACTR4; which
CC       acts as an activator of PP1 activity (By similarity). Interacts
CC       with PPP1R15A and PPP1R15B; the interactions mediate binding to
CC       EIF2S1. Interacts with PPP1R7. Interacts with YLPM1. Forms a
CC       complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and NCOA5. Interacts
CC       with NOM1 and PPP1R8. Interacts with PPP1R16B. Interacts with RPSA
CC       only in the presence of PPP1R16B. Component of the PTW/PP1
CC       phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and
CC       PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R10/PNUTS and
CC       PPP1R8. Interacts with WDR82 in the presence of PPP1R10/PNUTS.
CC       Interacts with TRIM28; the interaction dephosphorylates TRIM28 on
CC       'Ser-824' and forms a complex at the p21 promoter site. Interacts
CC       with isoform 1 and isoform 4 of NEK2. Interacts with FER; this
CC       promotes phosphorylation at Thr-320. Interacts with DAB2; the
CC       interaction is mutually exclusive with the AXIN1:PPP1CA
CC       interaction. Interacts with FOXP3 (PubMed:23396208). Interacts
CC       with CENPA (PubMed:25556658). Interacts with ATG16L1
CC       (PubMed:26083323). Found in a complex with PPP1CA, PPP1CC, SHC1
CC       and PEAK1 (PubMed:23846654). {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:19581931,
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
CC       to bind to the viral genome. {ECO:0000269|PubMed:29769351}.
CC   -!- INTERACTION:
CC       Q6ZMQ8:AATK; NbExp=3; IntAct=EBI-357253, EBI-2008380;
CC       P31749:AKT1; NbExp=4; IntAct=EBI-357253, EBI-296087;
CC       O14727:APAF1; NbExp=2; IntAct=EBI-357253, EBI-446492;
CC       O15169:AXIN1; NbExp=4; IntAct=EBI-357253, EBI-710484;
CC       P38398:BRCA1; NbExp=2; IntAct=EBI-357253, EBI-349905;
CC       O95400:CD2BP2; NbExp=2; IntAct=EBI-357253, EBI-768015;
CC       Q99459:CDC5L; NbExp=2; IntAct=EBI-357253, EBI-374880;
CC       P12830:CDH1; NbExp=2; IntAct=EBI-357253, EBI-727477;
CC       Q8TEP8:CEP192; NbExp=2; IntAct=EBI-357253, EBI-2339778;
CC       Q9NX63:CHCHD3; NbExp=2; IntAct=EBI-357253, EBI-743375;
CC       O08785:Clock (xeno); NbExp=2; IntAct=EBI-357253, EBI-79859;
CC       Q6PJW8:CNST; NbExp=4; IntAct=EBI-357253, EBI-750390;
CC       Q96S65:CSRNP1; NbExp=7; IntAct=EBI-357253, EBI-4311573;
CC       Q9H175:CSRNP2; NbExp=9; IntAct=EBI-357253, EBI-5235958;
CC       Q92796:DLG3; NbExp=2; IntAct=EBI-357253, EBI-80440;
CC       P55199:ELL; NbExp=2; IntAct=EBI-357253, EBI-1245868;
CC       Q9BZS1:FOXP3; NbExp=2; IntAct=EBI-357253, EBI-983719;
CC       P36313:ICP34.5 (xeno); NbExp=4; IntAct=EBI-357253, EBI-6149234;
CC       Q8NI77:KIF18A; NbExp=3; IntAct=EBI-357253, EBI-355426;
CC       Q8NG31:KNL1; NbExp=2; IntAct=EBI-357253, EBI-1001161;
CC       Q5S007:LRRK2; NbExp=6; IntAct=EBI-357253, EBI-5323863;
CC       O00566:MPHOSPH10; NbExp=2; IntAct=EBI-357253, EBI-5235884;
CC       Q76TK5:ORF23 (xeno); NbExp=2; IntAct=EBI-357253, EBI-14033469;
CC       Q96QC0:PPP1R10; NbExp=4; IntAct=EBI-357253, EBI-1210346;
CC       Q96KQ4:PPP1R13B; NbExp=10; IntAct=EBI-357253, EBI-1105153;
CC       Q8WUF5:PPP1R13L; NbExp=8; IntAct=EBI-357253, EBI-5550163;
CC       O75807:PPP1R15A; NbExp=5; IntAct=EBI-357253, EBI-714746;
CC       Q5SWA1:PPP1R15B; NbExp=5; IntAct=EBI-357253, EBI-2815482;
CC       Q96T49:PPP1R16B; NbExp=3; IntAct=EBI-357253, EBI-10293968;
CC       Q6NYC8:PPP1R18; NbExp=5; IntAct=EBI-357253, EBI-2557469;
CC       P41236:PPP1R2; NbExp=11; IntAct=EBI-357253, EBI-1056517;
CC       Q5T8A7:PPP1R26; NbExp=2; IntAct=EBI-357253, EBI-308500;
CC       Q86WC6:PPP1R27; NbExp=6; IntAct=EBI-357253, EBI-5235602;
CC       Q6NXS1:PPP1R2B; NbExp=5; IntAct=EBI-357253, EBI-10251630;
CC       Q7Z5V6:PPP1R32; NbExp=3; IntAct=EBI-357253, EBI-4311771;
CC       O75864:PPP1R37; NbExp=5; IntAct=EBI-357253, EBI-5235692;
CC       Q86XI6:PPP1R3B; NbExp=3; IntAct=EBI-357253, EBI-3918864;
CC       Q9UQK1:PPP1R3C; NbExp=4; IntAct=EBI-357253, EBI-2506727;
CC       O95685:PPP1R3D; NbExp=3; IntAct=EBI-357253, EBI-1045661;
CC       Q15435:PPP1R7; NbExp=7; IntAct=EBI-357253, EBI-1024281;
CC       Q12972:PPP1R8; NbExp=7; IntAct=EBI-357253, EBI-716633;
CC       Q12972-1:PPP1R8; NbExp=6; IntAct=EBI-357253, EBI-16012257;
CC       Q12972-2:PPP1R8; NbExp=5; IntAct=EBI-357253, EBI-12252736;
CC       O35867:Ppp1r9a (xeno); NbExp=3; IntAct=EBI-357253, EBI-7092421;
CC       Q96SB3:PPP1R9B; NbExp=6; IntAct=EBI-357253, EBI-351275;
CC       O35274:Ppp1r9b (xeno); NbExp=8; IntAct=EBI-357253, EBI-80022;
CC       P60484:PTEN; NbExp=2; IntAct=EBI-357253, EBI-696162;
CC       P06400:RB1; NbExp=2; IntAct=EBI-357253, EBI-491274;
CC       Q5UIP0:RIF1; NbExp=4; IntAct=EBI-357253, EBI-711331;
CC       Q14684:RRP1B; NbExp=3; IntAct=EBI-357253, EBI-372051;
CC       A8K8P3:SFI1; NbExp=2; IntAct=EBI-357253, EBI-743371;
CC       Q562F6:SGO2; NbExp=4; IntAct=EBI-357253, EBI-989213;
CC       Q9H788:SH2D4A; NbExp=3; IntAct=EBI-357253, EBI-747035;
CC       Q8TEC5:SH3RF2; NbExp=3; IntAct=EBI-357253, EBI-2130111;
CC       P63208:SKP1; NbExp=3; IntAct=EBI-357253, EBI-307486;
CC       Q7Z699:SPRED1; NbExp=4; IntAct=EBI-357253, EBI-5235340;
CC       Q9HCH5:SYTL2; NbExp=2; IntAct=EBI-357253, EBI-2690103;
CC       Q14C87:TMEM132D; NbExp=2; IntAct=EBI-357253, EBI-5235567;
CC       Q5JTV8:TOR1AIP1; NbExp=2; IntAct=EBI-357253, EBI-2559665;
CC       Q13625:TP53BP2; NbExp=9; IntAct=EBI-357253, EBI-77642;
CC       Q4KMQ1:TPRN; NbExp=3; IntAct=EBI-357253, EBI-3942777;
CC       Q4KMQ1-2:TPRN; NbExp=3; IntAct=EBI-357253, EBI-11978969;
CC       Q8TEL6:TRPC4AP; NbExp=2; IntAct=EBI-357253, EBI-2559060;
CC       P49815:TSC2; NbExp=2; IntAct=EBI-357253, EBI-396587;
CC       P55072:VCP; NbExp=2; IntAct=EBI-357253, EBI-355164;
CC       Q9Y2W2:WBP11; NbExp=4; IntAct=EBI-357253, EBI-714455;
CC       Q9H4A3:WNK1; NbExp=2; IntAct=EBI-357253, EBI-457907;
CC       P16989:YBX3; NbExp=3; IntAct=EBI-357253, EBI-358193;
CC       P49750:YLPM1; NbExp=3; IntAct=EBI-357253, EBI-712871;
CC       Q9HBF4:ZFYVE1; NbExp=2; IntAct=EBI-357253, EBI-4401611;
CC       O95405:ZFYVE9; NbExp=3; IntAct=EBI-357253, EBI-296817;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11739654,
CC       ECO:0000269|PubMed:29769351}. Nucleus
CC       {ECO:0000269|PubMed:11739654, ECO:0000269|PubMed:17965019}.
CC       Nucleus, nucleoplasm {ECO:0000269|PubMed:11739654,
CC       ECO:0000269|PubMed:17965019}. Nucleus, nucleolus
CC       {ECO:0000269|PubMed:11739654, ECO:0000269|PubMed:17965019}.
CC       Note=Primarily nuclear and largely excluded from the nucleolus.
CC       Highly mobile in cells and can be relocalized through interaction
CC       with targeting subunits. NOM1 plays a role in targeting this
CC       protein to the nucleolus. In the presence of PPP1R8 relocalizes
CC       from the nucleus to nuclear speckles. Shuttles toward the cytosol
CC       during infection with VEEV (PubMed:29769351).
CC       {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         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=P62136-3; Sequence=VSP_046754;
CC         Note=No experimental confirmation available. Gene prediction
CC         based on EST data.;
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
CC       of 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,
CC       at least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1,
CC       ACTB and OGT (PubMed:19377461). However, the corresponding article
CC       has been retracted (PubMed:24336203).
CC       {ECO:0000269|PubMed:19377461, ECO:0000269|PubMed:24336203}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=The things we forget
CC       - Issue 32 of March 2003;
CC       URL="https://web.expasy.org/spotlight/back_issues/032";
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   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   SMR; P62136; -.
DR   BioGrid; 111493; 371.
DR   CORUM; P62136; -.
DR   DIP; DIP-221N; -.
DR   DIP; DIP-38195N; -.
DR   ELM; P62136; -.
DR   IntAct; P62136; 399.
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; P62136; -.
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; P62136; -.
DR   PeptideAtlas; P62136; -.
DR   PRIDE; P62136; -.
DR   ProteomicsDB; 1632; -.
DR   ProteomicsDB; 57365; -. [P62136-1]
DR   ProteomicsDB; 57366; -. [P62136-2]
DR   TopDownProteomics; P62136-1; -. [P62136-1]
DR   DNASU; 5499; -.
DR   Ensembl; ENST00000312989; ENSP00000326031; ENSG00000172531. [P62136-2]
DR   Ensembl; ENST00000358239; ENSP00000350974; ENSG00000172531. [P62136-3]
DR   Ensembl; ENST00000376745; ENSP00000365936; ENSG00000172531. [P62136-1]
DR   GeneID; 5499; -.
DR   KEGG; hsa:5499; -.
DR   UCSC; uc001oku.2; human. [P62136-1]
DR   CTD; 5499; -.
DR   DisGeNET; 5499; -.
DR   GeneCards; PPP1CA; -.
DR   HGNC; HGNC:9281; PPP1CA.
DR   HPA; CAB004545; -.
DR   HPA; HPA046833; -.
DR   MIM; 176875; gene.
DR   neXtProt; NX_P62136; -.
DR   OpenTargets; ENSG00000172531; -.
DR   PharmGKB; PA33609; -.
DR   eggNOG; ENOG410IN85; Eukaryota.
DR   eggNOG; ENOG410XPVF; LUCA.
DR   GeneTree; ENSGT00940000153472; -.
DR   HOGENOM; HOG000172697; -.
DR   InParanoid; P62136; -.
DR   KO; K06269; -.
DR   OMA; YLVMESR; -.
DR   OrthoDB; 766640at2759; -.
DR   PhylomeDB; P62136; -.
DR   TreeFam; TF354243; -.
DR   BRENDA; 3.1.3.16; 2681.
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   ChiTaRS; PPP1CA; human.
DR   EvolutionaryTrace; P62136; -.
DR   GeneWiki; PPP1CA; -.
DR   GenomeRNAi; 5499; -.
DR   Pharos; P62136; -.
DR   PRO; PR:P62136; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; ENSG00000172531; Expressed in 226 organ(s), highest expression level in endometrium epithelium.
DR   ExpressionAtlas; P62136; baseline and differential.
DR   Genevisible; P62136; HS.
DR   GO; GO:0005913; C:cell-cell 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:0000164; C:protein phosphatase type 1 complex; 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: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:1904886; P:beta-catenin destruction complex disassembly; ISS:ParkinsonsUK-UCL.
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:0032091; P:negative regulation of protein binding; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0070262; P:peptidyl-serine dephosphorylation; TAS:ARUK-UCL.
DR   GO; GO:0035970; P:peptidyl-threonine dephosphorylation; TAS:ARUK-UCL.
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:0036496; P:regulation of translational initiation by eIF2 alpha dephosphorylation; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0010288; P:response to lead ion; ISS:ARUK-UCL.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.21.10; -; 1.
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   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing;
KW   Carbohydrate metabolism; Cell cycle; Cell division; Complete proteome;
KW   Cytoplasm; Direct protein sequencing; Glycogen metabolism;
KW   Host-virus interaction; Hydrolase; Manganese; Metal-binding; Nucleus;
KW   Phosphoprotein; Protein phosphatase; Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:22814378,
FT                                ECO:0000269|Ref.8}.
FT   CHAIN         2    330       Serine/threonine-protein phosphatase PP1-
FT                                alpha catalytic subunit.
FT                                /FTId=PRO_0000058774.
FT   ACT_SITE    125    125       Proton donor. {ECO:0000250}.
FT   METAL        64     64       Manganese 1. {ECO:0000250}.
FT   METAL        66     66       Manganese 1. {ECO:0000250}.
FT   METAL        92     92       Manganese.
FT   METAL        92     92       Manganese 1. {ECO:0000250}.
FT   METAL        92     92       Manganese 2. {ECO:0000250}.
FT   METAL       124    124       Manganese.
FT   METAL       124    124       Manganese 2. {ECO:0000250}.
FT   METAL       173    173       Manganese.
FT   METAL       173    173       Manganese 2. {ECO:0000250}.
FT   METAL       248    248       Manganese.
FT   METAL       248    248       Manganese 2. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000244|PubMed:22814378,
FT                                ECO:0000269|Ref.8}.
FT   MOD_RES       2      2       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES      22     22       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     305    305       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P62137}.
FT   MOD_RES     306    306       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62137}.
FT   MOD_RES     320    320       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18088087,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000269|PubMed:16732323}.
FT   MOD_RES     325    325       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ      18     18       E -> EGSRVLTPHCAP (in isoform 2).
FT                                {ECO:0000303|PubMed:8384581}.
FT                                /FTId=VSP_043377.
FT   VAR_SEQ      19     62       Missing (in isoform 3). {ECO:0000305}.
FT                                /FTId=VSP_046754.
FT   HELIX         9     16       {ECO:0000244|PDB:6DNO}.
FT   HELIX        17     19       {ECO:0000244|PDB:6DNO}.
FT   HELIX        32     48       {ECO:0000244|PDB:6DNO}.
FT   STRAND       51     55       {ECO:0000244|PDB:6DNO}.
FT   STRAND       57     62       {ECO:0000244|PDB:6DNO}.
FT   HELIX        69     79       {ECO:0000244|PDB:6DNO}.
FT   STRAND       87     89       {ECO:0000244|PDB:6DNO}.
FT   STRAND       94     98       {ECO:0000244|PDB:6DNO}.
FT   HELIX       100    113       {ECO:0000244|PDB:6DNO}.
FT   TURN        115    117       {ECO:0000244|PDB:6DNO}.
FT   STRAND      118    120       {ECO:0000244|PDB:6DNO}.
FT   HELIX       124    126       {ECO:0000244|PDB:6ALZ}.
FT   HELIX       128    131       {ECO:0000244|PDB:6DNO}.
FT   TURN        132    135       {ECO:0000244|PDB:4G9J}.
FT   HELIX       136    143       {ECO:0000244|PDB:6DNO}.
FT   HELIX       146    156       {ECO:0000244|PDB:6DNO}.
FT   STRAND      162    165       {ECO:0000244|PDB:6DNO}.
FT   TURN        166    168       {ECO:0000244|PDB:6DNO}.
FT   STRAND      169    174       {ECO:0000244|PDB:6DNO}.
FT   HELIX       183    187       {ECO:0000244|PDB:6DNO}.
FT   STRAND      197    199       {ECO:0000244|PDB:6DNO}.
FT   HELIX       200    206       {ECO:0000244|PDB:6DNO}.
FT   STRAND      214    218       {ECO:0000244|PDB:6DNO}.
FT   STRAND      222    227       {ECO:0000244|PDB:6DNO}.
FT   HELIX       229    239       {ECO:0000244|PDB:6DNO}.
FT   STRAND      243    246       {ECO:0000244|PDB:6DNO}.
FT   STRAND      254    258       {ECO:0000244|PDB:6DNO}.
FT   TURN        259    262       {ECO:0000244|PDB:6DNO}.
FT   STRAND      263    267       {ECO:0000244|PDB:6DNO}.
FT   STRAND      274    276       {ECO:0000244|PDB:6DNO}.
FT   STRAND      280    285       {ECO:0000244|PDB:6DNO}.
FT   STRAND      290    298       {ECO:0000244|PDB:6DNO}.
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
//
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