Full text data of PPP1CB
PPP1CB
[Confidence: low (only semi-automatic identification from reviews)]
Serine/threonine-protein phosphatase PP1-beta catalytic subunit; PP-1B; PPP1CD; 3.1.3.16; 3.1.3.53
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Serine/threonine-protein phosphatase PP1-beta catalytic subunit; PP-1B; PPP1CD; 3.1.3.16; 3.1.3.53
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P62140
ID PP1B_HUMAN Reviewed; 327 AA.
AC P62140; B2R5V4; D6W565; P37140; Q5U087; Q6FG45;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Serine/threonine-protein phosphatase PP1-beta catalytic subunit;
DE Short=PP-1B;
DE Short=PPP1CD;
DE EC=3.1.3.16;
DE EC=3.1.3.53;
GN Name=PPP1CB;
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].
RX PubMed=8312365; DOI=10.1016/0167-4889(94)90138-4;
RA Barker H.M., Brewis N.D., Street A.J., Spurr N.K., Cohen P.T.W.;
RT "Three genes for protein phosphatase 1 map to different human
RT chromosomes: sequence, expression and gene localisation of protein
RT serine/threonine phosphatase 1 beta (PPP1CB).";
RL Biochim. Biophys. Acta 1220:212-218(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7796987; DOI=10.1007/s001250050306;
RA Prochazka M., Mochizuki H., Baier L.J., Cohen P.T.W., Bogardus C.;
RT "Molecular and linkage analysis of type-1 protein phosphatase
RT catalytic beta-subunit gene: lack of evidence for its major role in
RT insulin resistance in Pima Indians.";
RL Diabetologia 38:461-466(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Umbilical vein;
RX PubMed=10906760;
RX DOI=10.1002/1097-4644(2000)79:1<113::AID-JCB110>3.3.CO;2-0;
RA Verin A.D., Csortos C., Durbin S.D., Aydanyan A., Wang P.,
RA Patterson C.E., Garcia J.G.;
RT "Characterization of the protein phosphatase 1 catalytic subunit in
RT endothelium: involvement in contractile responses.";
RL J. Cell. Biochem. 79:113-125(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Endometrium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [11]
RP PROTEIN SEQUENCE OF 2-14, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [12]
RP INTERACTION WITH PPP1R12C.
RX PubMed=11399775; DOI=10.1074/jbc.M102615200;
RA Tan I., Ng C.H., Lim L., Leung T.;
RT "Phosphorylation of a novel myosin binding subunit of protein
RT phosphatase 1 reveals a conserved mechanism in the regulation of actin
RT cytoskeleton.";
RL J. Biol. Chem. 276:21209-21216(2001).
RN [13]
RP SUBCELLULAR LOCATION.
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 [14]
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 [15]
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 [16]
RP ENZYME 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 PPP1R16B.
RX PubMed=18586956; DOI=10.1152/ajplung.00325.2007;
RA Csortos C., Czikora I., Bogatcheva N.V., Adyshev D.M., Poirier C.,
RA Olah G., Verin A.D.;
RT "TIMAP is a positive regulator of pulmonary endothelial barrier
RT function.";
RL Am. J. Physiol. 295:L440-L450(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316, AND MASS
RP SPECTROMETRY.
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 [19]
RP IDENTIFICATION IN THE MLL5-L COMPLEX.
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 [20]
RP IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, FUNCTION, AND
RP INTERACTION WITH PPP1R8.
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 [21]
RP INTERACTION WITH NUAK1 AND PPP1R12A.
RX PubMed=20354225; DOI=10.1126/scisignal.2000616;
RA Zagorska A., Deak M., Campbell D.G., Banerjee S., Hirano M.,
RA Aizawa S., Prescott A.R., Alessi D.R.;
RT "New roles for the LKB1-NUAK pathway in controlling myosin phosphatase
RT complexes and cell adhesion.";
RL Sci. Signal. 3:RA25-RA25(2010).
RN [22]
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 [23]
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 [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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).
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 (PP1) is essential for cell division, it participates
CC in the regulation of glycogen metabolism, muscle contractility and
CC protein synthesis. Involved in regulation of ionic conductances
CC and long-term synaptic plasticity. Component of the PTW/PP1
CC phosphatase complex, which plays a role in the control of
CC chromatin structure and cell cycle progression during the
CC transition from mitosis into interphase.
CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC phosphate.
CC -!- CATALYTIC ACTIVITY: [Myosin light-chain] phosphate + H(2)O =
CC [myosin light-chain] + phosphate.
CC -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity).
CC -!- ENZYME REGULATION: Inhibited by the toxins okadaic acid,
CC tautomycin and microcystin Leu-Arg (By similarity). The
CC phosphatase activity of the PPP1R15A-PP1 complex toward EIF2S1 is
CC specifically inhibited by Salubrinal, a drug that protects cells
CC from endoplasmic reticulum stress.
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. The targeting or regulatory
CC subunits determine the substrate specificity of PP1. PPP1R12A,
CC PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in
CC skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F
CC (in brain) mediate binding to glycogen. Part of a complex
CC containing PPP1R15B, PP1 and NCK1/2 (By similarity). Component of
CC the MLL5-L complex, at least composed of KMT2E/MLL5, STK38,
CC PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R7
CC and PPP1R12C. PPP1R15A and PPP1R15B mediate binding to EIF2S1.
CC Interacts with PPP1R16B. Component of the PTW/PP1 phosphatase
CC complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or
CC PPP1CB or PPP1CC. Interacts with PPP1R8. Interacts with TRIM28;
CC the interaction is weak. Interacts with PPP1R12A and NUAK1; the
CC interaction is direct.
CC -!- INTERACTION:
CC P38398:BRCA1; NbExp=3; IntAct=EBI-352350, EBI-349905;
CC O08785:Clock (xeno); NbExp=2; IntAct=EBI-352350, EBI-79859;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleoplasm.
CC Nucleus, nucleolus. Note=Highly mobile in cells and can be
CC relocalized through interaction with targeting subunits. In the
CC presence of PPP1R8 relocalizes from the nucleus to nuclear
CC speckles.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The things we forget -
CC Issue 32 of March 2003;
CC URL="http://web.expasy.org/spotlight/back_issues/sptlt032.shtml";
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DR EMBL; X80910; CAA56870.1; -; mRNA.
DR EMBL; U11005; AAA85093.1; -; Genomic_DNA.
DR EMBL; U10998; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; U10999; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; U11000; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; U11001; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; U11002; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; U11003; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; U11004; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; AF092905; AAF01137.1; -; mRNA.
DR EMBL; CR542263; CAG47059.1; -; mRNA.
DR EMBL; CR542285; CAG47080.1; -; mRNA.
DR EMBL; BT019744; AAV38549.1; -; mRNA.
DR EMBL; AK312329; BAG35251.1; -; mRNA.
DR EMBL; BX647970; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC097724; AAY24124.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00527.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00528.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00529.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00530.1; -; Genomic_DNA.
DR EMBL; BC002697; AAH02697.1; -; mRNA.
DR EMBL; BC012045; AAH12045.1; -; mRNA.
DR PIR; S41052; S41052.
DR RefSeq; NP_002700.1; NM_002709.2.
DR RefSeq; NP_996759.1; NM_206876.1.
DR UniGene; Hs.702907; -.
DR ProteinModelPortal; P62140; -.
DR SMR; P62140; 1-308.
DR IntAct; P62140; 30.
DR MINT; MINT-208135; -.
DR STRING; 9606.ENSP00000296122; -.
DR BindingDB; P62140; -.
DR PhosphoSite; P62140; -.
DR DMDM; 49065814; -.
DR OGP; P37140; -.
DR PaxDb; P62140; -.
DR PRIDE; P62140; -.
DR DNASU; 5500; -.
DR Ensembl; ENST00000296122; ENSP00000296122; ENSG00000213639.
DR Ensembl; ENST00000358506; ENSP00000351298; ENSG00000213639.
DR Ensembl; ENST00000395366; ENSP00000378769; ENSG00000213639.
DR GeneID; 5500; -.
DR KEGG; hsa:5500; -.
DR UCSC; uc002rmg.3; human.
DR CTD; 5500; -.
DR GeneCards; GC02P028974; -.
DR HGNC; HGNC:9282; PPP1CB.
DR HPA; CAB022558; -.
DR MIM; 600590; gene.
DR neXtProt; NX_P62140; -.
DR PharmGKB; PA33610; -.
DR eggNOG; COG0639; -.
DR HOGENOM; HOG000172697; -.
DR HOVERGEN; HBG000216; -.
DR InParanoid; P62140; -.
DR KO; K06269; -.
DR OMA; PDLQGME; -.
DR PhylomeDB; P62140; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR ChiTaRS; PPP1CB; human.
DR GeneWiki; PPP1CB; -.
DR GenomeRNAi; 5500; -.
DR NextBio; 21280; -.
DR PRO; PR:P62140; -.
DR ArrayExpress; P62140; -.
DR Bgee; P62140; -.
DR CleanEx; HS_PPP1CB; -.
DR Genevestigator; P62140; -.
DR GO; GO:0042587; C:glycogen granule; IEA:Ensembl.
DR GO; GO:0070688; C:MLL5-L complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; ISS:UniProtKB.
DR GO; GO:0050115; F:myosin-light-chain-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:Ensembl.
DR GO; GO:0030155; P:regulation of cell adhesion; IDA: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:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR GO; GO:0019433; P:triglyceride catabolic process; TAS:Reactome.
DR InterPro; IPR004843; PEstase_dom.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Carbohydrate metabolism; Cell cycle; Cell division;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Glycogen metabolism; Hydrolase; Iron; Manganese; Metal-binding;
KW Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 327 Serine/threonine-protein phosphatase PP1-
FT beta catalytic subunit.
FT /FTId=PRO_0000058779.
FT ACT_SITE 124 124 Proton donor (By similarity).
FT METAL 63 63 Iron (By similarity).
FT METAL 65 65 Iron (By similarity).
FT METAL 91 91 Iron (By similarity).
FT METAL 91 91 Manganese (By similarity).
FT METAL 123 123 Manganese (By similarity).
FT METAL 172 172 Manganese (By similarity).
FT METAL 247 247 Manganese (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 316 316 Phosphothreonine.
FT CONFLICT 51 51 L -> P (in Ref. 5; AAV38549).
SQ SEQUENCE 327 AA; 37187 MW; E8356022E9B94ECD CRC64;
MADGELNVDS LITRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI LLELEAPLKI
CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL
RGNHECASIN RIYGFYDECK RRFNIKLWKT FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ
SMEQIRRIMR PTDVPDTGLL CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL
DLICRAHQVV EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK
KAKYQYGGLN SGRPVTPPRT ANPPKKR
//
ID PP1B_HUMAN Reviewed; 327 AA.
AC P62140; B2R5V4; D6W565; P37140; Q5U087; Q6FG45;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Serine/threonine-protein phosphatase PP1-beta catalytic subunit;
DE Short=PP-1B;
DE Short=PPP1CD;
DE EC=3.1.3.16;
DE EC=3.1.3.53;
GN Name=PPP1CB;
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].
RX PubMed=8312365; DOI=10.1016/0167-4889(94)90138-4;
RA Barker H.M., Brewis N.D., Street A.J., Spurr N.K., Cohen P.T.W.;
RT "Three genes for protein phosphatase 1 map to different human
RT chromosomes: sequence, expression and gene localisation of protein
RT serine/threonine phosphatase 1 beta (PPP1CB).";
RL Biochim. Biophys. Acta 1220:212-218(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7796987; DOI=10.1007/s001250050306;
RA Prochazka M., Mochizuki H., Baier L.J., Cohen P.T.W., Bogardus C.;
RT "Molecular and linkage analysis of type-1 protein phosphatase
RT catalytic beta-subunit gene: lack of evidence for its major role in
RT insulin resistance in Pima Indians.";
RL Diabetologia 38:461-466(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Umbilical vein;
RX PubMed=10906760;
RX DOI=10.1002/1097-4644(2000)79:1<113::AID-JCB110>3.3.CO;2-0;
RA Verin A.D., Csortos C., Durbin S.D., Aydanyan A., Wang P.,
RA Patterson C.E., Garcia J.G.;
RT "Characterization of the protein phosphatase 1 catalytic subunit in
RT endothelium: involvement in contractile responses.";
RL J. Cell. Biochem. 79:113-125(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Endometrium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [11]
RP PROTEIN SEQUENCE OF 2-14, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [12]
RP INTERACTION WITH PPP1R12C.
RX PubMed=11399775; DOI=10.1074/jbc.M102615200;
RA Tan I., Ng C.H., Lim L., Leung T.;
RT "Phosphorylation of a novel myosin binding subunit of protein
RT phosphatase 1 reveals a conserved mechanism in the regulation of actin
RT cytoskeleton.";
RL J. Biol. Chem. 276:21209-21216(2001).
RN [13]
RP SUBCELLULAR LOCATION.
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 [14]
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 [15]
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 [16]
RP ENZYME 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 PPP1R16B.
RX PubMed=18586956; DOI=10.1152/ajplung.00325.2007;
RA Csortos C., Czikora I., Bogatcheva N.V., Adyshev D.M., Poirier C.,
RA Olah G., Verin A.D.;
RT "TIMAP is a positive regulator of pulmonary endothelial barrier
RT function.";
RL Am. J. Physiol. 295:L440-L450(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316, AND MASS
RP SPECTROMETRY.
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 [19]
RP IDENTIFICATION IN THE MLL5-L COMPLEX.
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 [20]
RP IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, FUNCTION, AND
RP INTERACTION WITH PPP1R8.
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 [21]
RP INTERACTION WITH NUAK1 AND PPP1R12A.
RX PubMed=20354225; DOI=10.1126/scisignal.2000616;
RA Zagorska A., Deak M., Campbell D.G., Banerjee S., Hirano M.,
RA Aizawa S., Prescott A.R., Alessi D.R.;
RT "New roles for the LKB1-NUAK pathway in controlling myosin phosphatase
RT complexes and cell adhesion.";
RL Sci. Signal. 3:RA25-RA25(2010).
RN [22]
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 [23]
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 [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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).
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 (PP1) is essential for cell division, it participates
CC in the regulation of glycogen metabolism, muscle contractility and
CC protein synthesis. Involved in regulation of ionic conductances
CC and long-term synaptic plasticity. Component of the PTW/PP1
CC phosphatase complex, which plays a role in the control of
CC chromatin structure and cell cycle progression during the
CC transition from mitosis into interphase.
CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC phosphate.
CC -!- CATALYTIC ACTIVITY: [Myosin light-chain] phosphate + H(2)O =
CC [myosin light-chain] + phosphate.
CC -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity).
CC -!- ENZYME REGULATION: Inhibited by the toxins okadaic acid,
CC tautomycin and microcystin Leu-Arg (By similarity). The
CC phosphatase activity of the PPP1R15A-PP1 complex toward EIF2S1 is
CC specifically inhibited by Salubrinal, a drug that protects cells
CC from endoplasmic reticulum stress.
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. The targeting or regulatory
CC subunits determine the substrate specificity of PP1. PPP1R12A,
CC PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in
CC skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F
CC (in brain) mediate binding to glycogen. Part of a complex
CC containing PPP1R15B, PP1 and NCK1/2 (By similarity). Component of
CC the MLL5-L complex, at least composed of KMT2E/MLL5, STK38,
CC PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R7
CC and PPP1R12C. PPP1R15A and PPP1R15B mediate binding to EIF2S1.
CC Interacts with PPP1R16B. Component of the PTW/PP1 phosphatase
CC complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or
CC PPP1CB or PPP1CC. Interacts with PPP1R8. Interacts with TRIM28;
CC the interaction is weak. Interacts with PPP1R12A and NUAK1; the
CC interaction is direct.
CC -!- INTERACTION:
CC P38398:BRCA1; NbExp=3; IntAct=EBI-352350, EBI-349905;
CC O08785:Clock (xeno); NbExp=2; IntAct=EBI-352350, EBI-79859;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleoplasm.
CC Nucleus, nucleolus. Note=Highly mobile in cells and can be
CC relocalized through interaction with targeting subunits. In the
CC presence of PPP1R8 relocalizes from the nucleus to nuclear
CC speckles.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The things we forget -
CC Issue 32 of March 2003;
CC URL="http://web.expasy.org/spotlight/back_issues/sptlt032.shtml";
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DR EMBL; X80910; CAA56870.1; -; mRNA.
DR EMBL; U11005; AAA85093.1; -; Genomic_DNA.
DR EMBL; U10998; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; U10999; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; U11000; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; U11001; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; U11002; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; U11003; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; U11004; AAA85093.1; JOINED; Genomic_DNA.
DR EMBL; AF092905; AAF01137.1; -; mRNA.
DR EMBL; CR542263; CAG47059.1; -; mRNA.
DR EMBL; CR542285; CAG47080.1; -; mRNA.
DR EMBL; BT019744; AAV38549.1; -; mRNA.
DR EMBL; AK312329; BAG35251.1; -; mRNA.
DR EMBL; BX647970; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC097724; AAY24124.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00527.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00528.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00529.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00530.1; -; Genomic_DNA.
DR EMBL; BC002697; AAH02697.1; -; mRNA.
DR EMBL; BC012045; AAH12045.1; -; mRNA.
DR PIR; S41052; S41052.
DR RefSeq; NP_002700.1; NM_002709.2.
DR RefSeq; NP_996759.1; NM_206876.1.
DR UniGene; Hs.702907; -.
DR ProteinModelPortal; P62140; -.
DR SMR; P62140; 1-308.
DR IntAct; P62140; 30.
DR MINT; MINT-208135; -.
DR STRING; 9606.ENSP00000296122; -.
DR BindingDB; P62140; -.
DR PhosphoSite; P62140; -.
DR DMDM; 49065814; -.
DR OGP; P37140; -.
DR PaxDb; P62140; -.
DR PRIDE; P62140; -.
DR DNASU; 5500; -.
DR Ensembl; ENST00000296122; ENSP00000296122; ENSG00000213639.
DR Ensembl; ENST00000358506; ENSP00000351298; ENSG00000213639.
DR Ensembl; ENST00000395366; ENSP00000378769; ENSG00000213639.
DR GeneID; 5500; -.
DR KEGG; hsa:5500; -.
DR UCSC; uc002rmg.3; human.
DR CTD; 5500; -.
DR GeneCards; GC02P028974; -.
DR HGNC; HGNC:9282; PPP1CB.
DR HPA; CAB022558; -.
DR MIM; 600590; gene.
DR neXtProt; NX_P62140; -.
DR PharmGKB; PA33610; -.
DR eggNOG; COG0639; -.
DR HOGENOM; HOG000172697; -.
DR HOVERGEN; HBG000216; -.
DR InParanoid; P62140; -.
DR KO; K06269; -.
DR OMA; PDLQGME; -.
DR PhylomeDB; P62140; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR ChiTaRS; PPP1CB; human.
DR GeneWiki; PPP1CB; -.
DR GenomeRNAi; 5500; -.
DR NextBio; 21280; -.
DR PRO; PR:P62140; -.
DR ArrayExpress; P62140; -.
DR Bgee; P62140; -.
DR CleanEx; HS_PPP1CB; -.
DR Genevestigator; P62140; -.
DR GO; GO:0042587; C:glycogen granule; IEA:Ensembl.
DR GO; GO:0070688; C:MLL5-L complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; ISS:UniProtKB.
DR GO; GO:0050115; F:myosin-light-chain-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:Ensembl.
DR GO; GO:0030155; P:regulation of cell adhesion; IDA: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:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR GO; GO:0019433; P:triglyceride catabolic process; TAS:Reactome.
DR InterPro; IPR004843; PEstase_dom.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Carbohydrate metabolism; Cell cycle; Cell division;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Glycogen metabolism; Hydrolase; Iron; Manganese; Metal-binding;
KW Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 327 Serine/threonine-protein phosphatase PP1-
FT beta catalytic subunit.
FT /FTId=PRO_0000058779.
FT ACT_SITE 124 124 Proton donor (By similarity).
FT METAL 63 63 Iron (By similarity).
FT METAL 65 65 Iron (By similarity).
FT METAL 91 91 Iron (By similarity).
FT METAL 91 91 Manganese (By similarity).
FT METAL 123 123 Manganese (By similarity).
FT METAL 172 172 Manganese (By similarity).
FT METAL 247 247 Manganese (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 316 316 Phosphothreonine.
FT CONFLICT 51 51 L -> P (in Ref. 5; AAV38549).
SQ SEQUENCE 327 AA; 37187 MW; E8356022E9B94ECD CRC64;
MADGELNVDS LITRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI LLELEAPLKI
CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL
RGNHECASIN RIYGFYDECK RRFNIKLWKT FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ
SMEQIRRIMR PTDVPDTGLL CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL
DLICRAHQVV EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK
KAKYQYGGLN SGRPVTPPRT ANPPKKR
//
MIM
600590
*RECORD*
*FIELD* NO
600590
*FIELD* TI
*600590 PROTEIN PHOSPHATASE 1, CATALYTIC SUBUNIT, BETA ISOFORM; PPP1CB
;;PROTEIN PHOSPHATASE 1-BETA;;
read morePROTEIN PHOSPHATASE 1, CATALYTIC SUBUNIT, DELTA ISOFORM; PPP1CD;;
PROTEIN PHOSPHATASE 1-DELTA
*FIELD* TX
DESCRIPTION
Protein phosphatase-1 (PP1) is 1 of 4 major serine/threonine-specific
protein phosphatases involved in the dephosphorylation of a variety of
proteins. These enzymes work in opposition to the protein kinases to
control the level of phosphorylation. PP1 has 3 catalytic subunits,
designated alpha (176875), beta, and gamma (176914). PP1-beta is also
referred to as PP1-delta.
CLONING
Barker et al. (1994) isolated a cDNA for PP1-beta (symbolized PPP1CB)
from a teratocarcinoma library. Three different PPP1CB mRNAs were seen
on Northern blots corresponding to alternate splicing variants. The
3-prime noncoding region of PPP1CB was approximately 90% conserved
between man and rodents, suggesting that this region may have functional
importance.
MAPPING
Barker et al. (1994) assigned the gene for human PPP1CB to chromosome 2
using somatic cell hybrid DNAs and further localized it to 2p23 by
fluorescence in situ hybridization. Saadat et al. (1994) confirmed the
human map position as 2p23 and showed that rodent homologs mapped to rat
6q21-q23 and mouse 12D.
*FIELD* RF
1. Barker, H. M.; Brewis, N. D.; Street, A. J.; Spurr, N. K.; Cohen,
P. T. W.: Three genes for protein phosphatase 1 map to different
human chromosomes: sequence, expression and gene localisation of protein
serine/threonine phosphatase 1 beta (PPP1CB). Biochim. Biophys. Acta 1220:
212-218, 1994.
2. Saadat, M.; Kakinoki, Y.; Mizuno, Y.; Kikuchi, K.; Yoshida, M.
C.: Chromosomal localization of human, rat, and mouse protein phosphatase
type 1 beta catalytic subunit genes (PPP1CB) by fluorescence in situ
hybridization. Jpn. J. Genet. 69: 697-700, 1994.
*FIELD* CD
Victor A. McKusick: 6/6/1995
*FIELD* ED
mgross: 10/08/2003
carol: 8/25/1998
terry: 6/15/1995
mark: 6/6/1995
*RECORD*
*FIELD* NO
600590
*FIELD* TI
*600590 PROTEIN PHOSPHATASE 1, CATALYTIC SUBUNIT, BETA ISOFORM; PPP1CB
;;PROTEIN PHOSPHATASE 1-BETA;;
read morePROTEIN PHOSPHATASE 1, CATALYTIC SUBUNIT, DELTA ISOFORM; PPP1CD;;
PROTEIN PHOSPHATASE 1-DELTA
*FIELD* TX
DESCRIPTION
Protein phosphatase-1 (PP1) is 1 of 4 major serine/threonine-specific
protein phosphatases involved in the dephosphorylation of a variety of
proteins. These enzymes work in opposition to the protein kinases to
control the level of phosphorylation. PP1 has 3 catalytic subunits,
designated alpha (176875), beta, and gamma (176914). PP1-beta is also
referred to as PP1-delta.
CLONING
Barker et al. (1994) isolated a cDNA for PP1-beta (symbolized PPP1CB)
from a teratocarcinoma library. Three different PPP1CB mRNAs were seen
on Northern blots corresponding to alternate splicing variants. The
3-prime noncoding region of PPP1CB was approximately 90% conserved
between man and rodents, suggesting that this region may have functional
importance.
MAPPING
Barker et al. (1994) assigned the gene for human PPP1CB to chromosome 2
using somatic cell hybrid DNAs and further localized it to 2p23 by
fluorescence in situ hybridization. Saadat et al. (1994) confirmed the
human map position as 2p23 and showed that rodent homologs mapped to rat
6q21-q23 and mouse 12D.
*FIELD* RF
1. Barker, H. M.; Brewis, N. D.; Street, A. J.; Spurr, N. K.; Cohen,
P. T. W.: Three genes for protein phosphatase 1 map to different
human chromosomes: sequence, expression and gene localisation of protein
serine/threonine phosphatase 1 beta (PPP1CB). Biochim. Biophys. Acta 1220:
212-218, 1994.
2. Saadat, M.; Kakinoki, Y.; Mizuno, Y.; Kikuchi, K.; Yoshida, M.
C.: Chromosomal localization of human, rat, and mouse protein phosphatase
type 1 beta catalytic subunit genes (PPP1CB) by fluorescence in situ
hybridization. Jpn. J. Genet. 69: 697-700, 1994.
*FIELD* CD
Victor A. McKusick: 6/6/1995
*FIELD* ED
mgross: 10/08/2003
carol: 8/25/1998
terry: 6/15/1995
mark: 6/6/1995