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Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (PPP1CD) (EC 3.1.3.16) (EC 3.1.3.53)

 PP1B_HUMAN              Reviewed;         327 AA.
P62140; B2R5V4; D6W565; P37140; Q5U087; Q6FG45;
21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
18-JUL-2018, entry version 166.
RecName: Full=Serine/threonine-protein phosphatase PP1-beta catalytic subunit;
Short=PP-1B;
Short=PPP1CD;
EC=3.1.3.16;
EC=3.1.3.53;
Name=PPP1CB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8312365; DOI=10.1016/0167-4889(94)90138-4;
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7796987; DOI=10.1007/BF00410284;
Prochazka M., Mochizuki H., Baier L.J., Cohen P.T.W., Bogardus C.;
"Molecular and linkage analysis of type-1 protein phosphatase
catalytic beta-subunit gene: lack of evidence for its major role in
insulin resistance in Pima Indians.";
Diabetologia 38:461-466(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Umbilical vein;
PubMed=10906760;
DOI=10.1002/1097-4644(2000)79:1<113::AID-JCB110>3.0.CO;2-9;
Verin A.D., Csortos C., Durbin S.D., Aydanyan A., Wang P.,
Patterson C.E., Garcia J.G.;
"Characterization of the protein phosphatase 1 catalytic subunit in
endothelium: involvement in contractile responses.";
J. Cell. Biochem. 79:113-125(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Endometrium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
PROTEIN SEQUENCE OF 2-14, AND ACETYLATION AT ALA-2.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[12]
INTERACTION WITH PPP1R12C.
PubMed=11399775; DOI=10.1074/jbc.M102615200;
Tan I., Ng C.H., Lim L., Leung T.;
"Phosphorylation of a novel myosin binding subunit of protein
phosphatase 1 reveals a conserved mechanism in the regulation of actin
cytoskeleton.";
J. Biol. Chem. 276:21209-21216(2001).
[13]
SUBCELLULAR LOCATION.
PubMed=11739654;
Trinkle-Mulcahy L., Sleeman J.E., Lamond A.I.;
"Dynamic targeting of protein phosphatase 1 within the nuclei of
living mammalian cells.";
J. Cell Sci. 114:4219-4228(2001).
[14]
INTERACTION WITH PPP1R15A.
PubMed=11564868; DOI=10.1128/MCB.21.20.6841-6850.2001;
Connor J.H., Weiser D.C., Li S., Hallenbeck J.M., Shenolikar S.;
"Growth arrest and DNA damage-inducible protein GADD34 assembles a
novel signaling complex containing protein phosphatase 1 and inhibitor
1.";
Mol. Cell. Biol. 21:6841-6850(2001).
[15]
INTERACTION WITH PPP1R7.
PubMed=12226088; DOI=10.1074/jbc.M206838200;
Ceulemans H., Vulsteke V., De Maeyer M., Tatchell K., Stalmans W.,
Bollen M.;
"Binding of the concave surface of the Sds22 superhelix to the alpha
4/alpha 5/alpha 6-triangle of protein phosphatase-1.";
J. Biol. Chem. 277:47331-47337(2002).
[16]
ENZYME REGULATION.
PubMed=15705855; DOI=10.1126/science.1101902;
Boyce M., Bryant K.F., Jousse C., Long K., Harding H.P., Scheuner D.,
Kaufman R.J., Ma D., Coen D.M., Ron D., Yuan J.;
"A selective inhibitor of eIF2alpha dephosphorylation protects cells
from ER stress.";
Science 307:935-939(2005).
[17]
INTERACTION WITH PPP1R16B.
PubMed=18586956; DOI=10.1152/ajplung.00325.2007;
Csortos C., Czikora I., Bogatcheva N.V., Adyshev D.M., Poirier C.,
Olah G., Verin A.D.;
"TIMAP is a positive regulator of pulmonary endothelial barrier
function.";
Am. J. Physiol. 295:L440-L450(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
CAUTION.
PubMed=19377461; DOI=10.1038/nature07954;
Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G.,
Kitagawa H., Kato S.;
"GlcNAcylation of a histone methyltransferase in retinoic-acid-induced
granulopoiesis.";
Nature 459:455-459(2009).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
CAUTION AND RETRACTION.
PubMed=24336203; DOI=10.1038/nature12896;
Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G.,
Kitagawa H., Kato S.;
"Retraction: GlcNAcylation of a histone methyltransferase in retinoic-
acid-induced granulopoiesis.";
Nature 505:574-574(2014).
[25]
IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, FUNCTION, AND
INTERACTION WITH PPP1R8.
PubMed=20516061; DOI=10.1074/jbc.M110.109801;
Lee J.H., You J., Dobrota E., Skalnik D.G.;
"Identification and characterization of a novel human PP1 phosphatase
complex.";
J. Biol. Chem. 285:24466-24476(2010).
[26]
INTERACTION WITH RRP1B, AND SUBCELLULAR LOCATION.
PubMed=20926688; DOI=10.1091/mbc.E10-04-0287;
Chamousset D., De Wever V., Moorhead G.B., Chen Y., Boisvert F.M.,
Lamond A.I., Trinkle-Mulcahy L.;
"RRP1B targets PP1 to mammalian cell nucleoli and is associated with
pre-60S ribosomal subunits.";
Mol. Biol. Cell 21:4212-4226(2010).
[27]
INTERACTION WITH NUAK1 AND PPP1R12A.
PubMed=20354225; DOI=10.1126/scisignal.2000616;
Zagorska A., Deak M., Campbell D.G., Banerjee S., Hirano M.,
Aizawa S., Prescott A.R., Alessi D.R.;
"New roles for the LKB1-NUAK pathway in controlling myosin phosphatase
complexes and cell adhesion.";
Sci. Signal. 3:RA25-RA25(2010).
[28]
INTERACTION WITH TRIM28.
PubMed=20424263; DOI=10.1126/scisignal.2000781;
Li X., Lin H.H., Chen H., Xu X., Shih H.M., Ann D.K.;
"SUMOylation of the transcriptional co-repressor KAP1 is regulated by
the serine and threonine phosphatase PP1.";
Sci. Signal. 3:RA32-RA32(2010).
[29]
FUNCTION IN CIRCADIAN CLOCK.
PubMed=21712997; DOI=10.1371/journal.pone.0021325;
Schmutz I., Wendt S., Schnell A., Kramer A., Mansuy I.M., Albrecht U.;
"Protein phosphatase 1 (PP1) is a post-translational regulator of the
mammalian circadian clock.";
PLoS ONE 6:E21325-E21325(2011).
[30]
FUNCTION, INTERACTION WITH FOXP3, AND INDUCTION.
PubMed=23396208; DOI=10.1038/nm.3085;
Nie H., Zheng Y., Li R., Guo T.B., He D., Fang L., Liu X., Xiao L.,
Chen X., Wan B., Chin Y.E., Zhang J.Z.;
"Phosphorylation of FOXP3 controls regulatory T cell function and is
inhibited by TNF-alpha in rheumatoid arthritis.";
Nat. Med. 19:322-328(2013).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[32]
INVOLVEMENT IN NSLH2, AND VARIANTS NSLH2 ARG-49 AND PRO-56.
PubMed=27264673; DOI=10.1002/ajmg.a.37781;
Gripp K.W., Aldinger K.A., Bennett J.T., Baker L., Tusi J.,
Powell-Hamilton N., Stabley D., Sol-Church K., Timms A.E.,
Dobyns W.B.;
"A novel rasopathy caused by recurrent de novo missense mutations in
PPP1CB closely resembles Noonan syndrome with loose anagen hair.";
Am. J. Med. Genet. A 170:2237-2247(2016).
[33]
INVOLVEMENT IN NSLH2, AND VARIANTS NSLH2 ARG-49; ALA-183; VAL-183;
TYR-252 AND LYS-274.
PubMed=27681385; DOI=10.1007/s00439-016-1731-1;
Ma L., Bayram Y., McLaughlin H.M., Cho M.T., Krokosky A., Turner C.E.,
Lindstrom K., Bupp C.P., Mayberry K., Mu W., Bodurtha J.,
Weinstein V., Zadeh N., Alcaraz W., Powis Z., Shao Y., Scott D.A.,
Lewis A.M., White J.J., Jhangiani S.N., Gulec E.Y., Lalani S.R.,
Lupski J.R., Retterer K., Schnur R.E., Wentzensen I.M., Bale S.,
Chung W.K.;
"De novo missense variants in PPP1CB are associated with intellectual
disability and congenital heart disease.";
Hum. Genet. 135:1399-1409(2016).
[34]
INVOLVEMENT IN NSLH2, AND VARIANT NSLH2 ARG-49.
PubMed=27868344; DOI=10.1002/ajmg.a.38056;
Zambrano R.M., Marble M., Chalew S.A., Lilje C., Vargas A.,
Lacassie Y.;
"Further evidence that variants in PPP1CB cause a rasopathy similar to
Noonan syndrome with loose anagen hair.";
Am. J. Med. Genet. A 173:565-567(2017).
[35]
INVOLVEMENT IN NSLH2, AND VARIANT NSLH2 ARG-49.
PubMed=28211982; DOI=10.1002/ajmg.a.38070;
Bertola D., Yamamoto G., Buscarilli M., Jorge A., Passos-Bueno M.R.,
Kim C.;
"The recurrent PPP1CB mutation p.Pro49Arg in an additional Noonan-like
syndrome individual: Broadening the clinical phenotype.";
Am. J. Med. Genet. A 173:824-828(2017).
[36]
INTERACTION WITH SERPINE1.
PubMed=28296156; DOI=10.1111/jcmm.13127;
Yao H., He G., Chen C., Yan S., Lu L., Song L., Vijayan K.V., Li Q.,
Xiong L., Miao X., Deng X.;
"PAI1: a novel PP1-interacting protein that mediates human plasma's
anti-apoptotic effect in endothelial cells.";
J. Cell. Mol. Med. 21:2068-2076(2017).
-!- FUNCTION: Protein phosphatase that associates with over 200
regulatory proteins to form highly specific holoenzymes which
dephosphorylate hundreds of biological targets. Protein
phosphatase (PP1) is essential for cell division, it participates
in the regulation of glycogen metabolism, muscle contractility and
protein synthesis. Involved in regulation of ionic conductances
and long-term synaptic plasticity. Component of the PTW/PP1
phosphatase complex, which plays a role in the control of
chromatin structure and cell cycle progression during the
transition from mitosis into interphase. In balance with CSNK1D
and CSNK1E, determines the circadian period length, through the
regulation of the speed and rhythmicity of PER1 and PER2
phosphorylation. May dephosphorylate CSNK1D and CSNK1E.
Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-
cells (Treg) from patients with rheumatoid arthritis, thereby
inactivating FOXP3 and rendering Treg cells functionally defective
(PubMed:23396208). {ECO:0000269|PubMed:20516061,
ECO:0000269|PubMed:21712997, ECO:0000269|PubMed:23396208}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- CATALYTIC ACTIVITY: [Myosin light-chain] phosphate + H(2)O =
[myosin light-chain] + phosphate.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 manganese ions per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Inhibited by the toxins okadaic acid,
tautomycin and microcystin Leu-Arg (By similarity). The
phosphatase activity of the PPP1R15A-PP1 complex toward EIF2S1 is
specifically inhibited by Salubrinal, a drug that protects cells
from endoplasmic reticulum stress. {ECO:0000250,
ECO:0000269|PubMed:15705855}.
-!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or
PPP1CC, which is folded into its native form by inhibitor 2 and
glycogen synthetase kinase 3, and then complexed to one or several
targeting or regulatory subunits. The targeting or regulatory
subunits determine the substrate specificity of PP1. PPP1R12A,
PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in
skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F
(in brain) mediate binding to glycogen. Part of a complex
containing PPP1R15B, PP1 and NCK1/2 (By similarity). Interacts
with PPP1R7 and PPP1R12C. PPP1R15A and PPP1R15B mediate binding to
EIF2S1. Interacts with PPP1R16B. Component of the PTW/PP1
phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and
PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R8. Interacts with
TRIM28; the interaction is weak. Interacts with PPP1R12A and
NUAK1; the interaction is direct. Interacts with FOXP3. Interacts
with RRP1B (PubMed:20926688). Interacts with SERPINE1
(PubMed:28296156). {ECO:0000250|UniProtKB:P62141,
ECO:0000269|PubMed:11399775, ECO:0000269|PubMed:11564868,
ECO:0000269|PubMed:12226088, ECO:0000269|PubMed:18586956,
ECO:0000269|PubMed:20354225, ECO:0000269|PubMed:20424263,
ECO:0000269|PubMed:20516061, ECO:0000269|PubMed:20926688,
ECO:0000269|PubMed:23396208, ECO:0000269|PubMed:28296156}.
-!- INTERACTION:
P35609:ACTN2; NbExp=3; IntAct=EBI-352350, EBI-77797;
P38398:BRCA1; NbExp=3; IntAct=EBI-352350, EBI-349905;
A6NKD9:CCDC85C; NbExp=4; IntAct=EBI-352350, EBI-2561671;
O08785:Clock (xeno); NbExp=2; IntAct=EBI-352350, EBI-79859;
Q9H175:CSRNP2; NbExp=5; IntAct=EBI-352350, EBI-5235958;
Q76TK5:ORF23 (xeno); NbExp=2; IntAct=EBI-352350, EBI-14033469;
O60927:PPP1R11; NbExp=8; IntAct=EBI-352350, EBI-1048104;
O14974:PPP1R12A; NbExp=8; IntAct=EBI-352350, EBI-351726;
A0A0S2Z4Q8:PPP1R12B; NbExp=3; IntAct=EBI-352350, EBI-16434210;
Q8WUF5:PPP1R13L; NbExp=6; IntAct=EBI-352350, EBI-5550163;
Q96I34:PPP1R16A; NbExp=9; IntAct=EBI-352350, EBI-710402;
Q96T49:PPP1R16B; NbExp=4; IntAct=EBI-352350, EBI-10293968;
P41236:PPP1R2; NbExp=3; IntAct=EBI-352350, EBI-1056517;
Q6NXS1:PPP1R2B; NbExp=5; IntAct=EBI-352350, EBI-10251630;
Q9UQK1:PPP1R3C; NbExp=6; IntAct=EBI-352350, EBI-2506727;
Q15435:PPP1R7; NbExp=10; IntAct=EBI-352350, EBI-1024281;
Q12972:PPP1R8; NbExp=4; IntAct=EBI-352350, EBI-716633;
Q5UIP0:RIF1; NbExp=4; IntAct=EBI-352350, EBI-711331;
Q9H788:SH2D4A; NbExp=17; IntAct=EBI-352350, EBI-747035;
Q13625-3:TP53BP2; NbExp=3; IntAct=EBI-352350, EBI-10175039;
O94763:URI1; NbExp=3; IntAct=EBI-352350, EBI-357067;
Q96MX6:WDR92; NbExp=3; IntAct=EBI-352350, EBI-2434101;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11739654}.
Nucleus {ECO:0000269|PubMed:11739654}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:11739654}. Nucleus, nucleolus
{ECO:0000269|PubMed:11739654, ECO:0000269|PubMed:20926688}.
Note=Highly mobile in cells and can be relocalized through
interaction with targeting subunits. In the presence of PPP1R8
relocalizes from the nucleus to nuclear speckles.
{ECO:0000269|PubMed:11739654}.
-!- INDUCTION: Up-regulated in synovial fluid mononuclear cells and
peripheral blood mononuclear cells from patients with rheumatoid
arthritis. {ECO:0000269|PubMed:23396208}.
-!- DISEASE: Noonan syndrome-like disorder with loose anagen hair 2
(NSLH2) [MIM:617506]: A syndrome characterized by Noonan
dysmorphic features such as macrocephaly, high forehead,
hypertelorism, palpebral ptosis, low-set and posteriorly rotated
ears, short and webbed neck, pectus anomalies, in association with
pluckable, sparse, thin and slow-growing hair.
{ECO:0000269|PubMed:27264673, ECO:0000269|PubMed:27681385,
ECO:0000269|PubMed:27868344, ECO:0000269|PubMed:28211982}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
{ECO:0000305}.
-!- CAUTION: Was originally thought to be part of the MLL5-L complex,
at least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1,
ACTB and OGT (PubMed:19377461). However, the corresponding article
has been retracted (PubMed:24336203).
{ECO:0000269|PubMed:19377461, ECO:0000269|PubMed:24336203}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The things we forget
- Issue 32 of March 2003;
URL="https://web.expasy.org/spotlight/back_issues/032";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X80910; CAA56870.1; -; mRNA.
EMBL; U11005; AAA85093.1; -; Genomic_DNA.
EMBL; U10998; AAA85093.1; JOINED; Genomic_DNA.
EMBL; U10999; AAA85093.1; JOINED; Genomic_DNA.
EMBL; U11000; AAA85093.1; JOINED; Genomic_DNA.
EMBL; U11001; AAA85093.1; JOINED; Genomic_DNA.
EMBL; U11002; AAA85093.1; JOINED; Genomic_DNA.
EMBL; U11003; AAA85093.1; JOINED; Genomic_DNA.
EMBL; U11004; AAA85093.1; JOINED; Genomic_DNA.
EMBL; AF092905; AAF01137.1; -; mRNA.
EMBL; CR542263; CAG47059.1; -; mRNA.
EMBL; CR542285; CAG47080.1; -; mRNA.
EMBL; BT019744; AAV38549.1; -; mRNA.
EMBL; AK312329; BAG35251.1; -; mRNA.
EMBL; BX647970; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC097724; AAY24124.1; -; Genomic_DNA.
EMBL; CH471053; EAX00527.1; -; Genomic_DNA.
EMBL; CH471053; EAX00528.1; -; Genomic_DNA.
EMBL; CH471053; EAX00529.1; -; Genomic_DNA.
EMBL; CH471053; EAX00530.1; -; Genomic_DNA.
EMBL; BC002697; AAH02697.1; -; mRNA.
EMBL; BC012045; AAH12045.1; -; mRNA.
CCDS; CCDS33169.1; -.
PIR; S41052; S41052.
RefSeq; NP_002700.1; NM_002709.2.
RefSeq; NP_996759.1; NM_206876.1.
UniGene; Hs.702907; -.
ProteinModelPortal; P62140; -.
SMR; P62140; -.
BioGrid; 111494; 268.
DIP; DIP-33220N; -.
IntAct; P62140; 245.
MINT; P62140; -.
STRING; 9606.ENSP00000296122; -.
DEPOD; P62140; -.
iPTMnet; P62140; -.
PhosphoSitePlus; P62140; -.
SwissPalm; P62140; -.
BioMuta; PPP1CB; -.
DMDM; 49065814; -.
OGP; P37140; -.
EPD; P62140; -.
PaxDb; P62140; -.
PeptideAtlas; P62140; -.
PRIDE; P62140; -.
ProteomicsDB; 57367; -.
TopDownProteomics; P62140; -.
DNASU; 5500; -.
Ensembl; ENST00000296122; ENSP00000296122; ENSG00000213639.
Ensembl; ENST00000358506; ENSP00000351298; ENSG00000213639.
Ensembl; ENST00000395366; ENSP00000378769; ENSG00000213639.
GeneID; 5500; -.
KEGG; hsa:5500; -.
CTD; 5500; -.
DisGeNET; 5500; -.
EuPathDB; HostDB:ENSG00000213639.9; -.
GeneCards; PPP1CB; -.
HGNC; HGNC:9282; PPP1CB.
HPA; CAB022558; -.
HPA; CAB069426; -.
HPA; HPA065425; -.
MalaCards; PPP1CB; -.
MIM; 600590; gene.
MIM; 617506; phenotype.
neXtProt; NX_P62140; -.
OpenTargets; ENSG00000213639; -.
PharmGKB; PA33610; -.
eggNOG; ENOG410IN85; Eukaryota.
eggNOG; ENOG410XPVF; LUCA.
GeneTree; ENSGT00530000062911; -.
HOGENOM; HOG000172697; -.
HOVERGEN; HBG000216; -.
InParanoid; P62140; -.
KO; K06269; -.
OMA; DHQEADI; -.
OrthoDB; EOG091G0EKF; -.
PhylomeDB; P62140; -.
TreeFam; TF354243; -.
Reactome; R-HSA-163560; Triglyceride catabolism.
Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
Reactome; R-HSA-5625900; RHO GTPases activate CIT.
Reactome; R-HSA-5627117; RHO GTPases Activate ROCKs.
Reactome; R-HSA-5627123; RHO GTPases activate PAKs.
SIGNOR; P62140; -.
ChiTaRS; PPP1CB; human.
GeneWiki; PPP1CB; -.
GenomeRNAi; 5500; -.
PRO; PR:P62140; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000213639; -.
CleanEx; HS_PPP1CB; -.
ExpressionAtlas; P62140; baseline and differential.
Genevisible; P62140; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0000164; C:protein phosphatase type 1 complex; IEA:InterPro.
GO; GO:0072357; C:PTW/PP1 phosphatase complex; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0017018; F:myosin phosphatase activity; ISS:UniProtKB.
GO; GO:0050115; F:myosin-light-chain-phosphatase activity; IDA:UniProtKB.
GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; IDA:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
Gene3D; 3.60.21.10; -; 1.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
InterPro; IPR037979; PPP1CA/PPP1CB.
InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
InterPro; IPR031675; STPPase_N.
PANTHER; PTHR11668:SF377; PTHR11668:SF377; 1.
Pfam; PF00149; Metallophos; 1.
Pfam; PF16891; STPPase_N; 1.
PRINTS; PR00114; STPHPHTASE.
SMART; SM00156; PP2Ac; 1.
PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
1: Evidence at protein level;
Acetylation; Biological rhythms; Carbohydrate metabolism; Cell cycle;
Cell division; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Glycogen metabolism;
Hydrolase; Manganese; Metal-binding; Nucleus; Phosphoprotein;
Protein phosphatase; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801}.
CHAIN 2 327 Serine/threonine-protein phosphatase PP1-
beta catalytic subunit.
/FTId=PRO_0000058779.
ACT_SITE 124 124 Proton donor. {ECO:0000250}.
METAL 63 63 Manganese 1. {ECO:0000250}.
METAL 65 65 Manganese 1. {ECO:0000250}.
METAL 91 91 Manganese 1. {ECO:0000250}.
METAL 91 91 Manganese 2. {ECO:0000250}.
METAL 123 123 Manganese 2. {ECO:0000250}.
METAL 172 172 Manganese 2. {ECO:0000250}.
METAL 247 247 Manganese 2. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801}.
MOD_RES 316 316 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
VARIANT 49 49 P -> R (in NSLH2; dbSNP:rs886037952).
{ECO:0000269|PubMed:27264673,
ECO:0000269|PubMed:27681385,
ECO:0000269|PubMed:27868344,
ECO:0000269|PubMed:28211982}.
/FTId=VAR_076839.
VARIANT 56 56 A -> P (in NSLH2; dbSNP:rs1114167429).
{ECO:0000269|PubMed:27264673}.
/FTId=VAR_076840.
VARIANT 183 183 E -> A (in NSLH2; dbSNP:rs886037954).
{ECO:0000269|PubMed:27681385}.
/FTId=VAR_079189.
VARIANT 183 183 E -> V (in NSLH2; dbSNP:rs886037954).
{ECO:0000269|PubMed:27681385}.
/FTId=VAR_079190.
VARIANT 252 252 D -> Y (in NSLH2; dbSNP:rs886037953).
{ECO:0000269|PubMed:27681385}.
/FTId=VAR_079191.
VARIANT 274 274 E -> K (in NSLH2; unknown pathological
significance; dbSNP:rs886037955).
{ECO:0000269|PubMed:27681385}.
/FTId=VAR_079192.
CONFLICT 51 51 L -> P (in Ref. 5; AAV38549).
{ECO:0000305}.
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


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