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Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PP-1A) (EC 3.1.3.16)

 PP1A_HUMAN              Reviewed;         330 AA.
P62136; A6NNR3; B2R908; P08129; P20653; P22802; Q07161;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
21-JUN-2004, sequence version 1.
22-NOV-2017, entry version 154.
RecName: Full=Serine/threonine-protein phosphatase PP1-alpha catalytic subunit;
Short=PP-1A;
EC=3.1.3.16 {ECO:0000269|PubMed:26083323};
Name=PPP1CA; Synonyms=PPP1A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=8392016; DOI=10.1016/0378-1119(93)90282-8;
Song Q., Khanna K.K., Lu H., Lavin M.F.;
"Cloning and characterization of a human protein phosphatase 1-
encoding cDNA.";
Gene 129:291-295(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=8384581; DOI=10.1101/gad.7.4.555;
Durfee T., Becherer K., Chen P.L., Yeh S.H., Yang Y., Kilburn A.E.,
Lee W.H., Elledge S.J.;
"The retinoblastoma protein associates with the protein phosphatase
type 1 catalytic subunit.";
Genes Dev. 7:555-569(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
Tung L.;
Submitted (APR-1991) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Synovial cell;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle, Pancreas, and Placenta;
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).
[8]
PROTEIN SEQUENCE OF 2-15 AND 247-261, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Heiserich L., Gottlieb E.;
Submitted (OCT-2008) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 23-330 (ISOFORM 1).
PubMed=2161401; DOI=10.1016/0888-7543(90)90536-4;
Barker H.M., Jones T.A., da Cruz e Silva E.F., Spurr N.K., Sheer D.,
Cohen P.T.W.;
"Localization of the gene encoding a type I protein phosphatase
catalytic subunit to human chromosome band 11q13.";
Genomics 7:159-166(1990).
[10]
INTERACTION WITH PPP1R15A AND HHV-1 ICP34.5.
PubMed=9023344; DOI=10.1073/pnas.94.3.843;
He B., Gross M., Roizman B.;
"The gamma(1)34.5 protein of herpes simplex virus 1 complexes with
protein phosphatase 1alpha to dephosphorylate the alpha subunit of the
eukaryotic translation initiation factor 2 and preclude the shutoff of
protein synthesis by double-stranded RNA-activated protein kinase.";
Proc. Natl. Acad. Sci. U.S.A. 94:843-848(1997).
[11]
SUBCELLULAR LOCATION, AND INTERACTION WITH PPP1R8.
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).
[12]
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).
[13]
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).
[14]
REVIEW.
PubMed=11839776;
Cohen P.T.W.;
"Protein phosphatase 1 -- targeted in many directions.";
J. Cell Sci. 115:241-256(2002).
[15]
INTERACTION WITH PPP1R16B AND RPSA.
PubMed=16263087; DOI=10.1016/j.bbrc.2005.10.089;
Kim K., Li L., Kozlowski K., Suh H.S., Cao W., Ballermann B.J.;
"The protein phosphatase-1 targeting subunit TIMAP regulates LAMR1
phosphorylation.";
Biochem. Biophys. Res. Commun. 338:1327-1334(2005).
[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 FER, AND PHOSPHORYLATION AT THR-320.
PubMed=16732323; DOI=10.1038/sj.onc.1209695;
Pasder O., Shpungin S., Salem Y., Makovsky A., Vilchick S.,
Michaeli S., Malovani H., Nir U.;
"Downregulation of Fer induces PP1 activation and cell-cycle arrest in
malignant cells.";
Oncogene 25:4194-4206(2006).
[18]
IDENTIFICATION IN A COMPLEX WITH ILF2; ILF3; YLPM1; KHDRBS1; RBMX AND
NCOA5, AND INTERACTION WITH YLPM1.
PubMed=17890166; DOI=10.1016/j.bbapap.2007.07.015;
Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K.,
Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.;
"The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative
nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-
G.";
Biochim. Biophys. Acta 1774:1339-1350(2007).
[19]
FUNCTION, INTERACTION WITH NEK2, AND DEPHOSPHORYLATION.
PubMed=17283141; DOI=10.1158/0008-5472.CAN-06-3071;
Mi J., Guo C., Brautigan D.L., Larner J.M.;
"Protein phosphatase-1alpha regulates centrosome splitting through
Nek2.";
Cancer Res. 67:1082-1089(2007).
[20]
INTERACTION WITH NEK2.
PubMed=17626005; DOI=10.1074/jbc.M704969200;
Wu W., Baxter J.E., Wattam S.L., Hayward D.G., Fardilha M., Knebel A.,
Ford E.M., da Cruz e Silva E.F., Fry A.M.;
"Alternative splicing controls nuclear translocation of the cell
cycle-regulated Nek2 kinase.";
J. Biol. Chem. 282:26431-26440(2007).
[21]
SUBCELLULAR LOCATION, AND INTERACTION WITH NOM1.
PubMed=17965019; DOI=10.1074/jbc.M706708200;
Gunawardena S.R., Ruis B.L., Meyer J.A., Kapoor M., Conklin K.F.;
"NOM1 targets protein phosphatase I to the nucleolus.";
J. Biol. Chem. 283:398-404(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320, 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).
[24]
IDENTIFICATION IN THE MLL5-L COMPLEX.
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).
[25]
INTERACTION WITH DAB2.
PubMed=19581931; DOI=10.1038/onc.2009.157;
Jiang Y., Luo W., Howe P.H.;
"Dab2 stabilizes Axin and attenuates Wnt/beta-catenin signaling by
preventing protein phosphatase 1 (PP1)-Axin interactions.";
Oncogene 28:2999-3007(2009).
[26]
IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, AND INTERACTION
WITH WDR82; PPP1R8 AND PPP1R10/PNUTS.
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).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(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]
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).
[30]
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).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-22; THR-320 AND
SER-325, 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).
[33]
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).
[34]
FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH ATG16L1.
PubMed=26083323; DOI=10.1080/15548627.2015.1060386;
Song H., Pu J., Wang L., Wu L., Xiao J., Liu Q., Chen J., Zhang M.,
Liu Y., Ni M., Mo J., Zheng Y., Wan D., Cai X., Cao Y., Xiao W.,
Ye L., Tu E., Lin Z., Wen J., Lu X., He J., Peng Y., Su J., Zhang H.,
Zhao Y., Lin M., Zhang Z.;
"ATG16L1 phosphorylation is oppositely regulated by CSNK2/casein
kinase 2 and PPP1/protein phosphatase 1 which determines the fate of
cardiomyocytes during hypoxia/reoxygenation.";
Autophagy 11:1308-1325(2015).
[35]
FUNCTION, AND INTERACTION WITH CENPA.
PubMed=25556658; DOI=10.1016/j.devcel.2014.11.030;
Yu Z., Zhou X., Wang W., Deng W., Fang J., Hu H., Wang Z., Li S.,
Cui L., Shen J., Zhai L., Peng S., Wong J., Dong S., Yuan Z., Ou G.,
Zhang X., Xu P., Lou J., Yang N., Chen P., Xu R.M., Li G.;
"Dynamic phosphorylation of CENP-A at Ser68 orchestrates its cell-
cycle-dependent deposition at centromeres.";
Dev. Cell 32:68-81(2015).
[36]
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).
[37]
X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 7-300 IN COMPLEX WITH
INHIBITORS, COFACTOR, MANGANESE-BINDING SITES, AND SUBUNIT.
PubMed=18992256; DOI=10.1016/j.jmb.2008.10.053;
Kelker M.S., Page R., Peti W.;
"Crystal structures of protein phosphatase-1 bound to nodularin-R and
tautomycin: a novel scaffold for structure-based drug design of
serine/threonine phosphatase inhibitors.";
J. Mol. Biol. 385:11-21(2009).
[38]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 7-330 IN COMPLEX WITH RAT
PPP1R9A AND PPP1R9B.
PubMed=20305656; DOI=10.1038/nsmb.1786;
Ragusa M.J., Dancheck B., Critton D.A., Nairn A.C., Page R., Peti W.;
"Spinophilin directs protein phosphatase 1 specificity by blocking
substrate binding sites.";
Nat. Struct. Mol. Biol. 17:459-464(2010).
-!- FUNCTION: Protein phosphatase that associates with over 200
regulatory proteins to form highly specific holoenzymes which
dephosphorylate hundreds of biological targets. Protein
phosphatase 1 (PP1) is essential for cell division, and
participates in the regulation of glycogen metabolism, muscle
contractility and protein synthesis. Involved in regulation of
ionic conductances and long-term synaptic plasticity. May play an
important role in dephosphorylating substrates such as the
postsynaptic density-associated Ca(2+)/calmodulin dependent
protein kinase II. 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. Regulates NEK2 function in terms of kinase activity
and centrosome number and splitting, both in the presence and
absence of radiation-induced DNA damage. Regulator of neural tube
and optic fissure closure, and enteric neural crest cell (ENCCs)
migration during development. 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).
Dephosphorylates CENPA (PubMed:25556658). Dephosphorylates the
'Ser-139' residue of ATG16L1 causing dissociation of ATG12-ATG5-
ATG16L1 complex, thereby inhibiting autophagy (PubMed:26083323).
{ECO:0000269|PubMed:17283141, ECO:0000269|PubMed:21712997,
ECO:0000269|PubMed:23396208, ECO:0000269|PubMed:25556658,
ECO:0000269|PubMed:26083323}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
{ECO:0000269|PubMed:26083323}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
Note=Binds 1 Fe cation per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:18992256};
Note=Binds 2 manganese ions per subunit.
{ECO:0000269|PubMed:18992256};
-!- ENZYME REGULATION: 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: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. PPP1R12A, PPP1R12B and PPP1R12C
mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B
(in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate
binding to glycogen. Interacts with PPP1R39 (By similarity).
Interacts with BTBD10 (By similarity). Interacts with KCTD20 (By
similarity). Interacts with PPP1R9A and PPP1R9B. Part of a complex
containing PPP1R15B, PP1 and NCK1/2. Interacts with PHACTR4; which
acts as an activator of PP1 activity (By similarity). Interacts
with PPP1R15A and PPP1R15B; the interactions mediate binding to
EIF2S1. Component of the MLL5-L complex, at least composed of
KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT.
Interacts with PPP1R7. Interacts with YLPM1. Forms a complex with
ILF2, ILF3, YLPM1, KHDRBS1, RBMX and NCOA5. Interacts with NOM1
and PPP1R8. Interacts with HHV-1 ICP34.5. Interacts with PPP1R16B.
Interacts with RPSA only in the presence of PPP1R16B. Component of
the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4,
WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with
PPP1R10/PNUTS and PPP1R8. Interacts with WDR82 in the presence of
PPP1R10/PNUTS. Interacts with TRIM28; the interaction
dephosphorylates TRIM28 on 'Ser-824' and forms a complex at the
p21 promoter site. Interacts with isoform 1 and isoform 4 of NEK2.
Interacts with FER; this promotes phosphorylation at Thr-320.
Interacts with DAB2; the interaction is mutually exclusive with
the AXIN1:PPP1CA interaction. Interacts with FOXP3
(PubMed:23396208). Interacts with CENPA (PubMed:25556658).
Interacts with ATG16L1 (PubMed:26083323).
{ECO:0000250|UniProtKB:P62137, ECO:0000250|UniProtKB:P62139,
ECO:0000269|PubMed:11564868, ECO:0000269|PubMed:11739654,
ECO:0000269|PubMed:12226088, ECO:0000269|PubMed:16263087,
ECO:0000269|PubMed:16732323, ECO:0000269|PubMed:17283141,
ECO:0000269|PubMed:17626005, ECO:0000269|PubMed:17890166,
ECO:0000269|PubMed:17965019, ECO:0000269|PubMed:18992256,
ECO:0000269|PubMed:19377461, ECO:0000269|PubMed:19581931,
ECO:0000269|PubMed:20305656, ECO:0000269|PubMed:20424263,
ECO:0000269|PubMed:20516061, ECO:0000269|PubMed:23396208,
ECO:0000269|PubMed:25556658, ECO:0000269|PubMed:26083323,
ECO:0000269|PubMed:9023344}.
-!- INTERACTION:
P31749:AKT1; NbExp=4; IntAct=EBI-357253, EBI-296087;
O14727:APAF1; NbExp=2; IntAct=EBI-357253, EBI-446492;
O15169:AXIN1; NbExp=4; IntAct=EBI-357253, EBI-710484;
P38398:BRCA1; NbExp=2; IntAct=EBI-357253, EBI-349905;
O95400:CD2BP2; NbExp=2; IntAct=EBI-357253, EBI-768015;
Q99459:CDC5L; NbExp=2; IntAct=EBI-357253, EBI-374880;
P12830:CDH1; NbExp=2; IntAct=EBI-357253, EBI-727477;
Q8TEP8:CEP192; NbExp=2; IntAct=EBI-357253, EBI-2339778;
Q9NX63:CHCHD3; NbExp=2; IntAct=EBI-357253, EBI-743375;
O08785:Clock (xeno); NbExp=2; IntAct=EBI-357253, EBI-79859;
Q6PJW8:CNST; NbExp=3; IntAct=EBI-357253, EBI-750390;
Q96S65:CSRNP1; NbExp=6; IntAct=EBI-357253, EBI-4311573;
Q9H175:CSRNP2; NbExp=8; IntAct=EBI-357253, EBI-5235958;
Q92796:DLG3; NbExp=2; IntAct=EBI-357253, EBI-80440;
P55199:ELL; NbExp=2; IntAct=EBI-357253, EBI-1245868;
Q9BZS1:FOXP3; NbExp=2; IntAct=EBI-357253, EBI-983719;
Q8NG31:KNL1; NbExp=2; IntAct=EBI-357253, EBI-1001161;
Q5S007:LRRK2; NbExp=6; IntAct=EBI-357253, EBI-5323863;
O00566:MPHOSPH10; NbExp=2; IntAct=EBI-357253, EBI-5235884;
Q76TK5:ORF23 (xeno); NbExp=2; IntAct=EBI-357253, EBI-14033469;
Q96QC0:PPP1R10; NbExp=3; IntAct=EBI-357253, EBI-1210346;
Q96KQ4:PPP1R13B; NbExp=9; IntAct=EBI-357253, EBI-1105153;
Q8WUF5:PPP1R13L; NbExp=7; IntAct=EBI-357253, EBI-5550163;
Q5SWA1:PPP1R15B; NbExp=5; IntAct=EBI-357253, EBI-2815482;
Q6NYC8:PPP1R18; NbExp=3; IntAct=EBI-357253, EBI-2557469;
P41236:PPP1R2; NbExp=9; IntAct=EBI-357253, EBI-1056517;
Q5T8A7:PPP1R26; NbExp=2; IntAct=EBI-357253, EBI-308500;
Q86WC6:PPP1R27; NbExp=6; IntAct=EBI-357253, EBI-5235602;
Q6NXS1:PPP1R2P3; NbExp=5; IntAct=EBI-357253, EBI-10251630;
Q7Z5V6:PPP1R32; NbExp=3; IntAct=EBI-357253, EBI-4311771;
O75864:PPP1R37; NbExp=4; IntAct=EBI-357253, EBI-5235692;
Q12972:PPP1R8; NbExp=6; IntAct=EBI-357253, EBI-716633;
Q12972-1:PPP1R8; NbExp=6; IntAct=EBI-357253, EBI-16012257;
Q12972-2:PPP1R8; NbExp=4; IntAct=EBI-357253, EBI-12252736;
O35867:Ppp1r9a (xeno); NbExp=3; IntAct=EBI-357253, EBI-7092421;
Q96SB3:PPP1R9B; NbExp=3; IntAct=EBI-357253, EBI-351275;
O35274:Ppp1r9b (xeno); NbExp=5; IntAct=EBI-357253, EBI-80022;
P60484:PTEN; NbExp=2; IntAct=EBI-357253, EBI-696162;
P06400:RB1; NbExp=2; IntAct=EBI-357253, EBI-491274;
Q5UIP0:RIF1; NbExp=4; IntAct=EBI-357253, EBI-711331;
P36313:RL1 (xeno); NbExp=4; IntAct=EBI-357253, EBI-6149234;
A8K8P3:SFI1; NbExp=2; IntAct=EBI-357253, EBI-743371;
Q562F6:SGO2; NbExp=4; IntAct=EBI-357253, EBI-989213;
Q9H788:SH2D4A; NbExp=2; IntAct=EBI-357253, EBI-747035;
Q8TEC5:SH3RF2; NbExp=3; IntAct=EBI-357253, EBI-2130111;
P63208:SKP1; NbExp=3; IntAct=EBI-357253, EBI-307486;
Q7Z699:SPRED1; NbExp=4; IntAct=EBI-357253, EBI-5235340;
Q9HCH5:SYTL2; NbExp=2; IntAct=EBI-357253, EBI-2690103;
Q14C87:TMEM132D; NbExp=2; IntAct=EBI-357253, EBI-5235567;
Q13625:TP53BP2; NbExp=9; IntAct=EBI-357253, EBI-77642;
Q4KMQ1:TPRN; NbExp=3; IntAct=EBI-357253, EBI-3942777;
Q8TEL6:TRPC4AP; NbExp=2; IntAct=EBI-357253, EBI-2559060;
P49815:TSC2; NbExp=2; IntAct=EBI-357253, EBI-396587;
Q9Y2W2:WBP11; NbExp=3; IntAct=EBI-357253, EBI-714455;
Q9H4A3:WNK1; NbExp=2; IntAct=EBI-357253, EBI-457907;
P49750:YLPM1; NbExp=3; IntAct=EBI-357253, EBI-712871;
Q9HBF4:ZFYVE1; NbExp=2; IntAct=EBI-357253, EBI-4401611;
O95405:ZFYVE9; NbExp=3; IntAct=EBI-357253, EBI-296817;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleoplasm.
Nucleus, nucleolus. Note=Primarily nuclear and largely excluded
from the nucleolus. Highly mobile in cells and can be relocalized
through interaction with targeting subunits. NOM1 plays a role in
targeting this protein to the nucleolus. In the presence of PPP1R8
relocalizes from the nucleus to nuclear speckles.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P62136-1; Sequence=Displayed;
Name=2;
IsoId=P62136-2; Sequence=VSP_043377;
Note=No experimental confirmation available.;
Name=3;
IsoId=P62136-3; Sequence=VSP_046754;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- INDUCTION: Up-regulated in synovial fluid mononuclear cells and
peripheral blood mononuclear cells from patients with rheumatoid
arthritis. {ECO:0000269|PubMed:23396208}.
-!- PTM: Phosphorylated. Dephosphorylated at Thr-320 in the presence
of ionizing radiation. {ECO:0000269|PubMed:16732323}.
-!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
{ECO:0000305}.
-!- 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 http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X70848; CAA50197.1; -; mRNA.
EMBL; S57501; AAB26015.1; -; mRNA.
EMBL; M63960; AAA36508.1; -; mRNA.
EMBL; AK313586; BAG36355.1; -; mRNA.
EMBL; BT006629; AAP35275.1; -; mRNA.
EMBL; AP003419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001888; AAH01888.1; -; mRNA.
EMBL; BC004482; AAH04482.1; -; mRNA.
EMBL; BC008010; AAH08010.1; -; mRNA.
EMBL; J04759; AAA36475.1; -; mRNA.
CCDS; CCDS31618.1; -. [P62136-2]
CCDS; CCDS8160.1; -. [P62136-1]
CCDS; CCDS8161.1; -. [P62136-3]
RefSeq; NP_001008709.1; NM_001008709.1. [P62136-2]
RefSeq; NP_002699.1; NM_002708.3. [P62136-1]
RefSeq; NP_996756.1; NM_206873.1. [P62136-3]
UniGene; Hs.183994; -.
PDB; 3E7A; X-ray; 1.63 A; A/B=7-300.
PDB; 3E7B; X-ray; 1.70 A; A/B=7-300.
PDB; 3EGG; X-ray; 1.85 A; A/B=7-330.
PDB; 3EGH; X-ray; 2.00 A; A/B=7-330.
PDB; 3HVQ; X-ray; 2.20 A; A/B=7-330.
PDB; 3N5U; X-ray; 3.20 A; A/B=1-300.
PDB; 3V4Y; X-ray; 2.10 A; A/C/E/G=7-307.
PDB; 4G9J; X-ray; 3.10 A; A/B=1-330.
PDB; 4MOV; X-ray; 1.45 A; A/B=7-300.
PDB; 4MOY; X-ray; 2.20 A; A=7-300.
PDB; 4MP0; X-ray; 2.10 A; A/C=7-300.
PDB; 4XPN; X-ray; 2.29 A; A/C=7-300.
PDB; 5IOH; X-ray; 2.57 A; A/C=7-300.
PDBsum; 3E7A; -.
PDBsum; 3E7B; -.
PDBsum; 3EGG; -.
PDBsum; 3EGH; -.
PDBsum; 3HVQ; -.
PDBsum; 3N5U; -.
PDBsum; 3V4Y; -.
PDBsum; 4G9J; -.
PDBsum; 4MOV; -.
PDBsum; 4MOY; -.
PDBsum; 4MP0; -.
PDBsum; 4XPN; -.
PDBsum; 5IOH; -.
ProteinModelPortal; P62136; -.
SMR; P62136; -.
BioGrid; 111493; 328.
CORUM; P62136; -.
DIP; DIP-221N; -.
DIP; DIP-38195N; -.
ELM; P62136; -.
IntAct; P62136; 298.
MINT; MINT-5001223; -.
STRING; 9606.ENSP00000326031; -.
BindingDB; P62136; -.
ChEMBL; CHEMBL2164; -.
DEPOD; P62136; -.
iPTMnet; P62136; -.
PhosphoSitePlus; P62136; -.
SwissPalm; P62136; -.
BioMuta; PPP1CA; -.
DMDM; 49065811; -.
OGP; P08129; -.
EPD; P62136; -.
MaxQB; P62136; -.
PaxDb; P62136; -.
PeptideAtlas; P62136; -.
PRIDE; P62136; -.
TopDownProteomics; P62136-1; -. [P62136-1]
DNASU; 5499; -.
Ensembl; ENST00000312989; ENSP00000326031; ENSG00000172531. [P62136-2]
Ensembl; ENST00000358239; ENSP00000350974; ENSG00000172531. [P62136-3]
Ensembl; ENST00000376745; ENSP00000365936; ENSG00000172531. [P62136-1]
GeneID; 5499; -.
KEGG; hsa:5499; -.
UCSC; uc001oku.2; human. [P62136-1]
CTD; 5499; -.
DisGeNET; 5499; -.
EuPathDB; HostDB:ENSG00000172531.14; -.
GeneCards; PPP1CA; -.
HGNC; HGNC:9281; PPP1CA.
HPA; CAB004545; -.
HPA; HPA046833; -.
MIM; 176875; gene.
neXtProt; NX_P62136; -.
OpenTargets; ENSG00000172531; -.
PharmGKB; PA33609; -.
eggNOG; ENOG410IN85; Eukaryota.
eggNOG; ENOG410XPVF; LUCA.
GeneTree; ENSGT00900000141228; -.
HOGENOM; HOG000172697; -.
HOVERGEN; HBG000216; -.
InParanoid; P62136; -.
KO; K06269; -.
OMA; DKRKFQY; -.
OrthoDB; EOG091G0EKF; -.
PhylomeDB; P62136; -.
TreeFam; TF354243; -.
BRENDA; 3.1.3.16; 2681.
Reactome; R-HSA-163560; Triglyceride catabolism.
Reactome; R-HSA-180024; DARPP-32 events.
Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-HSA-400253; Circadian Clock.
SignaLink; P62136; -.
SIGNOR; P62136; -.
ChiTaRS; PPP1CA; human.
EvolutionaryTrace; P62136; -.
GeneWiki; PPP1CA; -.
GenomeRNAi; 5499; -.
PRO; PR:P62136; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000172531; -.
CleanEx; HS_PPP1CA; -.
ExpressionAtlas; P62136; baseline and differential.
Genevisible; P62136; HS.
GO; GO:0005913; C:cell-cell adherens junction; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0072357; C:PTW/PP1 phosphatase complex; IDA:UniProtKB.
GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:ParkinsonsUK-UCL.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; TAS:ProtInc.
GO; GO:1904886; P:beta-catenin destruction complex disassembly; ISS:ParkinsonsUK-UCL.
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:0016311; P:dephosphorylation; IDA:CACAO.
GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
GO; GO:0032091; P:negative regulation of protein binding; ISS:ParkinsonsUK-UCL.
GO; GO:0006470; P:protein dephosphorylation; IMP:CACAO.
GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IC:ParkinsonsUK-UCL.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
GO; GO:0036496; P:regulation of translational initiation by eIF2 alpha dephosphorylation; ISS:ParkinsonsUK-UCL.
Gene3D; 3.60.21.10; -; 1.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
InterPro; IPR031675; STPPase_N.
Pfam; PF00149; Metallophos; 1.
Pfam; PF16891; STPPase_N; 1.
PRINTS; PR00114; STPHPHTASE.
SMART; SM00156; PP2Ac; 1.
SUPFAM; SSF56300; SSF56300; 1.
PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing;
Carbohydrate metabolism; Cell cycle; Cell division; Complete proteome;
Cytoplasm; Direct protein sequencing; Glycogen metabolism; Hydrolase;
Manganese; Metal-binding; Nucleus; Phosphoprotein;
Protein phosphatase; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.8}.
CHAIN 2 330 Serine/threonine-protein phosphatase PP1-
alpha catalytic subunit.
/FTId=PRO_0000058774.
ACT_SITE 125 125 Proton donor. {ECO:0000250}.
METAL 64 64 Manganese 1. {ECO:0000250}.
METAL 66 66 Manganese 1. {ECO:0000250}.
METAL 92 92 Manganese.
METAL 92 92 Manganese 1. {ECO:0000250}.
METAL 92 92 Manganese 2. {ECO:0000250}.
METAL 124 124 Manganese.
METAL 124 124 Manganese 2. {ECO:0000250}.
METAL 173 173 Manganese.
METAL 173 173 Manganese 2. {ECO:0000250}.
METAL 248 248 Manganese.
METAL 248 248 Manganese 2. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.8}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 305 305 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62137}.
MOD_RES 306 306 Phosphotyrosine.
{ECO:0000250|UniProtKB:P62137}.
MOD_RES 320 320 Phosphothreonine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:16732323}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 18 18 E -> EGSRVLTPHCAP (in isoform 2).
{ECO:0000303|PubMed:8384581}.
/FTId=VSP_043377.
VAR_SEQ 19 62 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_046754.
HELIX 9 18 {ECO:0000244|PDB:4MOV}.
TURN 19 21 {ECO:0000244|PDB:4MOV}.
HELIX 32 48 {ECO:0000244|PDB:4MOV}.
STRAND 51 55 {ECO:0000244|PDB:4MOV}.
STRAND 57 62 {ECO:0000244|PDB:4MOV}.
HELIX 69 79 {ECO:0000244|PDB:4MOV}.
STRAND 87 89 {ECO:0000244|PDB:4MOV}.
STRAND 94 98 {ECO:0000244|PDB:4MOV}.
HELIX 100 113 {ECO:0000244|PDB:4MOV}.
TURN 115 117 {ECO:0000244|PDB:4MOV}.
STRAND 118 120 {ECO:0000244|PDB:4MOV}.
HELIX 128 134 {ECO:0000244|PDB:4MOV}.
HELIX 136 143 {ECO:0000244|PDB:4MOV}.
HELIX 146 156 {ECO:0000244|PDB:4MOV}.
STRAND 162 165 {ECO:0000244|PDB:4MOV}.
TURN 166 168 {ECO:0000244|PDB:4MOV}.
STRAND 169 171 {ECO:0000244|PDB:4MOV}.
HELIX 184 187 {ECO:0000244|PDB:4MOV}.
STRAND 197 199 {ECO:0000244|PDB:4MOV}.
HELIX 200 206 {ECO:0000244|PDB:4MOV}.
STRAND 214 218 {ECO:0000244|PDB:4MOV}.
STRAND 222 227 {ECO:0000244|PDB:4MOV}.
HELIX 229 239 {ECO:0000244|PDB:4MOV}.
STRAND 242 246 {ECO:0000244|PDB:4MOV}.
STRAND 254 258 {ECO:0000244|PDB:4MOV}.
TURN 259 262 {ECO:0000244|PDB:4MOV}.
STRAND 263 267 {ECO:0000244|PDB:4MOV}.
HELIX 272 274 {ECO:0000244|PDB:4MOV}.
STRAND 280 285 {ECO:0000244|PDB:4MOV}.
STRAND 291 296 {ECO:0000244|PDB:4MOV}.
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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