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

 PP1A_MOUSE              Reviewed;         330 AA.
P62137; P08129; P20653; P22802; Q3U7G7; Q9Z1G2;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
21-JUN-2004, sequence version 1.
18-JUL-2018, entry version 152.
RecName: Full=Serine/threonine-protein phosphatase PP1-alpha catalytic subunit;
Short=PP-1A;
EC=3.1.3.16;
Name=Ppp1ca; Synonyms=Ppp1a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Ortiz J.M., Lorenzo M.L., Eguiraun A., Andres I., Sangrador A.,
Allshire R., Hastie N.D.;
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and DBA/2J;
TISSUE=Extraembryonic tissue, Liver, Pancreas, and Placenta;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
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).
[4]
PROTEIN SEQUENCE OF 44-74; 114-122 AND 247-260, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 69-90.
PubMed=8077208;
Becker W., Kentrup H., Klumpp S., Schultz J.E., Joost H.G.;
"Molecular cloning of a protein serine/threonine phosphatase
containing a putative regulatory tetratricopeptide repeat domain.";
J. Biol. Chem. 269:22586-22592(1994).
[6]
INTERACTION WITH PPP1R15B.
PubMed=14638860; DOI=10.1083/jcb.200308075;
Jousse C., Oyadomari S., Novoa I., Lu P., Zhang Y., Harding H.P.,
Ron D.;
"Inhibition of a constitutive translation initiation factor 2alpha
phosphatase, CReP, promotes survival of stressed cells.";
J. Cell Biol. 163:767-775(2003).
[7]
IDENTIFICATION IN COMPLEX WITH PPP1R15B AND NCK1.
PubMed=16835242; DOI=10.1074/jbc.M513556200;
Latreille M., Larose L.;
"Nck in a complex containing the catalytic subunit of protein
phosphatase 1 regulates eukaryotic initiation factor 2alpha signaling
and cell survival to endoplasmic reticulum stress.";
J. Biol. Chem. 281:26633-26644(2006).
[8]
FUNCTION, AND INTERACTION WITH PHACTR4.
PubMed=17609112; DOI=10.1016/j.devcel.2007.04.018;
Kim T.H., Goodman J., Anderson K.V., Niswander L.;
"Phactr4 regulates neural tube and optic fissure closure by
controlling PP1-, Rb-, and E2F1-regulated cell-cycle progression.";
Dev. Cell 13:87-102(2007).
[9]
INTERACTION WITH BTBD10.
PubMed=18160256; DOI=10.1016/j.cellsig.2007.11.004;
Nawa M., Kanekura K., Hashimoto Y., Aiso S., Matsuoka M.;
"A novel Akt/PKB-interacting protein promotes cell adhesion and
inhibits familial amyotrophic lateral sclerosis-linked mutant SOD1-
induced neuronal death via inhibition of PP2A-mediated
dephosphorylation of Akt/PKB.";
Cell. Signal. 20:493-505(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-306, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[12]
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).
[13]
FUNCTION IN CIRCADIAN CLOCK, AND MUTAGENESIS OF ASP-64 AND ASP-95.
PubMed=21930935; DOI=10.1073/pnas.1107178108;
Lee H.M., Chen R., Kim H., Etchegaray J.P., Weaver D.R., Lee C.;
"The period of the circadian oscillator is primarily determined by the
balance between casein kinase 1 and protein phosphatase 1.";
Proc. Natl. Acad. Sci. U.S.A. 108:16451-16456(2011).
[14]
FUNCTION.
PubMed=22215812; DOI=10.1101/gad.179283.111;
Zhang Y., Kim T.H., Niswander L.;
"Phactr4 regulates directional migration of enteric neural crest
through PP1, integrin signaling, and cofilin activity.";
Genes Dev. 26:69-81(2012).
[15]
INTERACTION WITH KCTD20.
PubMed=24156551; DOI=10.1186/1471-2091-14-27;
Nawa M., Matsuoka M.;
"KCTD20, a relative of BTBD10, is a positive regulator of Akt.";
BMC Biochem. 14:27-27(2013).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-305, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- 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 CENPA (By
similarity). Dephosphorylates the 'Ser-139' residue of ATG16L1
causing dissociation of ATG12-ATG5-ATG16L1 complex, thereby
inhibiting autophagy (By similarity).
{ECO:0000250|UniProtKB:P62136, ECO:0000269|PubMed:17609112,
ECO:0000269|PubMed:21712997, ECO:0000269|PubMed:21930935,
ECO:0000269|PubMed:22215812}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- 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:0000250};
Note=Binds 2 manganese ions per subunit. {ECO:0000250};
-!- 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 PPP1R9A, PPP1R9B and PPP1R7.
Interacts with PPP1R15A; the interaction mediates binding to
EIF2S1. Interacts with YLPM1. Forms a complex with ILF2, ILF3,
YLPM1, KHDRBS1, RBMX and NCOA5. Interacts with NOM1 and PPP1R8.
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 PPP1R39.
Interacts with TRIM28; the interaction dephosphorylates TRIM28 on
'Ser-824' and forms a complex at the p21 promoter site (By
similarity). Interacts with PPP1R15B; the interaction mediates
binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and
NCK1/2. Interacts with NEK2. Interacts with FER; this promotes
phosphorylation at Thr-320 (By similarity). Interacts with
PHACTR4; which acts as an activator of PP1 activity. Interacts
with BTBD10 (PubMed:18160256). Interacts with KCTD20
(PubMed:24156551). Interacts with FOXP3 (By similarity). Interacts
with CENPA (By similarity). Interacts with ATG16L1 (By
similarity). Found in a complex with PPP1CA, PPP1CC, SHC1 and
PEAK1 (By similarity). {ECO:0000250|UniProtKB:P62136,
ECO:0000250|UniProtKB:P62139, ECO:0000269|PubMed:14638860,
ECO:0000269|PubMed:16835242, ECO:0000269|PubMed:17609112,
ECO:0000269|PubMed:18160256, ECO:0000269|PubMed:24156551}.
-!- INTERACTION:
Q9WTL8:Arntl; NbExp=2; IntAct=EBI-357187, EBI-644534;
O35625:Axin1; NbExp=2; IntAct=EBI-357187, EBI-2365912;
P41136:Id2; NbExp=2; IntAct=EBI-357187, EBI-309167;
P17918:Pcna; NbExp=2; IntAct=EBI-357187, EBI-1173716;
Q3UM45:Ppp1r7; NbExp=3; IntAct=EBI-357187, EBI-8318179;
Q9WTX5:Skp1; NbExp=2; IntAct=EBI-357187, EBI-1202363;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus,
nucleolus {ECO:0000250}. 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 (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated. Dephosphorylated at Thr-320 in the presence
of ionizing radiation (By similarity). {ECO:0000250}.
-!- 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";
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EMBL; U25809; AAC99814.1; -; mRNA.
EMBL; AK007932; BAB25358.1; -; mRNA.
EMBL; AK028392; BAC25928.1; -; mRNA.
EMBL; AK090070; BAC41078.1; -; mRNA.
EMBL; AK151582; BAE30522.1; -; mRNA.
EMBL; AK152667; BAE31402.1; -; mRNA.
EMBL; AK153517; BAE32060.1; -; mRNA.
EMBL; AK159575; BAE35196.1; -; mRNA.
EMBL; AK167244; BAE39365.1; -; mRNA.
EMBL; AK167538; BAE39605.1; -; mRNA.
EMBL; AK167880; BAE39893.1; -; mRNA.
EMBL; AK167981; BAE39973.1; -; mRNA.
EMBL; BC014828; AAH14828.1; -; mRNA.
CCDS; CCDS29421.1; -.
RefSeq; NP_114074.1; NM_031868.2.
UniGene; Mm.1970; -.
UniGene; Mm.474260; -.
ProteinModelPortal; P62137; -.
SMR; P62137; -.
BioGrid; 202335; 43.
IntAct; P62137; 170.
MINT; P62137; -.
STRING; 10090.ENSMUSP00000039109; -.
iPTMnet; P62137; -.
PhosphoSitePlus; P62137; -.
SwissPalm; P62137; -.
EPD; P62137; -.
MaxQB; P62137; -.
PaxDb; P62137; -.
PeptideAtlas; P62137; -.
PRIDE; P62137; -.
Ensembl; ENSMUST00000046094; ENSMUSP00000039109; ENSMUSG00000040385.
Ensembl; ENSMUST00000180575; ENSMUSP00000137997; ENSMUSG00000096994.
GeneID; 19045; -.
KEGG; mmu:19045; -.
UCSC; uc008fzg.1; mouse.
CTD; 5499; -.
MGI; MGI:103016; Ppp1ca.
eggNOG; ENOG410IN85; Eukaryota.
eggNOG; ENOG410XPVF; LUCA.
GeneTree; ENSGT00530000062911; -.
HOGENOM; HOG000172697; -.
HOVERGEN; HBG000216; -.
InParanoid; P62137; -.
KO; K06269; -.
OMA; DKRKFQY; -.
OrthoDB; EOG091G0EKF; -.
PhylomeDB; P62137; -.
TreeFam; TF354243; -.
Reactome; R-MMU-180024; DARPP-32 events.
ChiTaRS; Ppp1ca; mouse.
PRO; PR:P62137; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000040385; -.
Genevisible; P62137; MM.
GO; GO:0005913; C:cell-cell adherens junction; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0043197; C:dendritic spine; ISO:MGI.
GO; GO:0042587; C:glycogen granule; ISO:MGI.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0043204; C:perikaryon; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0000164; C:protein phosphatase type 1 complex; ISO:MGI.
GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:MGI.
GO; GO:0008157; F:protein phosphatase 1 binding; ISO:MGI.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:MGI.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:MGI.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0009987; P:cellular process; TAS:MGI.
GO; GO:0032922; P:circadian regulation of gene expression; IDA:UniProtKB.
GO; GO:0016311; P:dephosphorylation; ISO:MGI.
GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IMP:UniProtKB.
GO; GO:0005977; P:glycogen metabolic process; TAS:MGI.
GO; GO:0030324; P:lung development; IMP:MGI.
GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; IDA:UniProtKB.
GO; GO:0005979; P:regulation of glycogen biosynthetic process; ISO:MGI.
GO; GO:0005981; P:regulation of glycogen catabolic process; ISO:MGI.
GO; GO:0006417; P:regulation of translation; TAS:MGI.
GO; GO:0010288; P:response to lead ion; ISO:MGI.
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; Glycogen metabolism; Hydrolase; Manganese;
Metal-binding; Nucleus; Phosphoprotein; Protein phosphatase;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P62136}.
CHAIN 2 330 Serine/threonine-protein phosphatase PP1-
alpha catalytic subunit.
/FTId=PRO_0000058775.
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 1. {ECO:0000250}.
METAL 92 92 Manganese 2. {ECO:0000250}.
METAL 124 124 Manganese 2. {ECO:0000250}.
METAL 173 173 Manganese 2. {ECO:0000250}.
METAL 248 248 Manganese 2. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P62136}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:P62136}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000250|UniProtKB:P62136}.
MOD_RES 305 305 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 306 306 Phosphotyrosine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 320 320 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000250|UniProtKB:P62136}.
MUTAGEN 64 64 D->N: Dominant negatif, severely disrupts
circadian rhythmicity of transcription.
{ECO:0000269|PubMed:21930935}.
MUTAGEN 95 95 D->N: Dominant negatif, severely disrupts
circadian rhythmicity of transcription.
{ECO:0000269|PubMed:21930935}.
SEQUENCE 330 AA; 37540 MW; 8FBFD158A52282E0 CRC64;
MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP ILLELEAPLK
ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIRYPENFFL
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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H0490 Serine threonine-protein phosphatase PP1-alpha catalytic subunit (PPP1CA), Bovine, ELISA Kit 96T
H0446 Serine threonine-protein phosphatase 2A catalytic subunit alpha isoform (PPP2CA), Rat, ELISA Kit 96T
CA055_HUMAN Bovine ELISA Kit FOR Serine per threonine-protein phosphatase 2A catalytic subunit alpha isoform 96T
CSB-EL018503HU Human Serine per threonine-protein phosphatase PP1-alpha catalytic subunit(PPP1CA) ELISA kit 96T
SYPL2_MOUSE Bovine ELISA Kit FOR Serine per threonine-protein phosphatase 2A catalytic subunit alpha isoform 96T
H0444 Serine threonine-protein phosphatase 2A catalytic subunit alpha isoform (PPP2CA), Pig, ELISA Kit 96T
H0494 Serine threonine-protein phosphatase PP1-alpha catalytic subunit (PPP1CA), Rabbit, ELISA Kit 96T
H0493 Serine threonine-protein phosphatase PP1-alpha catalytic subunit (PPP1CA), Mouse, ELISA Kit 96T
H0492 Serine threonine-protein phosphatase PP1-alpha catalytic subunit (PPP1CA), Human, ELISA Kit 96T
E0026h Bovine ELISA Kit FOR Serine per threonine-protein phosphatase 2A catalytic subunit alpha isoform 96T
NXP20_MOUSE Mouse ELISA Kit FOR Serine per threonine-protein phosphatase 2B catalytic subunit alpha isoform 96T
E0375m Mouse ELISA Kit FOR Serine per threonine-protein phosphatase 2B catalytic subunit alpha isoform 96T
H0442 Serine threonine-protein phosphatase 2A catalytic subunit alpha isoform (PPP2CA), Human, ELISA Kit 96T
H0445 Serine threonine-protein phosphatase 2A catalytic subunit alpha isoform (PPP2CA), Rabbit, ELISA Kit 96T
H0441 Serine threonine-protein phosphatase 2A catalytic subunit alpha isoform (PPP2CA), Chicken, ELISA Kit 96T
H0440 Serine threonine-protein phosphatase 2A catalytic subunit alpha isoform (PPP2CA), Bovine, ELISA Kit 96T
H0443 Serine threonine-protein phosphatase 2A catalytic subunit alpha isoform (PPP2CA), Mouse, ELISA Kit 96T
PP1A_RAT ELISA Kit FOR Serine per threonine-protein phosphatase PP1-alpha catalytic subunit; organism: Rat; gene name: Ppp1ca 96T
PP1A_MOUSE ELISA Kit FOR Serine per threonine-protein phosphatase PP1-alpha catalytic subunit; organism: Mouse; gene name: Ppp1ca 96T
PP2AA_RAT ELISA Kit FOR Serine per threonine-protein phosphatase 2A catalytic subunit alpha isoform; organism: Rat; gene name: Ppp2ca 96T


 

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