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Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calmodulin-dependent calcineurin A subunit alpha isoform)

 PP2BA_HUMAN             Reviewed;         521 AA.
Q08209; A1A441; A8K3B7; A8W6Z7; A8W6Z8; B5BUA2; Q8TAW9;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
10-OCT-2018, entry version 198.
RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform;
EC=3.1.3.16 {ECO:0000269|PubMed:15671020, ECO:0000269|PubMed:18838687, ECO:0000269|PubMed:19154138, ECO:0000269|PubMed:23468591, ECO:0000305|PubMed:26248042};
AltName: Full=CAM-PRP catalytic subunit;
AltName: Full=Calmodulin-dependent calcineurin A subunit alpha isoform;
Name=PPP3CA {ECO:0000312|HGNC:HGNC:9314}; Synonyms=CALNA, CNA;
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=Brain;
PubMed=8392375; DOI=10.1016/0167-4889(93)90117-8;
Muramatsu T., Kincaid R.L.;
"Molecular cloning of a full-length cDNA encoding the catalytic
subunit of human calmodulin-dependent protein phosphatase (calcineurin
A alpha).";
Biochim. Biophys. Acta 1178:117-120(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), AND ALTERNATIVE
SPLICING.
PubMed=20590401; DOI=10.3109/10826084.2010.482449;
Chiocco M.J., Zhu X., Walther D., Pletnikova O., Troncoso J.C.,
Uhl G.R., Liu Q.R.;
"Fine mapping of calcineurin (PPP3CA) gene reveals novel alternative
splicing patterns, association of 5'UTR trinucleotide repeat with
addiction vulnerability, and differential isoform expression in
Alzheimer's disease.";
Subst. Use Misuse 45:1809-1826(2010).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
PubMed=21647268;
Landreville S., Lupien C.B., Vigneault F., Gaudreault M., Mathieu M.,
Rousseau A.P., Guerin S.L., Salesse C.;
"Identification of differentially expressed genes in uveal melanoma
using suppressive subtractive hybridization.";
Mol. Vis. 17:1324-1333(2011).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
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).
TISSUE=Amygdala;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[7]
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).
[8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Pancreas;
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).
[10]
INTERACTION WITH MYOZ1 AND MYOZ2.
PubMed=11114196; DOI=10.1073/pnas.260501097;
Frey N., Richardson J.A., Olson E.N.;
"Calsarcins, a novel family of sarcomeric calcineurin-binding
proteins.";
Proc. Natl. Acad. Sci. U.S.A. 97:14632-14637(2000).
[11]
INTERACTION WITH MYOZ3.
PubMed=11842093; DOI=10.1074/jbc.M200712200;
Frey N., Olson E.N.;
"Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin
family, interacts with multiple Z-disc proteins.";
J. Biol. Chem. 277:13998-14004(2002).
[12]
INTERACTION WITH RCAN1.
PubMed=12809556; DOI=10.1042/BJ20030267;
Genesca L., Aubareda A., Fuentes J.J., Estivill X., De La Luna S.,
Perez-Riba M.;
"Phosphorylation of calcipressin 1 increases its ability to inhibit
calcineurin and decreases calcipressin half-life.";
Biochem. J. 374:567-575(2003).
[13]
INTERACTION WITH CRTC2.
PubMed=15454081; DOI=10.1016/j.cell.2004.09.015;
Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G.,
Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H.,
Okamoto M., Montminy M.;
"The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive
coincidence detector.";
Cell 119:61-74(2004).
[14]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=15671020; DOI=10.1074/jbc.M411494200;
Wang Y., Shibasaki F., Mizuno K.;
"Calcium signal-induced cofilin dephosphorylation is mediated by
Slingshot via calcineurin.";
J. Biol. Chem. 280:12683-12689(2005).
[15]
INTERACTION WITH SYNPO2.
PubMed=17923693; DOI=10.1128/MCB.00950-07;
Faul C., Dhume A., Schecter A.D., Mundel P.;
"Protein kinase A, Ca2+/calmodulin-dependent kinase II, and
calcineurin regulate the intracellular trafficking of myopodin between
the Z-disc and the nucleus of cardiac myocytes.";
Mol. Cell. Biol. 27:8215-8227(2007).
[16]
FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH DMN1L.
PubMed=18838687; DOI=10.1073/pnas.0808249105;
Cereghetti G.M., Stangherlin A., Martins de Brito O., Chang C.R.,
Blackstone C., Bernardi P., Scorrano L.;
"Dephosphorylation by calcineurin regulates translocation of Drp1 to
mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 105:15803-15808(2008).
[17]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBCELLULAR LOCATION.
PubMed=19154138; DOI=10.1021/bi8019355;
Kilka S., Erdmann F., Migdoll A., Fischer G., Weiwad M.;
"The proline-rich N-terminal sequence of calcineurin Abeta determines
substrate binding.";
Biochemistry 48:1900-1910(2009).
[18]
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).
[19]
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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[21]
INVOLVEMENT IN IECEE1, AND VARIANTS IECEE1 ARG-92; GLN-281; LYS-282;
445-GLN--GLN-521 DEL AND THR-447.
PubMed=28942967; DOI=10.1016/j.ajhg.2017.08.013;
Myers C.T., Stong N., Mountier E.I., Helbig K.L., Freytag S.,
Sullivan J.E., Ben Zeev B., Nissenkorn A., Tzadok M., Heimer G.,
Shinde D.N., Rezazadeh A., Regan B.M., Oliver K.L., Ernst M.E.,
Lippa N.C., Mulhern M.S., Ren Z., Poduri A., Andrade D.M., Bird L.M.,
Bahlo M., Berkovic S.F., Lowenstein D.H., Scheffer I.E., Sadleir L.G.,
Goldstein D.B., Mefford H.C., Heinzen E.L.;
"De Novo Mutations in PPP3CA Cause Severe Neurodevelopmental Disease
with Seizures.";
Am. J. Hum. Genet. 101:516-524(2017).
[22]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH PPP3R1; IRON AND
ZINC, AND ACTIVE SITE.
PubMed=8524402; DOI=10.1038/378641a0;
Kissinger C.R., Parge H.E., Knighton D.R., Lewis C.T., Pelletier L.A.,
Tempczyk A., Kalish V.J., Tucker K.D., Showalter R.E., Moomaw E.W.,
Gastinel L.N., Habuka N., Chen X., Maldonado F., Barker J.E.,
Bacquet R., Villafranca J.E.;
"Crystal structures of human calcineurin and the human FKBP12-FK506-
calcineurin complex.";
Nature 378:641-644(1995).
[23]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-372 IN COMPLEX WITH PPIA;
PPP3R1; IRON AND ZINC.
PubMed=12218175; DOI=10.1073/PNAS.192206699;
Huai Q., Kim H.Y., Liu Y., Zhao Y., Mondragon A., Liu J.O., Ke H.;
"Crystal structure of calcineurin-cyclophilin-cyclosporin shows common
but distinct recognition of immunophilin-drug complexes.";
Proc. Natl. Acad. Sci. U.S.A. 99:12037-12042(2002).
[24]
X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 20-392 IN COMPLEX WITH PPIA
AND PPP3R1.
PubMed=12357034; DOI=10.1073/PNAS.212504399;
Jin L., Harrison S.C.;
"Crystal structure of human calcineurin complexed with cyclosporin A
and human cyclophilin.";
Proc. Natl. Acad. Sci. U.S.A. 99:13522-13526(2002).
[25]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-380 IN COMPLEX WITH
SUBSTRATE PEPTIDE; PPP3R1; IRON AND ZINC, AND FUNCTION.
PubMed=17498738; DOI=10.1016/j.jmb.2007.04.032;
Li H., Zhang L., Rao A., Harrison S.C., Hogan P.G.;
"Structure of calcineurin in complex with PVIVIT peptide: portrait of
a low-affinity signalling interaction.";
J. Mol. Biol. 369:1296-1306(2007).
[26]
STRUCTURE BY NMR OF 21-347 IN COMPLEX WITH PEPTIDE SUBSTRATE, AND
FUNCTION.
PubMed=17502104; DOI=10.1016/j.str.2007.03.015;
Takeuchi K., Roehrl M.H., Sun Z.Y., Wagner G.;
"Structure of the calcineurin-NFAT complex: defining a T cell
activation switch using solution NMR and crystal coordinates.";
Structure 15:587-597(2007).
[27]
X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 389-413 IN COMPLEX WITH
CALM1.
PubMed=18384083; DOI=10.1002/prot.22032;
Ye Q., Wang H., Zheng J., Wei Q., Jia Z.;
"The complex structure of calmodulin bound to a calcineurin peptide.";
Proteins 73:19-27(2008).
[28]
STRUCTURE BY NMR OF 391-414 IN COMPLEX WITH CALM1.
Chyan C., Huang J., Irene D., Lin T.;
"Structure of Calmodulin complexed with the Calmodulin Binding Domain
of Calcineurin.";
Submitted (JAN-2008) to the PDB data bank.
[29]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 395-411 IN COMPLEX WITH
CALM1.
PubMed=19404396; DOI=10.1371/JOURNAL.PONE.0005402;
Majava V., Kursula P.;
"Domain swapping and different oligomeric States for the complex
between calmodulin and the calmodulin-binding domain of calcineurin
a.";
PLoS ONE 4:E5402-E5402(2009).
[30]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 14-370 IN COMPLEX WITH
PPP3R1; AKAP5 PEPTIDE; IRON AND ZINC, FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=22343722; DOI=10.1038/nsmb.2238;
Li H., Pink M.D., Murphy J.G., Stein A., Dell'Acqua M.L., Hogan P.G.;
"Balanced interactions of calcineurin with AKAP79 regulate Ca2+-
calcineurin-NFAT signaling.";
Nat. Struct. Mol. Biol. 19:337-345(2012).
[31]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-370 IN COMPLEX WITH PPP3R1
AND AFRICAN SWINE FEVER VIRUS MAL-047/A238L, FUNCTION, AND CATALYTIC
ACTIVITY.
PubMed=23468591; DOI=10.1371/journal.pbio.1001492;
Grigoriu S., Bond R., Cossio P., Chen J.A., Ly N., Hummer G., Page R.,
Cyert M.S., Peti W.;
"The molecular mechanism of substrate engagement and immunosuppressant
inhibition of calcineurin.";
PLoS Biol. 11:E1001492-E1001492(2013).
[32]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 391-414 IN COMPLEX WITH
CALM1.
PubMed=25144868; DOI=10.1021/bi5004734;
Dunlap T.B., Guo H.F., Cook E.C., Holbrook E., Rumi-Masante J.,
Lester T.E., Colbert C.L., Vander Kooi C.W., Creamer T.P.;
"Stoichiometry of the calcineurin regulatory domain-calmodulin
complex.";
Biochemistry 53:5779-5790(2014).
[33]
X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 2-346 IN COMPLEX WITH IRON
AND ZINC, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
INTERACTION WITH RCAN3 AND NFATC2, MOTIF, AND MUTAGENESIS OF TYR-288;
TYR-341 AND 328-VAL--ARG-332.
PubMed=26248042; DOI=10.1371/journal.pone.0134569;
Guasch A., Aranguren-Ibanez A., Perez-Luque R., Aparicio D.,
Martinez-Hoyer S., Mulero M.C., Serrano-Candelas E., Perez-Riba M.,
Fita I.;
"Calcineurin Undergoes a Conformational Switch Evoked via Peptidyl-
Prolyl Isomerization.";
PLoS ONE 10:E0134569-E0134569(2015).
[34]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-370 IN COMPLEX WITH
PPP3R1; PEPTIDE SUBSTRATE; IRON AND ZINC, AND FUNCTION.
PubMed=27974827; DOI=10.1038/srep38920;
Sheftic S.R., Page R., Peti W.;
"Investigating the human Calcineurin Interaction Network using the
piLxVP SLiM.";
Sci. Rep. 6:38920-38920(2016).
-!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein
phosphatase which plays an essential role in the transduction of
intracellular Ca(2+)-mediated signals (PubMed:15671020,
PubMed:18838687, PubMed:19154138, PubMed:23468591). Many of the
substrates contain a PxIxIT motif and/or a LxVP motif
(PubMed:17498738, PubMed:17502104, PubMed:23468591,
PubMed:27974827, PubMed:22343722). In response to increased Ca(2+)
levels, dephosphorylates and activates phosphatase SSH1 which
results in cofilin dephosphorylation (PubMed:15671020). In
response to increased Ca(2+) levels following mitochondrial
depolarization, dephosphorylates DNM1L inducing DNM1L
translocation to the mitochondrion (PubMed:18838687).
Dephosphorylates heat shock protein HSPB1 (By similarity).
Dephosphorylates and activates transcription factor NFATC1
(PubMed:19154138). In response to increased Ca(2+) levels,
regulates NFAT-mediated transcription probably by
dephosphorylating NFAT and promoting its nuclear translocation
(PubMed:26248042). Dephosphorylates and inactivates transcription
factor ELK1 (PubMed:19154138). Dephosphorylates DARPP32
(PubMed:19154138). {ECO:0000250|UniProtKB:P48452,
ECO:0000269|PubMed:15671020, ECO:0000269|PubMed:17498738,
ECO:0000269|PubMed:17502104, ECO:0000269|PubMed:18838687,
ECO:0000269|PubMed:19154138, ECO:0000269|PubMed:22343722,
ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26248042,
ECO:0000269|PubMed:27974827}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
{ECO:0000269|PubMed:15671020, ECO:0000269|PubMed:18838687,
ECO:0000269|PubMed:19154138, ECO:0000269|PubMed:23468591,
ECO:0000305|PubMed:26248042}.
-!- COFACTOR:
Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
Evidence={ECO:0000269|PubMed:12218175,
ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
ECO:0000269|PubMed:26248042, ECO:0000269|PubMed:27974827,
ECO:0000269|PubMed:8524402};
Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000269|PubMed:12218175,
ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
ECO:0000269|PubMed:26248042, ECO:0000269|PubMed:27974827,
ECO:0000269|PubMed:8524402};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:12218175,
ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
ECO:0000269|PubMed:26248042, ECO:0000269|PubMed:27974827,
ECO:0000269|PubMed:8524402};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:12218175,
ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722,
ECO:0000269|PubMed:26248042, ECO:0000269|PubMed:27974827,
ECO:0000269|PubMed:8524402};
-!- ACTIVITY REGULATION: Activated by Ca(2+)-bound calmodulin
following an increase in intracellular Ca(2+). At low Ca(2+)
concentrations, the catalytic subunit (also known as calcineurin
A) is inactive and is bound to the regulatory subunit (also known
as calcineurin B) in which only two high-affinity binding sites
are occupied by Ca(2+). In response to elevated calcium levels,
the occupancy of the low-affinity sites on calcineurin B by Ca(2+)
causes a conformational change of the C-terminal regulatory domain
of calcineurin A, resulting in the exposure of the calmodulin-
binding domain and in the partial activation of calcineurin A. The
subsequent binding of Ca(2+)-bound calmodulin leads to the
displacement of the autoinhibitory domain from the active site and
possibly of the autoinhibitory segment from the substrate binding
site which fully activates calcineurin A. Inhibited by
immunosuppressant drug FK506 (tacrolimus) in complex with FKBP12
and also by immunosuppressant drug cyclosporin A (CsA) in complex
with PPIA/cyclophilin A; the inhibition is Ca(2+)-dependent
(PubMed:26248042). {ECO:0000250|UniProtKB:P16298,
ECO:0000269|PubMed:26248042}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.04 uM for NFATC1 {ECO:0000269|PubMed:19154138};
KM=2.22 uM for DARPP32 {ECO:0000269|PubMed:19154138};
-!- SUBUNIT: Forms a complex composed of a calmodulin-dependent
catalytic subunit (also known as calcineurin A) and a regulatory
Ca(2+)-binding subunit (also known as calcineurin B)
(PubMed:8524402, PubMed:12218175, PubMed:12357034,
PubMed:17498738, PubMed:22343722, PubMed:23468591,
PubMed:27974827). There are three catalytic subunits, each encoded
by a separate gene (PPP3CA, PPP3CB, and PPP3CC) and two regulatory
subunits which are also encoded by separate genes (PPP3R1 and
PPP3R2). In response to an increase in Ca(2+) intracellular
levels, forms a complex composed of PPP3CA/calcineurin A,
calcineurin B and calmodulin (By similarity). Interacts (via
calcineurin B binding domain) with regulatory subunit
PPP3R1/calcineurin B (PubMed:8524402, PubMed:12218175,
PubMed:12357034, PubMed:17498738, PubMed:22343722,
PubMed:23468591, PubMed:27974827). Interacts (via calmodulin-
binding domain) with CALM1/calmodulin; the interaction depends on
calmodulin binding to Ca(2+) (PubMed:18384083, Ref.28,
PubMed:19404396, PubMed:25144868). Forms a complex composed of
MYOZ2 and ACTN1 (By similarity). Within the complex interacts with
MYOZ2 (PubMed:11114196). Interacts with MYOZ1 (PubMed:11114196).
Interacts with MYOZ3 (PubMed:11842093). Interacts with CIB1; the
interaction increases upon cardiomyocyte hypertrophy (By
similarity). Interacts with CHP1 and CHP2 (By similarity).
Interacts with CRTC2 (PubMed:15454081). Interacts with DNM1L; the
interaction dephosphorylates DNM1L and promotes its translocation
to mitochondria (PubMed:18838687). Interacts with CMYA5; this
interaction represses calcineurin activity in muscle (By
similarity). Interacts (constitutively active form) with SYNPO2
(PubMed:17923693). Interacts with scaffold protein AKAP5 (via
IAIIIT motif); the interaction recruits PPP3CA to the plasma
membrane following L-type Ca(2+)-channel activation
(PubMed:22343722). Interacts with NFATC2 (PubMed:26248042).
Interacts with RCAN3 (PubMed:26248042). Interacts with PPIA
(PubMed:12218175, PubMed:12357034). Interacts with RCAN1
(PubMed:12809556). {ECO:0000250|UniProtKB:P48452,
ECO:0000250|UniProtKB:P63328, ECO:0000250|UniProtKB:P63329,
ECO:0000269|PubMed:11114196, ECO:0000269|PubMed:11842093,
ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
ECO:0000269|PubMed:12809556, ECO:0000269|PubMed:15454081,
ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:17923693,
ECO:0000269|PubMed:18384083, ECO:0000269|PubMed:18838687,
ECO:0000269|PubMed:19404396, ECO:0000269|PubMed:22343722,
ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:25144868,
ECO:0000269|PubMed:26248042, ECO:0000269|PubMed:27974827,
ECO:0000269|PubMed:8524402, ECO:0000269|Ref.28}.
-!- INTERACTION:
P24588:AKAP5; NbExp=6; IntAct=EBI-15637215, EBI-703640;
R4GN89:C16orf74; NbExp=3; IntAct=EBI-352922, EBI-10225238;
Q8VHW5:Cacng8 (xeno); NbExp=2; IntAct=EBI-352922, EBI-9086576;
P62993:GRB2; NbExp=3; IntAct=EBI-352922, EBI-401755;
O36972:Mal-047 (xeno); NbExp=2; IntAct=EBI-15637215, EBI-16039701;
O95644:NFATC1; NbExp=4; IntAct=EBI-15637215, EBI-6907210;
Q13469:NFATC2; NbExp=2; IntAct=EBI-15637215, EBI-716258;
P63098:PPP3R1; NbExp=7; IntAct=EBI-15637215, EBI-915984;
P54578:USP14; NbExp=3; IntAct=EBI-352922, EBI-1048016;
P46939:UTRN; NbExp=3; IntAct=EBI-15637215, EBI-295856;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19154138,
ECO:0000269|PubMed:22343722}. Cell membrane
{ECO:0000269|PubMed:22343722}; Peripheral membrane protein
{ECO:0000269|PubMed:22343722}. Cell membrane, sarcolemma
{ECO:0000250|UniProtKB:P63329}. Cytoplasm, myofibril, sarcomere, Z
line {ECO:0000250|UniProtKB:P63329}. Cell projection, dendritic
spine {ECO:0000269|PubMed:22343722}. Note=Colocalizes with ACTN1
and MYOZ2 at the Z line in heart and skeletal muscle (By
similarity). Recruited to the cell membrane by scaffold protein
AKAP5 following L-type Ca(2+)-channel activation
(PubMed:22343722). {ECO:0000250|UniProtKB:P63329,
ECO:0000269|PubMed:22343722}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q08209-1; Sequence=Displayed;
Name=2;
IsoId=Q08209-2; Sequence=VSP_018562;
Name=3;
IsoId=Q08209-3; Sequence=VSP_043378, VSP_018562;
Name=4;
IsoId=Q08209-4; Sequence=VSP_047755;
Name=5;
IsoId=Q08209-5; Sequence=VSP_054467;
-!- DOMAIN: The autoinhibitory domain prevents access to the catalytic
site. {ECO:0000250|UniProtKB:P63328}.
-!- DOMAIN: The autoinhibitory segment prevents access to the
substrate binding site. {ECO:0000250|UniProtKB:P63328}.
-!- DOMAIN: Possible isomerization of Pro-309 within the SAPNY motif
triggers a conformation switch which affects the organization and
thus accessibility of the active site and the substrate binding
region (PxIxIF motif). The trans- to cis-transition may favor
calcineurin A activation and substrate binding. The reverse
cis- to trans-transition may be enhanced by peptidyl-prolyl
isomerases such as PPIA. {ECO:0000269|PubMed:26248042}.
-!- DISEASE: Epileptic encephalopathy, infantile or early childhood, 1
(IECEE1) [MIM:617711]: A form of epileptic encephalopathy, a
heterogeneous group of severe childhood onset epilepsies
characterized by refractory seizures, neurodevelopmental
impairment, and poor prognosis. Development is normal prior to
seizure onset, after which cognitive and motor delays become
apparent. IECEE1 is an autosomal dominant condition with onset of
seizures between the first weeks and first years of life.
{ECO:0000269|PubMed:28942967}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Although African swine fever virus infects pigs and
not humans, human PPP3CA has been used for the crystallization.
PPP3CA interacts with African swine fever virus Mal-047/A238L (via
PKIIIT and FLCVK motifs); the interaction does not block catalytic
activity per se but inhibits PPP3CA function by blocking the
access to the two substrate recognition sites.
{ECO:0000269|PubMed:23468591}.
-!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Calcineurin entry;
URL="https://en.wikipedia.org/wiki/Calcineurin";
-----------------------------------------------------------------------
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EMBL; L14778; AAA02631.1; -; mRNA.
EMBL; EU192652; ABW74484.1; -; mRNA.
EMBL; EU192653; ABW74485.1; -; mRNA.
EMBL; AY904364; AAY17314.1; -; mRNA.
EMBL; AK290532; BAF83221.1; -; mRNA.
EMBL; AL353950; CAB89253.1; -; mRNA.
EMBL; AB451338; BAG70152.1; -; mRNA.
EMBL; AB451487; BAG70301.1; -; mRNA.
EMBL; AC092671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471057; EAX06125.1; -; Genomic_DNA.
EMBL; CH471057; EAX06124.1; -; Genomic_DNA.
EMBL; BC025714; AAH25714.1; -; mRNA.
CCDS; CCDS34037.1; -. [Q08209-1]
CCDS; CCDS47113.1; -. [Q08209-3]
CCDS; CCDS47114.1; -. [Q08209-2]
PIR; S35067; S35067.
RefSeq; NP_000935.1; NM_000944.4. [Q08209-1]
RefSeq; NP_001124163.1; NM_001130691.1. [Q08209-2]
RefSeq; NP_001124164.1; NM_001130692.1. [Q08209-3]
UniGene; Hs.435512; -.
PDB; 1AUI; X-ray; 2.10 A; A=1-521.
PDB; 1M63; X-ray; 2.80 A; A/E=1-372.
PDB; 1MF8; X-ray; 3.10 A; A=20-392.
PDB; 2JOG; NMR; -; A=21-347.
PDB; 2JZI; NMR; -; B=391-414.
PDB; 2P6B; X-ray; 2.30 A; A/C=1-380.
PDB; 2R28; X-ray; 1.86 A; C/D=389-413.
PDB; 2W73; X-ray; 1.45 A; K/L/M/O=395-411.
PDB; 3LL8; X-ray; 2.00 A; A/C=14-370.
PDB; 4F0Z; X-ray; 1.70 A; A=1-370.
PDB; 4Q5U; X-ray; 1.95 A; C=391-414.
PDB; 5C1V; X-ray; 3.35 A; A/B=2-346.
PDB; 5SVE; X-ray; 2.60 A; A=1-370.
PDBsum; 1AUI; -.
PDBsum; 1M63; -.
PDBsum; 1MF8; -.
PDBsum; 2JOG; -.
PDBsum; 2JZI; -.
PDBsum; 2P6B; -.
PDBsum; 2R28; -.
PDBsum; 2W73; -.
PDBsum; 3LL8; -.
PDBsum; 4F0Z; -.
PDBsum; 4Q5U; -.
PDBsum; 5C1V; -.
PDBsum; 5SVE; -.
DisProt; DP00092; -.
ProteinModelPortal; Q08209; -.
SMR; Q08209; -.
BioGrid; 111522; 69.
ComplexPortal; CPX-1003; Calcineurin-Calmodulin complex, alpha-R1 variant.
ComplexPortal; CPX-1048; Calcineurin-Calmodulin complex, alpha-R2 variant.
ComplexPortal; CPX-1114; Calcineurin-Calmodulin-AKAP5 complex, alpha-R2 variant.
ComplexPortal; CPX-674; Calcineurin-Calmodulin-AKAP5 complex, alpha-R1 variant.
CORUM; Q08209; -.
DIP; DIP-6095N; -.
ELM; Q08209; -.
IntAct; Q08209; 29.
MINT; Q08209; -.
STRING; 9606.ENSP00000378323; -.
BindingDB; Q08209; -.
ChEMBL; CHEMBL4445; -.
DrugBank; DB08231; MYRISTIC ACID.
DEPOD; Q08209; -.
iPTMnet; Q08209; -.
PhosphoSitePlus; Q08209; -.
SwissPalm; Q08209; -.
BioMuta; PPP3CA; -.
DMDM; 1352673; -.
EPD; Q08209; -.
MaxQB; Q08209; -.
PaxDb; Q08209; -.
PeptideAtlas; Q08209; -.
PRIDE; Q08209; -.
ProteomicsDB; 58579; -.
ProteomicsDB; 58580; -. [Q08209-2]
ProteomicsDB; 58581; -. [Q08209-3]
DNASU; 5530; -.
Ensembl; ENST00000323055; ENSP00000320580; ENSG00000138814. [Q08209-3]
Ensembl; ENST00000394853; ENSP00000378322; ENSG00000138814. [Q08209-2]
Ensembl; ENST00000394854; ENSP00000378323; ENSG00000138814. [Q08209-1]
Ensembl; ENST00000512215; ENSP00000422781; ENSG00000138814. [Q08209-4]
GeneID; 5530; -.
KEGG; hsa:5530; -.
UCSC; uc003hvu.3; human. [Q08209-1]
CTD; 5530; -.
DisGeNET; 5530; -.
EuPathDB; HostDB:ENSG00000138814.16; -.
GeneCards; PPP3CA; -.
HGNC; HGNC:9314; PPP3CA.
HPA; CAB018581; -.
HPA; HPA012778; -.
MalaCards; PPP3CA; -.
MIM; 114105; gene.
MIM; 617711; phenotype.
neXtProt; NX_Q08209; -.
OpenTargets; ENSG00000138814; -.
PharmGKB; PA33678; -.
eggNOG; KOG0375; Eukaryota.
eggNOG; COG0639; LUCA.
GeneTree; ENSGT00530000063087; -.
HOGENOM; HOG000172699; -.
HOVERGEN; HBG002819; -.
InParanoid; Q08209; -.
KO; K04348; -.
OMA; LWSLKIW; -.
OrthoDB; EOG091G094R; -.
PhylomeDB; Q08209; -.
TreeFam; TF105557; -.
Reactome; R-HSA-180024; DARPP-32 events.
Reactome; R-HSA-2025928; Calcineurin activates NFAT.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-4086398; Ca2+ pathway.
Reactome; R-HSA-5607763; CLEC7A (Dectin-1) induces NFAT activation.
SIGNOR; Q08209; -.
ChiTaRS; PPP3CA; human.
EvolutionaryTrace; Q08209; -.
GeneWiki; PPP3CA; -.
GenomeRNAi; 5530; -.
PMAP-CutDB; Q08209; -.
PRO; PR:Q08209; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000138814; Expressed in 244 organ(s), highest expression level in caudate nucleus.
CleanEx; HS_PPP3CA; -.
ExpressionAtlas; Q08209; baseline and differential.
Genevisible; Q08209; HS.
GO; GO:0005955; C:calcineurin complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
GO; GO:0036057; C:slit diaphragm; IEA:Ensembl.
GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IDA:UniProtKB.
GO; GO:0016018; F:cyclosporin A binding; IDA:UniProtKB.
GO; GO:0008144; F:drug binding; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IDA:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; NAS:UniProtKB.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IDA:UniProtKB.
GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; IDA:UniProtKB.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0016311; P:dephosphorylation; TAS:UniProtKB.
GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0033555; P:multicellular organismal response to stress; IEA:Ensembl.
GO; GO:0035562; P:negative regulation of chromatin binding; IEA:Ensembl.
GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IEA:Ensembl.
GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl.
GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; IEA:Ensembl.
GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IEA:Ensembl.
GO; GO:1903244; P:positive regulation of cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
GO; GO:0045785; P:positive regulation of cell adhesion; IMP:ARUK-UCL.
GO; GO:0030335; P:positive regulation of cell migration; IMP:ARUK-UCL.
GO; GO:1905205; P:positive regulation of connective tissue replacement; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl.
GO; GO:0045807; P:positive regulation of endocytosis; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
GO; GO:0051592; P:response to calcium ion; IDA:UniProtKB.
GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
GO; GO:0042110; P:T cell activation; TAS:UniProtKB.
GO; GO:0014883; P:transition between fast and slow fiber; IEA:Ensembl.
GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; TAS:Reactome.
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.
Pfam; PF00149; Metallophos; 1.
PRINTS; PR00114; STPHPHTASE.
SMART; SM00156; PP2Ac; 1.
PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Calmodulin-binding;
Cell membrane; Cell projection; Complete proteome; Cytoplasm;
Disease mutation; Epilepsy; Hydrolase; Iron; Membrane; Metal-binding;
Nitration; Phosphoprotein; Protein phosphatase; Reference proteome;
Zinc.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 521 Serine/threonine-protein phosphatase 2B
catalytic subunit alpha isoform.
/FTId=PRO_0000058822.
REGION 56 340 Catalytic. {ECO:0000305}.
REGION 327 336 Interaction with PxIxIF motif in
substrate. {ECO:0000269|PubMed:17498738,
ECO:0000269|PubMed:17502104,
ECO:0000269|PubMed:22343722,
ECO:0000269|PubMed:23468591,
ECO:0000269|PubMed:26248042}.
REGION 341 369 Calcineurin B binding.
{ECO:0000269|PubMed:12218175,
ECO:0000269|PubMed:12357034,
ECO:0000269|PubMed:17498738,
ECO:0000269|PubMed:23468591,
ECO:0000269|PubMed:27974827,
ECO:0000269|PubMed:8524402}.
REGION 392 406 Calmodulin-binding.
{ECO:0000269|PubMed:18384083,
ECO:0000269|PubMed:19404396,
ECO:0000269|PubMed:25144868,
ECO:0000269|Ref.28}.
REGION 407 414 Autoinhibitory segment.
{ECO:0000250|UniProtKB:P16298}.
REGION 465 487 Autoinhibitory domain.
{ECO:0000269|PubMed:8524402}.
MOTIF 307 311 SAPNY motif.
{ECO:0000305|PubMed:26248042}.
ACT_SITE 151 151 Proton donor.
{ECO:0000305|PubMed:8524402}.
METAL 90 90 Iron. {ECO:0000244|PDB:1AUI,
ECO:0000244|PDB:1M63,
ECO:0000244|PDB:2P6B,
ECO:0000244|PDB:3LL8,
ECO:0000244|PDB:5C1V,
ECO:0000244|PDB:5SVE,
ECO:0000269|PubMed:12218175,
ECO:0000269|PubMed:17498738,
ECO:0000269|PubMed:22343722,
ECO:0000269|PubMed:26248042,
ECO:0000269|PubMed:27974827,
ECO:0000269|PubMed:8524402}.
METAL 92 92 Iron; via tele nitrogen.
{ECO:0000244|PDB:1AUI,
ECO:0000244|PDB:1M63,
ECO:0000244|PDB:2P6B,
ECO:0000244|PDB:3LL8,
ECO:0000244|PDB:5C1V,
ECO:0000244|PDB:5SVE,
ECO:0000269|PubMed:12218175,
ECO:0000269|PubMed:17498738,
ECO:0000269|PubMed:22343722,
ECO:0000269|PubMed:26248042,
ECO:0000269|PubMed:27974827,
ECO:0000269|PubMed:8524402}.
METAL 118 118 Iron. {ECO:0000244|PDB:1AUI,
ECO:0000244|PDB:1M63,
ECO:0000244|PDB:2P6B,
ECO:0000244|PDB:3LL8,
ECO:0000244|PDB:5C1V,
ECO:0000244|PDB:5SVE,
ECO:0000269|PubMed:12218175,
ECO:0000269|PubMed:17498738,
ECO:0000269|PubMed:22343722,
ECO:0000269|PubMed:26248042,
ECO:0000269|PubMed:27974827,
ECO:0000269|PubMed:8524402}.
METAL 118 118 Zinc. {ECO:0000244|PDB:1AUI,
ECO:0000244|PDB:1M63,
ECO:0000244|PDB:2P6B,
ECO:0000244|PDB:3LL8,
ECO:0000244|PDB:5C1V,
ECO:0000244|PDB:5SVE,
ECO:0000269|PubMed:12218175,
ECO:0000269|PubMed:17498738,
ECO:0000269|PubMed:22343722,
ECO:0000269|PubMed:26248042,
ECO:0000269|PubMed:27974827,
ECO:0000269|PubMed:8524402}.
METAL 150 150 Zinc. {ECO:0000244|PDB:1AUI,
ECO:0000244|PDB:1M63,
ECO:0000244|PDB:2P6B,
ECO:0000244|PDB:3LL8,
ECO:0000244|PDB:5C1V,
ECO:0000244|PDB:5SVE,
ECO:0000269|PubMed:12218175,
ECO:0000269|PubMed:17498738,
ECO:0000269|PubMed:22343722,
ECO:0000269|PubMed:26248042,
ECO:0000269|PubMed:27974827,
ECO:0000269|PubMed:8524402}.
METAL 199 199 Zinc; via tele nitrogen.
{ECO:0000244|PDB:1AUI,
ECO:0000244|PDB:1M63,
ECO:0000244|PDB:2P6B,
ECO:0000244|PDB:3LL8,
ECO:0000244|PDB:5C1V,
ECO:0000244|PDB:5SVE,
ECO:0000269|PubMed:12218175,
ECO:0000269|PubMed:17498738,
ECO:0000269|PubMed:22343722,
ECO:0000269|PubMed:26248042,
ECO:0000269|PubMed:27974827,
ECO:0000269|PubMed:8524402}.
METAL 281 281 Zinc; via pros nitrogen.
{ECO:0000244|PDB:1AUI,
ECO:0000244|PDB:1M63,
ECO:0000244|PDB:2P6B,
ECO:0000244|PDB:3LL8,
ECO:0000244|PDB:5C1V,
ECO:0000244|PDB:5SVE,
ECO:0000269|PubMed:12218175,
ECO:0000269|PubMed:17498738,
ECO:0000269|PubMed:22343722,
ECO:0000269|PubMed:26248042,
ECO:0000269|PubMed:27974827,
ECO:0000269|PubMed:8524402}.
SITE 352 352 Interaction with PxVP motif in substrate.
{ECO:0000269|PubMed:23468591,
ECO:0000269|PubMed:27974827}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 224 224 Nitrated tyrosine.
{ECO:0000250|UniProtKB:P63328}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000250|UniProtKB:P63329}.
MOD_RES 492 492 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 20 86 Missing (in isoform 5).
{ECO:0000303|PubMed:21647268}.
/FTId=VSP_054467.
VAR_SEQ 87 318 Missing (in isoform 4).
{ECO:0000303|PubMed:20590401}.
/FTId=VSP_047755.
VAR_SEQ 318 359 Missing (in isoform 3).
{ECO:0000303|PubMed:20590401}.
/FTId=VSP_043378.
VAR_SEQ 448 457 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:20590401}.
/FTId=VSP_018562.
VARIANT 92 92 H -> R (in IECEE1; unknown pathological
significance).
{ECO:0000269|PubMed:28942967}.
/FTId=VAR_080348.
VARIANT 281 281 H -> Q (in IECEE1; unknown pathological
significance).
{ECO:0000269|PubMed:28942967}.
/FTId=VAR_080349.
VARIANT 282 282 E -> K (in IECEE1; unknown pathological
significance).
{ECO:0000269|PubMed:28942967}.
/FTId=VAR_080350.
VARIANT 445 521 Missing (in IECEE1; unknown pathological
significance).
{ECO:0000269|PubMed:28942967}.
/FTId=VAR_080351.
VARIANT 447 447 A -> T (in IECEE1; unknown pathological
significance).
{ECO:0000269|PubMed:28942967}.
/FTId=VAR_080352.
MUTAGEN 288 288 Y->F: Partial loss of Ca(2+)-mediated
transcription factor NFAT activation;
when associated with F-341.
{ECO:0000269|PubMed:26248042}.
MUTAGEN 288 288 Y->N,A: Loss of Ca(2+)-mediated
transcription factor NFAT activation;
when associated with F-341.
{ECO:0000269|PubMed:26248042}.
MUTAGEN 328 332 Missing: Loss of Ca(2+)-mediated
transcription factor NFAT activation;
when associated with F-341.
{ECO:0000269|PubMed:26248042}.
MUTAGEN 341 341 Y->F: Resistant to cyclosporin A-mediated
inhibition. Loss of Ca(2+)-mediated
transcription factor NFAT activation;
when associated with N-288, A-228 or 328-
V--R-332 DEL. Partial loss in Ca(2+)-
mediated transcription factor NFAT
activation; when associated with F-288.
{ECO:0000269|PubMed:26248042}.
STRAND 13 15 {ECO:0000244|PDB:5SVE}.
HELIX 31 34 {ECO:0000244|PDB:4F0Z}.
HELIX 43 51 {ECO:0000244|PDB:4F0Z}.
HELIX 58 73 {ECO:0000244|PDB:4F0Z}.
STRAND 77 81 {ECO:0000244|PDB:4F0Z}.
STRAND 83 88 {ECO:0000244|PDB:4F0Z}.
HELIX 95 105 {ECO:0000244|PDB:4F0Z}.
TURN 108 110 {ECO:0000244|PDB:3LL8}.
STRAND 113 115 {ECO:0000244|PDB:4F0Z}.
STRAND 120 123 {ECO:0000244|PDB:4F0Z}.
HELIX 126 139 {ECO:0000244|PDB:4F0Z}.
TURN 141 143 {ECO:0000244|PDB:4F0Z}.
STRAND 144 146 {ECO:0000244|PDB:4F0Z}.
HELIX 154 159 {ECO:0000244|PDB:4F0Z}.
HELIX 162 169 {ECO:0000244|PDB:4F0Z}.
HELIX 172 183 {ECO:0000244|PDB:4F0Z}.
STRAND 188 191 {ECO:0000244|PDB:4F0Z}.
TURN 192 194 {ECO:0000244|PDB:4F0Z}.
STRAND 195 200 {ECO:0000244|PDB:4F0Z}.
STRAND 206 208 {ECO:0000244|PDB:2JOG}.
HELIX 210 213 {ECO:0000244|PDB:4F0Z}.
STRAND 218 220 {ECO:0000244|PDB:4F0Z}.
STRAND 223 225 {ECO:0000244|PDB:4F0Z}.
HELIX 226 232 {ECO:0000244|PDB:4F0Z}.
TURN 237 240 {ECO:0000244|PDB:4F0Z}.
STRAND 247 250 {ECO:0000244|PDB:4F0Z}.
TURN 252 254 {ECO:0000244|PDB:4F0Z}.
STRAND 255 260 {ECO:0000244|PDB:4F0Z}.
HELIX 262 271 {ECO:0000244|PDB:4F0Z}.
STRAND 276 279 {ECO:0000244|PDB:4F0Z}.
STRAND 287 290 {ECO:0000244|PDB:4F0Z}.
TURN 295 297 {ECO:0000244|PDB:4F0Z}.
STRAND 298 306 {ECO:0000244|PDB:4F0Z}.
HELIX 311 313 {ECO:0000244|PDB:4F0Z}.
STRAND 319 325 {ECO:0000244|PDB:4F0Z}.
STRAND 328 334 {ECO:0000244|PDB:4F0Z}.
HELIX 344 346 {ECO:0000244|PDB:4F0Z}.
HELIX 349 369 {ECO:0000244|PDB:4F0Z}.
HELIX 396 409 {ECO:0000244|PDB:2W73}.
HELIX 470 477 {ECO:0000244|PDB:1AUI}.
HELIX 478 481 {ECO:0000244|PDB:1AUI}.
SEQUENCE 521 AA; 58688 MW; 16480D62DDBF1F40 CRC64;
MSEPKAIDPK LSTTDRVVKA VPFPPSHRLT AKEVFDNDGK PRVDILKAHL MKEGRLEESV
ALRIITEGAS ILRQEKNLLD IDAPVTVCGD IHGQFFDLMK LFEVGGSPAN TRYLFLGDYV
DRGYFSIECV LYLWALKILY PKTLFLLRGN HECRHLTEYF TFKQECKIKY SERVYDACMD
AFDCLPLAAL MNQQFLCVHG GLSPEINTLD DIRKLDRFKE PPAYGPMCDI LWSDPLEDFG
NEKTQEHFTH NTVRGCSYFY SYPAVCEFLQ HNNLLSILRA HEAQDAGYRM YRKSQTTGFP
SLITIFSAPN YLDVYNNKAA VLKYENNVMN IRQFNCSPHP YWLPNFMDVF TWSLPFVGEK
VTEMLVNVLN ICSDDELGSE EDGFDGATAA ARKEVIRNKI RAIGKMARVF SVLREESESV
LTLKGLTPTG MLPSGVLSGG KQTLQSATVE AIEADEAIKG FSPQHKITSF EEAKGLDRIN
ERMPPRRDAM PSDANLNSIN KALTSETNGT DSNGSNSSNI Q


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