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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) (CNA alpha)

 PP2BA_MOUSE             Reviewed;         521 AA.
P63328; P12816; P20652; Q3UCU1; Q64135;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
29-SEP-2021, entry version 173.
RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform;
EC=3.1.3.16 {ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:7791792};
AltName: Full=CAM-PRP catalytic subunit;
AltName: Full=Calmodulin-dependent calcineurin A subunit alpha isoform;
Short=CNA alpha {ECO:0000305|PubMed:26794871};
Name=Ppp3ca; Synonyms=Calna;
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] (ISOFORM 1).
PubMed=2162844;
Kincaid R.L., Giri P.R., Higuchi S., Tamura J., Dixon S.C., Marietta C.A.,
Amorese D.A., Martin B.M.;
"Cloning and characterization of molecular isoforms of the catalytic
subunit of calcineurin using nonisotopic methods.";
J. Biol. Chem. 265:11312-11319(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Bone marrow;
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]
PROTEIN SEQUENCE OF 64-73; 101-122 AND 425-459, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 95-116.
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 215-521 (ISOFORM 1).
PubMed=2848250; DOI=10.1073/pnas.85.23.8983;
Kincaid R.L., Nightingale M.S., Martin B.M.;
"Characterization of a cDNA clone encoding the calmodulin-binding domain of
mouse brain calcineurin.";
Proc. Natl. Acad. Sci. U.S.A. 85:8983-8987(1988).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 467-491, FUNCTION, CATALYTIC ACTIVITY, AND
MUTAGENESIS OF ASP-477.
PubMed=7791792; DOI=10.1128/mcb.15.7.3857;
Fruman D.A., Pai S.-Y., Burakoff S.J., Bierer B.E.;
"Characterization of a mutant calcineurin A alpha gene expressed by EL4
lymphoma cells.";
Mol. Cell. Biol. 15:3857-3863(1995).
[7]
IDENTIFICATION IN A COMPLEX WITH ACTN1 AND MYOZ2, AND 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).
[8]
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).
[9]
NITRATION [LARGE SCALE ANALYSIS] AT TYR-224, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16800626; DOI=10.1021/bi060474w;
Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G.,
Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C.,
Bigelow D.J.;
"Endogenously nitrated proteins in mouse brain: links to neurodegenerative
disease.";
Biochemistry 45:8009-8022(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, 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).
[11]
INTERACTION WITH CIB1.
PubMed=20639889; DOI=10.1038/nm.2181;
Heineke J., Auger-Messier M., Correll R.N., Xu J., Benard M.J., Yuan W.,
Drexler H., Parise L.V., Molkentin J.D.;
"CIB1 is a regulator of pathological cardiac hypertrophy.";
Nat. Med. 16:872-879(2010).
[12]
INTERACTION WITH CMYA5.
PubMed=21427212; DOI=10.1096/fj.10-169219;
Kielbasa O.M., Reynolds J.G., Wu C.L., Snyder C.M., Cho M.Y., Weiler H.,
Kandarian S., Naya F.J.;
"Myospryn is a calcineurin-interacting protein that negatively modulates
slow-fiber-type transformation and skeletal muscle regeneration.";
FASEB J. 25:2276-2286(2011).
[13]
INTERACTION WITH CRTC1 AND CRTC2.
PubMed=30611118; DOI=10.1016/j.isci.2018.12.012;
Sonntag T., Ostojic J., Vaughan J.M., Moresco J.J., Yoon Y.S.,
Yates J.R. III, Montminy M.;
"Mitogenic Signals Stimulate the CREB Coactivator CRTC3 through PP2A
Recruitment.";
IScience 11:134-145(2018).
[14]
INTERACTION WITH UNC119.
PubMed=31696965; DOI=10.15252/embj.2018101409;
Chaya T., Tsutsumi R., Varner L.R., Maeda Y., Yoshida S., Furukawa T.;
"Cul3-Klhl18 ubiquitin ligase modulates rod transducin translocation during
light-dark adaptation.";
EMBO J. 2019:E101409-E101409(2019).
[15]
X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) IN COMPLEX WITH PPP3R1; IRON AND
ZINC, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF
348-ALA--GLN-521; 389-ASP--GLN-521; 406-MET--GLN-521 AND 442-GLN--GLN-521.
PubMed=26794871; DOI=10.1038/cr.2016.14;
Li S.J., Wang J., Ma L., Lu C., Wang J., Wu J.W., Wang Z.X.;
"Cooperative autoinhibition and multi-level activation mechanisms of
calcineurin.";
Cell Res. 26:336-349(2016).
-!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase
which plays an essential role in the transduction of intracellular
Ca(2+)-mediated signals (PubMed:7791792, PubMed:26794871). Many of the
substrates contain a PxIxIT motif and/or a LxVP motif (By similarity).
In response to increased Ca(2+) levels, dephosphorylates and activates
phosphatase SSH1 which results in cofilin dephosphorylation (By
similarity). In response to increased Ca(2+) levels following
mitochondrial depolarization, dephosphorylates DNM1L inducing DNM1L
translocation to the mitochondrion (By similarity). Dephosphorylates
heat shock protein HSPB1 (By similarity). Dephosphorylates and
activates transcription factor NFATC1 (By similarity). Dephosphorylates
and inactivates transcription factor ELK1 (By similarity).
Dephosphorylates DARPP32 (By similarity). May dephosphorylate CRTC2 at
'Ser-171' resulting in CRTC2 dissociation from 14-3-3 proteins (By
similarity). {ECO:0000250|UniProtKB:P48452,
ECO:0000250|UniProtKB:Q08209, ECO:0000269|PubMed:26794871,
ECO:0000269|PubMed:7791792}.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
ChEBI:CHEBI:83421; EC=3.1.3.16;
Evidence={ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:7791792};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
ChEBI:CHEBI:61977; EC=3.1.3.16;
Evidence={ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:7791792};
-!- COFACTOR:
Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
Evidence={ECO:0000269|PubMed:26794871};
Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000269|PubMed:26794871};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:26794871};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:26794871};
-!- ACTIVITY REGULATION: Activated by Ca(2+)-bound calmodulin following an
increase in intracellular Ca(2+) (PubMed:26794871). 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+) (PubMed:26794871). 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
(PubMed:26794871). 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 (PubMed:26794871).
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 (By
similarity). {ECO:0000250|UniProtKB:P48452,
ECO:0000269|PubMed:26794871}.
-!- 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:26794871). 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:26794871). Interacts (via calmodulin-
binding domain) with calmodulin; the interaction depends on calmodulin
binding to Ca(2+) (By similarity). Forms a complex composed of MYOZ2
and ACTN1 (PubMed:11114196). Within the complex interacts with MYOZ2
(PubMed:11114196). Interacts with MYOZ1 (PubMed:11114196). Interacts
with MYOZ3 (By similarity). Interacts with CIB1; the interaction
increases upon cardiomyocyte hypertrophy (PubMed:20639889). Interacts
with CHP1 and CHP2 (By similarity). Interacts with CRTC1
(PubMed:30611118). Interacts with CRTC2 (PubMed:30611118). Interacts
with DNM1L; the interaction dephosphorylates DNM1L and promotes its
translocation to mitochondria (By similarity). Interacts with CMYA5;
this interaction represses calcineurin activity in muscle
(PubMed:21427212). Interacts (constitutively active form) with SYNPO2
(By similarity). Interacts with scaffold protein AKAP5 (via IAIIIT
motif); the interaction recruits PPP3CA to the plasma membrane
following L-type Ca(2+)-channel activation (By similarity). Interacts
with NFATC2 (By similarity). Interacts with RCAN3 (By similarity).
Interacts with PPIA (By similarity). Interacts with RCAN1
(PubMed:12809556). Interacts with UNC119 (PubMed:31696965).
{ECO:0000250|UniProtKB:P48452, ECO:0000250|UniProtKB:P63329,
ECO:0000250|UniProtKB:Q08209, ECO:0000269|PubMed:11114196,
ECO:0000269|PubMed:12809556, ECO:0000269|PubMed:20639889,
ECO:0000269|PubMed:21427212, ECO:0000269|PubMed:26794871,
ECO:0000269|PubMed:30611118, ECO:0000269|PubMed:31696965}.
-!- INTERACTION:
P63328; Q3U182: Crtc2; NbExp=2; IntAct=EBI-397208, EBI-8018890;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q08209}. Cell
membrane {ECO:0000250|UniProtKB:Q08209}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q08209}. Cell membrane, sarcolemma
{ECO:0000250|UniProtKB:P63329}. Cytoplasm, myofibril, sarcomere, Z line
{ECO:0000250|UniProtKB:P63329}. Cell projection, dendritic spine
{ECO:0000250|UniProtKB:Q08209}. Note=Colocalizes with ACTN1 and MYOZ2
at the Z line in heart and skeletal muscle. Recruited to the cell
membrane by scaffold protein AKAP5 following L-type Ca(2+)-channel
activation. {ECO:0000250|UniProtKB:P63329,
ECO:0000250|UniProtKB:Q08209}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P63328-1; Sequence=Displayed;
Name=2;
IsoId=P63328-2; Sequence=VSP_018563;
-!- DOMAIN: The autoinhibitory domain prevents access to the catalytic
site. {ECO:0000269|PubMed:26794871}.
-!- DOMAIN: The autoinhibitory segment prevents access to the substrate
binding site. {ECO:0000269|PubMed:26794871}.
-!- 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:0000250|UniProtKB:Q08209}.
-!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.
{ECO:0000305}.
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EMBL; J05479; AAA37359.1; -; mRNA.
EMBL; AK146387; BAE27131.1; -; mRNA.
EMBL; AK150393; BAE29521.1; -; mRNA.
EMBL; J04134; AAA37432.1; -; mRNA.
EMBL; S78668; AAB34675.1; -; mRNA.
CCDS; CCDS17860.1; -. [P63328-1]
CCDS; CCDS80027.1; -. [P63328-2]
PIR; A42232; A31257.
RefSeq; NP_001280551.1; NM_001293622.1. [P63328-2]
RefSeq; NP_032939.1; NM_008913.5. [P63328-1]
PDB; 4ORB; X-ray; 3.11 A; A=1-521.
PDBsum; 4ORB; -.
BMRB; P63328; -.
SMR; P63328; -.
BioGRID; 202344; 40.
ComplexPortal; CPX-1010; Calcineurin-Calmodulin complex, alpha-R1 variant.
ComplexPortal; CPX-1049; Calcineurin-Calmodulin complex, alpha-R2 variant.
ComplexPortal; CPX-1115; Calcineurin-Calmodulin-AKAP5 complex, alpha-R2 variant.
ComplexPortal; CPX-881; Calcineurin-Calmodulin-AKAP5 complex, alpha-R1 variant.
DIP; DIP-31543N; -.
IntAct; P63328; 14.
MINT; P63328; -.
STRING; 10090.ENSMUSP00000053101; -.
iPTMnet; P63328; -.
PhosphoSitePlus; P63328; -.
SwissPalm; P63328; -.
MaxQB; P63328; -.
PaxDb; P63328; -.
PeptideAtlas; P63328; -.
PRIDE; P63328; -.
ProteomicsDB; 289791; -. [P63328-1]
ProteomicsDB; 289792; -. [P63328-2]
Antibodypedia; 2193; 589 antibodies.
DNASU; 19055; -.
Ensembl; ENSMUST00000056758; ENSMUSP00000053101; ENSMUSG00000028161. [P63328-1]
Ensembl; ENSMUST00000070198; ENSMUSP00000071040; ENSMUSG00000028161. [P63328-2]
GeneID; 19055; -.
KEGG; mmu:19055; -.
UCSC; uc008rmg.2; mouse. [P63328-1]
UCSC; uc008rmh.2; mouse. [P63328-2]
CTD; 5530; -.
MGI; MGI:107164; Ppp3ca.
VEuPathDB; HostDB:ENSMUSG00000028161; -.
eggNOG; KOG0375; Eukaryota.
GeneTree; ENSGT00940000156306; -.
HOGENOM; CLU_004962_6_0_1; -.
InParanoid; P63328; -.
OMA; MESFCCL; -.
PhylomeDB; P63328; -.
TreeFam; TF105557; -.
Reactome; R-MMU-2025928; Calcineurin activates NFAT.
Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-MMU-4086398; Ca2+ pathway.
Reactome; R-MMU-5607763; CLEC7A (Dectin-1) induces NFAT activation.
BioGRID-ORCS; 19055; 1 hit in 62 CRISPR screens.
ChiTaRS; Ppp3ca; mouse.
PRO; PR:P63328; -.
Proteomes; UP000000589; Chromosome 3.
RNAct; P63328; protein.
Bgee; ENSMUSG00000028161; Expressed in caudate-putamen and 314 other tissues.
Genevisible; P63328; MM.
GO; GO:0005955; C:calcineurin complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0043197; C:dendritic spine; ISO:MGI.
GO; GO:0098978; C:glutamatergic synapse; IMP:SynGO.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
GO; GO:0036057; C:slit diaphragm; IEA:Ensembl.
GO; GO:0045202; C:synapse; ISO:MGI.
GO; GO:0030018; C:Z disc; IDA:MGI.
GO; GO:0051117; F:ATPase binding; ISO:MGI.
GO; GO:0004723; F:calcium-dependent protein serine/threonine phosphatase activity; ISO:MGI.
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; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:MGI.
GO; GO:0046983; F:protein dimerization activity; ISO:MGI.
GO; GO:0106306; F:protein serine phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISO:MGI.
GO; GO:0106307; F:protein threonine phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0097720; P:calcineurin-mediated signaling; ISO:MGI.
GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IDA:MGI.
GO; GO:0006816; P:calcium ion transport; IMP:MGI.
GO; GO:0019722; P:calcium-mediated signaling; IGI:MGI.
GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IGI:MGI.
GO; GO:0071333; P:cellular response to glucose stimulus; ISO:MGI.
GO; GO:0016311; P:dephosphorylation; IDA:MGI.
GO; GO:0060079; P:excitatory postsynaptic potential; IGI:MGI.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:MGI.
GO; GO:0033555; P:multicellular organismal response to stress; IDA:MGI.
GO; GO:0035562; P:negative regulation of chromatin binding; IMP:MGI.
GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IMP:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
GO; GO:0046676; P:negative regulation of insulin secretion; ISO:MGI.
GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; IDA:BHF-UCL.
GO; GO:0070262; P:peptidyl-serine dephosphorylation; ISO:MGI.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IGI:BHF-UCL.
GO; GO:1903244; P:positive regulation of cardiac muscle hypertrophy in response to stress; IDA:BHF-UCL.
GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:1905205; P:positive regulation of connective tissue replacement; IGI:BHF-UCL.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:MGI.
GO; GO:0045807; P:positive regulation of endocytosis; IMP:ARUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IMP:SynGO.
GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
GO; GO:0006606; P:protein import into nucleus; IDA:MGI.
GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
GO; GO:0051592; P:response to calcium ion; ISS:UniProtKB.
GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
GO; GO:0014883; P:transition between fast and slow fiber; IDA:MGI.
CDD; cd07416; MPP_PP2B; 1.
Gene3D; 3.60.21.10; -; 1.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
InterPro; IPR041751; MPP_PP2B.
InterPro; IPR043360; PP2B.
InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
PANTHER; PTHR45673; PTHR45673; 1.
Pfam; PF00149; Metallophos; 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; Calmodulin-binding;
Cell junction; Cell membrane; Cell projection; Cytoplasm;
Direct protein sequencing; Hydrolase; Iron; Membrane; Metal-binding;
Nitration; Phosphoprotein; Protein phosphatase; Reference proteome;
Synapse; Zinc.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000250|UniProtKB:Q08209"
CHAIN 2..521
/note="Serine/threonine-protein phosphatase 2B catalytic
subunit alpha isoform"
/id="PRO_0000058823"
REGION 56..340
/note="Catalytic"
/evidence="ECO:0000305"
REGION 327..336
/note="Interaction with PxIxIF motif in substrate"
/evidence="ECO:0000250|UniProtKB:Q08209"
REGION 341..369
/note="Calcineurin B binding"
/evidence="ECO:0000269|PubMed:26794871"
REGION 392..406
/note="Calmodulin-binding"
/evidence="ECO:0000269|PubMed:26794871"
REGION 407..414
/note="Autoinhibitory segment"
/evidence="ECO:0000269|PubMed:26794871"
REGION 465..487
/note="Autoinhibitory domain"
/evidence="ECO:0000269|PubMed:26794871"
REGION 475..521
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOTIF 307..311
/note="SAPNY motif"
/evidence="ECO:0000250|UniProtKB:Q08209"
COMPBIAS 493..521
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
ACT_SITE 151
/note="Proton donor"
/evidence="ECO:0000250|UniProtKB:Q08209"
METAL 90
/note="Iron"
/evidence="ECO:0000269|PubMed:26794871,
ECO:0007744|PDB:4ORB"
METAL 92
/note="Iron; via tele nitrogen"
/evidence="ECO:0000269|PubMed:26794871,
ECO:0007744|PDB:4ORB"
METAL 118
/note="Iron"
/evidence="ECO:0000269|PubMed:26794871,
ECO:0007744|PDB:4ORB"
METAL 118
/note="Zinc"
/evidence="ECO:0000269|PubMed:26794871,
ECO:0007744|PDB:4ORB"
METAL 150
/note="Zinc"
/evidence="ECO:0000269|PubMed:26794871,
ECO:0007744|PDB:4ORB"
METAL 199
/note="Zinc; via tele nitrogen"
/evidence="ECO:0000269|PubMed:26794871,
ECO:0007744|PDB:4ORB"
METAL 281
/note="Zinc; via pros nitrogen"
/evidence="ECO:0000269|PubMed:26794871,
ECO:0007744|PDB:4ORB"
SITE 352
/note="Interaction with PxVP motif in substrate"
/evidence="ECO:0000250|UniProtKB:Q08209"
MOD_RES 2
/note="N-acetylserine"
/evidence="ECO:0000250|UniProtKB:Q08209"
MOD_RES 224
/note="3'-nitrotyrosine"
/evidence="ECO:0007744|PubMed:16800626"
MOD_RES 469
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P63329"
MOD_RES 492
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
VAR_SEQ 448..457
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:16141072"
/id="VSP_018563"
MUTAGEN 348..521
/note="Missing: Loss of catalytic activity. Loss of
interaction with PPP3R1/calreticulin B and calmodulin."
/evidence="ECO:0000269|PubMed:26794871"
MUTAGEN 389..521
/note="Missing: Increases catalytic activity independently
of calmodulin. Loss of interaction with calmodulin. Does
not affect interaction with PPP3R1/calreticulin B."
/evidence="ECO:0000269|PubMed:26794871"
MUTAGEN 406..521
/note="Missing: Increases catalytic activity independently
of calmodulin. Does not affect interaction with
PPP3R1/calreticulin B and calmodulin."
/evidence="ECO:0000269|PubMed:26794871"
MUTAGEN 442..521
/note="Missing: Increases basal catalytic activity. Does
not affect interaction with PPP3R1/calreticulin B and
calmodulin."
/evidence="ECO:0000269|PubMed:26794871"
MUTAGEN 477
/note="D->N: Greatly reduces inhibition of calcineurin
phosphatase activity."
/evidence="ECO:0000269|PubMed:7791792"
HELIX 31..34
/evidence="ECO:0007829|PDB:4ORB"
HELIX 43..51
/evidence="ECO:0007829|PDB:4ORB"
HELIX 58..72
/evidence="ECO:0007829|PDB:4ORB"
STRAND 77..81
/evidence="ECO:0007829|PDB:4ORB"
STRAND 83..88
/evidence="ECO:0007829|PDB:4ORB"
HELIX 95..105
/evidence="ECO:0007829|PDB:4ORB"
TURN 108..110
/evidence="ECO:0007829|PDB:4ORB"
STRAND 113..115
/evidence="ECO:0007829|PDB:4ORB"
STRAND 120..123
/evidence="ECO:0007829|PDB:4ORB"
HELIX 126..139
/evidence="ECO:0007829|PDB:4ORB"
TURN 141..143
/evidence="ECO:0007829|PDB:4ORB"
STRAND 144..146
/evidence="ECO:0007829|PDB:4ORB"
HELIX 154..159
/evidence="ECO:0007829|PDB:4ORB"
HELIX 161..169
/evidence="ECO:0007829|PDB:4ORB"
HELIX 172..182
/evidence="ECO:0007829|PDB:4ORB"
STRAND 188..191
/evidence="ECO:0007829|PDB:4ORB"
TURN 192..194
/evidence="ECO:0007829|PDB:4ORB"
STRAND 195..200
/evidence="ECO:0007829|PDB:4ORB"
HELIX 209..213
/evidence="ECO:0007829|PDB:4ORB"
STRAND 223..225
/evidence="ECO:0007829|PDB:4ORB"
HELIX 226..232
/evidence="ECO:0007829|PDB:4ORB"
TURN 237..240
/evidence="ECO:0007829|PDB:4ORB"
STRAND 248..250
/evidence="ECO:0007829|PDB:4ORB"
TURN 252..254
/evidence="ECO:0007829|PDB:4ORB"
STRAND 255..260
/evidence="ECO:0007829|PDB:4ORB"
HELIX 262..271
/evidence="ECO:0007829|PDB:4ORB"
STRAND 275..279
/evidence="ECO:0007829|PDB:4ORB"
STRAND 286..290
/evidence="ECO:0007829|PDB:4ORB"
TURN 295..297
/evidence="ECO:0007829|PDB:4ORB"
STRAND 298..306
/evidence="ECO:0007829|PDB:4ORB"
HELIX 311..313
/evidence="ECO:0007829|PDB:4ORB"
STRAND 318..325
/evidence="ECO:0007829|PDB:4ORB"
STRAND 328..334
/evidence="ECO:0007829|PDB:4ORB"
HELIX 344..346
/evidence="ECO:0007829|PDB:4ORB"
HELIX 349..369
/evidence="ECO:0007829|PDB:4ORB"
HELIX 470..476
/evidence="ECO:0007829|PDB:4ORB"
HELIX 478..481
/evidence="ECO:0007829|PDB:4ORB"
SEQUENCE 521 AA; 58644 MW; 16530C27DDBF1F05 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 SYPAVCDFLQ HNNLLSILRA HEAQDAGYRM YRKSQTTGFP
SLITIFSAPN YLDVYNNKAA VLKYENNVMN IRQFNCSPHP YWLPNFMDVF TWSLPFVGEK
VTEMLVNVLN ICSDDELGSE EDGFDGATAA ARKEVIRNKI RAIGKMARVF SVLREESESV
LTLKGLTPTG MLPSGVLSGG KQTLQSATVE AIEADEAIKG FSPQHKITSF EEAKGLDRIN
ERMPPRRDAM PSDANLNSIN KALASETNGT DSNGSNSSNI Q


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WP622: Long-Day Flowering Time Pathway
WP1120: Ovarian Infertility Genes
WP1209: EBV LMP1 signaling
WP1659: Glycine, serine and threonine metabolism
WP34: Ovarian Infertility Genes
WP1584: Type II diabetes mellitus
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Related Genes :
[Ppp3ca Calna] 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) (CNA alpha)
[PPP3CA CALNA CNA] 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)
[Ppp3ca Calna] 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)
[PPP3CA] 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)
[PPP3CB CALNA2 CALNB CNA2] Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calmodulin-dependent calcineurin A subunit beta isoform) (CNA beta)
[CNA1 CNAG_04796] Serine/threonine-protein phosphatase 2B catalytic subunit A1 (EC 3.1.3.16) (Calcineurin A1)
[PPP2CA] Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (PP2A-alpha) (EC 3.1.3.16) (Replication protein C) (RP-C)
[Ppp2ca] Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (PP2A-alpha) (EC 3.1.3.16)
[Ppp2ca] Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (PP2A-alpha) (EC 3.1.3.16)
[PPP2CA] Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (PP2A-alpha) (EC 3.1.3.16)
[cna-1 99H12.070 NCU03804] Serine/threonine-protein phosphatase 2B catalytic subunit (EC 3.1.3.16) (Calmodulin-dependent calcineurin A subunit)
[PPP3R1 CNA2 CNB] Calcineurin subunit B type 1 (Protein phosphatase 2B regulatory subunit 1) (Protein phosphatase 3 regulatory subunit B alpha isoform 1)
[PPP1CA PPP1A] Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PP-1A) (EC 3.1.3.16)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[PPP1CA PPP1A] Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PP-1A) (EC 3.1.3.16)
[PPP2CA] Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (PP2A-alpha) (EC 3.1.3.16)
[Ppp2cb] Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform (PP2A-beta) (EC 3.1.3.16)
[PIK3CA] Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform (PI3-kinase subunit alpha) (PI3K-alpha) (PI3Kalpha) (PtdIns-3-kinase subunit alpha) (EC 2.7.1.137) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha) (PtdIns-3-kinase subunit p110-alpha) (p110alpha) (Phosphoinositide 3-kinase alpha) (Phosphoinositide-3-kinase catalytic alpha polypeptide) (Serine/threonine protein kinase PIK3CA) (EC 2.7.11.1)
[Camk2a] Calcium/calmodulin-dependent protein kinase type II subunit alpha (CaM kinase II subunit alpha) (CaMK-II subunit alpha) (EC 2.7.11.17)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[Pik3ca] Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform (PI3-kinase subunit alpha) (PI3K-alpha) (PI3Kalpha) (PtdIns-3-kinase subunit alpha) (EC 2.7.1.137) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha) (PtdIns-3-kinase subunit p110-alpha) (p110alpha) (Phosphoinositide-3-kinase catalytic alpha polypeptide) (Serine/threonine protein kinase PIK3CA) (EC 2.7.11.1)
[Pik3ca] Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform (PI3-kinase subunit alpha) (PI3K-alpha) (PI3Kalpha) (PtdIns-3-kinase subunit alpha) (EC 2.7.1.137) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha) (PtdIns-3-kinase subunit p110-alpha) (p110alpha) (Phosphoinositide-3-kinase catalytic alpha polypeptide) (Serine/threonine protein kinase PIK3CA) (EC 2.7.11.1)
[PPP1CC] Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (PP-1G) (EC 3.1.3.16) (Protein phosphatase 1C catalytic subunit)
[] Genome polyprotein [Cleaved into: Protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[Ppp2cb] Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform (PP2A-beta) (EC 3.1.3.16)
[PIK3CA] Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform (PI3-kinase subunit alpha) (PI3K-alpha) (PI3Kalpha) (PtdIns-3-kinase subunit alpha) (EC 2.7.1.137) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha) (PtdIns-3-kinase subunit p110-alpha) (p110alpha) (Phosphoinositide-3-kinase catalytic alpha polypeptide) (Serine/threonine protein kinase PIK3CA) (EC 2.7.11.1)
[PP2A3 PP2A4 At2g42500 MHK10.22] Serine/threonine-protein phosphatase PP2A-3 catalytic subunit (EC 3.1.3.16) (Protein phosphatase 2A isoform 3)
[PP2A4 EP7 PP2A3 At3g58500 F14P22.90] Serine/threonine-protein phosphatase PP2A-4 catalytic subunit (EC 3.1.3.16) (Protein phosphatase 2A isoform 4)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]

Bibliography :
No related Items