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Nuclear factor of activated T-cells, cytoplasmic 1 (NF-ATc1) (NFATc1) (NFAT transcription complex cytosolic component) (NF-ATc) (NFATc)

 NFAC1_HUMAN             Reviewed;         943 AA.
O95644; B5B2M4; B5B2M5; B5B2M6; B5B2M7; B5B2M8; B5B2M9; B5B2N1;
Q12865; Q15793; Q2M1S3;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 3.
20-JUN-2018, entry version 194.
RecName: Full=Nuclear factor of activated T-cells, cytoplasmic 1;
Short=NF-ATc1;
Short=NFATc1;
AltName: Full=NFAT transcription complex cytosolic component;
Short=NF-ATc;
Short=NFATc;
Name=NFATC1; Synonyms=NFAT2, NFATC;
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 A-ALPHA).
TISSUE=Peripheral blood lymphocyte, and T-cell;
PubMed=8202141; DOI=10.1038/369497a0;
Northrop J.P., Ho S.N., Chen L., Thomas D.J., Timmerman L.A.,
Nolan G.P., Admon A., Crabtree G.R.;
"NF-AT components define a family of transcription factors targeted in
T-cell activation.";
Nature 369:497-502(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B-BETA).
TISSUE=B-cell;
PubMed=8702849; DOI=10.1074/jbc.271.34.20914;
Park J., Takeuchi A., Sharma S.;
"Characterization of a new isoform of the NFAT (nuclear factor of
activated T cells) gene family member NFATc.";
J. Biol. Chem. 271:20914-20921(1996).
[3]
ERRATUM.
Park J., Takeuchi A., Sharma S.;
J. Biol. Chem. 271:33705-33705(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A-ALPHA; B-ALPHA AND C-BETA).
TISSUE=B-cell lymphoma;
PubMed=10072078; DOI=10.1016/S1074-7613(00)80026-6;
Chuvpilo S., Zimmer M., Kerstan A., Gloeckner J., Avots A., Escher C.,
Fischer C., Inashkina I., Jankevics E., Berberich-Siebelt F.,
Schmitt E., Serfling E.;
"Alternative polyadenylation events contribute to the induction of NF-
ATc in effector T cells.";
Immunity 10:261-269(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C-ALPHA; IA-DELTAIX AND
IB-DELTAIX), ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=18675896; DOI=10.1016/j.ygeno.2008.06.011;
Vihma H., Pruunsild P., Timmusk T.;
"Alternative splicing and expression of human and mouse NFAT genes.";
Genomics 92:279-291(2008).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A-ALPHA).
TISSUE=Brain;
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).
[9]
IDENTIFICATION OF ISOFORM A-ALPHA'.
PubMed=9111316; DOI=10.1128/MCB.17.5.2475;
Lyakh L., Ghosh P., Rice N.R.;
"Expression of NFAT-family proteins in normal human T cells.";
Mol. Cell. Biol. 17:2475-2484(1997).
[10]
PHOSPHORYLATION BY GSK3B.
PubMed=9072970; DOI=10.1126/science.275.5308.1930;
Beals C.R., Sheridan C.M., Turck C.W., Gardner P., Crabtree G.R.;
"Nuclear export of NF-ATc enhanced by glycogen synthase kinase-3.";
Science 275:1930-1934(1997).
[11]
REVIEW.
PubMed=10089876; DOI=10.1016/S0092-8674(00)80571-1;
Crabtree G.R.;
"Generic signals and specific outcomes: signaling through Ca2+,
calcineurin, and NF-AT.";
Cell 96:611-614(1999).
[12]
ALTERNATIVE SPLICING, CHARACTERIZATION, AND FUNCTION.
PubMed=10358178;
Chuvpilo S., Avots A., Berberich-Siebelt F., Gloeckner J., Fischer C.,
Kerstan A., Escher C., Inashkina I., Hlubek F., Jankevics E.,
Brabletz T., Serfling E.;
"Multiple NF-ATc isoforms with individual transcriptional properties
are synthesized in T lymphocytes.";
J. Immunol. 162:7294-7301(1999).
[13]
MUTAGENESIS OF SER-172 AND SER-187.
PubMed=10652349; DOI=10.1074/jbc.275.5.3543;
Porter C.M., Havens M.A., Clipstone N.A.;
"Identification of amino acid residues and protein kinases involved in
the regulation of NFATc subcellular localization.";
J. Biol. Chem. 275:3543-3551(2000).
[14]
PHOSPHORYLATION AT SER-245; SER-269 AND SER-294.
PubMed=12351631; DOI=10.1074/jbc.M207029200;
Sheridan C.M., Heist E.K., Beals C.R., Crabtree G.R., Gardner P.;
"Protein kinase A negatively modulates the nuclear accumulation of NF-
ATc1 by priming for subsequent phosphorylation by glycogen synthase
kinase-3.";
J. Biol. Chem. 277:48664-48676(2002).
[15]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=16511445; DOI=10.1038/nature04631;
Gwack Y., Sharma S., Nardone J., Tanasa B., Iuga A., Srikanth S.,
Okamura H., Bolton D., Feske S., Hogan P.G., Rao A.;
"A genome-wide Drosophila RNAi screen identifies DYRK-family kinases
as regulators of NFAT.";
Nature 441:646-650(2006).
[16]
INTERACTION WITH HOMER2 AND HOMER3.
PubMed=18218901; DOI=10.1126/science.1151227;
Huang G.N., Huso D.L., Bouyain S., Tu J., McCorkell K.A., May M.J.,
Zhu Y., Lutz M., Collins S., Dehoff M., Kang S., Whartenby K.,
Powell J., Leahy D., Worley P.F.;
"NFAT binding and regulation of T cell activation by the cytoplasmic
scaffolding Homer proteins.";
Science 319:476-481(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233, 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).
[18]
STRUCTURE BY NMR OF 416-591.
PubMed=8990122; DOI=10.1038/385172a0;
Wolfe S.A., Zhou P., Dotsch V., Chen L., You A., Ho S.N.,
Crabtree G.R., Wagner G., Verdine G.L.;
"Unusual Rel-like architecture in the DNA-binding domain of the
transcription factor NFATc.";
Nature 385:172-176(1997).
[19]
STRUCTURE BY NMR OF 416-591 IN COMPLEX WITH DNA.
PubMed=9506523; DOI=10.1016/S0092-8674(00)81136-8;
Zhou P., Sun L.J., Dotsch V., Wagner G., Verdine G.L.;
"Solution structure of the core NFATC1/DNA complex.";
Cell 92:687-696(1998).
[20]
VARIANT [LARGE SCALE ANALYSIS] THR-315.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Plays a role in the inducible expression of cytokine
genes in T-cells, especially in the induction of the IL-2 or IL-4
gene transcription. Also controls gene expression in embryonic
cardiac cells. Could regulate not only the activation and
proliferation but also the differentiation and programmed death of
T-lymphocytes as well as lymphoid and non-lymphoid cells
(PubMed:10358178). Required for osteoclastogenesis and regulates
many genes important for osteoclast differentiation and function
(By similarity). {ECO:0000250|UniProtKB:O88942,
ECO:0000269|PubMed:10358178}.
-!- SUBUNIT: Member of the multicomponent NFATC transcription complex
that consists of at least two components, a pre-existing
cytoplasmic component NFATC2 and an inducible nuclear component
NFATC1. Other members such as NFATC4, NFATC3 or members of the
activating protein-1 family, MAF, GATA4 and Cbp/p300 can also bind
the complex. NFATC proteins bind to DNA as monomers
(PubMed:9506523). Interacts with HOMER2 and HOMER3
(PubMed:18218901). {ECO:0000269|PubMed:18218901,
ECO:0000269|PubMed:9506523}.
-!- INTERACTION:
P18846:ATF1; NbExp=3; IntAct=EBI-6907210, EBI-852794;
P15336:ATF2; NbExp=2; IntAct=EBI-6907210, EBI-1170906;
P18847:ATF3; NbExp=2; IntAct=EBI-6907210, EBI-712767;
P16220:CREB1; NbExp=3; IntAct=EBI-6907210, EBI-711855;
P31276:HOXC13; NbExp=2; IntAct=EBI-6907210, EBI-2293590;
P05412:JUN; NbExp=5; IntAct=EBI-6907210, EBI-852823;
O15294:OGT; NbExp=2; IntAct=EBI-6907210, EBI-539828;
Q08209-1:PPP3CA; NbExp=4; IntAct=EBI-6907210, EBI-15637215;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16511445}.
Nucleus {ECO:0000269|PubMed:16511445}. Note=Cytoplasmic for the
phosphorylated form and nuclear after activation that is
controlled by calcineurin-mediated dephosphorylation. Rapid
nuclear exit of NFATC is thought to be one mechanism by which
cells distinguish between sustained and transient calcium signals.
The subcellular localization of NFATC plays a key role in the
regulation of gene transcription (PubMed:16511445). Nuclear
translocation of NFATC1 is enhanced in the presence of TNFSF11.
Nuclear translocation is decreased in the presence of FBN1 which
can bind and sequester TNFSF11 (By similarity).
{ECO:0000250|UniProtKB:O88942, ECO:0000269|PubMed:16511445}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=10;
Comment=Isoform C-alpha and isoform C-beta are the strongest
activator of gene transcription, followed by isoform A-alpha and
isoform A-beta, whereas isoform B-alpha and isoform B-beta are
the weakest. Isoform B-alpha, isoform B-beta, isoform C-alpha
and isoform C-beta, both present in T-cells, can modulate their
transcriptional activity.;
Name=C-alpha;
IsoId=O95644-1; Sequence=Displayed;
Name=A-alpha; Synonyms=IA-VIII;
IsoId=O95644-2; Sequence=VSP_005591, VSP_005592;
Name=A-beta; Synonyms=IB-VIII;
IsoId=O95644-3; Sequence=VSP_005590, VSP_005591, VSP_005592;
Name=B-alpha; Synonyms=IA-IXS;
IsoId=O95644-4; Sequence=VSP_005593;
Name=B-beta; Synonyms=IB-IXS;
IsoId=O95644-5; Sequence=VSP_005590, VSP_005593;
Name=C-beta; Synonyms=IB-IXL;
IsoId=O95644-6; Sequence=VSP_005590;
Name=A-alpha';
IsoId=O95644-8; Sequence=VSP_018978, VSP_005591, VSP_005592;
Note=Produced by alternative initiation at Met-37 of isoform
A-alpha. No experimental confirmation available.;
Name=IA-deltaIX;
IsoId=O95644-10; Sequence=VSP_047820;
Name=IB-deltaIX;
IsoId=O95644-11; Sequence=VSP_005590, VSP_047820;
Name=10;
IsoId=O95644-17; Sequence=VSP_053806, VSP_005593;
Note=No experimental evidence available.;
-!- TISSUE SPECIFICITY: Expressed in thymus, peripheral leukocytes as
T-cells and spleen. Isoforms A are preferentially expressed in
effector T-cells (thymus and peripheral leukocytes) whereas
isoforms B and isoforms C are preferentially expressed in naive T-
cells (spleen). Isoforms B are expressed in naive T-cells after
first antigen exposure and isoforms A are expressed in effector T-
cells after second antigen exposure. Isoforms IA are widely
expressed but not detected in liver nor pancreas, neural
expression is strongest in corpus callosum. Isoforms IB are
expressed mostly in muscle, cerebellum, placenta and thymus,
neural expression in fetal and adult brain, strongest in corpus
callosum. {ECO:0000269|PubMed:18675896}.
-!- INDUCTION: Only isoforms A are inducibly expressed in T
lymphocytes upon activation of the T-cell receptor (TCR) complex.
Induced after co-addition of phorbol 12-myristate 13-acetate (PMA)
and ionomycin. Also induced after co-addition of 12-O-
tetradecanoylphorbol-13-acetate (TPA) and ionomycin. Weakly
induced with PMA, ionomycin and cyclosporin A.
-!- DOMAIN: Rel Similarity Domain (RSD) allows DNA-binding and
cooperative interactions with AP1 factors.
-!- DOMAIN: The N-terminal transactivation domain (TAD-A) binds to and
is activated by Cbp/p300. The dephosphorylated form contains two
unmasked nuclear localization signals (NLS), which allow
translocation of the protein to the nucleus.
-!- DOMAIN: Isoforms C have a C-terminal part with an additional
trans-activation domain, TAD-B, which acts as a transcriptional
activator. Isoforms B have a shorter C-terminal part without
complete TAD-B which acts as a transcriptional repressor.
-!- PTM: Phosphorylated by NFATC-kinase and GSK3B; phosphorylation
induces NFATC1 nuclear exit and dephosphorylation by calcineurin
promotes nuclear import. Phosphorylation by PKA and DYRK2
negatively modulates nuclear accumulation, and promotes subsequent
phosphorylation by GSK3B or casein kinase 1.
{ECO:0000269|PubMed:12351631, ECO:0000269|PubMed:16511445,
ECO:0000269|PubMed:9072970}.
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EMBL; U08015; AAA19601.1; -; mRNA.
EMBL; U59736; AAC50869.1; -; mRNA.
EMBL; U80917; AAD00450.1; -; mRNA.
EMBL; U80918; AAD00451.1; -; mRNA.
EMBL; U80919; AAD00452.1; -; mRNA.
EMBL; EU887559; ACG55579.1; -; mRNA.
EMBL; EU887560; ACG55580.1; -; mRNA.
EMBL; EU887561; ACG55581.1; -; mRNA.
EMBL; EU887562; ACG55582.1; -; mRNA.
EMBL; EU887563; ACG55583.1; -; mRNA.
EMBL; EU887564; ACG55584.1; -; mRNA.
EMBL; EU887565; ACG55585.1; -; mRNA.
EMBL; EU887566; ACG55586.1; -; mRNA.
EMBL; AC018445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC023090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471117; EAW66621.1; -; Genomic_DNA.
EMBL; CH471117; EAW66622.1; -; Genomic_DNA.
EMBL; BC104753; AAI04754.1; -; mRNA.
EMBL; BC112243; AAI12244.1; -; mRNA.
CCDS; CCDS12015.1; -. [O95644-4]
CCDS; CCDS12016.1; -. [O95644-17]
CCDS; CCDS32850.1; -. [O95644-6]
CCDS; CCDS59326.1; -. [O95644-2]
CCDS; CCDS59327.1; -. [O95644-5]
CCDS; CCDS62467.1; -. [O95644-1]
CCDS; CCDS62468.1; -. [O95644-10]
CCDS; CCDS62469.1; -. [O95644-11]
CCDS; CCDS62470.1; -. [O95644-3]
PIR; S45262; S45262.
RefSeq; NP_001265598.1; NM_001278669.1. [O95644-1]
RefSeq; NP_001265599.1; NM_001278670.1. [O95644-10]
RefSeq; NP_001265601.1; NM_001278672.1. [O95644-11]
RefSeq; NP_001265602.1; NM_001278673.1.
RefSeq; NP_001265604.1; NM_001278675.1. [O95644-3]
RefSeq; NP_006153.2; NM_006162.4. [O95644-4]
RefSeq; NP_765975.1; NM_172387.2. [O95644-6]
RefSeq; NP_765976.1; NM_172388.2. [O95644-17]
RefSeq; NP_765977.1; NM_172389.2. [O95644-5]
RefSeq; NP_765978.1; NM_172390.2. [O95644-2]
UniGene; Hs.534074; -.
UniGene; Hs.701518; -.
PDB; 1A66; NMR; -; A=414-591.
PDB; 1NFA; NMR; -; A=416-591.
PDB; 5SVE; X-ray; 2.60 A; C=384-400.
PDBsum; 1A66; -.
PDBsum; 1NFA; -.
PDBsum; 5SVE; -.
ProteinModelPortal; O95644; -.
SMR; O95644; -.
BioGrid; 110845; 141.
DIP; DIP-44311N; -.
IntAct; O95644; 47.
MINT; O95644; -.
STRING; 9606.ENSP00000327850; -.
ChEMBL; CHEMBL3876; -.
DrugBank; DB00852; Pseudoephedrine.
iPTMnet; O95644; -.
PhosphoSitePlus; O95644; -.
BioMuta; NFATC1; -.
MaxQB; O95644; -.
PaxDb; O95644; -.
PeptideAtlas; O95644; -.
PRIDE; O95644; -.
ProteomicsDB; 50973; -.
ProteomicsDB; 50974; -. [O95644-2]
ProteomicsDB; 50975; -. [O95644-3]
ProteomicsDB; 50976; -. [O95644-4]
ProteomicsDB; 50977; -. [O95644-5]
ProteomicsDB; 50978; -. [O95644-6]
ProteomicsDB; 50979; -. [O95644-8]
Ensembl; ENST00000253506; ENSP00000253506; ENSG00000131196. [O95644-4]
Ensembl; ENST00000318065; ENSP00000316553; ENSG00000131196. [O95644-5]
Ensembl; ENST00000329101; ENSP00000327850; ENSG00000131196. [O95644-6]
Ensembl; ENST00000397790; ENSP00000380892; ENSG00000131196. [O95644-17]
Ensembl; ENST00000427363; ENSP00000389377; ENSG00000131196. [O95644-1]
Ensembl; ENST00000542384; ENSP00000442435; ENSG00000131196. [O95644-10]
Ensembl; ENST00000586434; ENSP00000466489; ENSG00000131196. [O95644-11]
Ensembl; ENST00000591814; ENSP00000466194; ENSG00000131196. [O95644-2]
Ensembl; ENST00000592223; ENSP00000467181; ENSG00000131196. [O95644-3]
GeneID; 4772; -.
KEGG; hsa:4772; -.
UCSC; uc002lnc.3; human. [O95644-1]
CTD; 4772; -.
DisGeNET; 4772; -.
EuPathDB; HostDB:ENSG00000131196.17; -.
GeneCards; NFATC1; -.
HGNC; HGNC:7775; NFATC1.
HPA; CAB004513; -.
HPA; HPA071732; -.
MIM; 600489; gene.
neXtProt; NX_O95644; -.
OpenTargets; ENSG00000131196; -.
PharmGKB; PA31582; -.
eggNOG; ENOG410IHFR; Eukaryota.
eggNOG; ENOG41105U2; LUCA.
GeneTree; ENSGT00550000074562; -.
HOGENOM; HOG000231780; -.
HOVERGEN; HBG069754; -.
InParanoid; O95644; -.
KO; K04446; -.
OMA; HNNNQFF; -.
OrthoDB; EOG091G01QP; -.
PhylomeDB; O95644; -.
TreeFam; TF326480; -.
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; O95644; -.
ChiTaRS; NFATC1; human.
EvolutionaryTrace; O95644; -.
GeneWiki; NFATC1; -.
GenomeRNAi; 4772; -.
PRO; PR:O95644; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000131196; -.
CleanEx; HS_NFATC1; -.
ExpressionAtlas; O95644; baseline and differential.
Genevisible; O95644; HS.
GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003700; F:DNA binding transcription factor activity; TAS:ProtInc.
GO; GO:0005528; F:FK506 binding; TAS:ProtInc.
GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; ISS:BHF-UCL.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; ISS:BHF-UCL.
GO; GO:0001225; F:RNA polymerase II transcription coactivator binding; IEA:Ensembl.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; ISS:BHF-UCL.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; ISS:BHF-UCL.
GO; GO:0001205; F:transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific DNA binding; ISS:BHF-UCL.
GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IDA:UniProtKB.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0035556; P:intracellular signal transduction; IDA:MGI.
GO; GO:1905064; P:negative regulation of vascular smooth muscle cell differentiation; IDA:BHF-UCL.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:ParkinsonsUK-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; TAS:Reactome.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 2.60.40.340; -; 1.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR002909; IPT_dom.
InterPro; IPR008366; NFAT.
InterPro; IPR015647; NFAT1.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR032397; RHD_dimer.
InterPro; IPR011539; RHD_DNA_bind_dom.
InterPro; IPR037059; RHD_DNA_bind_dom_sf.
PANTHER; PTHR12533; PTHR12533; 1.
PANTHER; PTHR12533:SF5; PTHR12533:SF5; 1.
Pfam; PF16179; RHD_dimer; 1.
Pfam; PF00554; RHD_DNA_bind; 1.
PRINTS; PR01789; NUCFACTORATC.
SMART; SM00429; IPT; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS50254; REL_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative initiation; Alternative splicing;
Complete proteome; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation.
CHAIN 1 943 Nuclear factor of activated T-cells,
cytoplasmic 1.
/FTId=PRO_0000030329.
REPEAT 203 219 1.
REPEAT 233 249 2.
REPEAT 282 298 3.
DOMAIN 410 592 RHD. {ECO:0000255|PROSITE-
ProRule:PRU00265}.
DNA_BIND 439 446
REGION 118 123 Calcineurin-binding.
REGION 126 218 Trans-activation domain A (TAD-A).
REGION 203 298 3 X SP repeats.
REGION 703 943 Trans-activation domain B (TAD-B).
MOTIF 265 267 Nuclear localization signal.
MOTIF 310 321 Nuclear export signal.
MOTIF 682 684 Nuclear localization signal.
MOTIF 924 933 Nuclear export signal.
MOD_RES 233 233 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 237 237 Phosphoserine.
{ECO:0000250|UniProtKB:O88942}.
MOD_RES 245 245 Phosphoserine; by PKA.
{ECO:0000269|PubMed:12351631}.
MOD_RES 269 269 Phosphoserine; by PKA.
{ECO:0000269|PubMed:12351631}.
MOD_RES 294 294 Phosphoserine; by PKA.
{ECO:0000269|PubMed:12351631}.
VAR_SEQ 1 472 Missing (in isoform 10). {ECO:0000305}.
/FTId=VSP_053806.
VAR_SEQ 1 42 MPSTSFPVPSKFPLGPAAAVFGRGETLGPAPRAGGTMKSAE
E -> MTGLEDQEFDFEFLFEFNQRDEGAAAAAP (in
isoform A-beta, isoform B-beta, isoform
C-beta and isoform IB-deltaIX).
{ECO:0000303|PubMed:10072078,
ECO:0000303|PubMed:18675896,
ECO:0000303|PubMed:8702849}.
/FTId=VSP_005590.
VAR_SEQ 1 36 Missing (in isoform A-alpha').
{ECO:0000305}.
/FTId=VSP_018978.
VAR_SEQ 698 927 Missing (in isoform IA-deltaIX and
isoform IB-deltaIX).
{ECO:0000303|PubMed:18675896}.
/FTId=VSP_047820.
VAR_SEQ 698 716 VPIIKTEPTDDYEPAPTCG -> GNAIFLTVSREHERVGCF
F (in isoform A-alpha, isoform A-alpha'
and isoform A-beta).
{ECO:0000303|PubMed:10072078,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8202141}.
/FTId=VSP_005591.
VAR_SEQ 717 943 Missing (in isoform A-alpha, isoform A-
alpha' and isoform A-beta).
{ECO:0000303|PubMed:10072078,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8202141}.
/FTId=VSP_005592.
VAR_SEQ 826 943 Missing (in isoform B-alpha, isoform B-
beta and isoform 10).
{ECO:0000303|PubMed:10072078,
ECO:0000303|PubMed:8702849}.
/FTId=VSP_005593.
VARIANT 68 68 P -> T (in dbSNP:rs1051978).
/FTId=VAR_057145.
VARIANT 315 315 A -> T (in a colorectal cancer sample;
somatic mutation; dbSNP:rs779866756).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036529.
VARIANT 751 751 C -> G (in dbSNP:rs754093).
/FTId=VAR_057146.
MUTAGEN 169 169 S->A: No effect on subcellular
localization.
MUTAGEN 172 172 S->A: Partial nuclear translocation.
{ECO:0000269|PubMed:10652349}.
MUTAGEN 187 187 S->A: No effect on subcellular
localization.
{ECO:0000269|PubMed:10652349}.
CONFLICT 232 232 G -> S (in Ref. 2; AAC50869).
{ECO:0000305}.
CONFLICT 235 235 R -> Q (in Ref. 1; AAA19601).
{ECO:0000305}.
STRAND 426 432 {ECO:0000244|PDB:1A66}.
STRAND 443 445 {ECO:0000244|PDB:1A66}.
STRAND 454 456 {ECO:0000244|PDB:1A66}.
STRAND 460 465 {ECO:0000244|PDB:1A66}.
STRAND 468 470 {ECO:0000244|PDB:1A66}.
STRAND 472 480 {ECO:0000244|PDB:1A66}.
STRAND 483 485 {ECO:0000244|PDB:1A66}.
STRAND 509 511 {ECO:0000244|PDB:1A66}.
STRAND 514 521 {ECO:0000244|PDB:1A66}.
STRAND 523 525 {ECO:0000244|PDB:1A66}.
HELIX 541 545 {ECO:0000244|PDB:1A66}.
STRAND 551 553 {ECO:0000244|PDB:1NFA}.
STRAND 559 570 {ECO:0000244|PDB:1A66}.
TURN 571 573 {ECO:0000244|PDB:1A66}.
STRAND 574 586 {ECO:0000244|PDB:1A66}.
SEQUENCE 943 AA; 101243 MW; E72FAB10ECEB2D66 CRC64;
MPSTSFPVPS KFPLGPAAAV FGRGETLGPA PRAGGTMKSA EEEHYGYASS NVSPALPLPT
AHSTLPAPCH NLQTSTPGII PPADHPSGYG AALDGGPAGY FLSSGHTRPD GAPALESPRI
EITSCLGLYH NNNQFFHDVE VEDVLPSSKR SPSTATLSLP SLEAYRDPSC LSPASSLSSR
SCNSEASSYE SNYSYPYASP QTSPWQSPCV SPKTTDPEEG FPRGLGACTL LGSPRHSPST
SPRASVTEES WLGARSSRPA SPCNKRKYSL NGRQPPYSPH HSPTPSPHGS PRVSVTDDSW
LGNTTQYTSS AIVAAINALT TDSSLDLGDG VPVKSRKTTL EQPPSVALKV EPVGEDLGSP
PPPADFAPED YSSFQHIRKG GFCDQYLAVP QHPYQWAKPK PLSPTSYMSP TLPALDWQLP
SHSGPYELRI EVQPKSHHRA HYETEGSRGA VKASAGGHPI VQLHGYLENE PLMLQLFIGT
ADDRLLRPHA FYQVHRITGK TVSTTSHEAI LSNTKVLEIP LLPENSMRAV IDCAGILKLR
NSDIELRKGE TDIGRKNTRV RLVFRVHVPQ PSGRTLSLQV ASNPIECSQR SAQELPLVEK
QSTDSYPVVG GKKMVLSGHN FLQDSKVIFV EKAPDGHHVW EMEAKTDRDL CKPNSLVVEI
PPFRNQRITS PVHVSFYVCN GKRKRSQYQR FTYLPANVPI IKTEPTDDYE PAPTCGPVSQ
GLSPLPRPYY SQQLAMPPDP SSCLVAGFPP CPQRSTLMPA APGVSPKLHD LSPAAYTKGV
ASPGHCHLGL PQPAGEAPAV QDVPRPVATH PGSPGQPPPA LLPQQVSAPP SSSCPPGLEH
SLCPSSPSPP LPPATQEPTC LQPCSPACPP ATGRPQHLPS TVRRDESPTA GPRLLPEVHE
DGSPNLAPIP VTVKREPEEL DQLYLDDVNE IIRNDLSSTS THS


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