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Nuclear factor of activated T-cells, cytoplasmic 2 (NF-ATc2) (NFATc2) (NFAT pre-existing subunit) (NF-ATp) (T-cell transcription factor NFAT1)

 NFAC2_HUMAN             Reviewed;         925 AA.
Q13469; B5B2N8; B5B2N9; B5B2P0; B5B2P2; B5B2P3; Q13468; Q5TFW7;
Q5TFW8; Q9NPX6; Q9NQH3; Q9UJR2;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 2.
12-SEP-2018, entry version 209.
RecName: Full=Nuclear factor of activated T-cells, cytoplasmic 2;
Short=NF-ATc2;
Short=NFATc2;
AltName: Full=NFAT pre-existing subunit;
Short=NF-ATp;
AltName: Full=T-cell transcription factor NFAT1;
Name=NFATC2; Synonyms=NFAT1, NFATP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), ALTERNATIVE SPLICING,
AND TISSUE SPECIFICITY.
PubMed=8668213; DOI=10.1128/MCB.16.7.3955;
Luo C., Burgeon E., Carew J.A., McCaffrey P.G., Badalian T.M.,
Lane W.S., Hogan P.G., Rao A.;
"Recombinant NFAT1 (NFATp) is regulated by calcineurin in T cells and
mediates transcription of several cytokine genes.";
Mol. Cell. Biol. 16:3955-3966(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), AND
ALTERNATIVE SPLICING.
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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).
[6]
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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[8]
FUNCTION, AND INTERACTION WITH FOXP3.
PubMed=15790681; DOI=10.1073/pnas.0501675102;
Bettelli E., Dastrange M., Oukka M.;
"Foxp3 interacts with nuclear factor of activated T cells and NF-kappa
B to repress cytokine gene expression and effector functions of T
helper cells.";
Proc. Natl. Acad. Sci. U.S.A. 102:5138-5143(2005).
[9]
DOMAIN.
PubMed=17467953; DOI=10.1016/j.ygeno.2007.02.003;
Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P.,
Piskacek M.;
"Nine-amino-acid transactivation domain: establishment and prediction
utilities.";
Genomics 89:756-768(2007).
[10]
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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-330; SER-755;
SER-759 AND SER-859, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-757 AND SER-759, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
FUNCTION.
PubMed=21871017; DOI=10.1042/BJ20110530;
Yiu G.K., Kaunisto A., Chin Y.R., Toker A.;
"NFAT promotes carcinoma invasive migration through glypican-6.";
Biochem. J. 440:157-166(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-110; SER-326
AND SER-856, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-148, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
INTERACTION WITH PPP3CA.
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).
[17]
UBIQUITINATION.
PubMed=26766444; DOI=10.1016/j.devcel.2015.12.015;
Scholz B., Korn C., Wojtarowicz J., Mogler C., Augustin I.,
Boutros M., Niehrs C., Augustin H.G.;
"Endothelial RSPO3 controls vascular stability and pruning through
non-canonical WNT/Ca(2+)/NFAT signaling.";
Dev. Cell 36:79-93(2016).
[18] {ECO:0000244|PDB:3QRF}
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 396-678 IN COMPLEX WITH DNA
AND FOXP3, AND INTERACTION WITH FOXP3.
PubMed=21458306; DOI=10.1016/j.immuni.2011.02.017;
Bandukwala H.S., Wu Y., Feuerer M., Chen Y., Barboza B., Ghosh S.,
Stroud J.C., Benoist C., Mathis D., Rao A., Chen L.;
"Structure of a domain-swapped FOXP3 dimer on DNA and its function in
regulatory T cells.";
Immunity 34:479-491(2011).
-!- FUNCTION: Plays a role in the inducible expression of cytokine
genes in T-cells, especially in the induction of the IL-2, IL-3,
IL-4, TNF-alpha or GM-CSF. Promotes invasive migration through the
activation of GPC6 expression and WNT5A signaling pathway.
{ECO:0000269|PubMed:15790681, ECO:0000269|PubMed:21871017}.
-!- 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. The phosphorylated form specifically interacts with
XPO1; which mediates nuclear export. NFATC proteins bind to DNA as
monomers. Interacts with NFATC2IP (By similarity). Interacts with
FOXP3 (PubMed:15790681, PubMed:21458306). Interacts with TBX21
('Thr-303' phosphorylated form) (By similarity). Interacts with
KAT2A (By similarity). Interacts with HOMER2 and HOMER3
(PubMed:18218901). Interacts with protein phosphatase
PPP3CA/calcineurin A (PubMed:26248042).
{ECO:0000250|UniProtKB:Q60591, ECO:0000269|PubMed:15790681,
ECO:0000269|PubMed:18218901, ECO:0000269|PubMed:21458306,
ECO:0000269|PubMed:26248042}.
-!- INTERACTION:
P16220:CREB1; NbExp=2; IntAct=EBI-716258, EBI-711855;
P05412:JUN; NbExp=6; IntAct=EBI-10087113, EBI-852823;
Q5S007:LRRK2; NbExp=3; IntAct=EBI-716258, EBI-5323863;
Q08209-1:PPP3CA; NbExp=2; IntAct=EBI-716258, EBI-15637215;
Q9UPT9:USP22; NbExp=2; IntAct=EBI-716258, EBI-723510;
Q86Y07-1:VRK2; NbExp=3; IntAct=EBI-716258, EBI-1207633;
Q86Y07-2:VRK2; NbExp=4; IntAct=EBI-716258, EBI-1207636;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=C, NFATc2_IB_IIL;
IsoId=Q13469-1; Sequence=Displayed;
Name=2; Synonyms=B;
IsoId=Q13469-2; Sequence=VSP_005595;
Name=3; Synonyms=NFATc2_IA_IIL;
IsoId=Q13469-3; Sequence=VSP_042757, VSP_005595;
Name=4;
IsoId=Q13469-4; Sequence=VSP_042757;
Name=5;
IsoId=Q13469-5; Sequence=VSP_055926, VSP_005595;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in thymus, spleen, heart, testis,
brain, placenta, muscle and pancreas. Isoform 1 is highly
expressed in the small intestine, heart, testis, prostate, thymus,
placenta and thyroid. Isoform 3 is highly expressed in stomach,
uterus, placenta, trachea and thyroid.
{ECO:0000269|PubMed:8668213}.
-!- INDUCTION: 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.
-!- DOMAIN: the 9aaTAD motif is a transactivation domain present in a
large number of yeast and animal transcription factors.
{ECO:0000269|PubMed:17467953}.
-!- DOMAIN: Rel Similarity Domain (RSD) allows DNA-binding and
cooperative interactions with AP1 factors. {ECO:0000250}.
-!- PTM: In resting cells, phosphorylated by NFATC-kinase on at least
18 sites in the 99-363 region. Upon cell stimulation, all these
sites except Ser-243 are dephosphorylated by calcineurin.
Dephosphorylation induces a conformational change that
simultaneously exposes an NLS and masks an NES, which results in
nuclear localization. Simultaneously, Ser-53 or Ser-56 is
phosphorylated; which is required for full transcriptional
activity. {ECO:0000250|UniProtKB:Q60591}.
-!- PTM: Ubiquitinated in endothelial cells by RNF213 downstream of
the non-canonical Wnt signaling pathway, leading to its
degradation by the proteasome. {ECO:0000269|PubMed:26766444}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NFATC2ID44004ch20q13.html";
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EMBL; U43341; AAC50886.1; -; mRNA.
EMBL; U43342; AAC50887.1; -; mRNA.
EMBL; EU887573; ACG55593.1; -; mRNA.
EMBL; EU887574; ACG55594.1; -; mRNA.
EMBL; EU887575; ACG55595.1; -; mRNA.
EMBL; EU887576; ACG55596.1; -; mRNA.
EMBL; EU887577; ACG55597.1; -; mRNA.
EMBL; EU887578; ACG55598.1; -; mRNA.
EMBL; AL132866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL035682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL035684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471077; EAW75602.1; -; Genomic_DNA.
EMBL; CH471077; EAW75603.1; -; Genomic_DNA.
EMBL; BC136418; AAI36419.1; -; mRNA.
EMBL; BC144074; AAI44075.1; -; mRNA.
CCDS; CCDS13437.1; -. [Q13469-1]
CCDS; CCDS33488.1; -. [Q13469-2]
CCDS; CCDS46614.1; -. [Q13469-3]
CCDS; CCDS68156.1; -. [Q13469-5]
CCDS; CCDS68157.1; -. [Q13469-4]
PIR; G02326; G02326.
RefSeq; NP_001129493.1; NM_001136021.2. [Q13469-3]
RefSeq; NP_001245221.1; NM_001258292.1. [Q13469-4]
RefSeq; NP_001245223.1; NM_001258294.1. [Q13469-5]
RefSeq; NP_001245225.1; NM_001258296.1. [Q13469-5]
RefSeq; NP_036472.2; NM_012340.4. [Q13469-2]
RefSeq; NP_775114.1; NM_173091.3. [Q13469-1]
UniGene; Hs.744148; -.
PDB; 1A02; X-ray; 2.70 A; N=392-678.
PDB; 1OWR; X-ray; 3.00 A; M/N/P/Q=396-678.
PDB; 1P7H; X-ray; 2.60 A; L/M/N/O=393-678.
PDB; 1PZU; X-ray; 3.10 A; B/D/H/I/L/M=396-678.
PDB; 1S9K; X-ray; 3.10 A; C=399-678.
PDB; 2AS5; X-ray; 2.70 A; M/N=392-678.
PDB; 2O93; X-ray; 3.05 A; L/M/O=396-678.
PDB; 3QRF; X-ray; 2.80 A; M/N=396-678.
PDBsum; 1A02; -.
PDBsum; 1OWR; -.
PDBsum; 1P7H; -.
PDBsum; 1PZU; -.
PDBsum; 1S9K; -.
PDBsum; 2AS5; -.
PDBsum; 2O93; -.
PDBsum; 3QRF; -.
ProteinModelPortal; Q13469; -.
SMR; Q13469; -.
BioGrid; 110846; 184.
ComplexPortal; CPX-480; AP-1 transcription factor complex FOS-JUN-NFATC2.
CORUM; Q13469; -.
DIP; DIP-27630N; -.
ELM; Q13469; -.
IntAct; Q13469; 16.
MINT; Q13469; -.
STRING; 9606.ENSP00000379330; -.
iPTMnet; Q13469; -.
PhosphoSitePlus; Q13469; -.
BioMuta; NFATC2; -.
DMDM; 68846905; -.
EPD; Q13469; -.
MaxQB; Q13469; -.
PaxDb; Q13469; -.
PeptideAtlas; Q13469; -.
PRIDE; Q13469; -.
ProteomicsDB; 59464; -.
ProteomicsDB; 59465; -. [Q13469-2]
ProteomicsDB; 59466; -. [Q13469-3]
Ensembl; ENST00000371564; ENSP00000360619; ENSG00000101096. [Q13469-2]
Ensembl; ENST00000396009; ENSP00000379330; ENSG00000101096. [Q13469-1]
Ensembl; ENST00000414705; ENSP00000396471; ENSG00000101096. [Q13469-3]
Ensembl; ENST00000609507; ENSP00000477342; ENSG00000101096. [Q13469-5]
Ensembl; ENST00000609943; ENSP00000477370; ENSG00000101096. [Q13469-4]
Ensembl; ENST00000610033; ENSP00000477142; ENSG00000101096. [Q13469-5]
GeneID; 4773; -.
KEGG; hsa:4773; -.
UCSC; uc002xwc.4; human. [Q13469-1]
CTD; 4773; -.
DisGeNET; 4773; -.
EuPathDB; HostDB:ENSG00000101096.19; -.
GeneCards; NFATC2; -.
HGNC; HGNC:7776; NFATC2.
HPA; CAB018567; -.
HPA; HPA008789; -.
HPA; HPA024369; -.
MIM; 600490; gene.
neXtProt; NX_Q13469; -.
OpenTargets; ENSG00000101096; -.
PharmGKB; PA31583; -.
eggNOG; ENOG410IHFR; Eukaryota.
eggNOG; ENOG41105U2; LUCA.
GeneTree; ENSGT00550000074562; -.
HOGENOM; HOG000231780; -.
HOVERGEN; HBG069754; -.
InParanoid; Q13469; -.
KO; K17332; -.
OMA; MWKTSPD; -.
OrthoDB; EOG091G01QP; -.
PhylomeDB; Q13469; -.
TreeFam; TF326480; -.
Reactome; R-HSA-2025928; Calcineurin activates NFAT.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-5607763; CLEC7A (Dectin-1) induces NFAT activation.
Reactome; R-HSA-8877330; RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs).
SIGNOR; Q13469; -.
ChiTaRS; NFATC2; human.
EvolutionaryTrace; Q13469; -.
GeneWiki; NFATC2; -.
GenomeRNAi; 4773; -.
PRO; PR:Q13469; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101096; Expressed in 189 organ(s), highest expression level in thoracic mammary gland.
CleanEx; HS_NFATC2; -.
Genevisible; Q13469; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0044798; C:nuclear transcription factor complex; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; TAS:UniProtKB.
GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:UniProtKB.
GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0008134; F:transcription factor binding; IEA:Ensembl.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0050853; P:B cell receptor signaling pathway; IMP:UniProtKB.
GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IEA:Ensembl.
GO; GO:0016477; P:cell migration; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0001816; P:cytokine production; IEA:Ensembl.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0014904; P:myotube cell development; IEA:Ensembl.
GO; GO:1905064; P:negative regulation of vascular smooth muscle cell differentiation; IDA:BHF-UCL.
GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:UniProtKB.
GO; GO:1901741; P:positive regulation of myoblast fusion; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0045589; P:regulation of regulatory T cell differentiation; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
GO; GO:0042493; P:response to drug; IMP:UniProtKB.
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; 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.
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 splicing; Complete proteome;
Cytoplasm; DNA-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 925 Nuclear factor of activated T-cells,
cytoplasmic 2.
/FTId=PRO_0000205178.
REPEAT 184 200 1.
REPEAT 213 229 2.
REPEAT 272 286 3; approximate.
DOMAIN 392 574 RHD. {ECO:0000255|PROSITE-
ProRule:PRU00265}.
DNA_BIND 421 428
REGION 111 116 Calcineurin-binding.
{ECO:0000269|PubMed:26248042}.
REGION 119 199 Trans-activation domain A (TAD-A).
REGION 161 175 Required for cytoplasmic retention of the
phosphorylated form. {ECO:0000250}.
REGION 184 286 3 X approximate SP repeats.
MOTIF 26 34 9aaTAD.
MOTIF 251 253 Nuclear localization signal.
MOTIF 664 666 Nuclear localization signal.
MOTIF 904 913 Nuclear export signal.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000250|UniProtKB:Q60591}.
MOD_RES 107 107 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 148 148 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 168 168 Phosphoserine.
{ECO:0000250|UniProtKB:Q60591}.
MOD_RES 171 171 Phosphoserine.
{ECO:0000250|UniProtKB:Q60591}.
MOD_RES 172 172 Phosphoserine.
{ECO:0000250|UniProtKB:Q60591}.
MOD_RES 174 174 Phosphoserine.
{ECO:0000250|UniProtKB:Q60591}.
MOD_RES 175 175 Phosphoserine.
{ECO:0000250|UniProtKB:Q60591}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000250|UniProtKB:Q60591}.
MOD_RES 180 180 Phosphoserine.
{ECO:0000250|UniProtKB:Q60591}.
MOD_RES 213 213 Phosphoserine.
{ECO:0000250|UniProtKB:Q60591}.
MOD_RES 217 217 Phosphoserine.
{ECO:0000250|UniProtKB:Q60591}.
MOD_RES 221 221 Phosphoserine.
{ECO:0000250|UniProtKB:Q60591}.
MOD_RES 236 236 Phosphoserine.
{ECO:0000250|UniProtKB:Q60591}.
MOD_RES 243 243 Phosphoserine.
{ECO:0000250|UniProtKB:Q60591}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000250|UniProtKB:Q60591}.
MOD_RES 268 268 Phosphoserine.
{ECO:0000250|UniProtKB:Q60591}.
MOD_RES 274 274 Phosphoserine.
{ECO:0000250|UniProtKB:Q60591}.
MOD_RES 276 276 Phosphoserine.
{ECO:0000250|UniProtKB:Q60591}.
MOD_RES 280 280 Phosphoserine.
{ECO:0000250|UniProtKB:Q60591}.
MOD_RES 326 326 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 330 330 Phosphoserine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:19690332}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000250|UniProtKB:Q60591}.
MOD_RES 755 755 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 757 757 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 759 759 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 856 856 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 859 859 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
VAR_SEQ 1 219 Missing (in isoform 5).
{ECO:0000303|PubMed:18675896}.
/FTId=VSP_055926.
VAR_SEQ 1 43 MNAPERQPQPDGGDAPGHEPGGSPQDELDFSILFDYEYLNP
NE -> MQREAAFRLGHCHPLRIMGSVDQ (in isoform
3 and isoform 4).
{ECO:0000303|PubMed:18675896,
ECO:0000303|PubMed:8668213}.
/FTId=VSP_042757.
VAR_SEQ 908 925 VNEIIRKEFSGPPARNQT -> ELIDTHLSWIQNIL (in
isoform 2, isoform 3 and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:18675896,
ECO:0000303|PubMed:8668213}.
/FTId=VSP_005595.
VARIANT 446 446 H -> R (in dbSNP:rs12479626).
/FTId=VAR_051783.
CONFLICT 65 65 L -> M (in Ref. 1; AAC50886/AAC50887).
{ECO:0000305}.
STRAND 397 399 {ECO:0000244|PDB:1OWR}.
STRAND 402 405 {ECO:0000244|PDB:1P7H}.
STRAND 408 414 {ECO:0000244|PDB:1P7H}.
STRAND 436 439 {ECO:0000244|PDB:2AS5}.
STRAND 442 445 {ECO:0000244|PDB:1P7H}.
STRAND 450 452 {ECO:0000244|PDB:2AS5}.
STRAND 454 461 {ECO:0000244|PDB:1P7H}.
STRAND 464 466 {ECO:0000244|PDB:1P7H}.
STRAND 474 478 {ECO:0000244|PDB:1P7H}.
STRAND 481 483 {ECO:0000244|PDB:3QRF}.
STRAND 490 492 {ECO:0000244|PDB:1A02}.
STRAND 494 496 {ECO:0000244|PDB:1P7H}.
STRAND 498 503 {ECO:0000244|PDB:1P7H}.
HELIX 505 507 {ECO:0000244|PDB:1P7H}.
STRAND 510 512 {ECO:0000244|PDB:1P7H}.
STRAND 515 520 {ECO:0000244|PDB:1P7H}.
HELIX 523 526 {ECO:0000244|PDB:1P7H}.
STRAND 529 531 {ECO:0000244|PDB:1P7H}.
STRAND 541 552 {ECO:0000244|PDB:1P7H}.
TURN 553 555 {ECO:0000244|PDB:1P7H}.
STRAND 556 563 {ECO:0000244|PDB:1P7H}.
HELIX 571 576 {ECO:0000244|PDB:1A02}.
STRAND 579 584 {ECO:0000244|PDB:1P7H}.
STRAND 586 589 {ECO:0000244|PDB:1P7H}.
STRAND 595 602 {ECO:0000244|PDB:1P7H}.
STRAND 608 614 {ECO:0000244|PDB:1P7H}.
STRAND 616 618 {ECO:0000244|PDB:1P7H}.
STRAND 620 626 {ECO:0000244|PDB:1P7H}.
TURN 630 632 {ECO:0000244|PDB:1P7H}.
STRAND 637 641 {ECO:0000244|PDB:1P7H}.
STRAND 646 648 {ECO:0000244|PDB:3QRF}.
STRAND 654 662 {ECO:0000244|PDB:1P7H}.
TURN 663 665 {ECO:0000244|PDB:1P7H}.
STRAND 671 676 {ECO:0000244|PDB:1P7H}.
SEQUENCE 925 AA; 100146 MW; 8DAE86855CCB58D3 CRC64;
MNAPERQPQP DGGDAPGHEP GGSPQDELDF SILFDYEYLN PNEEEPNAHK VASPPSGPAY
PDDVLDYGLK PYSPLASLSG EPPGRFGEPD RVGPQKFLSA AKPAGASGLS PRIEITPSHE
LIQAVGPLRM RDAGLLVEQP PLAGVAASPR FTLPVPGFEG YREPLCLSPA SSGSSASFIS
DTFSPYTSPC VSPNNGGPDD LCPQFQNIPA HYSPRTSPIM SPRTSLAEDS CLGRHSPVPR
PASRSSSPGA KRRHSCAEAL VALPPGASPQ RSRSPSPQPS SHVAPQDHGS PAGYPPVAGS
AVIMDALNSL ATDSPCGIPP KMWKTSPDPS PVSAAPSKAG LPRHIYPAVE FLGPCEQGER
RNSAPESILL VPPTWPKPLV PAIPICSIPV TASLPPLEWP LSSQSGSYEL RIEVQPKPHH
RAHYETEGSR GAVKAPTGGH PVVQLHGYME NKPLGLQIFI GTADERILKP HAFYQVHRIT
GKTVTTTSYE KIVGNTKVLE IPLEPKNNMR ATIDCAGILK LRNADIELRK GETDIGRKNT
RVRLVFRVHI PESSGRIVSL QTASNPIECS QRSAHELPMV ERQDTDSCLV YGGQQMILTG
QNFTSESKVV FTEKTTDGQQ IWEMEATVDK DKSQPNMLFV EIPEYRNKHI RTPVKVNFYV
INGKRKRSQP QHFTYHPVPA IKTEPTDEYD PTLICSPTHG GLGSQPYYPQ HPMVAESPSC
LVATMAPCQQ FRTGLSSPDA RYQQQNPAAV LYQRSKSLSP SLLGYQQPAL MAAPLSLADA
HRSVLVHAGS QGQSSALLHP SPTNQQASPV IHYSPTNQQL RCGSHQEFQH IMYCENFAPG
TTRPGPPPVS QGQRLSPGSY PTVIQQQNAT SQRAAKNGPP VSDQKEVLPA GVTIKQEQNL
DQTYLDDVNE IIRKEFSGPP ARNQT


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