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Nuclear factor of activated T-cells, cytoplasmic 4 (NF-ATc4) (NFATc4) (T-cell transcription factor NFAT3) (NF-AT3)

 NFAC4_HUMAN             Reviewed;         902 AA.
Q14934; B4DDG5; B4DY55; B5B2U7; B5B2U8; B5B2U9; B5B2V0; B5B2V1;
B5B2V2; B5B2V3; B5B2V4; B5B2V5; B5B2V7; B5B2V8; B5B2V9; B5B2W0;
B5B2W1; B5B2W2; B5B2W3; B5B2W4; B5B2W5; B5B2W6; B5B2W7; B5B2W8;
B5B2W9; B5B2X0; Q7Z598; Q96H68;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 2.
25-OCT-2017, entry version 163.
RecName: Full=Nuclear factor of activated T-cells, cytoplasmic 4;
Short=NF-ATc4;
Short=NFATc4;
AltName: Full=T-cell transcription factor NFAT3;
Short=NF-AT3;
Name=NFATC4; Synonyms=NFAT3;
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), FUNCTION, AND VARIANTS ALA-160
AND PRO-800.
TISSUE=T-cell;
PubMed=7749981; DOI=10.1016/1074-7613(95)90027-6;
Hoey T., Sun Y.-L., Williamson K., Xu X.;
"Isolation of two new members of the NF-AT gene family and functional
characterization of the NF-AT proteins.";
Immunity 2:461-472(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;
11; 12; 13; 14; 15; 16; 17; 18; 19; 20; 21; 22; 23 AND 24), 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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 12 AND 16).
TISSUE=Adrenal gland, and Testis;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 61-902 (ISOFORMS 1/2/4/6), AND VARIANTS
ALA-160 AND PRO-800.
TISSUE=Ovary, and Rhabdomyosarcoma;
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).
[5]
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).
[6]
INTERACTION WITH CREBBP.
PubMed=11514544; DOI=10.1074/jbc.M102961200;
Yang T.T.C., Davis R.J., Chow C.-W.;
"Requirement of two NFATc4 transactivation domains for CBP
potentiation.";
J. Biol. Chem. 276:39569-39576(2001).
[7]
FUNCTION, PHOSPHORYLATION AT SER-168 AND SER-170, AND MUTAGENESIS OF
SER-168 AND SER-170.
PubMed=11997522; DOI=10.1128/MCB.22.11.3892-3904.2002;
Yang T.T.C., Xiong Q., Enslen H., Davis R.J., Chow C.-W.;
"Phosphorylation of NFATc4 by p38 mitogen-activated protein kinases.";
Mol. Cell. Biol. 22:3892-3904(2002).
[8]
INTERACTION WITH MAPK8 AND MAPK9, PHOSPHORYLATION AT SER-213 AND
SER-217, AND MUTAGENESIS OF SER-213 AND SER-217.
PubMed=17875713; DOI=10.1158/0008-5472.CAN-06-4788;
Yao K., Cho Y.-Y., Bergen H.R. III, Madden B.J., Choi B.Y., Ma W.-Y.,
Bode A.M., Dong Z.;
"Nuclear factor of activated T3 is a negative regulator of Ras-JNK1/2-
AP-1 induced cell transformation.";
Cancer Res. 67:8725-8735(2007).
[9]
FUNCTION, INTERACTION WITH RPS6KA3, AND PHOSPHORYLATION AT SER-289 AND
SER-344.
PubMed=17213202; DOI=10.1074/jbc.M611322200;
Cho Y.-Y., Yao K., Bode A.M., Bergen H.R. III, Madden B.J., Oh S.-M.,
Ermakova S., Kang B.S., Choi H.S., Shim J.-H., Dong Z.;
"RSK2 mediates muscle cell differentiation through regulation of
NFAT3.";
J. Biol. Chem. 282:8380-8392(2007).
[10]
FUNCTION.
PubMed=18668201; DOI=10.1007/s00018-008-8273-1;
Qin X., Wang X.-H., Yang Z.-H., Ding L.-H., Xu X.-J., Cheng L.,
Niu C., Sun H.-W., Zhang H., Ye Q.-N.;
"Repression of NFAT3 transcriptional activity by estrogen receptors.";
Cell. Mol. Life Sci. 65:2752-2762(2008).
[11]
PHOSPHORYLATION, AND UBIQUITINATION.
PubMed=19026640; DOI=10.1016/j.febslet.2008.11.009;
Fan Y., Xie P., Zhang T., Zhang H., Gu D., She M., Li H.;
"Regulation of the stability and transcriptional activity of NFATc4 by
ubiquitination.";
FEBS Lett. 582:4008-4014(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[13]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-168 AND SER-170.
PubMed=18347059; DOI=10.1128/MCB.01847-07;
Yang T.T.C., Yu R.Y.L., Agadir A., Gao G.-J., Campos-Gonzalez R.,
Tournier C., Chow C.-W.;
"Integration of protein kinases mTOR and extracellular signal-
regulated kinase 5 in regulating nucleocytoplasmic localization of
NFATc4.";
Mol. Cell. Biol. 28:3489-3501(2008).
[14]
INTERACTION WITH IRAK1.
PubMed=18691762; DOI=10.1016/j.molimm.2008.06.023;
Wang D., Fasciano S., Li L.;
"The interleukin-1 receptor associated kinase 1 contributes to the
regulation of NFAT.";
Mol. Immunol. 45:3902-3908(2008).
[15]
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).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-689, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[17]
STRUCTURE BY NMR OF 585-691.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the TIG domain from human nuclear factor of
activated T-cells, cytoplasmic 4.";
Submitted (FEB-2008) to the PDB data bank.
-!- FUNCTION: Plays a role in the inducible expression of cytokine
genes in T-cells, especially in the induction of the IL-2 and IL-
4. Transcriptionally repressed by estrogen receptors; this
inhibition is further enhanced by estrogen. Increases the
transcriptional activity of PPARG and has a direct role in
adipocyte differentiation. May play an important role in myotube
differentiation. May play a critical role in cardiac development
and hypertrophy. May play a role in deafferentation-induced
apoptosis of sensory neurons. {ECO:0000269|PubMed:11997522,
ECO:0000269|PubMed:17213202, ECO:0000269|PubMed:18668201,
ECO:0000269|PubMed:7749981}.
-!- 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. Interacts
with CREBBP, GATA4, IRAK1, MAPK8, MAPK9 and RPS6KA3.
{ECO:0000269|PubMed:11514544, ECO:0000269|PubMed:17213202,
ECO:0000269|PubMed:17875713, ECO:0000269|PubMed:18691762}.
-!- INTERACTION:
P0CG48:UBC; NbExp=3; IntAct=EBI-3905796, EBI-3390054;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18347059}.
Nucleus {ECO:0000269|PubMed:18347059}. 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=24;
Name=1; Synonyms=ID-IXL;
IsoId=Q14934-1; Sequence=Displayed;
Name=2; Synonyms=IA-IXL;
IsoId=Q14934-2; Sequence=VSP_036701;
Name=3; Synonyms=IA-IXi;
IsoId=Q14934-3; Sequence=VSP_036701, VSP_036705;
Note=Due to an intron retention.;
Name=4; Synonyms=IC-IXL;
IsoId=Q14934-4; Sequence=VSP_036702;
Name=5; Synonyms=IC-IXi;
IsoId=Q14934-5; Sequence=VSP_036702, VSP_036705;
Note=Due to an intron retention.;
Name=6; Synonyms=IB-IXL;
IsoId=Q14934-6; Sequence=VSP_036703;
Name=7; Synonyms=IB-IXi;
IsoId=Q14934-7; Sequence=VSP_036703, VSP_036705;
Note=Due to an intron retention.;
Name=8; Synonyms=ID-IXi;
IsoId=Q14934-8; Sequence=VSP_036705;
Note=Due to an intron retention.;
Name=9; Synonyms=IE-IXL;
IsoId=Q14934-9; Sequence=VSP_036700;
Name=10; Synonyms=IE-IXi;
IsoId=Q14934-10; Sequence=VSP_036700, VSP_036705;
Note=Due to an intron retention.;
Name=11; Synonyms=IA-IXS;
IsoId=Q14934-11; Sequence=VSP_036701, VSP_036704;
Name=12; Synonyms=IEi-IXL;
IsoId=Q14934-12; Sequence=VSP_036699;
Note=Due to an intron retention.;
Name=13; Synonyms=IEi-IXi;
IsoId=Q14934-13; Sequence=VSP_036699, VSP_036705;
Note=Due to an intron retention.;
Name=14; Synonyms=IC-IXS;
IsoId=Q14934-14; Sequence=VSP_036702, VSP_036704;
Name=15; Synonyms=IB-IXS;
IsoId=Q14934-15; Sequence=VSP_036703, VSP_036704;
Name=16; Synonyms=ID-IXS;
IsoId=Q14934-16; Sequence=VSP_036704;
Name=17; Synonyms=IE-IXS;
IsoId=Q14934-17; Sequence=VSP_036700, VSP_036704;
Name=18; Synonyms=IEi-IXS;
IsoId=Q14934-18; Sequence=VSP_036699, VSP_036704;
Note=Due to an intron retention.;
Name=19; Synonyms=IV-IXL;
IsoId=Q14934-19; Sequence=VSP_036698;
Name=20; Synonyms=IV-IXi;
IsoId=Q14934-20; Sequence=VSP_036698, VSP_036705;
Note=Due to an intron retention.;
Name=21; Synonyms=IV-IXS;
IsoId=Q14934-21; Sequence=VSP_036698, VSP_036704;
Name=22; Synonyms=VI-IXL;
IsoId=Q14934-22; Sequence=VSP_036697;
Name=23; Synonyms=VI-IXi;
IsoId=Q14934-23; Sequence=VSP_036697, VSP_036705;
Note=Due to an intron retention.;
Name=24; Synonyms=VI-IXS;
IsoId=Q14934-24; Sequence=VSP_036697, VSP_036704;
-!- TISSUE SPECIFICITY: Highly expressed in placenta, lung, kidney,
testis and ovary. Weakly expressed in spleen and thymus. Not
expressed in peripheral blood lymphocytes. Detected in
hippocampus. {ECO:0000269|PubMed:18675896}.
-!- DOMAIN: Rel Similarity Domain (RSD) allows DNA-binding and
cooperative interactions with AP1 factors. {ECO:0000250}.
-!- PTM: Phosphorylated by NFATC-kinases; dephosphorylated by
calcineurin. Phosphorylated on Ser-168 and Ser-170 by MTOR, IRAK1,
MAPK7 and MAPK14, on Ser-213 and Ser-217 by MAPK8 and MAPK9, and
on Ser-289 and Ser-344 by RPS6KA3. Phosphorylated by GSK3B.
{ECO:0000269|PubMed:11997522, ECO:0000269|PubMed:17213202,
ECO:0000269|PubMed:17875713, ECO:0000269|PubMed:18347059,
ECO:0000269|PubMed:19026640}.
-!- PTM: Ubiquitinated, leading to its degradation by the proteasome
and reduced transcriptional activity. Ubiquitination and reduction
in transcriptional activity can be further facilitated through
GSK3B-dependent phosphorylation. Polyubiquitin linkage is mainly
through 'Lys-48'. {ECO:0000269|PubMed:19026640}.
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EMBL; L41066; AAA79175.1; -; mRNA.
EMBL; EU887632; ACG55652.1; -; mRNA.
EMBL; EU887633; ACG55653.1; -; mRNA.
EMBL; EU887634; ACG55654.1; -; mRNA.
EMBL; EU887635; ACG55655.1; -; mRNA.
EMBL; EU887636; ACG55656.1; -; mRNA.
EMBL; EU887637; ACG55657.1; -; mRNA.
EMBL; EU887638; ACG55658.1; -; mRNA.
EMBL; EU887639; ACG55659.1; -; mRNA.
EMBL; EU887640; ACG55660.1; -; mRNA.
EMBL; EU887641; ACG55661.1; -; mRNA.
EMBL; EU887642; ACG55662.1; -; mRNA.
EMBL; EU887643; ACG55663.1; -; mRNA.
EMBL; EU887644; ACG55664.1; -; mRNA.
EMBL; EU887645; ACG55665.1; -; mRNA.
EMBL; EU887646; ACG55666.1; -; mRNA.
EMBL; EU887647; ACG55667.1; -; mRNA.
EMBL; EU887648; ACG55668.1; -; mRNA.
EMBL; EU887649; ACG55669.1; -; mRNA.
EMBL; EU887650; ACG55670.1; -; mRNA.
EMBL; EU887651; ACG55671.1; -; mRNA.
EMBL; EU887652; ACG55672.1; -; mRNA.
EMBL; EU887653; ACG55673.1; -; mRNA.
EMBL; EU887654; ACG55674.1; -; mRNA.
EMBL; EU887655; ACG55675.1; -; mRNA.
EMBL; AK293185; BAG56726.1; -; mRNA.
EMBL; AK302271; BAG63617.1; -; mRNA.
EMBL; BC008857; AAH08857.2; -; mRNA.
EMBL; BC053855; AAH53855.1; -; mRNA.
CCDS; CCDS45089.1; -. [Q14934-3]
CCDS; CCDS55909.1; -. [Q14934-11]
CCDS; CCDS55910.1; -. [Q14934-16]
CCDS; CCDS55911.1; -. [Q14934-12]
CCDS; CCDS73625.1; -. [Q14934-10]
CCDS; CCDS9629.1; -. [Q14934-1]
RefSeq; NP_001129494.1; NM_001136022.2. [Q14934-3]
RefSeq; NP_001185894.1; NM_001198965.1. [Q14934-16]
RefSeq; NP_001185895.1; NM_001198966.2. [Q14934-12]
RefSeq; NP_001185896.1; NM_001198967.2. [Q14934-11]
RefSeq; NP_001275731.1; NM_001288802.1. [Q14934-10]
RefSeq; NP_001306972.1; NM_001320043.1. [Q14934-2]
RefSeq; NP_004545.2; NM_004554.4. [Q14934-1]
RefSeq; XP_011535099.1; XM_011536797.2. [Q14934-9]
RefSeq; XP_011535101.1; XM_011536799.2. [Q14934-17]
UniGene; Hs.77810; -.
PDB; 2YRP; NMR; -; A=585-691.
PDBsum; 2YRP; -.
ProteinModelPortal; Q14934; -.
SMR; Q14934; -.
BioGrid; 110849; 16.
IntAct; Q14934; 11.
MINT; MINT-1535456; -.
STRING; 9606.ENSP00000388910; -.
iPTMnet; Q14934; -.
PhosphoSitePlus; Q14934; -.
BioMuta; NFATC4; -.
DMDM; 215274090; -.
MaxQB; Q14934; -.
PaxDb; Q14934; -.
PeptideAtlas; Q14934; -.
PRIDE; Q14934; -.
DNASU; 4776; -.
Ensembl; ENST00000250373; ENSP00000250373; ENSG00000100968. [Q14934-1]
Ensembl; ENST00000413692; ENSP00000388910; ENSG00000100968. [Q14934-3]
Ensembl; ENST00000422617; ENSP00000396788; ENSG00000100968. [Q14934-10]
Ensembl; ENST00000424781; ENSP00000388668; ENSG00000100968. [Q14934-7]
Ensembl; ENST00000539237; ENSP00000439350; ENSG00000100968. [Q14934-5]
Ensembl; ENST00000553469; ENSP00000451502; ENSG00000100968. [Q14934-14]
Ensembl; ENST00000553708; ENSP00000450590; ENSG00000100968. [Q14934-8]
Ensembl; ENST00000553879; ENSP00000452349; ENSG00000100968. [Q14934-12]
Ensembl; ENST00000554050; ENSP00000451151; ENSG00000100968. [Q14934-16]
Ensembl; ENST00000554344; ENSP00000450469; ENSG00000100968. [Q14934-12]
Ensembl; ENST00000554473; ENSP00000450810; ENSG00000100968. [Q14934-21]
Ensembl; ENST00000554591; ENSP00000452039; ENSG00000100968. [Q14934-11]
Ensembl; ENST00000554661; ENSP00000450733; ENSG00000100968. [Q14934-18]
Ensembl; ENST00000554966; ENSP00000450644; ENSG00000100968. [Q14934-15]
Ensembl; ENST00000555167; ENSP00000451395; ENSG00000100968. [Q14934-20]
Ensembl; ENST00000555393; ENSP00000451801; ENSG00000100968. [Q14934-23]
Ensembl; ENST00000555453; ENSP00000450686; ENSG00000100968. [Q14934-9]
Ensembl; ENST00000555590; ENSP00000451224; ENSG00000100968. [Q14934-6]
Ensembl; ENST00000555802; ENSP00000451590; ENSG00000100968. [Q14934-22]
Ensembl; ENST00000556169; ENSP00000451454; ENSG00000100968. [Q14934-17]
Ensembl; ENST00000556279; ENSP00000452270; ENSG00000100968. [Q14934-4]
Ensembl; ENST00000556759; ENSP00000451183; ENSG00000100968. [Q14934-19]
Ensembl; ENST00000557451; ENSP00000451284; ENSG00000100968. [Q14934-13]
Ensembl; ENST00000557767; ENSP00000451496; ENSG00000100968. [Q14934-24]
GeneID; 4776; -.
KEGG; hsa:4776; -.
UCSC; uc001wpc.5; human. [Q14934-1]
CTD; 4776; -.
DisGeNET; 4776; -.
EuPathDB; HostDB:ENSG00000100968.13; -.
GeneCards; NFATC4; -.
HGNC; HGNC:7778; NFATC4.
HPA; CAB032859; -.
HPA; HPA031641; -.
HPA; HPA076526; -.
MIM; 602699; gene.
neXtProt; NX_Q14934; -.
OpenTargets; ENSG00000100968; -.
PharmGKB; PA31584; -.
eggNOG; ENOG410IIAD; Eukaryota.
eggNOG; ENOG4111EMW; LUCA.
GeneTree; ENSGT00550000074562; -.
HOVERGEN; HBG104364; -.
InParanoid; Q14934; -.
KO; K17334; -.
OMA; VFIERGP; -.
OrthoDB; EOG091G01QP; -.
PhylomeDB; Q14934; -.
TreeFam; TF326480; -.
SIGNOR; Q14934; -.
EvolutionaryTrace; Q14934; -.
GeneWiki; NFATC4; -.
GenomeRNAi; 4776; -.
PRO; PR:Q14934; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100968; -.
CleanEx; HS_NFATC4; -.
ExpressionAtlas; Q14934; baseline and differential.
Genevisible; Q14934; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO; GO:0008134; F:transcription factor binding; IEA:Ensembl.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IGI:BHF-UCL.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IEA:Ensembl.
GO; GO:0045333; P:cellular respiration; IEA:Ensembl.
GO; GO:1904637; P:cellular response to ionomycin; IEA:Ensembl.
GO; GO:0071285; P:cellular response to lithium ion; IEA:Ensembl.
GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
GO; GO:0055001; P:muscle cell development; 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:1902894; P:negative regulation of pri-miRNA transcription from RNA polymerase II promoter; IGI:BHF-UCL.
GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
GO; GO:2000297; P:negative regulation of synapse maturation; IEA:Ensembl.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IEA:Ensembl.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:0048167; P:regulation of synaptic plasticity; IEA:Ensembl.
GO; GO:0051145; P:smooth muscle cell differentiation; IEA:Ensembl.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
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.
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; Differentiation; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 902 Nuclear factor of activated T-cells,
cytoplasmic 4.
/FTId=PRO_0000205182.
REPEAT 213 229 SP 1.
REPEAT 277 293 SP 2; approximate.
DOMAIN 401 582 RHD. {ECO:0000255|PROSITE-
ProRule:PRU00265}.
DOMAIN 586 683 IPT/TIG.
DNA_BIND 430 437
REGION 114 119 Calcineurin-binding.
REGION 213 293 2 approximate SP repeats.
MOTIF 268 270 Nuclear localization signal.
MOTIF 672 674 Nuclear localization signal.
COMPBIAS 41 327 Pro-rich.
COMPBIAS 717 836 Pro-rich.
MOD_RES 168 168 Phosphoserine; by MAPK7 and MAPK14.
{ECO:0000269|PubMed:11997522,
ECO:0000269|PubMed:18347059}.
MOD_RES 170 170 Phosphoserine; by MAPK7 and MAPK14.
{ECO:0000269|PubMed:11997522,
ECO:0000269|PubMed:18347059}.
MOD_RES 213 213 Phosphoserine; by MAPK8 and MAPK9.
{ECO:0000269|PubMed:17875713}.
MOD_RES 217 217 Phosphoserine; by MAPK8 and MAPK9.
{ECO:0000269|PubMed:17875713}.
MOD_RES 289 289 Phosphoserine; by RPS6KA3.
{ECO:0000269|PubMed:17213202}.
MOD_RES 344 344 Phosphoserine; by RPS6KA3.
{ECO:0000269|PubMed:17213202}.
CROSSLNK 689 689 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 712 Missing (in isoform 22, isoform 23 and
isoform 24).
{ECO:0000303|PubMed:18675896}.
/FTId=VSP_036697.
VAR_SEQ 1 465 Missing (in isoform 19, isoform 20 and
isoform 21).
{ECO:0000303|PubMed:18675896}.
/FTId=VSP_036698.
VAR_SEQ 1 70 Missing (in isoform 12, isoform 13 and
isoform 18).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:18675896}.
/FTId=VSP_036699.
VAR_SEQ 1 32 MGAASCEDEELEFKLVFGEEKEAPPLGAGGLG -> MPASI
SSIFPGPTLLLSCGS (in isoform 9, isoform 10
and isoform 17).
{ECO:0000303|PubMed:18675896}.
/FTId=VSP_036700.
VAR_SEQ 1 1 M -> MITTLPSLLPASLASISHRVTNLPSNSLSHNPGLSK
PDFPGNSSPGLPSSSSPGRDLGAPAGSM (in isoform
2, isoform 3 and isoform 11).
{ECO:0000303|PubMed:18675896}.
/FTId=VSP_036701.
VAR_SEQ 1 1 M -> MADGGADSAAQRLPEGPGRVAPGRDLGAPAGSM
(in isoform 4, isoform 5 and isoform 14).
{ECO:0000303|PubMed:18675896}.
/FTId=VSP_036702.
VAR_SEQ 1 1 M -> MLSGRDLGAPAGSM (in isoform 6,
isoform 7 and isoform 15).
{ECO:0000303|PubMed:18675896}.
/FTId=VSP_036703.
VAR_SEQ 773 880 Missing (in isoform 11, isoform 14,
isoform 15, isoform 16, isoform 17,
isoform 18, isoform 21 and isoform 24).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:18675896}.
/FTId=VSP_036704.
VAR_SEQ 881 902 VSEIIGRDLSGFPAPPGEEPPA -> GGCGTGGCECECVQE
IALHVC (in isoform 3, isoform 5, isoform
7, isoform 8, isoform 10, isoform 13,
isoform 20 and isoform 23).
{ECO:0000303|PubMed:18675896}.
/FTId=VSP_036705.
VARIANT 160 160 G -> A (in dbSNP:rs2229309).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7749981}.
/FTId=VAR_046985.
VARIANT 246 246 S -> N (in dbSNP:rs2228231).
/FTId=VAR_046986.
VARIANT 800 800 S -> P (in dbSNP:rs7149586).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7749981}.
/FTId=VAR_046987.
MUTAGEN 168 168 S->A: Promotes nuclear localization and
increases transcriptional activity; when
associated with A-170.
{ECO:0000269|PubMed:11997522}.
MUTAGEN 170 170 S->A: Promotes nuclear localization and
increases transcriptional activity; when
associated with A-168.
{ECO:0000269|PubMed:11997522}.
MUTAGEN 213 213 S->A: Decreased transcriptional activity;
when associated with A-217.
{ECO:0000269|PubMed:17875713}.
MUTAGEN 217 217 S->A: Decreased transcriptional activity;
when associated with A-213.
{ECO:0000269|PubMed:17875713}.
CONFLICT 359 359 E -> K (in Ref. 3; BAG56726).
{ECO:0000305}.
CONFLICT 646 646 L -> P (in Ref. 3; BAG63617).
{ECO:0000305}.
STRAND 587 594 {ECO:0000244|PDB:2YRP}.
STRAND 602 610 {ECO:0000244|PDB:2YRP}.
STRAND 616 620 {ECO:0000244|PDB:2YRP}.
TURN 638 640 {ECO:0000244|PDB:2YRP}.
STRAND 645 649 {ECO:0000244|PDB:2YRP}.
STRAND 662 669 {ECO:0000244|PDB:2YRP}.
STRAND 671 673 {ECO:0000244|PDB:2YRP}.
STRAND 679 684 {ECO:0000244|PDB:2YRP}.
STRAND 687 689 {ECO:0000244|PDB:2YRP}.
SEQUENCE 902 AA; 95449 MW; AE94C5D1325D24D7 CRC64;
MGAASCEDEE LEFKLVFGEE KEAPPLGAGG LGEELDSEDA PPCCRLALGE PPPYGAAPIG
IPRPPPPRPG MHSPPPRPAP SPGTWESQPA RSVRLGGPGG GAGGAGGGRV LECPSIRITS
ISPTPEPPAA LEDNPDAWGD GSPRDYPPPE GFGGYREAGG QGGGAFFSPS PGSSSLSSWS
FFSDASDEAA LYAACDEVES ELNEAASRFG LGSPLPSPRA SPRPWTPEDP WSLYGPSPGG
RGPEDSWLLL SAPGPTPASP RPASPCGKRR YSSSGTPSSA SPALSRRGSL GEEGSEPPPP
PPLPLARDPG SPGPFDYVGA PPAESIPQKT RRTSSEQAVA LPRSEEPASC NGKLPLGAEE
SVAPPGGSRK EVAGMDYLAV PSPLAWSKAR IGGHSPIFRT SALPPLDWPL PSQYEQLELR
IEVQPRAHHR AHYETEGSRG AVKAAPGGHP VVKLLGYSEK PLTLQMFIGT ADERNLRPHA
FYQVHRITGK MVATASYEAV VSGTKVLEMT LLPENNMAAN IDCAGILKLR NSDIELRKGE
TDIGRKNTRV RLVFRVHVPQ GGGKVVSVQA ASVPIECSQR SAQELPQVEA YSPSACSVRG
GEELVLTGSN FLPDSKVVFI ERGPDGKLQW EEEATVNRLQ SNEVTLTLTV PEYSNKRVSR
PVQVYFYVSN GRRKRSPTQS FRFLPVICKE EPLPDSSLRG FPSASATPFG TDMDFSPPRP
PYPSYPHEDP ACETPYLSEG FGYGMPPLYP QTGPPPSYRP GLRMFPETRG TTGCAQPPAV
SFLPRPFPSD PYGGRGSSFS LGLPFSPPAP FRPPPLPASP PLEGPFPSQS DVHPLPAEGY
NKVGPGYGPG EGAPEQEKSR GGYSSGFRDS VPIQGITLEE VSEIIGRDLS GFPAPPGEEP
PA


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