Nfatc2
entrez
18019
canonical
uniprot
Q60591
canonical
ensembl
ENSMUSG00000027544
resolver
ensp
ENSMUSP00000029057
resolver
ensp
ENSMUSP00000074198
resolver
ensp
ENSMUSP00000104812
resolver
ensp
ENSMUSP00000118329
resolver
ensp
ENSMUSP00000130875
resolver
enst
ENSMUST00000029057
resolver
enst
ENSMUST00000137451
resolver
enst
ENSMUST00000171689
resolver
genesymbol
Nfatc2
resolver
genesymbol_syn
AI607462
resolver
genesymbol_syn
Nfat1
resolver
genesymbol_syn
Nfatp
resolver
uniprot
A2APK2
resolver
uniprot
A2APK3
resolver
uniprot
A2AQC5
resolver
uniprot
A2AQC6
resolver
uniprot
A2AQC7
resolver
uniprot
A2AQC8
resolver
uniprot
B5B2P6
resolver
uniprot
B5B2P7
resolver
uniprot
B5B2P8
resolver
uniprot
B5B2Q2
resolver
uniprot
B5B2Q3
resolver
uniprot
B5B2Q4
resolver
uniprot
B5B2Q6
resolver
uniprot
B5B2R4
resolver
uniprot
B5B2R5
resolver
uniprot
F7BTI4
resolver
uniprot
F7CVK2
resolver
uniprot
Q3TTU8
resolver
uniprot
Q60984
resolver
uniprot
Q60985
resolver
uniprot
Q8C443
resolver
uniprot
Q91Y65
resolver
uniprot_entry
A2AQC8_MOUSE
resolver
uniprot_entry
B5B2P6_MOUSE
resolver
uniprot_entry
B5B2P7_MOUSE
resolver
uniprot_entry
B5B2P8_MOUSE
resolver
uniprot_entry
B5B2Q2_MOUSE
resolver
uniprot_entry
B5B2Q4_MOUSE
resolver
uniprot_entry
B5B2Q6_MOUSE
resolver
uniprot_entry
B5B2R4_MOUSE
resolver
uniprot_entry
B5B2R5_MOUSE
resolver
uniprot_entry
F7BTI4_MOUSE
resolver
uniprot_entry
F7CVK2_MOUSE
resolver
uniprot_entry
NFAC2_MOUSE
resolver
uniprot_entry
Q3TTU8_MOUSE
resolver
uniprot_entry
Q8C443_MOUSE
resolver
uniprot_sec
A2APK2
resolver
uniprot_sec
A2APK3
resolver
uniprot_sec
A2AQC5
resolver
uniprot_sec
A2AQC6
resolver
uniprot_sec
A2AQC7
resolver
uniprot_sec
B5B2Q3
resolver
uniprot_sec
Q60984
resolver
uniprot_sec
Q60985
resolver
uniprot_sec
Q91Y65
resolver
amino_acid_sequence
MDVPEPQPDPDGGDGPGHEPGGSPQDELDFSILFDYDYLNPIEEEPIAHKAISSPSGLAYPDDVLDYGLKPCNPLASLSGEPPGRFGEPDSIGFQNFLSPVKPAGASGPSPRIEITPSHELMQAGGALRGRDAGLSPEQPALALAGVAASPRFTLPVPGYEGYREPLCLSPASSGSSASFISDTFSPYTSPCVSPNNAGPDDLCPQFQNIPAHYSPRTSPIMSPRTSLAEDSCLGRHSPVPRPASRSSSPGAKRRHSCAEALVAPLPAASPQRSRSPSPQPSPHVALQDDSIPAGYPPTAGSAVLMDALNTLATDSPCGIPSKIWKTSPDPTPVSTAPSKAGLARHIYPTVEFLGPCEQEERRNSAPESILLVPPTWPKQLVPAIPICSIPVTASLPPLEWPLSNQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMENKPLGLQIFIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHVPEPSGRIVSLQAASNPIECSQRSAHELPMVERQDMDSCLVYGGQQMILTGQNFTAESKVVFMEKTTDGQQIWEMEATVDKDKSQPNMLFVEIPEYRNKHIRVPVKVNFYVINGKRKRSQPQHFTYHPVPAIKTEPSDEYEPSLICSPAHGGLGSQPYYPQHPMLAESPSCLVATMAPCQQFRSGLSSPDARYQQQSPAAALYQRSKSLSPGLLGYQQPSLLAAPLGLADAHRSVLVHAGSQGQGQGSTLPHTSSASQQASPVIHYSPTNQQLRGGGHQEFQHIMYCENFGPSSARPGPPPINQGQRLSPGAYPTVIQQQTAPSQRAAKNGPSDQKEALPTGVTVKQEQNLDQTYLDDVNEIIRKEFSGPPSRNQT
uniprot
proteins
function
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 or GM-CSF. Promotes invasive migration through the activation of GPC6 expression and WNT5A signaling pathway (By similarity). Is involved in the negative regulation of chondrogenesis (PubMed:10620601). Recruited by AKAP5 to ORAI1 pore-forming subunit of CRAC channels in Ca(2+) signaling microdomains where store-operated Ca(2+) influx is coupled to calmodulin and calcineurin signaling and activation of NFAT-dependent transcriptional responses. {ECO:0000250|UniProtKB:Q13469, ECO:0000269|PubMed:10620601, ECO:0000269|PubMed:32415068, ECO:0000269|PubMed:33941685}.
uniprot
proteins
mass_dalton
100020
uniprot
proteins
mutagenesis
MUTAGEN 112; /note="R->A: Lowers dephosphorylation."; /evidence="ECO:0000269|PubMed:9660947"; MUTAGEN 114; /note="E->A: Lowers dephosphorylation."; /evidence="ECO:0000269|PubMed:9660947"; MUTAGEN 116; /note="T->A: No dephosphorylation."; /evidence="ECO:0000269|PubMed:9660947"; MUTAGEN 164; /note="R->A: Induces aberrant nuclear localization of the phosphorylated form."; /evidence="ECO:0000269|PubMed:11030334"; MUTAGEN 423; /note="R->A: Decrease in binding to DNA."; /evidence="ECO:0000269|PubMed:7876165"; MUTAGEN 425; /note="H->A: No change in binding to DNA."; /evidence="ECO:0000269|PubMed:7876165"; MUTAGEN 426; /note="Y->A: Decrease in binding to DNA."; /evidence="ECO:0000269|PubMed:7876165"; MUTAGEN 428; /note="T->A: No change in binding to DNA."; /evidence="ECO:0000269|PubMed:7876165"; MUTAGEN 428; /note="T->C: No change in binding to DNA and confers DNA-binding sensitivity to sulfhydryl modifications."; /evidence="ECO:0000269|PubMed:7876165"; MUTAGEN 429; /note="E->A: Decrease in binding to DNA."; /evidence="ECO:0000269|PubMed:7876165
uniprot
proteins
post_translational_modification
PTM: In resting cells, phosphorylated by NFATC-kinase on at least 18 sites in the 99-365 region. Upon cell stimulation, all these sites except Ser-245 are dephosphorylated by calcineurin. Dephosphorylation induces a conformational change that simultaneously exposes an NLS and masks an NES, which results in nuclear localization. Simultaneously, one site among Ser-53; Ser-54 and Ser-56 is phosphorylated; which is required for full transcriptional activity. {ECO:0000269|PubMed:11030334}.; PTM: Ubiquitinated in endothelial cells by RNF213 downstream of the non-canonical Wnt signaling pathway, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q13469}.
uniprot
proteins
pubmed
10089876
uniprot
proteins
pubmed
10620601
uniprot
proteins
pubmed
11030334
uniprot
proteins
pubmed
11278367
uniprot
proteins
pubmed
17198697
uniprot
proteins
pubmed
17579027
uniprot
proteins
pubmed
18675896
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23616576
uniprot
proteins
pubmed
24970700
uniprot
proteins
pubmed
28424240
uniprot
proteins
pubmed
32415068
uniprot
proteins
pubmed
33941685
uniprot
proteins
pubmed
7876165
uniprot
proteins
pubmed
8235597
uniprot
proteins
pubmed
8668213
uniprot
proteins
pubmed
8943202
uniprot
proteins
pubmed
9660947
uniprot
proteins
sequence_length
927
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11030334, ECO:0000269|PubMed:24970700}. Nucleus {ECO:0000269|PubMed:11030334, ECO:0000269|PubMed:24970700}. 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.
uniprot
proteins