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Q14934 (NFAC4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear factor of activated T-cells, cytoplasmic 4

Short name=NF-ATc4
Short name=NFATc4
Alternative name(s):
T-cell transcription factor NFAT3
Short name=NF-AT3
Gene names
Name:NFATC4
Synonyms:NFAT3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length902 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.7 Ref.9 Ref.10

Subunit structure

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. Ref.6 Ref.8 Ref.9 Ref.14

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. Ref.13

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. Ref.2

Domain

Rel Similarity Domain (RSD) allows DNA-binding and cooperative interactions with AP1 factors By similarity.

Post-translational modification

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. Ref.7 Ref.8 Ref.9 Ref.11 Ref.13

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'. Ref.11

Sequence similarities

Contains 1 IPT/TIG domain.

Contains 1 RHD (Rel-like) domain.

Ontologies

Keywords
   Biological processDifferentiation
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular respiration

Inferred from electronic annotation. Source: Ensembl

cellular response to UV

Inferred from electronic annotation. Source: Ensembl

cellular response to lithium ion

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Traceable author statement Ref.1. Source: ProtInc

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from electronic annotation. Source: Ensembl

muscle cell development

Inferred from electronic annotation. Source: Ensembl

patterning of blood vessels

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of tumor necrosis factor production

Inferred from electronic annotation. Source: Ensembl

regulation of synaptic plasticity

Inferred from electronic annotation. Source: Ensembl

smooth muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from electronic annotation. Source: Ensembl

intermediate filament cytoskeleton

Inferred from direct assay. Source: HPA

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from electronic annotation. Source: Ensembl

transcription coactivator activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

UBCP0CG483EBI-3905796,EBI-3390054

Alternative products

This entry describes 24 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14934-1)

Also known as: ID-IXL;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q14934-2)

Also known as: IA-IXL;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MITTLPSLLPASLASISHRVTNLPSNSLSHNPGLSKPDFPGNSSPGLPSSSSPGRDLGAPAGSM
Isoform 3 (identifier: Q14934-3)

Also known as: IA-IXi;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MITTLPSLLPASLASISHRVTNLPSNSLSHNPGLSKPDFPGNSSPGLPSSSSPGRDLGAPAGSM
     881-902: VSEIIGRDLSGFPAPPGEEPPA → GGCGTGGCECECVQEIALHVC
Note: Due to an intron retention.
Isoform 4 (identifier: Q14934-4)

Also known as: IC-IXL;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MADGGADSAAQRLPEGPGRVAPGRDLGAPAGSM
Isoform 5 (identifier: Q14934-5)

Also known as: IC-IXi;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MADGGADSAAQRLPEGPGRVAPGRDLGAPAGSM
     881-902: VSEIIGRDLSGFPAPPGEEPPA → GGCGTGGCECECVQEIALHVC
Note: Due to an intron retention.
Isoform 6 (identifier: Q14934-6)

Also known as: IB-IXL;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLSGRDLGAPAGSM
Isoform 7 (identifier: Q14934-7)

Also known as: IB-IXi;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLSGRDLGAPAGSM
     881-902: VSEIIGRDLSGFPAPPGEEPPA → GGCGTGGCECECVQEIALHVC
Note: Due to an intron retention.
Isoform 8 (identifier: Q14934-8)

Also known as: ID-IXi;

The sequence of this isoform differs from the canonical sequence as follows:
     881-902: VSEIIGRDLSGFPAPPGEEPPA → GGCGTGGCECECVQEIALHVC
Note: Due to an intron retention.
Isoform 9 (identifier: Q14934-9)

Also known as: IE-IXL;

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: MGAASCEDEELEFKLVFGEEKEAPPLGAGGLG → MPASISSIFPGPTLLLSCGS
Isoform 10 (identifier: Q14934-10)

Also known as: IE-IXi;

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: MGAASCEDEELEFKLVFGEEKEAPPLGAGGLG → MPASISSIFPGPTLLLSCGS
     881-902: VSEIIGRDLSGFPAPPGEEPPA → GGCGTGGCECECVQEIALHVC
Note: Due to an intron retention.
Isoform 11 (identifier: Q14934-11)

Also known as: IA-IXS;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MITTLPSLLPASLASISHRVTNLPSNSLSHNPGLSKPDFPGNSSPGLPSSSSPGRDLGAPAGSM
     773-880: Missing.
Isoform 12 (identifier: Q14934-12)

Also known as: IEi-IXL;

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: Missing.
Note: Due to an intron retention.
Isoform 13 (identifier: Q14934-13)

Also known as: IEi-IXi;

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: Missing.
     881-902: VSEIIGRDLSGFPAPPGEEPPA → GGCGTGGCECECVQEIALHVC
Note: Due to an intron retention.
Isoform 14 (identifier: Q14934-14)

Also known as: IC-IXS;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MADGGADSAAQRLPEGPGRVAPGRDLGAPAGSM
     773-880: Missing.
Isoform 15 (identifier: Q14934-15)

Also known as: IB-IXS;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLSGRDLGAPAGSM
     773-880: Missing.
Isoform 16 (identifier: Q14934-16)

Also known as: ID-IXS;

The sequence of this isoform differs from the canonical sequence as follows:
     773-880: Missing.
Isoform 17 (identifier: Q14934-17)

Also known as: IE-IXS;

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: MGAASCEDEELEFKLVFGEEKEAPPLGAGGLG → MPASISSIFPGPTLLLSCGS
     773-880: Missing.
Isoform 18 (identifier: Q14934-18)

Also known as: IEi-IXS;

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: Missing.
     773-880: Missing.
Note: Due to an intron retention.
Isoform 19 (identifier: Q14934-19)

Also known as: IV-IXL;

The sequence of this isoform differs from the canonical sequence as follows:
     1-465: Missing.
Isoform 20 (identifier: Q14934-20)

Also known as: IV-IXi;

The sequence of this isoform differs from the canonical sequence as follows:
     1-465: Missing.
     881-902: VSEIIGRDLSGFPAPPGEEPPA → GGCGTGGCECECVQEIALHVC
Note: Due to an intron retention.
Isoform 21 (identifier: Q14934-21)

Also known as: IV-IXS;

The sequence of this isoform differs from the canonical sequence as follows:
     1-465: Missing.
     773-880: Missing.
Isoform 22 (identifier: Q14934-22)

Also known as: VI-IXL;

The sequence of this isoform differs from the canonical sequence as follows:
     1-712: Missing.
Isoform 23 (identifier: Q14934-23)

Also known as: VI-IXi;

The sequence of this isoform differs from the canonical sequence as follows:
     1-712: Missing.
     881-902: VSEIIGRDLSGFPAPPGEEPPA → GGCGTGGCECECVQEIALHVC
Note: Due to an intron retention.
Isoform 24 (identifier: Q14934-24)

Also known as: VI-IXS;

The sequence of this isoform differs from the canonical sequence as follows:
     1-712: Missing.
     773-880: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 902902Nuclear factor of activated T-cells, cytoplasmic 4
PRO_0000205182

Regions

Repeat213 – 22917SP 1
Repeat277 – 29317SP 2; approximate
Domain401 – 582182RHD
Domain586 – 68398IPT/TIG
DNA binding430 – 4378
Region114 – 1196Calcineurin-binding
Region213 – 293812 approximate SP repeats
Motif268 – 2703Nuclear localization signal
Motif672 – 6743Nuclear localization signal
Compositional bias41 – 327287Pro-rich
Compositional bias717 – 836120Pro-rich

Amino acid modifications

Modified residue1681Phosphoserine; by MAPK7 and MAPK14 Ref.7 Ref.13
Modified residue1701Phosphoserine; by MAPK7 and MAPK14 Ref.7 Ref.13
Modified residue2131Phosphoserine; by MAPK8 and MAPK9 Ref.8
Modified residue2171Phosphoserine; by MAPK8 and MAPK9 Ref.8
Modified residue2891Phosphoserine; by RPS6KA3 Ref.9
Modified residue3441Phosphoserine; by RPS6KA3 Ref.9

Natural variations

Alternative sequence1 – 712712Missing in isoform 22, isoform 23 and isoform 24.
VSP_036697
Alternative sequence1 – 465465Missing in isoform 19, isoform 20 and isoform 21.
VSP_036698
Alternative sequence1 – 7070Missing in isoform 12, isoform 13 and isoform 18.
VSP_036699
Alternative sequence1 – 3232MGAAS…AGGLG → MPASISSIFPGPTLLLSCGS in isoform 9, isoform 10 and isoform 17.
VSP_036700
Alternative sequence11M → MITTLPSLLPASLASISHRV TNLPSNSLSHNPGLSKPDFP GNSSPGLPSSSSPGRDLGAP AGSM in isoform 2, isoform 3 and isoform 11.
VSP_036701
Alternative sequence11M → MADGGADSAAQRLPEGPGRV APGRDLGAPAGSM in isoform 4, isoform 5 and isoform 14.
VSP_036702
Alternative sequence11M → MLSGRDLGAPAGSM in isoform 6, isoform 7 and isoform 15.
VSP_036703
Alternative sequence773 – 880108Missing in isoform 11, isoform 14, isoform 15, isoform 16, isoform 17, isoform 18, isoform 21 and isoform 24.
VSP_036704
Alternative sequence881 – 90222VSEII…EEPPA → GGCGTGGCECECVQEIALHV C in isoform 3, isoform 5, isoform 7, isoform 8, isoform 10, isoform 13, isoform 20 and isoform 23.
VSP_036705
Natural variant1601G → A. Ref.1 Ref.4
Corresponds to variant rs2229309 [ dbSNP | Ensembl ].
VAR_046985
Natural variant2461S → N.
Corresponds to variant rs2228231 [ dbSNP | Ensembl ].
VAR_046986
Natural variant8001S → P. Ref.1 Ref.4
Corresponds to variant rs7149586 [ dbSNP | Ensembl ].
VAR_046987

Experimental info

Mutagenesis1681S → A: Promotes nuclear localization and increases transcriptional activity; when associated with A-170. Ref.7
Mutagenesis1701S → A: Promotes nuclear localization and increases transcriptional activity; when associated with A-168. Ref.7
Mutagenesis2131S → A: Decreased transcriptional activity; when associated with A-217. Ref.8
Mutagenesis2171S → A: Decreased transcriptional activity; when associated with A-213. Ref.8
Sequence conflict3591E → K in BAG56726. Ref.3
Sequence conflict6461L → P in BAG63617. Ref.3

Secondary structure

................... 902
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ID-IXL) [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: AE94C5D1325D24D7

FASTA90295,449
        10         20         30         40         50         60 
MGAASCEDEE LEFKLVFGEE KEAPPLGAGG LGEELDSEDA PPCCRLALGE PPPYGAAPIG 

        70         80         90        100        110        120 
IPRPPPPRPG MHSPPPRPAP SPGTWESQPA RSVRLGGPGG GAGGAGGGRV LECPSIRITS 

       130        140        150        160        170        180 
ISPTPEPPAA LEDNPDAWGD GSPRDYPPPE GFGGYREAGG QGGGAFFSPS PGSSSLSSWS 

       190        200        210        220        230        240 
FFSDASDEAA LYAACDEVES ELNEAASRFG LGSPLPSPRA SPRPWTPEDP WSLYGPSPGG 

       250        260        270        280        290        300 
RGPEDSWLLL SAPGPTPASP RPASPCGKRR YSSSGTPSSA SPALSRRGSL GEEGSEPPPP 

       310        320        330        340        350        360 
PPLPLARDPG SPGPFDYVGA PPAESIPQKT RRTSSEQAVA LPRSEEPASC NGKLPLGAEE 

       370        380        390        400        410        420 
SVAPPGGSRK EVAGMDYLAV PSPLAWSKAR IGGHSPIFRT SALPPLDWPL PSQYEQLELR 

       430        440        450        460        470        480 
IEVQPRAHHR AHYETEGSRG AVKAAPGGHP VVKLLGYSEK PLTLQMFIGT ADERNLRPHA 

       490        500        510        520        530        540 
FYQVHRITGK MVATASYEAV VSGTKVLEMT LLPENNMAAN IDCAGILKLR NSDIELRKGE 

       550        560        570        580        590        600 
TDIGRKNTRV RLVFRVHVPQ GGGKVVSVQA ASVPIECSQR SAQELPQVEA YSPSACSVRG 

       610        620        630        640        650        660 
GEELVLTGSN FLPDSKVVFI ERGPDGKLQW EEEATVNRLQ SNEVTLTLTV PEYSNKRVSR 

       670        680        690        700        710        720 
PVQVYFYVSN GRRKRSPTQS FRFLPVICKE EPLPDSSLRG FPSASATPFG TDMDFSPPRP 

       730        740        750        760        770        780 
PYPSYPHEDP ACETPYLSEG FGYGMPPLYP QTGPPPSYRP GLRMFPETRG TTGCAQPPAV 

       790        800        810        820        830        840 
SFLPRPFPSD PYGGRGSSFS LGLPFSPPAP FRPPPLPASP PLEGPFPSQS DVHPLPAEGY 

       850        860        870        880        890        900 
NKVGPGYGPG EGAPEQEKSR GGYSSGFRDS VPIQGITLEE VSEIIGRDLS GFPAPPGEEP 


PA 

« Hide

Isoform 2 (IA-IXL) [UniParc].

Checksum: 977A42276D24A2DD
Show »

FASTA965101,680
Isoform 3 (IA-IXi) [UniParc].

Checksum: 91DDEA6EACD24AD1
Show »

FASTA964101,513
Isoform 4 (IC-IXL) [UniParc].

Checksum: E72E379E8F1087A2
Show »

FASTA93498,436
Isoform 5 (IC-IXi) [UniParc].

Checksum: B5A8538C98F73584
Show »

FASTA93398,269
Isoform 6 (IB-IXL) [UniParc].

Checksum: 36C042AAF575636D
Show »

FASTA91596,662
Isoform 7 (IB-IXi) [UniParc].

Checksum: CBDD67F6FD13FA0B
Show »

FASTA91496,495
Isoform 8 (ID-IXi) [UniParc].

Checksum: 2F5A1C31D55440FA
Show »

FASTA90195,282
Isoform 9 (IE-IXL) [UniParc].

Checksum: CD0C3EF25B5761B6
Show »

FASTA89094,146
Isoform 10 (IE-IXi) [UniParc].

Checksum: E7A13F58DF1121B1
Show »

FASTA88993,978
Isoform 11 (IA-IXS) [UniParc].

Checksum: AA5ED1F6E0713077
Show »

FASTA85790,525
Isoform 12 (IEi-IXL) [UniParc].

Checksum: 22978126C7D764DB
Show »

FASTA83288,270
Isoform 13 (IEi-IXi) [UniParc].

Checksum: CC1EEBC45F144C10
Show »

FASTA83188,103
Isoform 14 (IC-IXS) [UniParc].

Checksum: 4BF3996D8C2BA62C
Show »

FASTA82687,282
Isoform 15 (IB-IXS) [UniParc].

Checksum: F9035684E3A5FE7E
Show »

FASTA80785,508
Isoform 16 (ID-IXS) [UniParc].

Checksum: 8378E0D0BB0888D2
Show »

FASTA79484,294
Isoform 17 (IE-IXS) [UniParc].

Checksum: 4B73A89F510DC96E
Show »

FASTA78282,991
Isoform 18 (IEi-IXS) [UniParc].

Checksum: E589F6754CC1B54C
Show »

FASTA72477,115
Isoform 19 (IV-IXL) [UniParc].

Checksum: EEA72B2EDFA7E67A
Show »

FASTA43747,373
Isoform 20 (IV-IXi) [UniParc].

Checksum: ACB4E3DC2F96ED8B
Show »

FASTA43647,206
Isoform 21 (IV-IXS) [UniParc].

Checksum: 043037F5F05D38C5
Show »

FASTA32936,219
Isoform 22 (VI-IXL) [UniParc].

Checksum: 3B4512C612A69FDF
Show »

FASTA19020,104
Isoform 23 (VI-IXi) [UniParc].

Checksum: CE8D0B112EEF4803
Show »

FASTA18919,937
Isoform 24 (VI-IXS) [UniParc].

Checksum: DC673A88B52B383F
Show »

FASTA828,950

References

« Hide 'large scale' references
[1]"Isolation of two new members of the NF-AT gene family and functional characterization of the NF-AT proteins."
Hoey T., Sun Y.-L., Williamson K., Xu X.
Immunity 2:461-472(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, VARIANTS ALA-160 AND PRO-800.
Tissue: T-cell.
[2]"Alternative splicing and expression of human and mouse NFAT genes."
Vihma H., Pruunsild P., Timmusk T.
Genomics 92:279-291(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: 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), TISSUE SPECIFICITY.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 12 AND 16).
Tissue: Adrenal gland and Testis.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-902 (ISOFORMS 1/2/4/6), VARIANTS ALA-160 AND PRO-800.
Tissue: Ovary and Rhabdomyosarcoma.
[5]"Generic signals and specific outcomes: signaling through Ca2+, calcineurin, and NF-AT."
Crabtree G.R.
Cell 96:611-614(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[6]"Requirement of two NFATc4 transactivation domains for CBP potentiation."
Yang T.T.C., Davis R.J., Chow C.-W.
J. Biol. Chem. 276:39569-39576(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CREBBP.
[7]"Phosphorylation of NFATc4 by p38 mitogen-activated protein kinases."
Yang T.T.C., Xiong Q., Enslen H., Davis R.J., Chow C.-W.
Mol. Cell. Biol. 22:3892-3904(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-168 AND SER-170, MUTAGENESIS OF SER-168 AND SER-170.
[8]"Nuclear factor of activated T3 is a negative regulator of Ras-JNK1/2-AP-1 induced cell transformation."
Yao K., Cho Y.-Y., Bergen H.R. III, Madden B.J., Choi B.Y., Ma W.-Y., Bode A.M., Dong Z.
Cancer Res. 67:8725-8735(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAPK8 AND MAPK9, PHOSPHORYLATION AT SER-213 AND SER-217, MUTAGENESIS OF SER-213 AND SER-217.
[9]"RSK2 mediates muscle cell differentiation through regulation of NFAT3."
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.
J. Biol. Chem. 282:8380-8392(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RPS6KA3, PHOSPHORYLATION AT SER-289 AND SER-344.
[10]"Repression of NFAT3 transcriptional activity by estrogen receptors."
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.
Cell. Mol. Life Sci. 65:2752-2762(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Regulation of the stability and transcriptional activity of NFATc4 by ubiquitination."
Fan Y., Xie P., Zhang T., Zhang H., Gu D., She M., Li H.
FEBS Lett. 582:4008-4014(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, UBIQUITINATION.
[12]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Integration of protein kinases mTOR and extracellular signal-regulated kinase 5 in regulating nucleocytoplasmic localization of NFATc4."
Yang T.T.C., Yu R.Y.L., Agadir A., Gao G.-J., Campos-Gonzalez R., Tournier C., Chow C.-W.
Mol. Cell. Biol. 28:3489-3501(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-168 AND SER-170.
[14]"The interleukin-1 receptor associated kinase 1 contributes to the regulation of NFAT."
Wang D., Fasciano S., Li L.
Mol. Immunol. 45:3902-3908(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IRAK1.
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Solution structure of the TIG domain from human nuclear factor of activated T-cells, cytoplasmic 4."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2008) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 585-691.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L41066 mRNA. Translation: AAA79175.1.
EU887632 mRNA. Translation: ACG55652.1.
EU887633 mRNA. Translation: ACG55653.1.
EU887634 mRNA. Translation: ACG55654.1.
EU887635 mRNA. Translation: ACG55655.1.
EU887636 mRNA. Translation: ACG55656.1.
EU887637 mRNA. Translation: ACG55657.1.
EU887638 mRNA. Translation: ACG55658.1.
EU887639 mRNA. Translation: ACG55659.1.
EU887640 mRNA. Translation: ACG55660.1.
EU887641 mRNA. Translation: ACG55661.1.
EU887642 mRNA. Translation: ACG55662.1.
EU887643 mRNA. Translation: ACG55663.1.
EU887644 mRNA. Translation: ACG55664.1.
EU887645 mRNA. Translation: ACG55665.1.
EU887646 mRNA. Translation: ACG55666.1.
EU887647 mRNA. Translation: ACG55667.1.
EU887648 mRNA. Translation: ACG55668.1.
EU887649 mRNA. Translation: ACG55669.1.
EU887650 mRNA. Translation: ACG55670.1.
EU887651 mRNA. Translation: ACG55671.1.
EU887652 mRNA. Translation: ACG55672.1.
EU887653 mRNA. Translation: ACG55673.1.
EU887654 mRNA. Translation: ACG55674.1.
EU887655 mRNA. Translation: ACG55675.1.
AK293185 mRNA. Translation: BAG56726.1.
AK302271 mRNA. Translation: BAG63617.1.
BC008857 mRNA. Translation: AAH08857.2.
BC053855 mRNA. Translation: AAH53855.1.
RefSeqNP_001129494.1. NM_001136022.2.
NP_001185894.1. NM_001198965.1.
NP_001185895.1. NM_001198966.2.
NP_001185896.1. NM_001198967.2.
NP_001275731.1. NM_001288802.1.
NP_004545.2. NM_004554.4.
UniGeneHs.77810.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YRPNMR-A585-691[»]
ProteinModelPortalQ14934.
SMRQ14934. Positions 405-691.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110849. 13 interactions.
IntActQ14934. 9 interactions.
MINTMINT-1535456.

PTM databases

PhosphoSiteQ14934.

Polymorphism databases

DMDM215274090.

Proteomic databases

PaxDbQ14934.
PRIDEQ14934.

Protocols and materials databases

DNASU4776.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250373; ENSP00000250373; ENSG00000100968. [Q14934-1]
ENST00000413692; ENSP00000388910; ENSG00000100968. [Q14934-3]
ENST00000422617; ENSP00000396788; ENSG00000100968. [Q14934-10]
ENST00000424781; ENSP00000388668; ENSG00000100968. [Q14934-7]
ENST00000539237; ENSP00000439350; ENSG00000100968. [Q14934-5]
ENST00000553469; ENSP00000451502; ENSG00000100968. [Q14934-14]
ENST00000553708; ENSP00000450590; ENSG00000100968. [Q14934-8]
ENST00000553879; ENSP00000452349; ENSG00000100968. [Q14934-12]
ENST00000554050; ENSP00000451151; ENSG00000100968. [Q14934-16]
ENST00000554344; ENSP00000450469; ENSG00000100968. [Q14934-12]
ENST00000554473; ENSP00000450810; ENSG00000100968. [Q14934-21]
ENST00000554591; ENSP00000452039; ENSG00000100968. [Q14934-11]
ENST00000554661; ENSP00000450733; ENSG00000100968. [Q14934-18]
ENST00000554966; ENSP00000450644; ENSG00000100968. [Q14934-15]
ENST00000555167; ENSP00000451395; ENSG00000100968. [Q14934-20]
ENST00000555393; ENSP00000451801; ENSG00000100968. [Q14934-23]
ENST00000555453; ENSP00000450686; ENSG00000100968. [Q14934-9]
ENST00000555590; ENSP00000451224; ENSG00000100968. [Q14934-6]
ENST00000555802; ENSP00000451590; ENSG00000100968. [Q14934-22]
ENST00000556169; ENSP00000451454; ENSG00000100968. [Q14934-17]
ENST00000556279; ENSP00000452270; ENSG00000100968. [Q14934-4]
ENST00000556759; ENSP00000451183; ENSG00000100968. [Q14934-19]
ENST00000557451; ENSP00000451284; ENSG00000100968. [Q14934-13]
ENST00000557767; ENSP00000451496; ENSG00000100968. [Q14934-24]
GeneID4776.
KEGGhsa:4776.
UCSCuc001wpc.3. human. [Q14934-1]
uc001wpd.3. human. [Q14934-19]
uc010alr.3. human. [Q14934-11]
uc010alt.3. human. [Q14934-5]
uc010alv.3. human. [Q14934-10]
uc010tok.2. human. [Q14934-3]
uc010tol.2. human. [Q14934-2]
uc010tom.2. human. [Q14934-7]
uc010ton.2. human. [Q14934-6]
uc010too.2. human. [Q14934-15]
uc010top.2. human. [Q14934-4]
uc010toq.2. human. [Q14934-14]
uc010tor.2. human. [Q14934-16]
uc010tot.2. human. [Q14934-9]
uc010tov.2. human. [Q14934-17]
uc010tow.2. human. [Q14934-18]
uc010tox.2. human. [Q14934-13]
uc010toy.2. human. [Q14934-21]
uc010toz.2. human. [Q14934-20]
uc010tpa.2. human. [Q14934-22]
uc010tpb.2. human. [Q14934-23]

Organism-specific databases

CTD4776.
GeneCardsGC14P024834.
HGNCHGNC:7778. NFATC4.
HPACAB032859.
HPA031641.
MIM602699. gene.
neXtProtNX_Q14934.
PharmGKBPA31584.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG70055.
HOVERGENHBG104364.
InParanoidQ14934.
KOK17334.
OMAWTPDDPW.
OrthoDBEOG79PJND.
PhylomeDBQ14934.
TreeFamTF326480.

Gene expression databases

ArrayExpressQ14934.
BgeeQ14934.
CleanExHS_NFATC4.
GenevestigatorQ14934.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR008366. NFAT.
IPR015647. NFAT1/4.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]
PANTHERPTHR12533. PTHR12533. 1 hit.
PTHR12533:SF5. PTHR12533:SF5. 1 hit.
PfamPF00554. RHD. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]
PRINTSPR01789. NUCFACTORATC.
SMARTSM00429. IPT. 1 hit.
[Graphical view]
SUPFAMSSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS50254. REL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ14934.
GeneWikiNFATC4.
GenomeRNAi4776.
NextBio18420.
PROQ14934.
SOURCESearch...

Entry information

Entry nameNFAC4_HUMAN
AccessionPrimary (citable) accession number: Q14934
Secondary accession number(s): B4DDG5 expand/collapse secondary AC list , 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
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM