Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q13469 (NFAC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 166. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear factor of activated T-cells, cytoplasmic 2

Short name=NF-ATc2
Short name=NFATc2
Alternative name(s):
NFAT pre-existing subunit
Short name=NF-ATp
T-cell transcription factor NFAT1
Gene names
Name:NFATC2
Synonyms:NFAT1, NFATP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length925 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, IL-3, IL-4, TNF-alpha or GM-CSF. Promotes invasive migration through the activation of GPC6 expression and WNT5A signaling pathway. Ref.11

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. The phosphorylated form specifically interacts with XPO1; which mediates nuclear export. NFATC proteins bind to DNA as monomers. Interacts with NFATC2IP By similarity.

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.

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. Ref.1

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. Ref.8

Rel Similarity Domain (RSD) allows DNA-binding and cooperative interactions with AP1 factors By similarity. Ref.8

Post-translational modification

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.

Sequence similarities

Contains 1 RHD (Rel-like) domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell receptor signaling pathway

Inferred from mutant phenotype PubMed 17875758. Source: UniProtKB

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

cell migration

Inferred from direct assay Ref.11. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from mutant phenotype PubMed 17875758. Source: UniProtKB

cytokine production

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

positive regulation of B cell proliferation

Inferred from mutant phenotype PubMed 17875758. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15790681. Source: MGI

regulation of transcription, DNA-templated

Traceable author statement Ref.1. Source: UniProtKB

response to drug

Inferred from mutant phenotype PubMed 17875758. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentactin cytoskeleton

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay PubMed 12656674. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 12656674. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

ribonucleoprotein complex

Inferred from electronic annotation. Source: Ensembl

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Traceable author statement Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16873067PubMed 19505873. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.1. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q13469-1)

Also known as: C; NFATc2_IB_IIL;

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: Q13469-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     908-925: VNEIIRKEFSGPPARNQT → ELIDTHLSWIQNIL
Isoform 3 (identifier: Q13469-3)

Also known as: NFATc2_IA_IIL;

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: MNAPERQPQPDGGDAPGHEPGGSPQDELDFSILFDYEYLNPNE → MQREAAFRLGHCHPLRIMGSVDQ
     908-925: VNEIIRKEFSGPPARNQT → ELIDTHLSWIQNIL
Isoform 4 (identifier: Q13469-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: MNAPERQPQPDGGDAPGHEPGGSPQDELDFSILFDYEYLNPNE → MQREAAFRLGHCHPLRIMGSVDQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 925925Nuclear factor of activated T-cells, cytoplasmic 2
PRO_0000205178

Regions

Repeat184 – 200171
Repeat213 – 229172
Repeat272 – 286153; approximate
Domain392 – 574183RHD
DNA binding421 – 4288
Region111 – 1166Calcineurin-binding
Region119 – 19981Trans-activation domain A (TAD-A)
Region161 – 17515Required for cytoplasmic retention of the phosphorylated form By similarity
Region184 – 2861033 X approximate SP repeats
Motif26 – 3499aaTAD
Motif251 – 2533Nuclear localization signal
Motif664 – 6663Nuclear localization signal
Motif904 – 91310Nuclear export signal

Amino acid modifications

Modified residue991Phosphoserine By similarity
Modified residue1481Phosphoserine Ref.9
Modified residue2131Phosphoserine By similarity
Modified residue2171Phosphoserine By similarity
Modified residue2211Phosphoserine By similarity
Modified residue2361Phosphoserine By similarity
Modified residue2431Phosphoserine By similarity
Modified residue2681Phosphoserine By similarity
Modified residue2741Phosphoserine By similarity
Modified residue2761Phosphoserine By similarity
Modified residue2801Phosphoserine By similarity
Modified residue3261Phosphoserine By similarity
Modified residue3301Phosphoserine Ref.7 Ref.9
Modified residue3631Phosphoserine By similarity
Modified residue7551Phosphoserine Ref.9
Modified residue7571Phosphoserine Ref.10
Modified residue7591Phosphoserine Ref.9 Ref.10
Modified residue8591Phosphoserine Ref.9

Natural variations

Alternative sequence1 – 4343MNAPE…LNPNE → MQREAAFRLGHCHPLRIMGS VDQ in isoform 3 and isoform 4.
VSP_042757
Alternative sequence908 – 92518VNEII…ARNQT → ELIDTHLSWIQNIL in isoform 2 and isoform 3.
VSP_005595
Natural variant4461H → R.
Corresponds to variant rs12479626 [ dbSNP | Ensembl ].
VAR_051783

Experimental info

Sequence conflict651L → M in AAC50886. Ref.1
Sequence conflict651L → M in AAC50887. Ref.1

Secondary structure

.................................................................. 925
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (C) (NFATc2_IB_IIL) [UniParc].

Last modified July 5, 2005. Version 2.
Checksum: 8DAE86855CCB58D3

FASTA925100,146
        10         20         30         40         50         60 
MNAPERQPQP DGGDAPGHEP GGSPQDELDF SILFDYEYLN PNEEEPNAHK VASPPSGPAY 

        70         80         90        100        110        120 
PDDVLDYGLK PYSPLASLSG EPPGRFGEPD RVGPQKFLSA AKPAGASGLS PRIEITPSHE 

       130        140        150        160        170        180 
LIQAVGPLRM RDAGLLVEQP PLAGVAASPR FTLPVPGFEG YREPLCLSPA SSGSSASFIS 

       190        200        210        220        230        240 
DTFSPYTSPC VSPNNGGPDD LCPQFQNIPA HYSPRTSPIM SPRTSLAEDS CLGRHSPVPR 

       250        260        270        280        290        300 
PASRSSSPGA KRRHSCAEAL VALPPGASPQ RSRSPSPQPS SHVAPQDHGS PAGYPPVAGS 

       310        320        330        340        350        360 
AVIMDALNSL ATDSPCGIPP KMWKTSPDPS PVSAAPSKAG LPRHIYPAVE FLGPCEQGER 

       370        380        390        400        410        420 
RNSAPESILL VPPTWPKPLV PAIPICSIPV TASLPPLEWP LSSQSGSYEL RIEVQPKPHH 

       430        440        450        460        470        480 
RAHYETEGSR GAVKAPTGGH PVVQLHGYME NKPLGLQIFI GTADERILKP HAFYQVHRIT 

       490        500        510        520        530        540 
GKTVTTTSYE KIVGNTKVLE IPLEPKNNMR ATIDCAGILK LRNADIELRK GETDIGRKNT 

       550        560        570        580        590        600 
RVRLVFRVHI PESSGRIVSL QTASNPIECS QRSAHELPMV ERQDTDSCLV YGGQQMILTG 

       610        620        630        640        650        660 
QNFTSESKVV FTEKTTDGQQ IWEMEATVDK DKSQPNMLFV EIPEYRNKHI RTPVKVNFYV 

       670        680        690        700        710        720 
INGKRKRSQP QHFTYHPVPA IKTEPTDEYD PTLICSPTHG GLGSQPYYPQ HPMVAESPSC 

       730        740        750        760        770        780 
LVATMAPCQQ FRTGLSSPDA RYQQQNPAAV LYQRSKSLSP SLLGYQQPAL MAAPLSLADA 

       790        800        810        820        830        840 
HRSVLVHAGS QGQSSALLHP SPTNQQASPV IHYSPTNQQL RCGSHQEFQH IMYCENFAPG 

       850        860        870        880        890        900 
TTRPGPPPVS QGQRLSPGSY PTVIQQQNAT SQRAAKNGPP VSDQKEVLPA GVTIKQEQNL 

       910        920 
DQTYLDDVNE IIRKEFSGPP ARNQT 

« Hide

Isoform 2 (B) [UniParc].

Checksum: 71C45C9B348AE9C8
Show »

FASTA92199,784
Isoform 3 (NFATc2_IA_IIL) [UniParc].

Checksum: 158B2F7F9966CCBA
Show »

FASTA90197,693
Isoform 4 [UniParc].

Checksum: 69D7F7B758842B37
Show »

FASTA90598,054

References

« Hide 'large scale' references
[1]"Recombinant NFAT1 (NFATp) is regulated by calcineurin in T cells and mediates transcription of several cytokine genes."
Luo C., Burgeon E., Carew J.A., McCaffrey P.G., Badalian T.M., Lane W.S., Hogan P.G., Rao A.
Mol. Cell. Biol. 16:3955-3966(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[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 AND 4), ALTERNATIVE SPLICING.
[3]"The DNA sequence and comparative analysis of human chromosome 20."
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. expand/collapse author list , 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.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS 1 AND 2).
[6]"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.
[7]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"Nine-amino-acid transactivation domain: establishment and prediction utilities."
Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M.
Genomics 89:756-768(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN.
[9]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-330; SER-755; SER-759 AND SER-859, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-757 AND SER-759, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"NFAT promotes carcinoma invasive migration through glypican-6."
Yiu G.K., Kaunisto A., Chin Y.R., Toker A.
Biochem. J. 440:157-166(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U43341 mRNA. Translation: AAC50886.1.
U43342 mRNA. Translation: AAC50887.1.
EU887573 mRNA. Translation: ACG55593.1.
EU887574 mRNA. Translation: ACG55594.1.
EU887577 mRNA. Translation: ACG55597.1.
EU887578 mRNA. Translation: ACG55598.1.
AL132866 Genomic DNA. Translation: CAC00528.2.
AL035682, AL035684, AL132866 Genomic DNA. Translation: CAI18852.1.
AL035682, AL035684, AL132866 Genomic DNA. Translation: CAI18853.1.
AL035684, AL035682, AL132866 Genomic DNA. Translation: CAI19205.1.
AL035684, AL035682, AL132866 Genomic DNA. Translation: CAI19206.1.
AL132866, AL035682, AL035684 Genomic DNA. Translation: CAI23549.1.
CH471077 Genomic DNA. Translation: EAW75602.1.
CH471077 Genomic DNA. Translation: EAW75603.1.
BC136418 mRNA. Translation: AAI36419.1.
BC144074 mRNA. Translation: AAI44075.1.
CCDSCCDS13437.1. [Q13469-1]
CCDS33488.1. [Q13469-2]
CCDS46614.1. [Q13469-3]
PIRG02326.
RefSeqNP_001129493.1. NM_001136021.2. [Q13469-3]
NP_001245221.1. NM_001258292.1.
NP_036472.2. NM_012340.4. [Q13469-2]
NP_775114.1. NM_173091.3. [Q13469-1]
UniGeneHs.744148.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A02X-ray2.70N392-678[»]
1OWRX-ray3.00M/N/P/Q396-678[»]
1P7HX-ray2.60L/M/N/O393-678[»]
1PZUX-ray3.10B/D/H/I/L/M396-678[»]
1S9KX-ray3.10C399-678[»]
2AS5X-ray2.70M/N392-678[»]
2O93X-ray3.05L/M/O396-678[»]
3QRFX-ray2.80M/N396-678[»]
ProteinModelPortalQ13469.
SMRQ13469. Positions 396-678.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110846. 25 interactions.
DIPDIP-27630N.
IntActQ13469. 11 interactions.
MINTMINT-1398456.
STRING9606.ENSP00000379330.

Chemistry

BindingDBQ13469.

PTM databases

PhosphoSiteQ13469.

Polymorphism databases

DMDM68846905.

Proteomic databases

MaxQBQ13469.
PaxDbQ13469.
PRIDEQ13469.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371564; ENSP00000360619; ENSG00000101096. [Q13469-2]
ENST00000396009; ENSP00000379330; ENSG00000101096. [Q13469-1]
ENST00000414705; ENSP00000396471; ENSG00000101096. [Q13469-3]
ENST00000609943; ENSP00000477370; ENSG00000101096.
GeneID4773.
KEGGhsa:4773.
UCSCuc002xwc.4. human. [Q13469-2]
uc002xwd.4. human. [Q13469-1]
uc010zyx.3. human. [Q13469-3]

Organism-specific databases

CTD4773.
GeneCardsGC20M050003.
HGNCHGNC:7776. NFATC2.
HPACAB018567.
HPA008789.
HPA024369.
MIM600490. gene.
neXtProtNX_Q13469.
PharmGKBPA31583.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG84065.
HOGENOMHOG000231780.
HOVERGENHBG069754.
InParanoidQ13469.
KOK17332.
OMAMWKTSPD.
OrthoDBEOG79PJND.
PhylomeDBQ13469.
TreeFamTF326480.

Enzyme and pathway databases

ReactomeREACT_118664. Calcineurin dephosphorylates NFATC1,2,3.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ13469.
BgeeQ13469.
CleanExHS_NFATC2.
GenevestigatorQ13469.

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.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]
PANTHERPTHR12533. PTHR12533. 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

EvolutionaryTraceQ13469.
GeneWikiNFATC2.
GenomeRNAi4773.
NextBio18400.
PROQ13469.
SOURCESearch...

Entry information

Entry nameNFAC2_HUMAN
AccessionPrimary (citable) accession number: Q13469
Secondary accession number(s): B5B2N8 expand/collapse secondary AC list , B5B2N9, B5B2P2, B5B2P3, Q13468, Q5TFW7, Q5TFW8, Q9NPX6, Q9NQH3, Q9UJR2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 5, 2005
Last modified: July 9, 2014
This is version 166 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 20

Human chromosome 20: entries, gene names and cross-references to MIM