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Q13469

- NFAC2_HUMAN

UniProt

Q13469 - NFAC2_HUMAN

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Protein
Nuclear factor of activated T-cells, cytoplasmic 2
Gene
NFATC2, NFAT1, NFATP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi421 – 4288

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. sequence-specific DNA binding Source: Ensembl
  4. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  5. transcription regulatory region DNA binding Source: Ensembl

GO - Biological processi

  1. B cell receptor signaling pathway Source: UniProtKB
  2. Fc-epsilon receptor signaling pathway Source: Reactome
  3. cell migration Source: UniProtKB
  4. cellular response to DNA damage stimulus Source: UniProtKB
  5. cytokine production Source: Ensembl
  6. innate immune response Source: Reactome
  7. positive regulation of B cell proliferation Source: UniProtKB
  8. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  9. positive regulation of transcription, DNA-templated Source: MGI
  10. regulation of transcription, DNA-templated Source: UniProtKB
  11. response to drug Source: UniProtKB
  12. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_163834. FCERI mediated Ca+2 mobilization.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:NFATC2
Synonyms:NFAT1, NFATP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:7776. NFATC2.

Subcellular locationi

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.

GO - Cellular componenti

  1. actin cytoskeleton Source: HPA
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
  6. plasma membrane Source: HPA
  7. ribonucleoprotein complex Source: Ensembl
  8. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31583.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 925925Nuclear factor of activated T-cells, cytoplasmic 2
PRO_0000205178Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei99 – 991Phosphoserine By similarity
Modified residuei148 – 1481Phosphoserine1 Publication
Modified residuei213 – 2131Phosphoserine By similarity
Modified residuei217 – 2171Phosphoserine By similarity
Modified residuei221 – 2211Phosphoserine By similarity
Modified residuei236 – 2361Phosphoserine By similarity
Modified residuei243 – 2431Phosphoserine By similarity
Modified residuei268 – 2681Phosphoserine By similarity
Modified residuei274 – 2741Phosphoserine By similarity
Modified residuei276 – 2761Phosphoserine By similarity
Modified residuei280 – 2801Phosphoserine By similarity
Modified residuei326 – 3261Phosphoserine By similarity
Modified residuei330 – 3301Phosphoserine2 Publications
Modified residuei363 – 3631Phosphoserine By similarity
Modified residuei755 – 7551Phosphoserine1 Publication
Modified residuei757 – 7571Phosphoserine1 Publication
Modified residuei759 – 7591Phosphoserine2 Publications
Modified residuei859 – 8591Phosphoserine1 Publication

Post-translational modificationi

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.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13469.
PaxDbiQ13469.
PRIDEiQ13469.

PTM databases

PhosphoSiteiQ13469.

Expressioni

Tissue specificityi

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.1 Publication

Inductioni

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.

Gene expression databases

ArrayExpressiQ13469.
BgeeiQ13469.
CleanExiHS_NFATC2.
GenevestigatoriQ13469.

Organism-specific databases

HPAiCAB018567.
HPA008789.
HPA024369.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRK2Q5S0073EBI-716258,EBI-5323863
USP22Q9UPT92EBI-716258,EBI-723510
VRK2Q86Y07-13EBI-716258,EBI-1207633
VRK2Q86Y07-24EBI-716258,EBI-1207636

Protein-protein interaction databases

BioGridi110846. 27 interactions.
DIPiDIP-27630N.
IntActiQ13469. 11 interactions.
MINTiMINT-1398456.
STRINGi9606.ENSP00000379330.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi397 – 3993
Beta strandi402 – 4054
Beta strandi408 – 4147
Beta strandi436 – 4394
Beta strandi442 – 4454
Beta strandi450 – 4523
Beta strandi454 – 4618
Beta strandi464 – 4663
Beta strandi474 – 4785
Beta strandi481 – 4833
Beta strandi490 – 4923
Beta strandi494 – 4963
Beta strandi498 – 5036
Helixi505 – 5073
Beta strandi510 – 5123
Beta strandi515 – 5206
Helixi523 – 5264
Beta strandi529 – 5313
Beta strandi541 – 55212
Turni553 – 5553
Beta strandi556 – 5638
Helixi571 – 5766
Beta strandi579 – 5846
Beta strandi586 – 5894
Beta strandi595 – 6028
Beta strandi608 – 6147
Beta strandi616 – 6183
Beta strandi620 – 6267
Turni630 – 6323
Beta strandi637 – 6415
Beta strandi646 – 6483
Beta strandi654 – 6629
Turni663 – 6653
Beta strandi671 – 6766

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ13469.
SMRiQ13469. Positions 396-678.

Miscellaneous databases

EvolutionaryTraceiQ13469.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati184 – 200171
Add
BLAST
Repeati213 – 229172
Add
BLAST
Repeati272 – 286153; approximate
Add
BLAST
Domaini392 – 574183RHD
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni111 – 1166Calcineurin-binding
Regioni119 – 19981Trans-activation domain A (TAD-A)
Add
BLAST
Regioni161 – 17515Required for cytoplasmic retention of the phosphorylated form By similarity
Add
BLAST
Regioni184 – 2861033 X approximate SP repeats
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi26 – 3499aaTAD
Motifi251 – 2533Nuclear localization signal
Motifi664 – 6663Nuclear localization signal
Motifi904 – 91310Nuclear export signal

Domaini

the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.1 Publication
Rel Similarity Domain (RSD) allows DNA-binding and cooperative interactions with AP1 factors By similarity.1 Publication

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG84065.
HOGENOMiHOG000231780.
HOVERGENiHBG069754.
InParanoidiQ13469.
KOiK17332.
OMAiMWKTSPD.
OrthoDBiEOG79PJND.
PhylomeDBiQ13469.
TreeFamiTF326480.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR008366. NFAT.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]
PANTHERiPTHR12533. PTHR12533. 1 hit.
PfamiPF00554. RHD. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]
PRINTSiPR01789. NUCFACTORATC.
SMARTiSM00429. IPT. 1 hit.
[Graphical view]
SUPFAMiSSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS50254. REL_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q13469-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MNAPERQPQP DGGDAPGHEP GGSPQDELDF SILFDYEYLN PNEEEPNAHK    50
VASPPSGPAY PDDVLDYGLK PYSPLASLSG EPPGRFGEPD RVGPQKFLSA 100
AKPAGASGLS PRIEITPSHE LIQAVGPLRM RDAGLLVEQP PLAGVAASPR 150
FTLPVPGFEG YREPLCLSPA SSGSSASFIS DTFSPYTSPC VSPNNGGPDD 200
LCPQFQNIPA HYSPRTSPIM SPRTSLAEDS CLGRHSPVPR PASRSSSPGA 250
KRRHSCAEAL VALPPGASPQ RSRSPSPQPS SHVAPQDHGS PAGYPPVAGS 300
AVIMDALNSL ATDSPCGIPP KMWKTSPDPS PVSAAPSKAG LPRHIYPAVE 350
FLGPCEQGER RNSAPESILL VPPTWPKPLV PAIPICSIPV TASLPPLEWP 400
LSSQSGSYEL RIEVQPKPHH RAHYETEGSR GAVKAPTGGH PVVQLHGYME 450
NKPLGLQIFI GTADERILKP HAFYQVHRIT GKTVTTTSYE KIVGNTKVLE 500
IPLEPKNNMR ATIDCAGILK LRNADIELRK GETDIGRKNT RVRLVFRVHI 550
PESSGRIVSL QTASNPIECS QRSAHELPMV ERQDTDSCLV YGGQQMILTG 600
QNFTSESKVV FTEKTTDGQQ IWEMEATVDK DKSQPNMLFV EIPEYRNKHI 650
RTPVKVNFYV INGKRKRSQP QHFTYHPVPA IKTEPTDEYD PTLICSPTHG 700
GLGSQPYYPQ HPMVAESPSC LVATMAPCQQ FRTGLSSPDA RYQQQNPAAV 750
LYQRSKSLSP SLLGYQQPAL MAAPLSLADA HRSVLVHAGS QGQSSALLHP 800
SPTNQQASPV IHYSPTNQQL RCGSHQEFQH IMYCENFAPG TTRPGPPPVS 850
QGQRLSPGSY PTVIQQQNAT SQRAAKNGPP VSDQKEVLPA GVTIKQEQNL 900
DQTYLDDVNE IIRKEFSGPP ARNQT 925
Length:925
Mass (Da):100,146
Last modified:July 5, 2005 - v2
Checksum:i8DAE86855CCB58D3
GO
Isoform 2 (identifier: Q13469-2) [UniParc]FASTAAdd to Basket

Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     908-925: VNEIIRKEFSGPPARNQT → ELIDTHLSWIQNIL

Show »
Length:921
Mass (Da):99,784
Checksum:i71C45C9B348AE9C8
GO
Isoform 3 (identifier: Q13469-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:901
Mass (Da):97,693
Checksum:i158B2F7F9966CCBA
GO
Isoform 4 (identifier: Q13469-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:905
Mass (Da):98,054
Checksum:i69D7F7B758842B37
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti446 – 4461H → R.
Corresponds to variant rs12479626 [ dbSNP | Ensembl ].
VAR_051783

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4343MNAPE…LNPNE → MQREAAFRLGHCHPLRIMGS VDQ in isoform 3 and isoform 4.
VSP_042757Add
BLAST
Alternative sequencei908 – 92518VNEII…ARNQT → ELIDTHLSWIQNIL in isoform 2 and isoform 3.
VSP_005595Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651L → M in AAC50886. 1 Publication
Sequence conflicti65 – 651L → M in AAC50887. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13437.1. [Q13469-1]
CCDS33488.1. [Q13469-2]
CCDS46614.1. [Q13469-3]
CCDS68157.1. [Q13469-4]
PIRiG02326.
RefSeqiNP_001129493.1. NM_001136021.2. [Q13469-3]
NP_001245221.1. NM_001258292.1. [Q13469-4]
NP_036472.2. NM_012340.4. [Q13469-2]
NP_775114.1. NM_173091.3. [Q13469-1]
UniGeneiHs.744148.

Genome annotation databases

EnsembliENST00000371564; ENSP00000360619; ENSG00000101096. [Q13469-2]
ENST00000396009; ENSP00000379330; ENSG00000101096. [Q13469-1]
ENST00000414705; ENSP00000396471; ENSG00000101096. [Q13469-3]
ENST00000609943; ENSP00000477370; ENSG00000101096.
GeneIDi4773.
KEGGihsa:4773.
UCSCiuc002xwc.4. human. [Q13469-2]
uc002xwd.4. human. [Q13469-1]
uc010zyx.3. human. [Q13469-3]

Polymorphism databases

DMDMi68846905.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS13437.1. [Q13469-1 ]
CCDS33488.1. [Q13469-2 ]
CCDS46614.1. [Q13469-3 ]
CCDS68157.1. [Q13469-4 ]
PIRi G02326.
RefSeqi NP_001129493.1. NM_001136021.2. [Q13469-3 ]
NP_001245221.1. NM_001258292.1. [Q13469-4 ]
NP_036472.2. NM_012340.4. [Q13469-2 ]
NP_775114.1. NM_173091.3. [Q13469-1 ]
UniGenei Hs.744148.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A02 X-ray 2.70 N 392-678 [» ]
1OWR X-ray 3.00 M/N/P/Q 396-678 [» ]
1P7H X-ray 2.60 L/M/N/O 393-678 [» ]
1PZU X-ray 3.10 B/D/H/I/L/M 396-678 [» ]
1S9K X-ray 3.10 C 399-678 [» ]
2AS5 X-ray 2.70 M/N 392-678 [» ]
2O93 X-ray 3.05 L/M/O 396-678 [» ]
3QRF X-ray 2.80 M/N 396-678 [» ]
ProteinModelPortali Q13469.
SMRi Q13469. Positions 396-678.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110846. 27 interactions.
DIPi DIP-27630N.
IntActi Q13469. 11 interactions.
MINTi MINT-1398456.
STRINGi 9606.ENSP00000379330.

Chemistry

BindingDBi Q13469.

PTM databases

PhosphoSitei Q13469.

Polymorphism databases

DMDMi 68846905.

Proteomic databases

MaxQBi Q13469.
PaxDbi Q13469.
PRIDEi Q13469.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371564 ; ENSP00000360619 ; ENSG00000101096 . [Q13469-2 ]
ENST00000396009 ; ENSP00000379330 ; ENSG00000101096 . [Q13469-1 ]
ENST00000414705 ; ENSP00000396471 ; ENSG00000101096 . [Q13469-3 ]
ENST00000609943 ; ENSP00000477370 ; ENSG00000101096 .
GeneIDi 4773.
KEGGi hsa:4773.
UCSCi uc002xwc.4. human. [Q13469-2 ]
uc002xwd.4. human. [Q13469-1 ]
uc010zyx.3. human. [Q13469-3 ]

Organism-specific databases

CTDi 4773.
GeneCardsi GC20M050003.
HGNCi HGNC:7776. NFATC2.
HPAi CAB018567.
HPA008789.
HPA024369.
MIMi 600490. gene.
neXtProti NX_Q13469.
PharmGKBi PA31583.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG84065.
HOGENOMi HOG000231780.
HOVERGENi HBG069754.
InParanoidi Q13469.
KOi K17332.
OMAi MWKTSPD.
OrthoDBi EOG79PJND.
PhylomeDBi Q13469.
TreeFami TF326480.

Enzyme and pathway databases

Reactomei REACT_163834. FCERI mediated Ca+2 mobilization.

Miscellaneous databases

EvolutionaryTracei Q13469.
GeneWikii NFATC2.
GenomeRNAii 4773.
NextBioi 18400.
PROi Q13469.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13469.
Bgeei Q13469.
CleanExi HS_NFATC2.
Genevestigatori Q13469.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProi IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR008366. NFAT.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view ]
PANTHERi PTHR12533. PTHR12533. 1 hit.
Pfami PF00554. RHD. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view ]
PRINTSi PR01789. NUCFACTORATC.
SMARTi SM00429. IPT. 1 hit.
[Graphical view ]
SUPFAMi SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS50254. REL_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiNFAC2_HUMAN
AccessioniPrimary (citable) accession number: Q13469
Secondary accession number(s): B5B2N8
, B5B2N9, B5B2P2, B5B2P3, Q13468, Q5TFW7, Q5TFW8, Q9NPX6, Q9NQH3, Q9UJR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 5, 2005
Last modified: September 3, 2014
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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