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Protein

Nuclear factor of activated T-cells, cytoplasmic 2

Gene

Nfatc2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi423 – 4308

GO - Molecular functioni

  1. chromatin binding Source: MGI
  2. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  3. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: NTNU_SB
  4. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
  5. sequence-specific DNA binding Source: MGI
  6. sequence-specific DNA binding transcription factor activity Source: MGI
  7. transcription factor binding Source: MGI
  8. transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  1. B cell receptor signaling pathway Source: MGI
  2. calcineurin-NFAT signaling cascade Source: MGI
  3. cell migration Source: UniProtKB
  4. cellular response to DNA damage stimulus Source: MGI
  5. cytokine production Source: MGI
  6. myotube cell development Source: MGI
  7. negative regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  8. positive regulation of B cell proliferation Source: MGI
  9. positive regulation of gene expression Source: UniProtKB
  10. positive regulation of myoblast fusion Source: MGI
  11. positive regulation of transcription, DNA-templated Source: MGI
  12. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  13. response to drug Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_348733. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:102463. Nfatc2.

Subcellular locationi

  1. Cytoplasm 1 Publication
  2. Nucleus 1 Publication

  3. 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: MGI
  2. cytoplasm Source: MGI
  3. cytosol Source: MGI
  4. nuclear transcription factor complex Source: MGI
  5. nucleoplasm Source: MGI
  6. nucleus Source: UniProtKB
  7. plasma membrane Source: MGI
  8. ribonucleoprotein complex Source: MGI
  9. transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi112 – 1121R → A: Lowers dephosphorylation. 1 Publication
Mutagenesisi114 – 1141E → A: Lowers dephosphorylation. 1 Publication
Mutagenesisi116 – 1161T → A: No dephosphorylation. 1 Publication
Mutagenesisi164 – 1641R → A: Induces aberrant nuclear localization of the phosphorylated form. 1 Publication
Mutagenesisi423 – 4231R → A: Decrease in binding to DNA. 1 Publication
Mutagenesisi425 – 4251H → A: No change in binding to DNA. 1 Publication
Mutagenesisi426 – 4261Y → A: Decrease in binding to DNA. 1 Publication
Mutagenesisi428 – 4281T → A: No change in binding to DNA. 1 Publication
Mutagenesisi428 – 4281T → C: No change in binding to DNA and confers DNA-binding sensitivity to sulfhydryl modifications. 1 Publication
Mutagenesisi429 – 4291E → A: Decrease in binding to DNA. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 927927Nuclear factor of activated T-cells, cytoplasmic 2PRO_0000205179Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231PhosphoserineBy similarity
Modified residuei53 – 531PhosphoserineCurated
Modified residuei54 – 541PhosphoserineCurated
Modified residuei56 – 561PhosphoserineCurated
Modified residuei99 – 991Phosphoserine1 Publication
Modified residuei136 – 1361Phosphoserine1 Publication
Modified residuei150 – 1501PhosphoserineBy similarity
Modified residuei170 – 1701Phosphoserine1 Publication
Modified residuei173 – 1731Phosphoserine1 Publication
Modified residuei174 – 1741Phosphoserine1 Publication
Modified residuei176 – 1761Phosphoserine1 Publication
Modified residuei177 – 1771Phosphoserine1 Publication
Modified residuei179 – 1791Phosphoserine1 Publication
Modified residuei182 – 1821Phosphoserine1 Publication
Modified residuei215 – 2151Phosphoserine1 Publication
Modified residuei219 – 2191Phosphoserine1 Publication
Modified residuei223 – 2231Phosphoserine1 Publication
Modified residuei238 – 2381Phosphoserine1 Publication
Modified residuei245 – 2451Phosphoserine1 Publication
Modified residuei270 – 2701Phosphoserine1 Publication
Modified residuei276 – 2761Phosphoserine1 Publication
Modified residuei278 – 2781Phosphoserine1 Publication
Modified residuei282 – 2821Phosphoserine1 Publication
Modified residuei328 – 3281Phosphoserine1 Publication
Modified residuei365 – 3651Phosphoserine1 Publication
Modified residuei757 – 7571PhosphoserineBy similarity
Modified residuei759 – 7591PhosphoserineBy similarity
Modified residuei761 – 7611PhosphoserineBy similarity

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ60591.

PTM databases

PhosphoSiteiQ60591.

Expressioni

Tissue specificityi

Expressed in thymus, spleen, heart, testis, brain, placenta, muscle and pancreas.1 Publication

Gene expression databases

BgeeiQ60591.
ExpressionAtlasiQ60591. baseline and differential.
GenevestigatoriQ60591.

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. Interacts with FOXP3 (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
VRK2Q86Y07-12EBI-643104,EBI-1207633From a different organism.

Protein-protein interaction databases

BioGridi201739. 1 interaction.
DIPiDIP-49476N.
IntActiQ60591. 9 interactions.
MINTiMINT-1565857.

Structurei

3D structure databases

ProteinModelPortaliQ60591.
SMRiQ60591. Positions 398-680.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati186 – 202171Add
BLAST
Repeati215 – 231172Add
BLAST
Repeati274 – 290173; approximateAdd
BLAST
Domaini394 – 576183RHDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni111 – 1166Calcineurin-binding
Regioni119 – 20183Trans-activation domain A (TAD-A)Add
BLAST
Regioni163 – 17715Required for cytoplasmic retention of the phosphorylated formAdd
BLAST
Regioni186 – 2921073 X approximate SP repeatsAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi253 – 2553Nuclear localization signal

Domaini

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

Sequence similaritiesi

Contains 1 RHD (Rel-like) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG84065.
GeneTreeiENSGT00550000074562.
HOVERGENiHBG069754.
InParanoidiQ60591.
KOiK17332.
OMAiEYLFEYE.
OrthoDBiEOG79PJND.
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. AlignAdd to basket

Isoform C (identifier: Q60591-3) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MDVPEPQPDP DGGDGPGHEP GGSPQDELDF SILFDYDYLN PIEEEPIAHK
60 70 80 90 100
AISSPSGLAY PDDVLDYGLK PCNPLASLSG EPPGRFGEPD SIGFQNFLSP
110 120 130 140 150
VKPAGASGPS PRIEITPSHE LMQAGGALRG RDAGLSPEQP ALALAGVAAS
160 170 180 190 200
PRFTLPVPGY EGYREPLCLS PASSGSSASF ISDTFSPYTS PCVSPNNAGP
210 220 230 240 250
DDLCPQFQNI PAHYSPRTSP IMSPRTSLAE DSCLGRHSPV PRPASRSSSP
260 270 280 290 300
GAKRRHSCAE ALVAPLPAAS PQRSRSPSPQ PSPHVALQDD SIPAGYPPTA
310 320 330 340 350
GSAVLMDALN TLATDSPCGI PSKIWKTSPD PTPVSTAPSK AGLARHIYPT
360 370 380 390 400
VEFLGPCEQE ERRNSAPESI LLVPPTWPKQ LVPAIPICSI PVTASLPPLE
410 420 430 440 450
WPLSNQSGSY ELRIEVQPKP HHRAHYETEG SRGAVKAPTG GHPVVQLHGY
460 470 480 490 500
MENKPLGLQI FIGTADERIL KPHAFYQVHR ITGKTVTTTS YEKIVGNTKV
510 520 530 540 550
LEIPLEPKNN MRATIDCAGI LKLRNADIEL RKGETDIGRK NTRVRLVFRV
560 570 580 590 600
HVPEPSGRIV SLQAASNPIE CSQRSAHELP MVERQDMDSC LVYGGQQMIL
610 620 630 640 650
TGQNFTAESK VVFMEKTTDG QQIWEMEATV DKDKSQPNML FVEIPEYRNK
660 670 680 690 700
HIRVPVKVNF YVINGKRKRS QPQHFTYHPV PAIKTEPSDE YEPSLICSPA
710 720 730 740 750
HGGLGSQPYY PQHPMLAESP SCLVATMAPC QQFRSGLSSP DARYQQQSPA
760 770 780 790 800
AALYQRSKSL SPGLLGYQQP SLLAAPLGLA DAHRSVLVHA GSQGQGQGST
810 820 830 840 850
LPHTSSASQQ ASPVIHYSPT NQQLRGGGHQ EFQHIMYCEN FGPSSARPGP
860 870 880 890 900
PPINQGQRLS PGAYPTVIQQ QTAPSQRAAK NGPSDQKEAL PTGVTVKQEQ
910 920
NLDQTYLDDV NEIIRKEFSG PPSRNQT
Length:927
Mass (Da):100,020
Last modified:July 27, 2011 - v3
Checksum:iF21E7BABE7DBB40F
GO
Isoform B (identifier: Q60591-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     910-927: VNEIIRKEFSGPPSRNQT → ELIDTHLSWIQNIL

Show »
Length:923
Mass (Da):99,642
Checksum:iA2B4B0476A75A83D
GO
Isoform D (identifier: Q60591-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     619-806: DGQQIWEMEA...QGSTLPHTSS → GPAGTCETRP...PGSSLVLLAL

Show »
Length:794
Mass (Da):85,181
Checksum:i1A8246FF98E219B8
GO
Isoform A (identifier: Q60591-1)

Sequence is not available

Note: Ref.2 (AAC52929) sequence is a chimeric cDNA.

Length:
Mass (Da):

Sequence cautioni

The sequence AAC52929.1 differs from that shown.Chimeric cDNA fused with Phyhd1 (Lrrc8a).Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 781L → P in AAK49895 (PubMed:11278367).Curated
Sequence conflicti287 – 2871L → P in AAC52929 (PubMed:8668213).Curated
Sequence conflicti287 – 2871L → P in AAC52930 (PubMed:8668213).Curated
Sequence conflicti287 – 2871L → P in AAC52931 (PubMed:8668213).Curated
Sequence conflicti802 – 8021P → R in AAC52929 (PubMed:8668213).Curated
Sequence conflicti802 – 8021P → R in AAC52930 (PubMed:8668213).Curated
Sequence conflicti802 – 8021P → R in AAC52931 (PubMed:8668213).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei619 – 806188DGQQI…PHTSS → GPAGTCETRPLPISLISADR LSPWLSRLQRNPPGSVFRCS VLLPAPGSSLVLLAL in isoform D. 1 PublicationVSP_005597Add
BLAST
Alternative sequencei910 – 92718VNEII…SRNQT → ELIDTHLSWIQNIL in isoform B. 1 PublicationVSP_005596Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02079 mRNA. Translation: AAC52929.1. Sequence problems.
U36575 mRNA. Translation: AAC52930.1.
U36576 mRNA. Translation: AAC52931.1.
AF289078 mRNA. Translation: AAK49895.1.
EU887588 mRNA. Translation: ACG55608.1.
AL840639, AL844575 Genomic DNA. Translation: CAM15662.1.
AL840639, AL844575 Genomic DNA. Translation: CAM15663.1.
AL844575 Genomic DNA. Translation: CAM15669.1.
AL844575, AL840639 Genomic DNA. Translation: CAM15670.1.
AL844575, AL840639 Genomic DNA. Translation: CAM15671.1.
CCDSiCCDS17112.1. [Q60591-3]
CCDS50803.1. [Q60591-2]
PIRiA48753.
RefSeqiNP_035029.2. NM_010899.3. [Q60591-3]
UniGeneiMm.116802.

Genome annotation databases

EnsembliENSMUST00000074618; ENSMUSP00000074198; ENSMUSG00000027544. [Q60591-3]
ENSMUST00000109184; ENSMUSP00000104812; ENSMUSG00000027544. [Q60591-2]
GeneIDi18019.
KEGGimmu:18019.
UCSCiuc008oau.1. mouse. [Q60591-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02079 mRNA. Translation: AAC52929.1. Sequence problems.
U36575 mRNA. Translation: AAC52930.1.
U36576 mRNA. Translation: AAC52931.1.
AF289078 mRNA. Translation: AAK49895.1.
EU887588 mRNA. Translation: ACG55608.1.
AL840639, AL844575 Genomic DNA. Translation: CAM15662.1.
AL840639, AL844575 Genomic DNA. Translation: CAM15663.1.
AL844575 Genomic DNA. Translation: CAM15669.1.
AL844575, AL840639 Genomic DNA. Translation: CAM15670.1.
AL844575, AL840639 Genomic DNA. Translation: CAM15671.1.
CCDSiCCDS17112.1. [Q60591-3]
CCDS50803.1. [Q60591-2]
PIRiA48753.
RefSeqiNP_035029.2. NM_010899.3. [Q60591-3]
UniGeneiMm.116802.

3D structure databases

ProteinModelPortaliQ60591.
SMRiQ60591. Positions 398-680.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201739. 1 interaction.
DIPiDIP-49476N.
IntActiQ60591. 9 interactions.
MINTiMINT-1565857.

PTM databases

PhosphoSiteiQ60591.

Proteomic databases

PRIDEiQ60591.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000074618; ENSMUSP00000074198; ENSMUSG00000027544. [Q60591-3]
ENSMUST00000109184; ENSMUSP00000104812; ENSMUSG00000027544. [Q60591-2]
GeneIDi18019.
KEGGimmu:18019.
UCSCiuc008oau.1. mouse. [Q60591-3]

Organism-specific databases

CTDi4773.
MGIiMGI:102463. Nfatc2.

Phylogenomic databases

eggNOGiNOG84065.
GeneTreeiENSGT00550000074562.
HOVERGENiHBG069754.
InParanoidiQ60591.
KOiK17332.
OMAiEYLFEYE.
OrthoDBiEOG79PJND.
TreeFamiTF326480.

Enzyme and pathway databases

ReactomeiREACT_348733. FCERI mediated Ca+2 mobilization.

Miscellaneous databases

ChiTaRSiNfatc2. mouse.
NextBioi293063.
PROiQ60591.
SOURCEiSearch...

Gene expression databases

BgeeiQ60591.
ExpressionAtlasiQ60591. baseline and differential.
GenevestigatoriQ60591.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE (ISOFORM A).
  2. "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 A; B AND C).
  3. "Identification and characterization of a novel nuclear factor of activated T-cells-1 isoform expressed in mouse brain."
    Plyte S., Boncristiano M., Fattori E., Galvagni F., Paccani S.R., Majolini M.B., Oliviero S., Ciliberto G., Telford J.L., Baldari C.T.
    J. Biol. Chem. 276:14350-14358(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D).
    Strain: C57BL/6.
    Tissue: Brain.
  4. "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] (ISOFORM C), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    Strain: C57BL/6.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "A similar DNA-binding motif in NFAT family proteins and the Rel homology region."
    Jain J., Burgeon E., Badalian T.M., Hogan P.G., Rao A.
    J. Biol. Chem. 270:4138-4145(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-423; HIS-425; TYR-426; THR-428 AND GLU-429.
  7. "NF-AT-driven interleukin-4 transcription potentiated by NIP45."
    Hodge M.R., Chun H.J., Rengarajan J., Alt A., Lieberson R., Glimcher L.H.
    Science 274:1903-1905(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFATC2IP.
  8. "Selective inhibition of NFAT activation by a peptide spanning the calcineurin targeting site of NFAT."
    Aramburu J., Garcia-Cozar F., Raghavan A., Okamura H., Rao A., Hogan P.G.
    Mol. Cell 1:627-637(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-112; GLU-114 AND THR-116.
  9. "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.
  10. "Concerted dephosphorylation of the transcription factor NFAT1 induces a conformational switch that regulates transcriptional activity."
    Okamura H., Aramburu J., Garcia-Rodriguez C., Viola J.P.B., Raghavan A., Tahiliani M., Zhang X., Qin J., Hogan P.G., Rao A.
    Mol. Cell 6:539-550(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-99; SER-136; SER-170; SER-173; SER-174; SER-176; SER-177; SER-179; SER-182; SER-215; SER-219; SER-223; SER-238; SER-245; SER-270; SER-276; SER-278; SER-282; SER-328 AND SER-365, SUBCELLULAR LOCATION, INTERACTION WITH XPO1, MUTAGENESIS OF ARG-164, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiNFAC2_MOUSE
AccessioniPrimary (citable) accession number: Q60591
Secondary accession number(s): A2APK2
, A2APK3, A2AQC5, A2AQC6, A2AQC7, B5B2Q3, Q60984, Q60985, Q91Y65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.