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Q60591

- NFAC2_MOUSE

UniProt

Q60591 - NFAC2_MOUSE

Protein

Nuclear factor of activated T-cells, cytoplasmic 2

Gene

Nfatc2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    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.By similarity

    Regions

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

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    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 regulatory region DNA binding Source: UniProtKB

    GO - Biological processi

    1. B cell receptor signaling pathway Source: Ensembl
    2. cell migration Source: UniProtKB
    3. cellular response to DNA damage stimulus Source: Ensembl
    4. cytokine production Source: MGI
    5. negative regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
    6. positive regulation of B cell proliferation Source: Ensembl
    7. positive regulation of gene expression Source: UniProtKB
    8. positive regulation of transcription, DNA-templated Source: MGI
    9. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    10. response to drug Source: Ensembl

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_188202. 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: Chromosome 2

    Organism-specific databases

    MGIiMGI:102463. Nfatc2.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    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: Ensembl
    2. cytoplasm Source: MGI
    3. cytosol Source: MGI
    4. nuclear transcription factor complex Source: MGI
    5. nucleoplasm Source: Reactome
    6. nucleus Source: UniProtKB
    7. plasma membrane Source: Ensembl
    8. ribonucleoprotein complex Source: MGI
    9. transcription factor complex Source: MGI

    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 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

    ArrayExpressiQ60591.
    BgeeiQ60591.
    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.2 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.
    InParanoidiB5B2Q3.
    KOiK17332.
    OMAiMWKTSPD.
    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. Align

    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

    MDVPEPQPDP DGGDGPGHEP GGSPQDELDF SILFDYDYLN PIEEEPIAHK    50
    AISSPSGLAY PDDVLDYGLK PCNPLASLSG EPPGRFGEPD SIGFQNFLSP 100
    VKPAGASGPS PRIEITPSHE LMQAGGALRG RDAGLSPEQP ALALAGVAAS 150
    PRFTLPVPGY EGYREPLCLS PASSGSSASF ISDTFSPYTS PCVSPNNAGP 200
    DDLCPQFQNI PAHYSPRTSP IMSPRTSLAE DSCLGRHSPV PRPASRSSSP 250
    GAKRRHSCAE ALVAPLPAAS PQRSRSPSPQ PSPHVALQDD SIPAGYPPTA 300
    GSAVLMDALN TLATDSPCGI PSKIWKTSPD PTPVSTAPSK AGLARHIYPT 350
    VEFLGPCEQE ERRNSAPESI LLVPPTWPKQ LVPAIPICSI PVTASLPPLE 400
    WPLSNQSGSY ELRIEVQPKP HHRAHYETEG SRGAVKAPTG GHPVVQLHGY 450
    MENKPLGLQI FIGTADERIL KPHAFYQVHR ITGKTVTTTS YEKIVGNTKV 500
    LEIPLEPKNN MRATIDCAGI LKLRNADIEL RKGETDIGRK NTRVRLVFRV 550
    HVPEPSGRIV SLQAASNPIE CSQRSAHELP MVERQDMDSC LVYGGQQMIL 600
    TGQNFTAESK VVFMEKTTDG QQIWEMEATV DKDKSQPNML FVEIPEYRNK 650
    HIRVPVKVNF YVINGKRKRS QPQHFTYHPV PAIKTEPSDE YEPSLICSPA 700
    HGGLGSQPYY PQHPMLAESP SCLVATMAPC QQFRSGLSSP DARYQQQSPA 750
    AALYQRSKSL SPGLLGYQQP SLLAAPLGLA DAHRSVLVHA GSQGQGQGST 800
    LPHTSSASQQ ASPVIHYSPT NQQLRGGGHQ EFQHIMYCEN FGPSSARPGP 850
    PPINQGQRLS PGAYPTVIQQ QTAPSQRAAK NGPSDQKEAL PTGVTVKQEQ 900
    NLDQTYLDDV NEIIRKEFSG PPSRNQT 927
    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. Reason: Chimeric cDNA fused with Phyhd1 (Lrrc8a).

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS17112.1. [Q60591-3 ]
    CCDS50803.1. [Q60591-2 ]
    PIRi A48753.
    RefSeqi NP_035029.2. NM_010899.3. [Q60591-3 ]
    UniGenei Mm.116802.

    3D structure databases

    ProteinModelPortali Q60591.
    SMRi Q60591. Positions 398-680.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201739. 1 interaction.
    DIPi DIP-49476N.
    IntActi Q60591. 9 interactions.
    MINTi MINT-1565857.

    PTM databases

    PhosphoSitei Q60591.

    Proteomic databases

    PRIDEi Q60591.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000074618 ; ENSMUSP00000074198 ; ENSMUSG00000027544 . [Q60591-3 ]
    ENSMUST00000109184 ; ENSMUSP00000104812 ; ENSMUSG00000027544 . [Q60591-2 ]
    GeneIDi 18019.
    KEGGi mmu:18019.
    UCSCi uc008oau.1. mouse. [Q60591-3 ]

    Organism-specific databases

    CTDi 4773.
    MGIi MGI:102463. Nfatc2.

    Phylogenomic databases

    eggNOGi NOG84065.
    GeneTreei ENSGT00550000074562.
    HOVERGENi HBG069754.
    InParanoidi B5B2Q3.
    KOi K17332.
    OMAi MWKTSPD.
    OrthoDBi EOG79PJND.
    TreeFami TF326480.

    Enzyme and pathway databases

    Reactomei REACT_188202. FCERI mediated Ca+2 mobilization.

    Miscellaneous databases

    ChiTaRSi NFATC2. mouse.
    NextBioi 293063.
    PROi Q60591.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60591.
    Bgeei Q60591.
    Genevestigatori Q60591.

    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

    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: October 1, 2014
    This is version 143 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