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Q13469

- NFAC2_HUMAN

UniProt

Q13469 - NFAC2_HUMAN

Protein

Nuclear factor of activated T-cells, cytoplasmic 2

Gene

NFATC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 2 (05 Jul 2005)
      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.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. cell migration Source: UniProtKB
    3. cellular response to DNA damage stimulus Source: UniProtKB
    4. cytokine production Source: Ensembl
    5. Fc-epsilon receptor signaling pathway Source: Reactome
    6. innate immune response Source: Reactome
    7. positive regulation of B cell proliferation Source: UniProtKB
    8. positive regulation of transcription, DNA-templated Source: MGI
    9. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    10. regulation of transcription, DNA-templated Source: UniProtKB
    11. response to drug Source: UniProtKB
    12. transcription, DNA-templated Source: UniProtKB-KW

    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

    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 2PRO_0000205178Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei99 – 991PhosphoserineBy similarity
    Modified residuei148 – 1481Phosphoserine1 Publication
    Modified residuei213 – 2131PhosphoserineBy similarity
    Modified residuei217 – 2171PhosphoserineBy similarity
    Modified residuei221 – 2211PhosphoserineBy similarity
    Modified residuei236 – 2361PhosphoserineBy similarity
    Modified residuei243 – 2431PhosphoserineBy similarity
    Modified residuei268 – 2681PhosphoserineBy similarity
    Modified residuei274 – 2741PhosphoserineBy similarity
    Modified residuei276 – 2761PhosphoserineBy similarity
    Modified residuei280 – 2801PhosphoserineBy similarity
    Modified residuei326 – 3261PhosphoserineBy similarity
    Modified residuei330 – 3301Phosphoserine2 Publications
    Modified residuei363 – 3631PhosphoserineBy 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.3 Publications

    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.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

    1
    925
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13469.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati184 – 200171Add
    BLAST
    Repeati213 – 229172Add
    BLAST
    Repeati272 – 286153; approximateAdd
    BLAST
    Domaini392 – 574183RHDPROSITE-ProRule annotationAdd
    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 formBy similarityAdd
    BLAST
    Regioni184 – 2861033 X approximate SP repeatsAdd
    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

    Sequence similaritiesi

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

    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 (5)i

    Sequence statusi: Complete.

    This entry describes 5 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
    Isoform 5 (identifier: Q13469-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-219: Missing.
         908-925: VNEIIRKEFSGPPARNQT → ELIDTHLSWIQNIL

    Note: No experimental confirmation available.

    Show »
    Length:702
    Mass (Da):76,700
    Checksum:iD3CA427C994A5605
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 651L → M in AAC50886. (PubMed:8668213)Curated
    Sequence conflicti65 – 651L → M in AAC50887. (PubMed:8668213)Curated

    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 – 219219Missing in isoform 5. 1 PublicationVSP_055926Add
    BLAST
    Alternative sequencei1 – 4343MNAPE…LNPNE → MQREAAFRLGHCHPLRIMGS VDQ in isoform 3 and isoform 4. 2 PublicationsVSP_042757Add
    BLAST
    Alternative sequencei908 – 92518VNEII…ARNQT → ELIDTHLSWIQNIL in isoform 2, isoform 3 and isoform 5. 3 PublicationsVSP_005595Add
    BLAST

    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.
    EU887575 mRNA. Translation: ACG55595.1.
    EU887576 mRNA. Translation: ACG55596.1.
    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_001245223.1. NM_001258294.1.
    NP_001245225.1. NM_001258296.1.
    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]
    ENST00000609507; ENSP00000477342; ENSG00000101096.
    ENST00000609943; ENSP00000477370; ENSG00000101096. [Q13469-4]
    ENST00000610033; ENSP00000477142; ENSG00000101096.
    GeneIDi4773.
    KEGGihsa:4773.
    UCSCiuc002xwc.4. human. [Q13469-2]
    uc002xwd.4. human. [Q13469-1]
    uc010zyv.3. human.
    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 .
    EU887575 mRNA. Translation: ACG55595.1 .
    EU887576 mRNA. Translation: ACG55596.1 .
    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_001245223.1. NM_001258294.1.
    NP_001245225.1. NM_001258296.1.
    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 ]
    ENST00000609507 ; ENSP00000477342 ; ENSG00000101096 .
    ENST00000609943 ; ENSP00000477370 ; ENSG00000101096 . [Q13469-4 ]
    ENST00000610033 ; ENSP00000477142 ; ENSG00000101096 .
    GeneIDi 4773.
    KEGGi hsa:4773.
    UCSCi uc002xwc.4. human. [Q13469-2 ]
    uc002xwd.4. human. [Q13469-1 ]
    uc010zyv.3. human.
    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

    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; 4 AND 5), 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, B5B2P0, 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: October 1, 2014
    This is version 168 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