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P40763

- STAT3_HUMAN

UniProt

P40763 - STAT3_HUMAN

Protein

Signal transducer and activator of transcription 3

Gene

STAT3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 2 (07 Jun 2004)
      Previous versions | rss
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    Functioni

    Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF and other growth factors. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the interleukin-6 (IL-6)-responsive elements identified in the promoters of various acute-phase protein genes. Activated by IL31 through IL31RA. Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity. Plays an important role in host defense in methicillin-resistant S.aureus lung infection by regulating the expression of the antimicrobial lectin REG3G By similarity.By similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. DNA binding Source: UniProtKB
    3. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: BHF-UCL
    4. protein binding Source: UniProtKB
    5. protein dimerization activity Source: UniProtKB
    6. protein kinase binding Source: UniProtKB
    7. protein phosphatase binding Source: UniProtKB
    8. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
    9. sequence-specific DNA binding Source: Ensembl
    10. sequence-specific DNA binding transcription factor activity Source: ProtInc
    11. signal transducer activity Source: ProtInc
    12. transcription factor binding Source: UniProtKB
    13. transcription regulatory region DNA binding Source: BHF-UCL

    GO - Biological processi

    1. acute-phase response Source: Ensembl
    2. astrocyte differentiation Source: UniProtKB
    3. cell proliferation Source: Ensembl
    4. cellular component movement Source: ProtInc
    5. cellular response to hormone stimulus Source: BHF-UCL
    6. cytokine-mediated signaling pathway Source: UniProtKB
    7. eating behavior Source: UniProtKB
    8. eye photoreceptor cell differentiation Source: UniProtKB
    9. glucose homeostasis Source: UniProtKB
    10. growth hormone receptor signaling pathway Source: BHF-UCL
    11. interleukin-6-mediated signaling pathway Source: UniProtKB
    12. intracellular receptor signaling pathway Source: BHF-UCL
    13. JAK-STAT cascade Source: UniProtKB
    14. JAK-STAT cascade involved in growth hormone signaling pathway Source: UniProtKB
    15. negative regulation of cell death Source: Ensembl
    16. negative regulation of neuron migration Source: Ensembl
    17. negative regulation of transcription from RNA polymerase II promoter Source: ProtInc
    18. nervous system development Source: ProtInc
    19. neurotrophin TRK receptor signaling pathway Source: Reactome
    20. phosphorylation Source: UniProtKB
    21. positive regulation of Notch signaling pathway Source: UniProtKB
    22. positive regulation of transcription, DNA-templated Source: UniProtKB
    23. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    24. protein import into nucleus Source: UniProtKB
    25. radial glial cell differentiation Source: UniProtKB
    26. regulation of multicellular organism growth Source: Ensembl
    27. regulation of transcription, DNA-templated Source: UniProtKB
    28. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    29. response to drug Source: Ensembl
    30. response to estradiol Source: BHF-UCL
    31. response to ethanol Source: Ensembl
    32. sexual reproduction Source: UniProtKB
    33. signal transduction Source: ProtInc
    34. stem cell maintenance Source: Ensembl
    35. temperature homeostasis Source: UniProtKB
    36. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Host-virus interaction, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_111040. Signaling by SCF-KIT.
    REACT_111133. Growth hormone receptor signaling.
    REACT_12049. Signalling to STAT3.
    REACT_121141. Signaling by FGFR1 fusion mutants.
    REACT_169118. Signaling by Leptin.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_17025. Downstream signal transduction.
    REACT_200759. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
    REACT_200812. Transcriptional regulation of pluripotent stem cells.
    REACT_27307. Interleukin-6 signaling.
    SignaLinkiP40763.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Signal transducer and activator of transcription 3
    Alternative name(s):
    Acute-phase response factor
    Gene namesi
    Name:STAT3
    Synonyms:APRF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:11364. STAT3.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Shuttles between the nucleus and the cytoplasm. Translocated into the nucleus upon tyrosine phosphorylation and dimerization, in response to signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4. Constitutive nuclear presence is independent of tyrosine phosphorylation. Predominantly present in the cytoplasm without stimuli. Upon leukemia inhibitory factor (LIF) stimulation, accumulates in the nucleus. The complex composed of BART and ARL2 plays an important role in the nuclear translocation and retention of STAT3. Identified in a complex with LYN and PAG1.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Hyperimmunoglobulin E recurrent infection syndrome, autosomal dominant (AD-HIES) [MIM:147060]: A rare disorder of immunity and connective tissue characterized by immunodeficiency, chronic eczema, recurrent Staphylococcal infections, increased serum IgE, eosinophilia, distinctive coarse facial appearance, abnormal dentition, hyperextensibility of the joints, and bone fractures.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti382 – 3821R → L in AD-HIES. 1 Publication
    VAR_037365
    Natural varianti382 – 3821R → Q in AD-HIES; loss of function. 2 Publications
    VAR_037366
    Natural varianti382 – 3821R → W in AD-HIES; loss of function. 2 Publications
    VAR_037367
    Natural varianti384 – 3841F → L in AD-HIES. 1 Publication
    VAR_037368
    Natural varianti384 – 3841F → S in AD-HIES. 1 Publication
    VAR_037369
    Natural varianti389 – 3891T → I in AD-HIES; loss of function. 1 Publication
    VAR_037370
    Natural varianti423 – 4231R → Q in AD-HIES. 1 Publication
    VAR_037371
    Natural varianti437 – 4371H → Y in AD-HIES; loss of function. 1 Publication
    VAR_037372
    Natural varianti463 – 4631Missing in AD-HIES; loss of function. 2 Publications
    VAR_037373
    Natural varianti611 – 6111S → N in AD-HIES. 1 Publication
    VAR_037375
    Natural varianti621 – 6211F → V in AD-HIES. 1 Publication
    VAR_037376
    Natural varianti622 – 6221T → I in AD-HIES. 1 Publication
    VAR_037377
    Natural varianti637 – 6371V → L in AD-HIES. 1 Publication
    VAR_037378
    Natural varianti637 – 6371V → M in AD-HIES. 1 Publication
    VAR_037379
    Natural varianti644 – 6441Missing in AD-HIES. 1 Publication
    VAR_037380
    Natural varianti657 – 6571Y → C in AD-HIES. 1 Publication
    VAR_037381

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi147060. phenotype.
    Orphaneti2314. Autosomal dominant hyper-IgE syndrome.
    PharmGKBiPA337.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 770769Signal transducer and activator of transcription 3PRO_0000182417Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei705 – 7051Phosphotyrosine; by FER and PTK64 Publications
    Modified residuei727 – 7271Phosphoserine; by DYRK2, NLK, NEK6, IRAK1, RPS6KA5, ZIPK/DAPK3 and PKC/PRKCE9 Publications

    Post-translational modificationi

    Tyrosine phosphorylated upon stimulation with EGF. Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4 By similarity. Activated through tyrosine phosphorylation by BMX. Tyrosine phosphorylated in response to IL6, IL11, LIF, CNTF, KITLG/SCF, CSF1, EGF, PDGF, IFN-alpha and OSM. Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus. Phosphorylated on serine upon DNA damage, probably by ATM or ATR. Serine phosphorylation is important for the formation of stable DNA-binding STAT3 homodimers and maximal transcriptional activity. ARL2BP may participate in keeping the phosphorylated state of STAT3 within the nucleus. Upon LPS challenge, phosphorylated within the nucleus by IRAK1. Upon erythropoietin treatment, phosphorylated on Ser-727 by RPS6KA5. Phosphoryation at Tyr-705 by PTK6 or FER leads to an increase of its transcriptional activity. Dephosphorylation on tyrosine residues by PTPN2 negatively regulates IL6/interleukin-6 signaling.By similarity16 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP40763.
    PaxDbiP40763.
    PeptideAtlasiP40763.
    PRIDEiP40763.

    PTM databases

    PhosphoSiteiP40763.

    Miscellaneous databases

    PMAP-CutDBP40763.

    Expressioni

    Tissue specificityi

    Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

    Gene expression databases

    ArrayExpressiP40763.
    BgeeiP40763.
    CleanExiHS_STAT3.
    GenevestigatoriP40763.

    Organism-specific databases

    HPAiCAB003859.
    HPA001671.

    Interactioni

    Subunit structurei

    Forms a homodimer or a heterodimer with a related family member (at least STAT1). Interacts with IL31RA, NCOA1, PELP1, SIPAR, SOCS7, STATIP1 and TMF1. Interacts with HCV core protein. Interacts with IL23R in presence of IL23. Interacts (via SH2 domain) with NLK. Interacts with ARL2BP; the interaction is enhanced by LIF and JAK1 expression By similarity. Interacts with KPNA4 and KPNA5; KPNA4 may be the primary mediator of nuclear import By similarity. Interacts with CAV2; the interaction is increased on insulin-induced tyrosine phosphorylation of CAV2 and leads to STAT3 activation By similarity. Interacts with ARL2BP; interaction is enhanced with ARL2. Interacts with NEK6 By similarity. Binds to CDK9 when activated and nuclear. Interacts with BMX. Interacts with ZIPK/DAPK3. Interacts with PIAS3; the interaction occurs on stimulation by IL6, CNTF or OSM and inhibits the DNA binding activity of STAT3. In prostate cancer cells, interacts with STAT3 and promotes DNA binding activity of STAT3. Interacts with STMN3, antagonizing its microtubule-destabilizing activity. Interacts with the 'Lys-129' acetylated form of BIRC5/survivin. Interacts with FER. Interacts (via SH2 domain) with EIF2AK2/PKR (via the kinase catalytic domain).By similarity18 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q9DUM34EBI-518675,EBI-7971837From a different organism.
    BCKDKO148742EBI-518675,EBI-1046765
    BICD1Q96G012EBI-518675,EBI-1104509
    CAPN1P073842EBI-518675,EBI-1542113
    CORO1AP311462EBI-518675,EBI-1046676
    CSF3RQ990624EBI-518675,EBI-7331284
    DAXXQ9UER74EBI-518675,EBI-77321
    DIRAS3O956613EBI-518675,EBI-6139214
    ECH1Q130112EBI-518675,EBI-711968
    ECHS1P300843EBI-518675,EBI-719602
    EGFRP0053313EBI-518675,EBI-297353
    ERBB2P046269EBI-518675,EBI-641062
    EZH2Q159105EBI-518675,EBI-530054
    GADD45GIP1Q8TAE83EBI-518675,EBI-372506
    GNL3Q9BVP22EBI-518675,EBI-641642
    KHDRBS1Q076662EBI-518675,EBI-1364
    MAP3K7O433184EBI-518675,EBI-358684
    MAPK9P459842EBI-518675,EBI-713568
    MAPK9P45984-13EBI-518675,EBI-713586
    MORC4Q8TE762EBI-518675,EBI-3940432
    MRPS31Q926652EBI-518675,EBI-720602
    NR4A1P227363EBI-518675,EBI-721550
    OGDHLQ9ULD02EBI-518675,EBI-3940481
    PGRP064013EBI-518675,EBI-78539
    PTPN1P180312EBI-518675,EBI-968788
    RELAQ042064EBI-518675,EBI-73886
    RETP079493EBI-518675,EBI-2480756
    RPS9P467812EBI-518675,EBI-351206
    SOX1O005702EBI-518675,EBI-2935583
    SRIP306262EBI-518675,EBI-750459
    STAT1P422243EBI-518675,EBI-1057697
    SULT2A1Q065202EBI-518675,EBI-3921363

    Protein-protein interaction databases

    BioGridi112651. 155 interactions.
    DIPiDIP-33584N.
    IntActiP40763. 93 interactions.
    MINTiMINT-146801.
    STRINGi9606.ENSP00000264657.

    Structurei

    3D structure databases

    ProteinModelPortaliP40763.
    SMRiP40763. Positions 2-715.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini580 – 67091SH2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi150 – 16213Essential for nuclear importAdd
    BLAST

    Sequence similaritiesi

    Belongs to the transcription factor STAT family.Curated
    Contains 1 SH2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain

    Phylogenomic databases

    eggNOGiNOG303257.
    HOGENOMiHOG000220792.
    HOVERGENiHBG055669.
    InParanoidiP40763.
    KOiK04692.
    OMAiNKESHAT.
    OrthoDBiEOG73JKTT.
    PhylomeDBiP40763.
    TreeFamiTF318648.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    1.10.532.10. 1 hit.
    1.20.1050.20. 1 hit.
    2.60.40.630. 1 hit.
    3.30.505.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR008967. p53-like_TF_DNA-bd.
    IPR000980. SH2.
    IPR001217. STAT.
    IPR013800. STAT_TF_alpha.
    IPR015988. STAT_TF_coiled-coil.
    IPR013801. STAT_TF_DNA-bd.
    IPR012345. STAT_TF_DNA-bd_sub.
    IPR013799. STAT_TF_prot_interaction.
    [Graphical view]
    PANTHERiPTHR11801. PTHR11801. 1 hit.
    PfamiPF00017. SH2. 1 hit.
    PF01017. STAT_alpha. 1 hit.
    PF02864. STAT_bind. 1 hit.
    PF02865. STAT_int. 1 hit.
    [Graphical view]
    SMARTiSM00252. SH2. 1 hit.
    SM00964. STAT_int. 1 hit.
    [Graphical view]
    SUPFAMiSSF47655. SSF47655. 1 hit.
    SSF48092. SSF48092. 1 hit.
    SSF49417. SSF49417. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEiPS50001. SH2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P40763-1) [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

    MAQWNQLQQL DTRYLEQLHQ LYSDSFPMEL RQFLAPWIES QDWAYAASKE    50
    SHATLVFHNL LGEIDQQYSR FLQESNVLYQ HNLRRIKQFL QSRYLEKPME 100
    IARIVARCLW EESRLLQTAA TAAQQGGQAN HPTAAVVTEK QQMLEQHLQD 150
    VRKRVQDLEQ KMKVVENLQD DFDFNYKTLK SQGDMQDLNG NNQSVTRQKM 200
    QQLEQMLTAL DQMRRSIVSE LAGLLSAMEY VQKTLTDEEL ADWKRRQQIA 250
    CIGGPPNICL DRLENWITSL AESQLQTRQQ IKKLEELQQK VSYKGDPIVQ 300
    HRPMLEERIV ELFRNLMKSA FVVERQPCMP MHPDRPLVIK TGVQFTTKVR 350
    LLVKFPELNY QLKIKVCIDK DSGDVAALRG SRKFNILGTN TKVMNMEESN 400
    NGSLSAEFKH LTLREQRCGN GGRANCDASL IVTEELHLIT FETEVYHQGL 450
    KIDLETHSLP VVVISNICQM PNAWASILWY NMLTNNPKNV NFFTKPPIGT 500
    WDQVAEVLSW QFSSTTKRGL SIEQLTTLAE KLLGPGVNYS GCQITWAKFC 550
    KENMAGKGFS FWVWLDNIID LVKKYILALW NEGYIMGFIS KERERAILST 600
    KPPGTFLLRF SESSKEGGVT FTWVEKDISG KTQIQSVEPY TKQQLNNMSF 650
    AEIIMGYKIM DATNILVSPL VYLYPDIPKE EAFGKYCRPE SQEHPEADPG 700
    SAAPYLKTKF ICVTPTTCSN TIDLPMSPRT LDSLMQFGNN GEGAEPSAGG 750
    QFESLTFDME LTSECATSPM 770
    Length:770
    Mass (Da):88,068
    Last modified:June 7, 2004 - v2
    Checksum:i6C00632211C8012D
    GO
    Isoform Del-701 (identifier: P40763-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         701-701: Missing.

    Note: Contains a phosphotyrosine at position 704.

    Show »
    Length:769
    Mass (Da):87,981
    Checksum:iA374A32AB9D28077
    GO
    Isoform 3 (identifier: P40763-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         716-722: TTCSNTI → FIDAVWK
         723-770: Missing.

    Show »
    Length:722
    Mass (Da):83,126
    Checksum:i09226A697966D947
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti133 – 1331T → A in BAF84622. (PubMed:14702039)Curated
    Sequence conflicti288 – 2881Q → H in AAA58374. (PubMed:7512451)Curated
    Sequence conflicti460 – 4601P → S in AAA58374. (PubMed:7512451)Curated
    Sequence conflicti548 – 5481K → N in AAA58374. (PubMed:7512451)Curated
    Sequence conflicti652 – 6521E → V in BAF84622. (PubMed:14702039)Curated
    Sequence conflicti667 – 6671V → L in AAA58374. (PubMed:7512451)Curated
    Sequence conflicti730 – 7301T → A in AAA58374. (PubMed:7512451)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321Q → K.
    Corresponds to variant rs1803125 [ dbSNP | Ensembl ].
    VAR_018683
    Natural varianti143 – 1431M → I.1 Publication
    Corresponds to variant rs17878478 [ dbSNP | Ensembl ].
    VAR_018679
    Natural varianti382 – 3821R → L in AD-HIES. 1 Publication
    VAR_037365
    Natural varianti382 – 3821R → Q in AD-HIES; loss of function. 2 Publications
    VAR_037366
    Natural varianti382 – 3821R → W in AD-HIES; loss of function. 2 Publications
    VAR_037367
    Natural varianti384 – 3841F → L in AD-HIES. 1 Publication
    VAR_037368
    Natural varianti384 – 3841F → S in AD-HIES. 1 Publication
    VAR_037369
    Natural varianti389 – 3891T → I in AD-HIES; loss of function. 1 Publication
    VAR_037370
    Natural varianti423 – 4231R → Q in AD-HIES. 1 Publication
    VAR_037371
    Natural varianti437 – 4371H → Y in AD-HIES; loss of function. 1 Publication
    VAR_037372
    Natural varianti463 – 4631Missing in AD-HIES; loss of function. 2 Publications
    VAR_037373
    Natural varianti561 – 5611F → Y.1 Publication
    Corresponds to variant rs1064116 [ dbSNP | Ensembl ].
    VAR_037374
    Natural varianti611 – 6111S → N in AD-HIES. 1 Publication
    VAR_037375
    Natural varianti621 – 6211F → V in AD-HIES. 1 Publication
    VAR_037376
    Natural varianti622 – 6221T → I in AD-HIES. 1 Publication
    VAR_037377
    Natural varianti637 – 6371V → L in AD-HIES. 1 Publication
    VAR_037378
    Natural varianti637 – 6371V → M in AD-HIES. 1 Publication
    VAR_037379
    Natural varianti644 – 6441Missing in AD-HIES. 1 Publication
    VAR_037380
    Natural varianti657 – 6571Y → C in AD-HIES. 1 Publication
    VAR_037381

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei701 – 7011Missing in isoform Del-701. 1 PublicationVSP_010474
    Alternative sequencei716 – 7227TTCSNTI → FIDAVWK in isoform 3. 1 PublicationVSP_055918
    Alternative sequencei723 – 77048Missing in isoform 3. 1 PublicationVSP_055919Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29277 mRNA. Translation: AAA58374.1.
    AJ012463 mRNA. Translation: CAA10032.1.
    JB252046 mRNA. No translation available.
    AK291933 mRNA. Translation: BAF84622.1.
    AY572796 Genomic DNA. Translation: AAS66986.1.
    AC087691 Genomic DNA. No translation available.
    CH471152 Genomic DNA. Translation: EAW60822.1.
    BC000627 mRNA. Translation: AAH00627.1.
    BC014482 mRNA. Translation: AAH14482.1.
    AF029311 mRNA. Translation: AAB84254.1.
    CCDSiCCDS32656.1. [P40763-1]
    CCDS32657.1. [P40763-2]
    PIRiA54444.
    RefSeqiNP_003141.2. NM_003150.3. [P40763-2]
    NP_644805.1. NM_139276.2. [P40763-1]
    NP_998827.1. NM_213662.1.
    UniGeneiHs.463059.

    Genome annotation databases

    EnsembliENST00000264657; ENSP00000264657; ENSG00000168610. [P40763-1]
    ENST00000404395; ENSP00000384943; ENSG00000168610. [P40763-2]
    ENST00000585517; ENSP00000467000; ENSG00000168610.
    ENST00000588969; ENSP00000467985; ENSG00000168610. [P40763-1]
    GeneIDi6774.
    KEGGihsa:6774.
    UCSCiuc002hzk.1. human. [P40763-1]
    uc002hzm.1. human. [P40763-2]

    Polymorphism databases

    DMDMi48429227.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    STAT3 entry

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    STAT3base

    STAT3 mutation db

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29277 mRNA. Translation: AAA58374.1 .
    AJ012463 mRNA. Translation: CAA10032.1 .
    JB252046 mRNA. No translation available.
    AK291933 mRNA. Translation: BAF84622.1 .
    AY572796 Genomic DNA. Translation: AAS66986.1 .
    AC087691 Genomic DNA. No translation available.
    CH471152 Genomic DNA. Translation: EAW60822.1 .
    BC000627 mRNA. Translation: AAH00627.1 .
    BC014482 mRNA. Translation: AAH14482.1 .
    AF029311 mRNA. Translation: AAB84254.1 .
    CCDSi CCDS32656.1. [P40763-1 ]
    CCDS32657.1. [P40763-2 ]
    PIRi A54444.
    RefSeqi NP_003141.2. NM_003150.3. [P40763-2 ]
    NP_644805.1. NM_139276.2. [P40763-1 ]
    NP_998827.1. NM_213662.1.
    UniGenei Hs.463059.

    3D structure databases

    ProteinModelPortali P40763.
    SMRi P40763. Positions 2-715.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112651. 155 interactions.
    DIPi DIP-33584N.
    IntActi P40763. 93 interactions.
    MINTi MINT-146801.
    STRINGi 9606.ENSP00000264657.

    Chemistry

    BindingDBi P40763.
    ChEMBLi CHEMBL4026.

    PTM databases

    PhosphoSitei P40763.

    Polymorphism databases

    DMDMi 48429227.

    Proteomic databases

    MaxQBi P40763.
    PaxDbi P40763.
    PeptideAtlasi P40763.
    PRIDEi P40763.

    Protocols and materials databases

    DNASUi 6774.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264657 ; ENSP00000264657 ; ENSG00000168610 . [P40763-1 ]
    ENST00000404395 ; ENSP00000384943 ; ENSG00000168610 . [P40763-2 ]
    ENST00000585517 ; ENSP00000467000 ; ENSG00000168610 .
    ENST00000588969 ; ENSP00000467985 ; ENSG00000168610 . [P40763-1 ]
    GeneIDi 6774.
    KEGGi hsa:6774.
    UCSCi uc002hzk.1. human. [P40763-1 ]
    uc002hzm.1. human. [P40763-2 ]

    Organism-specific databases

    CTDi 6774.
    GeneCardsi GC17M040465.
    GeneReviewsi STAT3.
    HGNCi HGNC:11364. STAT3.
    HPAi CAB003859.
    HPA001671.
    MIMi 102582. gene.
    147060. phenotype.
    neXtProti NX_P40763.
    Orphaneti 2314. Autosomal dominant hyper-IgE syndrome.
    PharmGKBi PA337.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG303257.
    HOGENOMi HOG000220792.
    HOVERGENi HBG055669.
    InParanoidi P40763.
    KOi K04692.
    OMAi NKESHAT.
    OrthoDBi EOG73JKTT.
    PhylomeDBi P40763.
    TreeFami TF318648.

    Enzyme and pathway databases

    Reactomei REACT_111040. Signaling by SCF-KIT.
    REACT_111133. Growth hormone receptor signaling.
    REACT_12049. Signalling to STAT3.
    REACT_121141. Signaling by FGFR1 fusion mutants.
    REACT_169118. Signaling by Leptin.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_17025. Downstream signal transduction.
    REACT_200759. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
    REACT_200812. Transcriptional regulation of pluripotent stem cells.
    REACT_27307. Interleukin-6 signaling.
    SignaLinki P40763.

    Miscellaneous databases

    ChiTaRSi STAT3. human.
    GeneWikii STAT3.
    GenomeRNAii 6774.
    NextBioi 26438.
    PMAP-CutDB P40763.
    PROi P40763.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P40763.
    Bgeei P40763.
    CleanExi HS_STAT3.
    Genevestigatori P40763.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    1.10.532.10. 1 hit.
    1.20.1050.20. 1 hit.
    2.60.40.630. 1 hit.
    3.30.505.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR008967. p53-like_TF_DNA-bd.
    IPR000980. SH2.
    IPR001217. STAT.
    IPR013800. STAT_TF_alpha.
    IPR015988. STAT_TF_coiled-coil.
    IPR013801. STAT_TF_DNA-bd.
    IPR012345. STAT_TF_DNA-bd_sub.
    IPR013799. STAT_TF_prot_interaction.
    [Graphical view ]
    PANTHERi PTHR11801. PTHR11801. 1 hit.
    Pfami PF00017. SH2. 1 hit.
    PF01017. STAT_alpha. 1 hit.
    PF02864. STAT_bind. 1 hit.
    PF02865. STAT_int. 1 hit.
    [Graphical view ]
    SMARTi SM00252. SH2. 1 hit.
    SM00964. STAT_int. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47655. SSF47655. 1 hit.
    SSF48092. SSF48092. 1 hit.
    SSF49417. SSF49417. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEi PS50001. SH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91-related transcription factor involved in the gp130-mediated signaling pathway."
      Akira S., Nishio Y., Inoue M., Wang X.-J., Wei S., Matsusaka T., Yoshida K., Sudo T., Naruto M., Kishimoto T.
      Cell 77:63-71(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT TYR-561.
      Tissue: Placenta.
    2. "Highly conserved amino-acid sequence between murine STAT3 and a revised human STAT3 sequence."
      Della Pietra L., Bressan A., Pezzotti A., Serlupi-Crescenzi O.
      Gene 213:119-124(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. SeattleSNPs variation discovery resource
      Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-143.
    6. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 DEL-701).
      Tissue: Kidney and Pancreas.
    9. Della Pietra L., Bressan A., Pezzotti A.R., Serlupi-Crescenzi O.
      Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 564-704.
      Tissue: Liver.
    10. "Requirement of serine phosphorylation for formation of STAT-promoter complexes."
      Zhang X., Blenis J., Li H.-C., Schindler C., Chen-Kiang S.
      Science 267:1990-1994(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SERINE RESIDUES.
    11. "Specific inhibition of Stat3 signal transduction by PIAS3."
      Chung C.D., Liao J., Liu B., Rao X., Jay P., Berta P., Shuai K.
      Science 278:1803-1805(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIAS3.
    12. "Etk, a Btk family tyrosine kinase, mediates cellular transformation by linking Src to STAT3 activation."
      Tsai Y.T., Su Y.H., Fang S.S., Huang T.N., Qiu Y., Jou Y.S., Shih H.M., Kung H.J., Chen R.H.
      Mol. Cell. Biol. 20:2043-2054(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY BMX, INTERACTION WITH BMX, FUNCTION.
    13. "The nuclear isoform of protein-tyrosine phosphatase TC-PTP regulates interleukin-6-mediated signaling pathway through STAT3 dephosphorylation."
      Yamamoto T., Sekine Y., Kashima K., Kubota A., Sato N., Aoki N., Matsuda T.
      Biochem. Biophys. Res. Commun. 297:811-817(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN IL6 SIGNALING, PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN2.
    14. "Functional interaction of STAT3 transcription factor with the coactivator NcoA/SRC1a."
      Giraud S., Bienvenu F., Avril S., Gascan H., Heery D.M., Coqueret O.
      J. Biol. Chem. 277:8004-8011(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOA1.
    15. "Activation of STAT3 by the hepatitis C virus core protein leads to cellular transformation."
      Yoshida T., Hanada T., Tokuhisa T., Kosai K., Sata M., Kohara M., Yoshimura A.
      J. Exp. Med. 196:641-653(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCV CORE PROTEIN.
    16. Cited for: INTERACTION WITH IL23R.
    17. "Identification and characterization of signal transducer and activator of transcription 3 recruitment sites within the epidermal growth factor receptor."
      Shao H., Cheng H.Y., Cook R.G., Tweardy D.J.
      Cancer Res. 63:3923-3930(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN EGFR SIGNALING, INTERACTION WITH EGFR.
    18. "Erythropoietin-induced serine 727 phosphorylation of STAT3 in erythroid cells is mediated by a MEK-, ERK-, and MSK1-dependent pathway."
      Wierenga A.T., Vogelzang I., Eggen B.J., Vellenga E.
      Exp. Hematol. 31:398-405(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-705 AND SER-727.
    19. "Signal transduction via the stem cell factor receptor/c-Kit."
      Ronnstrand L.
      Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ROLE IN KIT SIGNALING.
    20. "Characterization of the signaling capacities of the novel gp130-like cytokine receptor."
      Dreuw A., Radtke S., Pflanz S., Lippok B.E., Heinrich P.C., Hermanns H.M.
      J. Biol. Chem. 279:36112-36120(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH IL31RA.
    21. "IRAK1 serves as a novel regulator essential for lipopolysaccharide-induced interleukin-10 gene expression."
      Huang Y., Li T., Sane D.C., Li L.
      J. Biol. Chem. 279:51697-51703(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-727 BY IRAK1.
    22. "TMF/ARA160 is a BC-box-containing protein that mediates the degradation of Stat3."
      Perry E., Tsruya R., Levitsky P., Pomp O., Taller M., Weisberg S., Parris W., Kulkarni S., Malovani H., Pawson T., Shpungin S., Nir U.
      Oncogene 23:8908-8919(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TMF1.
    23. "Proline-, glutamic acid-, and leucine-rich protein-1 is essential in growth factor regulation of signal transducers and activators of transcription 3 activation."
      Manavathi B., Nair S.S., Wang R.-A., Kumar R., Vadlamudi R.K.
      Cancer Res. 65:5571-5577(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PELP1.
    24. "Physical and functional interactions between STAT3 and ZIP kinase."
      Sato N., Kawai T., Sugiyama K., Muromoto R., Imoto S., Sekine Y., Ishida M., Akira S., Matsuda T.
      Int. Immunol. 17:1543-1552(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-727 BY ZIPK/DAPK3, INTERACTION WITH ZIPK/DAPK3, SUBCELLULAR LOCATION.
    25. "Suppressor of cytokine signaling 7 inhibits prolactin, growth hormone, and leptin signaling by interacting with STAT5 or STAT3 and attenuating their nuclear translocation."
      Martens N., Uzan G., Wery M., Hooghe R., Hooghe-Peters E.L., Gertler A.
      J. Biol. Chem. 280:13817-13823(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SOCS7.
    26. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-704 (ISOFORM DEL-701), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Identification of STAT3 as a specific substrate of breast tumor kinase."
      Liu L., Gao Y., Qiu H., Miller W.T., Poli V., Reich N.C.
      Oncogene 25:4904-4912(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-705 BY PTK6.
    28. "Protein kinase Cepsilon interacts with signal transducers and activators of transcription 3 (Stat3), phosphorylates Stat3Ser727, and regulates its constitutive activation in prostate cancer."
      Aziz M.H., Manoharan H.T., Church D.R., Dreckschmidt N.E., Zhong W., Oberley T.D., Wilding G., Verma A.K.
      Cancer Res. 67:8828-8838(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRKCE, PHOSPHORYLATION AT SER-727.
    29. "STAT3 nuclear import is independent of tyrosine phosphorylation and mediated by importin-alpha3."
      Liu L., McBride K.M., Reich N.C.
      Proc. Natl. Acad. Sci. U.S.A. 102:8150-8155(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, NUCLEAR IMPORT MOTIF.
    30. "The functional role of an interleukin 6-inducible CDK9.STAT3 complex in human gamma-fibrinogen gene expression."
      Hou T., Ray S., Brasier A.R.
      J. Biol. Chem. 282:37091-37102(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDK9.
    31. "Role for DYRK family kinases on regulation of apoptosis."
      Yoshida K.
      Biochem. Pharmacol. 76:1389-1394(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-727 BY DYRK2.
    32. "Oncogenic association of the Cbp/PAG adaptor protein with the Lyn tyrosine kinase in human B-NHL rafts."
      Tauzin S., Ding H., Khatib K., Ahmad I., Burdevet D., van Echten-Deckert G., Lindquist J.A., Schraven B., Din N.U., Borisch B., Hoessli D.C.
      Blood 111:2310-2320(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH LYN AND PAG1.
    33. Cited for: INTERACTION WITH ARL2BP, PHOSPHORYLATION AT SERINE RESIDUES, SUBCELLULAR LOCATION.
    34. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    35. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    36. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    37. "The Fer tyrosine kinase cooperates with interleukin-6 to activate signal transducer and activator of transcription 3 and promote human prostate cancer cell growth."
      Zoubeidi A., Rocha J., Zouanat F.Z., Hamel L., Scarlata E., Aprikian A.G., Chevalier S.
      Mol. Cancer Res. 7:142-155(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FER, PHOSPHORYLATION BY FER.
    38. "Acetylation directs survivin nuclear localization to repress STAT3 oncogenic activity."
      Wang H., Holloway M.P., Ma L., Cooper Z.A., Riolo M., Samkari A., Elenitoba-Johnson K.S., Chin Y.E., Altura R.A.
      J. Biol. Chem. 285:36129-36137(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BIRC5/SURVIVIN.
    39. "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-727, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    40. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    41. "Mechanisms of STAT protein activation by oncogenic KIT mutants in neoplastic mast cells."
      Chaix A., Lopez S., Voisset E., Gros L., Dubreuil P., De Sepulveda P.
      J. Biol. Chem. 286:5956-5966(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-705 IN RESPONSE TO KIT SIGNALING, PHOSPHORYLATION AT SER-727.
    42. Cited for: FUNCTION, INTERACTION WITH EIF2AK2.
    43. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    44. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    45. Cited for: VARIANTS AD-HIES GLN-382; LEU-382; TRP-382; LEU-384; SER-384; GLN-423; VAL-463 DEL; ASN-611; VAL-621; ILE-622; LEU-637; MET-637; GLN-644 DEL AND CYS-657.
    46. "Dominant-negative mutations in the DNA-binding domain of STAT3 cause hyper-IgE syndrome."
      Minegishi Y., Saito M., Tsuchiya S., Tsuge I., Takada H., Hara T., Kawamura N., Ariga T., Pasic S., Stojkovic O., Metin A., Karasuyama H.
      Nature 448:1058-1062(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS AD-HIES GLN-382; TRP-382; ILE-389; TYR-437 AND VAL-463 DEL, CHARACTERIZATION OF VARIANTS AD-HIES GLN-382; TRP-382; ILE-389; TYR-437 AND VAL-463 DEL.

    Entry informationi

    Entry nameiSTAT3_HUMAN
    AccessioniPrimary (citable) accession number: P40763
    Secondary accession number(s): A8K7B8
    , K7ENL3, O14916, Q9BW54
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 162 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

    Miscellaneous

    Involved in the gp130-mediated signaling pathway.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3