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P42227 (STAT3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Signal transducer and activator of transcription 3
Alternative name(s):
Acute-phase response factor
Gene names
Name:Stat3
Synonyms:Aprf
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length770 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. STAT3B interacts with the N-terminal part of JUN to activate such promoters in a cooperative way. 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. Ref.14 Ref.23 Ref.24

Subunit structure

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 IL23R in presence of IL23. Interacts (via SH2 domain) with NLK. Interacts with KPNA4 and KPNA5; KPNA4 may be the primary mediator of nuclear import. Interacts with CAV2; the interaction is increased on insulin-induced tyrosine phosphorylation of CAV2 and leads to STAT3 activation. Interacts with ARL2BP; interaction is enhanced with ARL2. Binds to CDK9 when activated and nuclear By similarity. Interacts with ARL2BP; the interaction is enhanced by LIF and JAK1 expression. Interacts with NEK6. Interacts with BMX By similarity. Interacts with ZIPK/DAPK3 By similarity. Interacts with PIAS3; the interaction occurs on stimulation by IL6, CNTF or OSM and inhibits the DNA binding activity of STAT3. Interacts with STMN3, antagonizing its microtubule-destabilizing activity. Interacts with the 'Lys-129' acetylated form of BIRC5/survivin By similarity. Interacts with FER. Interacts (via SH2 domain) with EIF2AK2/PKR (via the kinase catalytic domain) By similarity. Ref.10 Ref.11 Ref.12 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21

Subcellular location

Cytoplasm. Nucleus. Note: 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 By similarity. 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. Ref.14 Ref.16

Tissue specificity

STAT3A is seen in the liver, spleen, and kidney. STAT3B is also detected in the liver, although in a much less abundant manner. Expressed in the lung and an increase in expression levels seen during methicillin-resistant S.aureus infection. Ref.24

Post-translational modification

Activated through tyrosine phosphorylation by BMX. Tyrosine phosphorylated in response to IL6, IL11, CNTF, LIF, KITLG/SCF, CSF1, EGF, PDGF, IFN-alpha and OSM. Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus. Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4. 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. Tyrosine phosphorylated upon stimulation with EGF. Upon LPS challenge, phosphorylated within the nucleus by IRAK1 By similarity. Upon UV-A treatment, phosphorylated on Ser-727 by RPS6KA5 By similarity. Dephosphorylation on tyrosine residues by PTPN2 negatively regulates IL6/interleukin-6 signaling By similarity. Phosphoryation at Tyr-705 by FER or PTK6 leads to an increase of its transcriptional activity. Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.21 Ref.22 Ref.24

Miscellaneous

Involved in the gp130-mediated signaling pathway.

Sequence similarities

Belongs to the transcription factor STAT family.

Contains 1 SH2 domain.

Ontologies

Keywords
   Biological processAcute phase
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainSH2 domain
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processJAK-STAT cascade

Traceable author statement PubMed 15664994. Source: UniProtKB

JAK-STAT cascade involved in growth hormone signaling pathway

Inferred from direct assay PubMed 8923468. Source: BHF-UCL

acute-phase response

Inferred from electronic annotation. Source: UniProtKB-KW

astrocyte differentiation

Inferred from mutant phenotype PubMed 15156153. Source: UniProtKB

cell proliferation

Inferred from direct assay PubMed 15659653. Source: MGI

cytokine-mediated signaling pathway

Non-traceable author statement PubMed 15664994. Source: UniProtKB

eating behavior

Inferred from mutant phenotype PubMed 15070774. Source: MGI

eye photoreceptor cell differentiation

Inferred from mutant phenotype PubMed 15207851. Source: MGI

glucose homeostasis

Inferred from mutant phenotype PubMed 15070774. Source: MGI

interleukin-6-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell death

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from genetic interaction PubMed 22891351. Source: MGI

negative regulation of glycolytic process

Inferred from mutant phenotype PubMed 22891351. Source: MGI

negative regulation of neuron migration

Inferred from genetic interaction PubMed 23321696. Source: MGI

phosphorylation

Inferred from direct assay Ref.24. Source: UniProtKB

positive regulation of Notch signaling pathway

Inferred from mutant phenotype PubMed 15156153. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15096606PubMed 15659653PubMed 19666510. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.24. Source: UniProtKB

protein import into nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

radial glial cell differentiation

Inferred from mutant phenotype PubMed 15156153. Source: UniProtKB

regulation of multicellular organism growth

Inferred from mutant phenotype PubMed 15070774. Source: MGI

regulation of transcription, DNA-templated

Non-traceable author statement PubMed 15664994. Source: UniProtKB

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

sexual reproduction

Inferred from mutant phenotype PubMed 15070774. Source: MGI

stem cell maintenance

Inferred from mutant phenotype PubMed 20720539. Source: MGI

temperature homeostasis

Inferred from mutant phenotype PubMed 15070774. Source: MGI

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 11579100. Source: MGI

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15156153. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 15156153. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 12826573. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 11579100PubMed 12746441PubMed 15096606PubMed 15659653. Source: MGI

calcium ion binding

Inferred from electronic annotation. Source: InterPro

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 15156153Ref.19PubMed 21812053. Source: UniProtKB

protein dimerization activity

Inferred from physical interaction PubMed 11579100. Source: MGI

protein kinase binding

Inferred from physical interaction Ref.15. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay PubMed 16801560. Source: MGI

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay PubMed 15096606. Source: MGI

signal transducer activity

Inferred from electronic annotation. Source: InterPro

transcription factor binding

Inferred from sequence or structural similarity. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Stat3A (identifier: P42227-1)

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.
Isoform Stat3B (identifier: P42227-2)

The sequence of this isoform differs from the canonical sequence as follows:
     716-770: TTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLTFDMDLTSECATSPM → FIDAVWK
Isoform Del-701 (identifier: P42227-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 770769Signal transducer and activator of transcription 3
PRO_0000182418

Regions

Domain580 – 67091SH2
Motif150 – 16213Essential for nuclear import

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue7051Phosphotyrosine; by FER and PTK6 Ref.13 Ref.14 Ref.20
Modified residue7271Phosphoserine; by DYRK2, NLK, NEK6, IRAK1, RPS6KA5, ZIPK/DAPK3 and PKC/PRKCE Probable

Natural variations

Alternative sequence7011Missing in isoform Del-701.
VSP_010475
Alternative sequence716 – 77055TTCSN…ATSPM → FIDAVWK in isoform Stat3B.
VSP_006287

Experimental info

Mutagenesis771V → A: No effect on nuclear import; when associated with A-78 and W-174. Ref.16
Mutagenesis781L → A: No effect on nuclear import; when associated with A-77 and W-174. Ref.16
Mutagenesis1741F → W: No effect on nuclear import; when associated with A-77 and A-78. Ref.16
Mutagenesis6091R → A: Nuclear localization to the same extent as wild-type; when associated with F-705. Ref.16
Mutagenesis7051Y → F: Nuclear localization to the same extent as wild-type; when associated with A-609. Ref.16
Mutagenesis7271S → A: Decreased transcriptional activation. Ref.15
Sequence conflict161E → K in AAA19452. Ref.2
Sequence conflict251S → T in AAA19452. Ref.2
Sequence conflict251S → T in AAC52612. Ref.4
Sequence conflict3941M → I in AAA37254. Ref.1

Secondary structure

................................................................................... 770
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Stat3A [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 6C00626711C8012D

FASTA77088,054
        10         20         30         40         50         60 
MAQWNQLQQL DTRYLEQLHQ LYSDSFPMEL RQFLAPWIES QDWAYAASKE SHATLVFHNL 

        70         80         90        100        110        120 
LGEIDQQYSR FLQESNVLYQ HNLRRIKQFL QSRYLEKPME IARIVARCLW EESRLLQTAA 

       130        140        150        160        170        180 
TAAQQGGQAN HPTAAVVTEK QQMLEQHLQD VRKRVQDLEQ KMKVVENLQD DFDFNYKTLK 

       190        200        210        220        230        240 
SQGDMQDLNG NNQSVTRQKM QQLEQMLTAL DQMRRSIVSE LAGLLSAMEY VQKTLTDEEL 

       250        260        270        280        290        300 
ADWKRRQQIA CIGGPPNICL DRLENWITSL AESQLQTRQQ IKKLEELQQK VSYKGDPIVQ 

       310        320        330        340        350        360 
HRPMLEERIV ELFRNLMKSA FVVERQPCMP MHPDRPLVIK TGVQFTTKVR LLVKFPELNY 

       370        380        390        400        410        420 
QLKIKVCIDK DSGDVAALRG SRKFNILGTN TKVMNMEESN NGSLSAEFKH LTLREQRCGN 

       430        440        450        460        470        480 
GGRANCDASL IVTEELHLIT FETEVYHQGL KIDLETHSLP VVVISNICQM PNAWASILWY 

       490        500        510        520        530        540 
NMLTNNPKNV NFFTKPPIGT WDQVAEVLSW QFSSTTKRGL SIEQLTTLAE KLLGPGVNYS 

       550        560        570        580        590        600 
GCQITWAKFC KENMAGKGFS FWVWLDNIID LVKKYILALW NEGYIMGFIS KERERAILST 

       610        620        630        640        650        660 
KPPGTFLLRF SESSKEGGVT FTWVEKDISG KTQIQSVEPY TKQQLNNMSF AEIIMGYKIM 

       670        680        690        700        710        720 
DATNILVSPL VYLYPDIPKE EAFGKYCRPE SQEHPEADPG SAAPYLKTKF ICVTPTTCSN 

       730        740        750        760        770 
TIDLPMSPRT LDSLMQFGNN GEGAEPSAGG QFESLTFDMD LTSECATSPM 

« Hide

Isoform Stat3B [UniParc].

Checksum: 09226A697966D947
Show »

FASTA72283,126
Isoform Del-701 [UniParc].

Checksum: A374A26FB9D28077
Show »

FASTA76987,967

References

« Hide 'large scale' references
[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 STAT3A), PROTEIN SEQUENCE OF 154-158; 181-185 AND 632-640.
Strain: BALB/c.
Tissue: Liver.
[2]"Acute phase response factor and additional members of the interferon-stimulated gene factor 3 family integrate diverse signals from cytokines, interferons, and growth factors."
Raz R., Durbin J.E., Levy D.E.
J. Biol. Chem. 269:24391-24395(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DEL-701).
Tissue: Brain.
[3]"Stat3: a STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6."
Zhong Z., Wen Z., Darnell J.E. Jr.
Science 264:95-98(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM STAT3A).
Tissue: Thymus.
[4]"Cooperative transcriptional activity of Jun and Stat3 beta, a short form of Stat3."
Schaefer T.S., Sanders L.K., Nathans D.
Proc. Natl. Acad. Sci. U.S.A. 92:9097-9101(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM STAT3B).
Strain: BALB/c and C57BL/6.
Tissue: Liver.
[5]"Structure of the mouse Stat 3/5 locus: evolution from Drosophila to zebrafish to mouse."
Miyoshi K., Cui Y., Riedlinger G., Robinson P., Lehoczky J., Zon L., Oka T., Dewar K., Hennighausen L.
Genomics 71:150-155(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM STAT3A).
Strain: 129/SvJ.
[6]"A mutant Stat5b with weaker DNA binding defines a key defective pathway in non-obese diabetic (NOD) mice."
Davoodi-Semiromi A., She J.-X.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM STAT3A).
Strain: C57BL/6J and NOD/LtJ.
[7]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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] (ISOFORM STAT3A).
Strain: FVB/N.
Tissue: Mammary gland.
[9]"Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation."
Wen Z., Zhong Z., Darnell J.E. Jr.
Cell 82:241-250(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-727, MUTAGENESIS.
[10]"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.
Tissue: Thymus.
[11]"FER kinase activation of Stat3 is determined by the N-terminal sequence."
Priel-Halachmi S., Ben-Dor I., Shpungin S., Tennenbaum T., Molavani H., Bachrach M., Salzberg S., Nir U.
J. Biol. Chem. 275:28902-28910(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY FER, INTERACTION WITH FER.
[12]"A Stat3-interacting protein (StIP1) regulates cytokine signal transduction."
Collum R.G., Brutsaert S., Lee G., Schindler C.
Proc. Natl. Acad. Sci. U.S.A. 97:10120-10125(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STATIP1.
[13]"MSK1 and JNKs mediate phosphorylation of STAT3 in UVA-irradiated mouse epidermal JB6 cells."
Zhang Y., Liu G., Dong Z.
J. Biol. Chem. 276:42534-42542(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-705 AND SER-727.
[14]"Identification of tyrosine residues in constitutively activated fibroblast growth factor receptor 3 involved in mitogenesis, Stat activation, and phosphatidylinositol 3-kinase activation."
Hart K.C., Robertson S.C., Donoghue D.J.
Mol. Biol. Cell 12:931-942(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-705.
[15]"Role of the TAK1-NLK-STAT3 pathway in TGF-beta-mediated mesoderm induction."
Ohkawara B., Shirakabe K., Hyodo-Miura J., Matsuo R., Ueno N., Matsumoto K., Shibuya H.
Genes Dev. 18:381-386(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NLK, PHOSPHORYLATION AT SER-727, MUTAGENESIS OF SER-727.
[16]"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, MUTAGENESIS OF VAL-77; LEU-78; PHE-174; ARG-609 AND TYR-705, INTERACTION WITH KPNA4 AND KPNA5, NUCLEAR IMPORT MOTIF.
[17]"SIPAR interacts with STAT3 to regulate its signal pathway."
Ning H., Rong Y., Zhang Y., Chang Z.
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 32:173-179(2005)
Cited for: INTERACTION WITH SIPAR.
Strain: Swiss Webster / NIH.
[18]"Stat3 regulates microtubules by antagonizing the depolymerization activity of stathmin."
Ng D.C., Lin B.H., Lim C.P., Huang G., Zhang T., Poli V., Cao X.
J. Cell Biol. 172:245-257(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STMN3.
[19]"BART is essential for nuclear retention of STAT3."
Muromoto R., Sekine Y., Imoto S., Ikeda O., Okayama T., Sato N., Matsuda T.
Int. Immunol. 20:395-403(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARL2BP.
[20]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[21]"Role of NEK6 in tumor promoter-induced transformation in JB6 C141 mouse skin epidermal cells."
Jeon Y.J., Lee K.Y., Cho Y.Y., Pugliese A., Kim H.G., Jeong C.H., Bode A.M., Dong Z.
J. Biol. Chem. 285:28126-28133(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-727, INTERACTION WITH NEK6.
[22]"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 IN RESPONSE TO KIT SIGNALING.
[23]"Cytoplasmic STAT3 represses autophagy by inhibiting PKR activity."
Shen S., Niso-Santano M., Adjemian S., Takehara T., Malik S.A., Minoux H., Souquere S., Marino G., Lachkar S., Senovilla L., Galluzzi L., Kepp O., Pierron G., Maiuri M.C., Hikita H., Kroemer R., Kroemer G.
Mol. Cell 48:667-680(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[24]"Innate Stat3-mediated induction of the antimicrobial protein Reg3gamma is required for host defense against MRSA pneumonia."
Choi S.M., McAleer J.P., Zheng M., Pociask D.A., Kaplan M.H., Qin S., Reinhart T.A., Kolls J.K.
J. Exp. Med. 210:551-561(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION.
[25]"Three-dimensional structure of the Stat3beta homodimer bound to DNA."
Becker S., Groner B., Mueller C.W.
Nature 394:145-151(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 136-716.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L29278 mRNA. Translation: AAA37254.1.
U08378 mRNA. Translation: AAA56668.1.
U06922 mRNA. Translation: AAA19452.1.
U30709 mRNA. Translation: AAC52612.1.
AF246978 Genomic DNA. Translation: AAL59017.1.
AY299489 mRNA. Translation: AAQ75418.1.
AY299490 mRNA. Translation: AAQ75419.1.
AL591466 Genomic DNA. Translation: CAM19461.1.
AL591466 Genomic DNA. Translation: CAX15620.1.
BC003806 mRNA. Translation: AAH03806.1.
CCDSCCDS25440.1. [P42227-1]
CCDS25441.1. [P42227-2]
CCDS48934.1. [P42227-3]
PIRI49508.
RefSeqNP_035616.1. NM_011486.4. [P42227-2]
NP_998824.1. NM_213659.2. [P42227-1]
NP_998825.1. NM_213660.2. [P42227-3]
UniGeneMm.249934.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BG1X-ray2.25A127-723[»]
3CWGX-ray3.05A/B127-688[»]
4E68X-ray2.58A127-723[»]
ProteinModelPortalP42227.
SMRP42227. Positions 2-715.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203523. 22 interactions.
DIPDIP-442N.
IntActP42227. 22 interactions.
MINTMINT-4135802.

Chemistry

BindingDBP42227.
ChEMBLCHEMBL5402.

PTM databases

PhosphoSiteP42227.

Proteomic databases

MaxQBP42227.
PaxDbP42227.
PRIDEP42227.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000092671; ENSMUSP00000090342; ENSMUSG00000004040. [P42227-3]
ENSMUST00000103114; ENSMUSP00000099403; ENSMUSG00000004040. [P42227-2]
ENSMUST00000127638; ENSMUSP00000120152; ENSMUSG00000004040. [P42227-1]
GeneID20848.
KEGGmmu:20848.
UCSCuc007lmp.1. mouse. [P42227-1]
uc007lmq.1. mouse. [P42227-3]

Organism-specific databases

CTD6774.
MGIMGI:103038. Stat3.

Phylogenomic databases

eggNOGNOG303257.
GeneTreeENSGT00750000117596.
HOGENOMHOG000220792.
HOVERGENHBG055669.
InParanoidA2A5D1.
KOK04692.
OMANKESHAT.
OrthoDBEOG73JKTT.
PhylomeDBP42227.
TreeFamTF318648.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.
REACT_200794. Mus musculus biological processes.

Gene expression databases

ArrayExpressP42227.
BgeeP42227.
GenevestigatorP42227.

Family and domain databases

Gene3D1.10.238.10. 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.
InterProIPR011992. 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]
PANTHERPTHR11801. PTHR11801. 1 hit.
PfamPF00017. SH2. 1 hit.
PF01017. STAT_alpha. 1 hit.
PF02864. STAT_bind. 1 hit.
PF02865. STAT_int. 1 hit.
[Graphical view]
SMARTSM00252. SH2. 1 hit.
SM00964. STAT_int. 1 hit.
[Graphical view]
SUPFAMSSF47655. SSF47655. 1 hit.
SSF48092. SSF48092. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEPS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTAT3. mouse.
EvolutionaryTraceP42227.
NextBio299623.
PROP42227.
SOURCESearch...

Entry information

Entry nameSTAT3_MOUSE
AccessionPrimary (citable) accession number: P42227
Secondary accession number(s): A2A5D1, B7ZC17
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot