Signal transducer and activator of transcription 3

Preferred order of sections

Names and origin

Protein names

Recommended name:
Signal transducer and activator of transcription 3

Alternative name(s):
Acute-phase response factor

Gene names

Name:	Stat3
Synonyms:	Aprf

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	770 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.14
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. 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.
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. 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
Miscellaneous	Involved in the gp130-mediated signaling pathway.
Sequence similarities	Belongs to the transcription factor STAT family. Contains 1 SH2 domain.

Ontologies

Keywords
Biological process	Acute phase Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	SH2 domain
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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 electronic annotation. Source: Compara 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 15096606 PubMed 15659653 PubMed 19666510. Source: MGI 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 response to drug Inferred from electronic annotation. Source: Compara response to estradiol stimulus Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara 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
Cellular_component	cytosol 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_function	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: Compara 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 transcription factor binding Inferred from sequence or structural similarity. Source: UniProtKB transcription regulatory region DNA binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Bank1	Q80VH0	4	EBI-602878,EBI-646949
Erbb2	P70424	4	EBI-602878,EBI-2945468
Hax1	O35387	11	EBI-602878,EBI-642449
IL6ST	P40189	2	EBI-602878,EBI-1030834	From a different organism.
Pgr	Q00175	4	EBI-602878,EBI-346821

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 770

770

Signal transducer and activator of transcription 3

PRO_0000182418

Regions

Domain

580 – 670

91

SH2

Motif

150 – 162

13

Essential for nuclear import

Amino acid modifications

Modified residue

705

1

Phosphotyrosine; by FER and PTK6 Ref.13 Ref.14 Ref.20

Modified residue

727

1

Phosphoserine; by DYRK2, NLK, NEK6, IRAK1, RPS6KA5, ZIPK/DAPK3 and PKC/PRKCE Probable

Natural variations

Alternative sequence

701

1

Missing in isoform Del-701.

VSP_010475

Alternative sequence

716 – 770

55

TTCSN…ATSPM → FIDAVWK in isoform Stat3B.

VSP_006287

Experimental info

Mutagenesis

77

1

V → A: No effect on nuclear import; when associated with A-78 and W-174. Ref.16

Mutagenesis

78

1

L → A: No effect on nuclear import; when associated with A-77 and W-174. Ref.16

Mutagenesis

174

1

F → W: No effect on nuclear import; when associated with A-77 and A-78. Ref.16

Mutagenesis

609

1

R → A: Nuclear localization to the same extent as wild-type; when associated with F-705. Ref.16

Mutagenesis

705

1

Y → F: Nuclear localization to the same extent as wild-type; when associated with A-609. Ref.16

Mutagenesis

727

1

S → A: Decreased transcriptional activation. Ref.15

Sequence conflict

16

1

E → K in AAA19452. Ref.2

Sequence conflict

25

1

S → T in AAA19452. Ref.2

Sequence conflict

25

1

S → T in AAC52612. Ref.4

Sequence conflict

394

1

M → I in AAA37254. Ref.1

Secondary structure

1

.

770

Helix Strand Turn

Details...

Sequences

Sequence		Length	Mass (Da)
Isoform Stat3A [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 6C00626711C8012D Show »	FASTA	770	88,054
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 »	FASTA	722	83,126
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 ICVTPFIDAV WK « Hide
Isoform Del-701 [UniParc]. Checksum: A374A26FB9D28077 Show »	FASTA	769	87,967
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 AAPYLKTKFI CVTPTTCSNT 730 740 750 760 IDLPMSPRTL DSLMQFGNNG EGAEPSAGGQ FESLTFDMDL TSECATSPM « Hide

References

	« Hide 'large scale' referencesShow '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. 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, MASS SPECTROMETRY. 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]	"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.

IPI

IPI00227814.
IPI00228955.
IPI00753792.

PIR

I49508.

RefSeq

NP_035616.1. NM_011486.4.
NP_998824.1. NM_213659.2.
NP_998825.1. NM_213660.2.

UniGene

Mm.249934.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BG1	X-ray	2.25	A	127-715	[»]
3CWG	X-ray	3.05	A/B	127-688	[»]
4E68	X-ray	2.58	A	127-715	[»]

ProteinModelPortal

P42227.

SMR

P42227. Positions 2-715.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-442N.

IntAct

P42227. 14 interactions.

MINT

MINT-4135802.

PTM databases

PhosphoSite

P42227.

Proteomic databases

PaxDb

P42227.

PRIDE

P42227.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000092671; ENSMUSP00000090342; ENSMUSG00000004040.
ENSMUST00000103114; ENSMUSP00000099403; ENSMUSG00000004040.
ENSMUST00000127638; ENSMUSP00000120152; ENSMUSG00000004040.

GeneID

20848.

KEGG

mmu:20848.

UCSC

uc007lmp.1. mouse.
uc007lmq.1. mouse.

Organism-specific databases

CTD

6774.

MGI

MGI:103038. Stat3.

Phylogenomic databases

eggNOG

NOG303257.

GeneTree

ENSGT00550000074337.

HOGENOM

HOG000220792.

HOVERGEN

HBG055669.

InParanoid

A2A5D1.

KO

K04692.

OMA

NKESHAT.

OrthoDB

EOG4G4GPS.

Enzyme and pathway databases

Reactome

REACT_107772. Immune System.

Gene expression databases

ArrayExpress

P42227.

Bgee

P42227.

Genevestigator

P42227.

GermOnline

ENSMUSG00000004040. Mus musculus.

Family and domain databases

Gene3D

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.

InterPro

IPR011992. EF-hand-like_dom.
IPR008967. p53-like_TF_DNA-bd.
IPR000980. SH2.
IPR013800. STAT_TF_alpha.
IPR015988. STAT_TF_coiled-coil.
IPR001217. STAT_TF_core.
IPR013801. STAT_TF_DNA-bd.
IPR012345. STAT_TF_DNA-bd_sub.
IPR013799. STAT_TF_prot_interaction.
[Graphical view]

PANTHER

PTHR11801. PTHR11801. 1 hit.

Pfam

PF00017. SH2. 1 hit.
PF01017. STAT_alpha. 1 hit.
PF02864. STAT_bind. 1 hit.
PF02865. STAT_int. 1 hit.
[Graphical view]

SMART

SM00252. SH2. 1 hit.
SM00964. STAT_int. 1 hit.
[Graphical view]

SUPFAM

SSF49417. P53_like_DNA_bnd. 1 hit.
SSF47655. STAT. 1 hit.
SSF48092. STAT. 1 hit.

PROSITE

PS50001. SH2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P42227.

ChEMBL

CHEMBL5402.

ChiTaRS

STAT3. mouse.

EvolutionaryTrace

P42227.

NextBio

299623.

SOURCE

Search...

Entry information

Entry name

STAT3_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 151 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents