Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Signal transducer and activator of transcription 3

Gene

STAT3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors. Once activated, recruits coactivators, such as NCOA1 or MED1, to the promoter region of the target gene (PubMed:17344214). 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. Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1 (PubMed:17344214). Mediates the effects of LEP on melanocortin production, body energy homeostasis and lactation (By similarity). May play an apoptotic role by transctivating BIRC5 expression under LEP activation (PubMed:18242580). Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity.By similarity7 Publications
(Microbial infection) 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

GO - Molecular functioni

  • chromatin DNA binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein dimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
  • RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  • RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding Source: BHF-UCL
  • signal transducer activity Source: ProtInc
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: BHF-UCL
  • transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding Source: BHF-UCL
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • transcription regulatory region DNA binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-1059683. Interleukin-6 signaling.
R-HSA-1433557. Signaling by SCF-KIT.
R-HSA-1839117. Signaling by FGFR1 fusion mutants.
R-HSA-186763. Downstream signal transduction.
R-HSA-198745. Signalling to STAT3.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-2586552. Signaling by Leptin.
R-HSA-2892247. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
R-HSA-452723. Transcriptional regulation of pluripotent stem cells.
R-HSA-982772. Growth hormone receptor signaling.
SignaLinkiP40763.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal transducer and activator of transcription 3Imported
Alternative name(s):
Acute-phase response factor
Gene namesi
Name:STAT3Imported
Synonyms:APRFImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: 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

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • mitochondrial inner membrane Source: Ensembl
  • nuclear chromatin Source: BHF-UCL
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • RNA polymerase II transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Hyperimmunoglobulin E recurrent infection syndrome, autosomal dominant (AD-HIES)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:147060
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; reduced DNA-binding ability. 3 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. 2 Publications
VAR_037370
Natural varianti395 – 3951N → Y in AD-HIES; unknown pathological significance; reduced DNA-binding ability. 1 Publication
VAR_075414
Natural varianti423 – 4231R → Q in AD-HIES. 1 Publication
VAR_037371
Natural varianti425 – 4251N → Y in AD-HIES; unknown pathological significance; reduced DNA-binding ability. 1 Publication
VAR_075415
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; reduced DNA-binding ability. 2 Publications
VAR_037379
Natural varianti644 – 6441Missing in AD-HIES. 1 Publication
VAR_037380
Natural varianti657 – 6571Y → C in AD-HIES; reduced DNA-binding ability. 2 Publications
VAR_037381
Autoimmune disease, multisystem, infantile-onset (ADMIO)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by early childhood onset of a spectrum of autoimmune manifestations affecting multiple organs, including insulin-dependent diabetes mellitus and autoimmune enteropathy or celiac disease. Other features include short stature, non-specific dermatitis, hypothyroidism, autoimmune arthritis, and delayed puberty.
See also OMIM:615952
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti392 – 3921K → R in ADMIO. 1 Publication
VAR_071885
Natural varianti646 – 6461N → K in ADMIO. 1 Publication
VAR_071886
Natural varianti658 – 6581K → N in ADMIO. 1 Publication
VAR_071887
Natural varianti716 – 7161T → M in ADMIO. 1 Publication
VAR_071888

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi434 – 4352EE → AA: Inhibits leptin-mediated transactivation of CCND1 promoter. No effect on interaction with INPP5F. 2 Publications
Mutagenesisi705 – 7051Y → F: Inhibits leptin-mediated transactivation of CCND1 promoter. 1 Publication

Keywords - Diseasei

Diabetes mellitus, Disease mutation, Dwarfism

Organism-specific databases

MalaCardsiSTAT3.
MIMi147060. phenotype.
615952. phenotype.
Orphaneti2314. Autosomal dominant hyper-IgE syndrome.
PharmGKBiPA337.

Chemistry

ChEMBLiCHEMBL4026.

Polymorphism and mutation databases

BioMutaiSTAT3.
DMDMi48429227.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 770769Signal transducer and activator of transcription 3PRO_0000182417Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei705 – 7051Phosphotyrosine; by FER and PTK6Combined sources4 Publications
Modified residuei714 – 7141PhosphothreonineCombined sources
Modified residuei727 – 7271Phosphoserine; by DYRK2, NLK, NEK6, IRAK1, RPS6KA5, ZIPK/DAPK3 and PKC/PRKCECombined sources7 Publications
Isoform Del-701 (identifier: P40763-2)
Modified residuei704 – 7041PhosphotyrosineCombined sources

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, LEP 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. Phosphorylation 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 similarity13 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP40763.
MaxQBiP40763.
PaxDbiP40763.
PeptideAtlasiP40763.
PRIDEiP40763.

PTM databases

iPTMnetiP40763.
PhosphoSiteiP40763.

Miscellaneous databases

PMAP-CutDBP40763.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP40763.
CleanExiHS_STAT3.
ExpressionAtlasiP40763. baseline and differential.
GenevisibleiP40763. HS.

Organism-specific databases

HPAiCAB003859.
CAB068241.
CAB068242.
HPA001671.
HPA058603.

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 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). Interacts with STAT3; the interaction is independent of STAT3 TYR-705 phosphorylation status (PubMed:25476455). Interacts with FGFR4 (PubMed:26675719).By similarity19 Publications
(Microbial infection) Interacts with HCV core protein.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-518675,EBI-518675
Q9DUM34EBI-518675,EBI-7971837From a different organism.
BCKDKO148742EBI-518675,EBI-1046765
BICD1Q96G012EBI-518675,EBI-1104509
BLKP514513EBI-518675,EBI-2105445
BMXP518134EBI-518675,EBI-696657
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
EGFRP0053314EBI-518675,EBI-297353
ERBB2P046269EBI-518675,EBI-641062
EZH2Q159105EBI-518675,EBI-530054
FZD2Q143325EBI-518675,EBI-6254477
GADD45GIP1Q8TAE84EBI-518675,EBI-372506
GNL3Q9BVP22EBI-518675,EBI-641642
KHDRBS1Q076662EBI-518675,EBI-1364
LMO2P257913EBI-518675,EBI-739696
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
SP1P080474EBI-518675,EBI-298336
SRIP306262EBI-518675,EBI-750459
STAT1P422243EBI-518675,EBI-1057697
SULT2A1Q065202EBI-518675,EBI-3921363
SYKP434054EBI-518675,EBI-78302

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein dimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB
  • RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112651. 228 interactions.
DIPiDIP-33584N.
IntActiP40763. 156 interactions.
MINTiMINT-146801.
STRINGi9606.ENSP00000264657.

Chemistry

BindingDBiP40763.

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

eggNOGiKOG3667. Eukaryota.
ENOG410XPN8. LUCA.
GeneTreeiENSGT00760000119236.
HOGENOMiHOG000220792.
HOVERGENiHBG055669.
InParanoidiP40763.
KOiK04692.
OMAiNSMSFAE.
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. AlignAdd to basket

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

        10         20         30         40         50
MAQWNQLQQL DTRYLEQLHQ LYSDSFPMEL RQFLAPWIES QDWAYAASKE
60 70 80 90 100
SHATLVFHNL LGEIDQQYSR FLQESNVLYQ HNLRRIKQFL QSRYLEKPME
110 120 130 140 150
IARIVARCLW EESRLLQTAA TAAQQGGQAN HPTAAVVTEK QQMLEQHLQD
160 170 180 190 200
VRKRVQDLEQ KMKVVENLQD DFDFNYKTLK SQGDMQDLNG NNQSVTRQKM
210 220 230 240 250
QQLEQMLTAL DQMRRSIVSE LAGLLSAMEY VQKTLTDEEL ADWKRRQQIA
260 270 280 290 300
CIGGPPNICL DRLENWITSL AESQLQTRQQ IKKLEELQQK VSYKGDPIVQ
310 320 330 340 350
HRPMLEERIV ELFRNLMKSA FVVERQPCMP MHPDRPLVIK TGVQFTTKVR
360 370 380 390 400
LLVKFPELNY QLKIKVCIDK DSGDVAALRG SRKFNILGTN TKVMNMEESN
410 420 430 440 450
NGSLSAEFKH LTLREQRCGN GGRANCDASL IVTEELHLIT FETEVYHQGL
460 470 480 490 500
KIDLETHSLP VVVISNICQM PNAWASILWY NMLTNNPKNV NFFTKPPIGT
510 520 530 540 550
WDQVAEVLSW QFSSTTKRGL SIEQLTTLAE KLLGPGVNYS GCQITWAKFC
560 570 580 590 600
KENMAGKGFS FWVWLDNIID LVKKYILALW NEGYIMGFIS KERERAILST
610 620 630 640 650
KPPGTFLLRF SESSKEGGVT FTWVEKDISG KTQIQSVEPY TKQQLNNMSF
660 670 680 690 700
AEIIMGYKIM DATNILVSPL VYLYPDIPKE EAFGKYCRPE SQEHPEADPG
710 720 730 740 750
SAAPYLKTKF ICVTPTTCSN TIDLPMSPRT LDSLMQFGNN GEGAEPSAGG
760 770
QFESLTFDME LTSECATSPM
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.

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; reduced DNA-binding ability. 3 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. 2 Publications
VAR_037370
Natural varianti392 – 3921K → R in ADMIO. 1 Publication
VAR_071885
Natural varianti395 – 3951N → Y in AD-HIES; unknown pathological significance; reduced DNA-binding ability. 1 Publication
VAR_075414
Natural varianti423 – 4231R → Q in AD-HIES. 1 Publication
VAR_037371
Natural varianti425 – 4251N → Y in AD-HIES; unknown pathological significance; reduced DNA-binding ability. 1 Publication
VAR_075415
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; reduced DNA-binding ability. 2 Publications
VAR_037379
Natural varianti644 – 6441Missing in AD-HIES. 1 Publication
VAR_037380
Natural varianti646 – 6461N → K in ADMIO. 1 Publication
VAR_071886
Natural varianti657 – 6571Y → C in AD-HIES; reduced DNA-binding ability. 2 Publications
VAR_037381
Natural varianti658 – 6581K → N in ADMIO. 1 Publication
VAR_071887
Natural varianti716 – 7161T → M in ADMIO. 1 Publication
VAR_071888

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:
EMBLi
GenBanki
DDBJi
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]
CCDS59288.1. [P40763-3]
PIRiA54444.
RefSeqiNP_003141.2. NM_003150.3. [P40763-2]
NP_644805.1. NM_139276.2. [P40763-1]
NP_998827.1. NM_213662.1. [P40763-3]
XP_005257673.2. XM_005257616.2. [P40763-2]
XP_005257674.2. XM_005257617.2. [P40763-1]
XP_011523447.1. XM_011525145.1. [P40763-1]
XP_011523448.1. XM_011525146.1. [P40763-3]
UniGeneiHs.463059.

Genome annotation databases

EnsembliENST00000264657; ENSP00000264657; ENSG00000168610. [P40763-1]
ENST00000404395; ENSP00000384943; ENSG00000168610. [P40763-2]
ENST00000585517; ENSP00000467000; ENSG00000168610. [P40763-3]
ENST00000588969; ENSP00000467985; ENSG00000168610. [P40763-1]
GeneIDi6774.
KEGGihsa:6774.
UCSCiuc002hzl.2. human. [P40763-1]

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:
EMBLi
GenBanki
DDBJi
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]
CCDS59288.1. [P40763-3]
PIRiA54444.
RefSeqiNP_003141.2. NM_003150.3. [P40763-2]
NP_644805.1. NM_139276.2. [P40763-1]
NP_998827.1. NM_213662.1. [P40763-3]
XP_005257673.2. XM_005257616.2. [P40763-2]
XP_005257674.2. XM_005257617.2. [P40763-1]
XP_011523447.1. XM_011525145.1. [P40763-1]
XP_011523448.1. XM_011525146.1. [P40763-3]
UniGeneiHs.463059.

3D structure databases

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

Protein-protein interaction databases

BioGridi112651. 228 interactions.
DIPiDIP-33584N.
IntActiP40763. 156 interactions.
MINTiMINT-146801.
STRINGi9606.ENSP00000264657.

Chemistry

BindingDBiP40763.
ChEMBLiCHEMBL4026.

PTM databases

iPTMnetiP40763.
PhosphoSiteiP40763.

Polymorphism and mutation databases

BioMutaiSTAT3.
DMDMi48429227.

Proteomic databases

EPDiP40763.
MaxQBiP40763.
PaxDbiP40763.
PeptideAtlasiP40763.
PRIDEiP40763.

Protocols and materials databases

DNASUi6774.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264657; ENSP00000264657; ENSG00000168610. [P40763-1]
ENST00000404395; ENSP00000384943; ENSG00000168610. [P40763-2]
ENST00000585517; ENSP00000467000; ENSG00000168610. [P40763-3]
ENST00000588969; ENSP00000467985; ENSG00000168610. [P40763-1]
GeneIDi6774.
KEGGihsa:6774.
UCSCiuc002hzl.2. human. [P40763-1]

Organism-specific databases

CTDi6774.
GeneCardsiSTAT3.
GeneReviewsiSTAT3.
HGNCiHGNC:11364. STAT3.
HPAiCAB003859.
CAB068241.
CAB068242.
HPA001671.
HPA058603.
MalaCardsiSTAT3.
MIMi102582. gene.
147060. phenotype.
615952. phenotype.
neXtProtiNX_P40763.
Orphaneti2314. Autosomal dominant hyper-IgE syndrome.
PharmGKBiPA337.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3667. Eukaryota.
ENOG410XPN8. LUCA.
GeneTreeiENSGT00760000119236.
HOGENOMiHOG000220792.
HOVERGENiHBG055669.
InParanoidiP40763.
KOiK04692.
OMAiNSMSFAE.
OrthoDBiEOG73JKTT.
PhylomeDBiP40763.
TreeFamiTF318648.

Enzyme and pathway databases

ReactomeiR-HSA-1059683. Interleukin-6 signaling.
R-HSA-1433557. Signaling by SCF-KIT.
R-HSA-1839117. Signaling by FGFR1 fusion mutants.
R-HSA-186763. Downstream signal transduction.
R-HSA-198745. Signalling to STAT3.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-2586552. Signaling by Leptin.
R-HSA-2892247. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
R-HSA-452723. Transcriptional regulation of pluripotent stem cells.
R-HSA-982772. Growth hormone receptor signaling.
SignaLinkiP40763.

Miscellaneous databases

ChiTaRSiSTAT3. human.
GeneWikiiSTAT3.
GenomeRNAii6774.
NextBioi26438.
PMAP-CutDBP40763.
PROiP40763.
SOURCEiSearch...

Gene expression databases

BgeeiP40763.
CleanExiHS_STAT3.
ExpressionAtlasiP40763. baseline and differential.
GenevisibleiP40763. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "leptin-induced growth stimulation of breast cancer cells involves recruitment of histone acetyltransferases and mediator complex to CYCLIN D1 promoter via activation of Stat3."
    Saxena N.K., Vertino P.M., Anania F.A., Sharma D.
    J. Biol. Chem. 282:13316-13325(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF 434-GLU-GLU-435 AND TYR-705.
  31. "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.
  32. "up-regulation of survivin by leptin/STAT3 signaling in MCF-7 cells."
    Jiang H., Yu J., Guo H., Song H., Chen S.
    Biochem. Biophys. Res. Commun. 368:1-5(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  33. "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.
  34. "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.
  35. Cited for: INTERACTION WITH ARL2BP, PHOSPHORYLATION AT SERINE RESIDUES, SUBCELLULAR LOCATION.
  36. "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.
  37. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  38. "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].
  39. "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.
  40. "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.
  41. "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.
  42. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  43. "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.
  44. Cited for: FUNCTION, INTERACTION WITH EIF2AK2.
  45. "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, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  46. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  47. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705; THR-714 AND SER-727, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-704 (ISOFORM DEL-701), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  48. "Inositol Polyphosphate-5-Phosphatase F (INPP5F) inhibits STAT3 activity and suppresses gliomas tumorigenicity."
    Kim H.S., Li A., Ahn S., Song H., Zhang W.
    Sci. Rep. 4:7330-7330(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INPP5F, MUTAGENESIS OF TYR-705.
  49. "Germline variant FGFR4 p.G388R exposes a membrane-proximal STAT3 binding site."
    Ulaganathan V.K., Sperl B., Rapp U.R., Ullrich A.
    Nature 528:570-574(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FGFR4.
  50. 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.
  51. "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.
  52. "Signal transducer and activator of transcription 3 mutation with invasive eosinophilic disease."
    Crosby K., Swender D., Chernin L., Hafez-Khayyata S., Ochs H., Tcheurekdjian H., Hostoffer R.
    Allergy Rhinol. (Providence) 3:E94-E97(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AD-HIES ILE-389.
  53. Cited for: INVOLVEMENT IN ADMIO, VARIANTS ADMIO ARG-392; LYS-646; ASN-658 AND MET-716.
  54. "Functional characterization of two new STAT3 mutations associated with hyper-IgE syndrome in a Mexican cohort."
    Alcantara-Montiel J.C., Staines-Boone T., Lopez-Herrera G., Espinosa-Rosales F., Espinosa-Padilla S.E., Hernandez-Rivas R., Santos-Argumedo L.
    Clin. Genet. 89:217-221(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS AD-HIES TRP-382; TYR-395; TYR-425; MET-637 AND CYS-657, CHARACTERIZATION OF VARIANTS AD-HIES TRP-382; TYR-395; TYR-425; MET-637 AND CYS-657, PHOSPHORYLATION AT TYR-705 AND SER-727.

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: April 13, 2016
This is version 180 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.