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Protein

Signal transducer and activator of transcription 3

Gene

Stat3

Organism
Mus musculus (Mouse)
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. 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. Acts as a regulator of inflammatory response by regulating differentiation of naive CD4+ T-cells into T-helper Th17 or regulatory T-cells (Treg): deacetylation and oxidation of lysine residues by LOXL3, leads to disrupt STAT3 dimerization and inhibit its transcription activity (By similarity). Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1 (By similarity). Mediates the effects of LEP on melanocortin production, body energy homeostasis and lactation (PubMed:12594516). May play an apoptotic role by transctivating BIRC5 expression under LEP activation (PubMed:16825198). Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity (By similarity). Plays a crucial role in basal beta cell functions, such as regulation of insulin secretion (PubMed:20215569). Plays an important role in host defense in methicillin-resistant S.aureus lung infection by regulating the expression of the antimicrobial lectin REG3G (PubMed:23401489).By similarity6 Publications

Miscellaneous

Involved in the gp130-mediated signaling pathway.

GO - Molecular functioni

GO - Biological processi

  • acute-phase response Source: UniProtKB-KW
  • aging Source: Ensembl
  • astrocyte differentiation Source: UniProtKB
  • cell proliferation Source: MGI
  • cellular response to cytokine stimulus Source: MGI
  • cellular response to hormone stimulus Source: MGI
  • cellular response to leptin stimulus Source: UniProtKB
  • cellular response to organic cyclic compound Source: MGI
  • cytokine-mediated signaling pathway Source: UniProtKB
  • eating behavior Source: MGI
  • energy homeostasis Source: UniProtKB
  • eye photoreceptor cell differentiation Source: MGI
  • glucose homeostasis Source: UniProtKB
  • growth hormone receptor signaling pathway Source: MGI
  • inflammatory response Source: UniProtKB
  • interleukin-12-mediated signaling pathway Source: Reactome
  • interleukin-6-mediated signaling pathway Source: UniProtKB
  • intracellular receptor signaling pathway Source: MGI
  • JAK-STAT cascade Source: UniProtKB
  • JAK-STAT cascade involved in growth hormone signaling pathway Source: BHF-UCL
  • leptin-mediated signaling pathway Source: UniProtKB
  • miRNA mediated inhibition of translation Source: MGI
  • mRNA transcription from RNA polymerase II promoter Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of cell proliferation Source: MGI
  • negative regulation of glycolytic process Source: MGI
  • negative regulation of hydrogen peroxide biosynthetic process Source: Ensembl
  • negative regulation of neuron death Source: Ensembl
  • negative regulation of neuron migration Source: MGI
  • negative regulation of stem cell differentiation Source: MGI
  • phosphorylation Source: UniProtKB
  • positive regulation of ATP biosynthetic process Source: Ensembl
  • positive regulation of cell proliferation Source: Ensembl
  • positive regulation of erythrocyte differentiation Source: UniProtKB
  • positive regulation of gene expression Source: BHF-UCL
  • positive regulation of gene silencing by miRNA Source: MGI
  • positive regulation of growth factor dependent skeletal muscle satellite cell proliferation Source: Ensembl
  • positive regulation of metalloendopeptidase activity Source: MGI
  • positive regulation of Notch signaling pathway Source: UniProtKB
  • positive regulation of pri-miRNA transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • positive regulation of tyrosine phosphorylation of STAT protein Source: Reactome
  • protein import into nucleus Source: UniProtKB
  • radial glial cell differentiation Source: UniProtKB
  • regulation of cell cycle Source: UniProtKB
  • regulation of feeding behavior Source: UniProtKB
  • regulation of mitochondrial membrane permeability Source: Ensembl
  • regulation of multicellular organism growth Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
  • response to drug Source: Ensembl
  • response to estradiol Source: MGI
  • response to ethanol Source: Ensembl
  • response to leptin Source: UniProtKB
  • sexual reproduction Source: MGI
  • stem cell population maintenance Source: MGI
  • temperature homeostasis Source: MGI
  • T-helper 17 cell lineage commitment Source: UniProtKB
  • transcription from RNA polymerase II promoter Source: MGI

Keywordsi

Molecular functionActivator, DNA-binding
Biological processAcute phase, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-1266695. Interleukin-7 signaling.
R-MMU-1433557. Signaling by SCF-KIT.
R-MMU-186763. Downstream signal transduction.
R-MMU-2586551. Signaling by Leptin.
R-MMU-447115. Interleukin-12 family signaling.
R-MMU-6783589. Interleukin-6 family signaling.
R-MMU-6783783. Interleukin-10 signaling.
R-MMU-6785807. Interleukin-4 and 13 signaling.
R-MMU-8849474. PTK6 Activates STAT3.
R-MMU-8854691. Interleukin-20 family signaling.
R-MMU-8875791. MET activates STAT3.
R-MMU-8983432. Interleukin-15 signaling.
R-MMU-8984722. Interleukin-35 Signalling.

Protein family/group databases

MoonProtiP42227.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal transducer and activator of transcription 3
Alternative name(s):
Acute-phase response factor
Gene namesi
Name:Stat3
Synonyms:Aprf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:103038. Stat3.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Early embryonic lethality, day 6.5-7.5. Conditional, tissue specific mutants are variably viable and show diverse defects including obesity, diabetes, thermal dysregulation and infertility.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi77V → A: No effect on nuclear import; when associated with A-78 and W-174. 1 Publication1
Mutagenesisi78L → A: No effect on nuclear import; when associated with A-77 and W-174. 1 Publication1
Mutagenesisi174F → W: No effect on nuclear import; when associated with A-77 and A-78. 1 Publication1
Mutagenesisi609R → A: Nuclear localization to the same extent as wild-type; when associated with F-705. 1 Publication1
Mutagenesisi705Y → F: Nuclear localization to the same extent as wild-type; when associated with A-609. 1 Publication1
Mutagenesisi727S → A: Decreased transcriptional activation. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5402.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001824182 – 770Signal transducer and activator of transcription 3Add BLAST769

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei601Allysine; alternateBy similarity1
Modified residuei601N6-acetyllysine; alternateBy similarity1
Modified residuei615Allysine; alternateBy similarity1
Modified residuei615N6-acetyllysine; alternateBy similarity1
Modified residuei631Allysine; alternateBy similarity1
Modified residuei631N6-acetyllysine; alternateBy similarity1
Modified residuei685Allysine; alternateBy similarity1
Modified residuei685N6-acetyllysine; alternateBy similarity1
Modified residuei705Phosphotyrosine; by FER and PTK6Combined sources2 Publications1
Modified residuei707N6-acetyllysineBy similarity1
Modified residuei714PhosphothreonineCombined sources1
Modified residuei727PhosphoserineCombined sources1
Modified residuei727Phosphoserine; by DYRK2, NLK, NEK6, IRAK1, RPS6KA5, ZIPK/DAPK3 and PKC/PRKCECombined sources4 Publications1

Post-translational modificationi

Activated through tyrosine phosphorylation by BMX. Tyrosine phosphorylated in response to IL6, IL11, CNTF, LIF, KITLG/SCF, CSF1, EGF, PDGF, IFN-alpha, LEP 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). Phosphorylation at Tyr-705 by FER or PTK6 leads to an increase of its transcriptional activity.By similarity9 Publications
Acetylated on lysine residues by CREBBP. Deacetylation by LOXL3 leads to disrupt STAT3 dimerization and inhibit STAT3 transcription activity. Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated.By similarity
Some lysine residues are oxidized to allysine by LOXL3, leading to disrupt STAT3 dimerization and inhibit STAT3 transcription activity. Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP42227.
MaxQBiP42227.
PaxDbiP42227.
PeptideAtlasiP42227.
PRIDEiP42227.

PTM databases

iPTMnetiP42227.
PhosphoSitePlusiP42227.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiENSMUSG00000004040.
ExpressionAtlasiP42227. baseline and differential.
GenevisibleiP42227. MM.

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) (By similarity). Interacts with FGFR4 (By similarity). Interacts with STAT3; the interaction is independent of STAT3 TYR-705 phosphorylation status (By similarity). Interacts with OCAD1 (PubMed:23972987).By similarity11 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • CCR5 chemokine receptor binding Source: Ensembl
  • glucocorticoid receptor binding Source: Ensembl
  • identical protein binding Source: IntAct
  • protein dimerization activity Source: MGI
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein phosphatase binding Source: MGI
  • RNA polymerase II repressing transcription factor binding Source: MGI
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi203523. 23 interactors.
CORUMiP42227.
DIPiDIP-442N.
IntActiP42227. 32 interactors.
MINTiMINT-4135802.
STRINGi10090.ENSMUSP00000120152.

Chemistry databases

BindingDBiP42227.

Structurei

Secondary structure

1770
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 8Combined sources6
Turni12 – 14Combined sources3
Helixi15 – 20Combined sources6
Beta strandi24 – 26Combined sources3
Helixi28 – 33Combined sources6
Helixi35 – 40Combined sources6
Helixi43 – 46Combined sources4
Helixi50 – 73Combined sources24
Helixi77 – 94Combined sources18
Helixi98 – 120Combined sources23
Helixi139 – 180Combined sources42
Helixi199 – 237Combined sources39
Helixi239 – 251Combined sources13
Helixi261 – 290Combined sources30
Turni297 – 301Combined sources5
Helixi302 – 320Combined sources19
Beta strandi321 – 328Combined sources8
Beta strandi338 – 340Combined sources3
Beta strandi345 – 353Combined sources9
Helixi356 – 358Combined sources3
Turni359 – 361Combined sources3
Beta strandi363 – 369Combined sources7
Helixi371 – 373Combined sources3
Beta strandi375 – 377Combined sources3
Beta strandi384 – 388Combined sources5
Beta strandi391 – 393Combined sources3
Helixi400 – 402Combined sources3
Beta strandi404 – 415Combined sources12
Beta strandi418 – 420Combined sources3
Helixi426 – 428Combined sources3
Helixi432 – 434Combined sources3
Beta strandi439 – 447Combined sources9
Beta strandi450 – 457Combined sources8
Beta strandi461 – 466Combined sources6
Helixi467 – 469Combined sources3
Helixi470 – 483Combined sources14
Helixi492 – 494Combined sources3
Helixi501 – 515Combined sources15
Helixi522 – 533Combined sources12
Helixi546 – 549Combined sources4
Beta strandi557 – 559Combined sources3
Helixi561 – 574Combined sources14
Beta strandi575 – 577Combined sources3
Helixi578 – 581Combined sources4
Helixi593 – 595Combined sources3
Turni596 – 600Combined sources5
Beta strandi608 – 610Combined sources3
Beta strandi619 – 621Combined sources3
Beta strandi626 – 628Combined sources3
Helixi642 – 645Combined sources4
Helixi650 – 653Combined sources4
Beta strandi664 – 666Combined sources3
Beta strandi671 – 673Combined sources3
Turni674 – 676Combined sources3
Turni679 – 683Combined sources5
Helixi684 – 686Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BG1X-ray2.25A127-723[»]
3CWGX-ray3.05A/B127-688[»]
4E68X-ray2.58A127-723[»]
4ZIAX-ray2.70A/B/C/D/E3-127[»]
ProteinModelPortaliP42227.
SMRiP42227.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42227.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini580 – 670SH2PROSITE-ProRule annotationAdd BLAST91

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi150 – 162Essential for nuclear importAdd BLAST13

Sequence similaritiesi

Belongs to the transcription factor STAT family.Curated

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiKOG3667. Eukaryota.
ENOG410XPN8. LUCA.
GeneTreeiENSGT00760000119236.
HOGENOMiHOG000220792.
HOVERGENiHBG055669.
InParanoidiP42227.
KOiK04692.
OMAiNSMSFAE.
OrthoDBiEOG091G03O3.
PhylomeDBiP42227.
TreeFamiTF318648.

Family and domain databases

CDDicd10374. SH2_STAT3. 1 hit.
Gene3Di1.10.532.10. 1 hit.
2.60.40.630. 1 hit.
3.30.505.10. 1 hit.
InterProiView protein in InterPro
IPR008967. p53-like_TF_DNA-bd.
IPR000980. SH2.
IPR036860. SH2_dom_sf.
IPR001217. STAT.
IPR035855. STAT3_SH2.
IPR036535. STAT_N_sf.
IPR013800. STAT_TF_alpha.
IPR015988. STAT_TF_coiled-coil.
IPR013801. STAT_TF_DNA-bd.
IPR012345. STAT_TF_DNA-bd_N.
IPR013799. STAT_TF_prot_interaction.
PANTHERiPTHR11801. PTHR11801. 1 hit.
PfamiView protein in Pfam
PF00017. SH2. 1 hit.
PF01017. STAT_alpha. 1 hit.
PF02864. STAT_bind. 1 hit.
PF02865. STAT_int. 1 hit.
SMARTiView protein in SMART
SM00964. STAT_int. 1 hit.
SUPFAMiSSF47655. SSF47655. 1 hit.
SSF48092. SSF48092. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiView protein in PROSITE
PS50001. SH2. 1 hit.

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 Stat3A (identifier: P42227-1) [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
QFESLTFDMD LTSECATSPM
Length:770
Mass (Da):88,054
Last modified:October 1, 1996 - v2
Checksum:i6C00626711C8012D
GO
Isoform Stat3B (identifier: P42227-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     716-770: TTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLTFDMDLTSECATSPM → FIDAVWK

Show »
Length:722
Mass (Da):83,126
Checksum:i09226A697966D947
GO
Isoform Del-701 (identifier: P42227-3) [UniParc]FASTAAdd to basket

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

Show »
Length:769
Mass (Da):87,967
Checksum:iA374A26FB9D28077
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti16E → K in AAA19452 (PubMed:7523373).Curated1
Sequence conflicti25S → T in AAA19452 (PubMed:7523373).Curated1
Sequence conflicti25S → T in AAC52612 (PubMed:7568080).Curated1
Sequence conflicti394M → I in AAA37254 (PubMed:7512451).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_010475701Missing in isoform Del-701. 1 Publication1
Alternative sequenceiVSP_006287716 – 770TTCSN…ATSPM → FIDAVWK in isoform Stat3B. 1 PublicationAdd BLAST55

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS25440.1. [P42227-1]
CCDS25441.1. [P42227-2]
CCDS48934.1. [P42227-3]
PIRiI49508.
RefSeqiNP_998824.1. NM_213659.3. [P42227-1]
NP_998825.1. NM_213660.3. [P42227-3]
UniGeneiMm.249934.
Mm.473190.

Genome annotation databases

EnsembliENSMUST00000092671; ENSMUSP00000090342; ENSMUSG00000004040. [P42227-3]
ENSMUST00000103114; ENSMUSP00000099403; ENSMUSG00000004040. [P42227-2]
ENSMUST00000127638; ENSMUSP00000120152; ENSMUSG00000004040. [P42227-1]
GeneIDi20848.
KEGGimmu:20848.
UCSCiuc007lmp.1. mouse. [P42227-1]
uc007lmq.1. mouse. [P42227-3]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiSTAT3_MOUSE
AccessioniPrimary (citable) accession number: P42227
Secondary accession number(s): A2A5D1, B7ZC17
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 1, 1996
Last modified: November 22, 2017
This is version 201 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families