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P40763

- STAT3_HUMAN

UniProt

P40763 - STAT3_HUMAN

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Protein
Signal transducer and activator of transcription 3
Gene
STAT3, APRF
Organism
Homo sapiens (Human)
Status
Reviewed - 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 and other growth factors. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the interleukin-6 (IL-6)-responsive elements identified in the promoters of various acute-phase protein genes. Activated by IL31 through IL31RA. Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity. Plays an important role in host defense in methicillin-resistant S.aureus lung infection by regulating the expression of the antimicrobial lectin REG3G By similarity.5 Publications

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

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

Names & Taxonomyi

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

Organism-specific databases

HGNCiHGNC:11364. STAT3.

Subcellular locationi

Cytoplasm. Nucleus
Note: Shuttles between the nucleus and the cytoplasm. Translocated into the nucleus upon tyrosine phosphorylation and dimerization, in response to signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4. Constitutive nuclear presence is independent of tyrosine phosphorylation. Predominantly present in the cytoplasm without stimuli. Upon leukemia inhibitory factor (LIF) stimulation, accumulates in the nucleus. The complex composed of BART and ARL2 plays an important role in the nuclear translocation and retention of STAT3. Identified in a complex with LYN and PAG1.3 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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

Keywords - Diseasei

Disease mutation

Organism-specific databases

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

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei705 – 7051Phosphotyrosine; by FER and PTK66 Publications
Modified residuei727 – 7271Phosphoserine; by DYRK2, NLK, NEK6, IRAK1, RPS6KA5, ZIPK/DAPK3 and PKC/PRKCE11 Publications

Post-translational modificationi

Tyrosine phosphorylated upon stimulation with EGF. Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4 By similarity. Activated through tyrosine phosphorylation by BMX. Tyrosine phosphorylated in response to IL6, IL11, LIF, CNTF, KITLG/SCF, CSF1, EGF, PDGF, IFN-alpha and OSM. Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus. Phosphorylated on serine upon DNA damage, probably by ATM or ATR. Serine phosphorylation is important for the formation of stable DNA-binding STAT3 homodimers and maximal transcriptional activity. ARL2BP may participate in keeping the phosphorylated state of STAT3 within the nucleus. Upon LPS challenge, phosphorylated within the nucleus by IRAK1. Upon erythropoietin treatment, phosphorylated on Ser-727 by RPS6KA5. Phosphoryation at Tyr-705 by PTK6 or FER leads to an increase of its transcriptional activity. Dephosphorylation on tyrosine residues by PTPN2 negatively regulates IL6/interleukin-6 signaling.12 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP40763.
PaxDbiP40763.
PeptideAtlasiP40763.
PRIDEiP40763.

PTM databases

PhosphoSiteiP40763.

Miscellaneous databases

PMAP-CutDBP40763.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiP40763.
BgeeiP40763.
CleanExiHS_STAT3.
GenevestigatoriP40763.

Organism-specific databases

HPAiCAB003859.
HPA001671.

Interactioni

Subunit structurei

Forms a homodimer or a heterodimer with a related family member (at least STAT1). Interacts with IL31RA, NCOA1, PELP1, SIPAR, SOCS7, STATIP1 and TMF1. Interacts with HCV core protein. Interacts with IL23R in presence of IL23. Interacts (via SH2 domain) with NLK. Interacts with ARL2BP; the interaction is enhanced by LIF and JAK1 expression By similarity. Interacts with KPNA4 and KPNA5; KPNA4 may be the primary mediator of nuclear import By similarity. Interacts with CAV2; the interaction is increased on insulin-induced tyrosine phosphorylation of CAV2 and leads to STAT3 activation By similarity. Interacts with ARL2BP; interaction is enhanced with ARL2. Interacts with NEK6 By similarity. Binds to CDK9 when activated and nuclear. Interacts with BMX. Interacts with ZIPK/DAPK3. Interacts with PIAS3; the interaction occurs on stimulation by IL6, CNTF or OSM and inhibits the DNA binding activity of STAT3. In prostate cancer cells, interacts with STAT3 and promotes DNA binding activity of STAT3. Interacts with STMN3, antagonizing its microtubule-destabilizing activity. Interacts with the 'Lys-129' acetylated form of BIRC5/survivin. Interacts with FER. Interacts (via SH2 domain) with EIF2AK2/PKR (via the kinase catalytic domain).18 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9DUM34EBI-518675,EBI-7971837From a different organism.
BCKDKO148742EBI-518675,EBI-1046765
BICD1Q96G012EBI-518675,EBI-1104509
CAPN1P073842EBI-518675,EBI-1542113
CORO1AP311462EBI-518675,EBI-1046676
CSF3RQ990624EBI-518675,EBI-7331284
DAXXQ9UER74EBI-518675,EBI-77321
DIRAS3O956613EBI-518675,EBI-6139214
ECH1Q130112EBI-518675,EBI-711968
ECHS1P300843EBI-518675,EBI-719602
EGFRP0053312EBI-518675,EBI-297353
ERBB2P046269EBI-518675,EBI-641062
EZH2Q159105EBI-518675,EBI-530054
GADD45GIP1Q8TAE84EBI-518675,EBI-372506
GNL3Q9BVP22EBI-518675,EBI-641642
KHDRBS1Q076662EBI-518675,EBI-1364
MAP3K7O433184EBI-518675,EBI-358684
MAPK9P459842EBI-518675,EBI-713568
MAPK9P45984-13EBI-518675,EBI-713586
MORC4Q8TE762EBI-518675,EBI-3940432
MRPS31Q926652EBI-518675,EBI-720602
NR4A1P227363EBI-518675,EBI-721550
OGDHLQ9ULD02EBI-518675,EBI-3940481
PGRP064013EBI-518675,EBI-78539
PTPN1P180312EBI-518675,EBI-968788
RELAQ042064EBI-518675,EBI-73886
RPS9P467812EBI-518675,EBI-351206
SOX1O005702EBI-518675,EBI-2935583
SRIP306262EBI-518675,EBI-750459
SULT2A1Q065202EBI-518675,EBI-3921363

Protein-protein interaction databases

BioGridi112651. 155 interactions.
DIPiDIP-33584N.
IntActiP40763. 84 interactions.
MINTiMINT-146801.
STRINGi9606.ENSP00000264657.

Structurei

3D structure databases

ProteinModelPortaliP40763.
SMRiP40763. Positions 2-715.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini580 – 67091SH2
Add
BLAST

Motif

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

Sequence similaritiesi

Contains 1 SH2 domain.

Keywords - Domaini

SH2 domain

Phylogenomic databases

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

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P40763-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

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

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

Note: Contains a phosphotyrosine at position 704.

Show »
Length:769
Mass (Da):87,981
Checksum:iA374A32AB9D28077
GO

Natural variant

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei701 – 7011Missing in isoform Del-701.
VSP_010474

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti133 – 1331T → A in BAF84622. 1 Publication
Sequence conflicti288 – 2881Q → H in AAA58374. 1 Publication
Sequence conflicti460 – 4601P → S in AAA58374. 1 Publication
Sequence conflicti548 – 5481K → N in AAA58374. 1 Publication
Sequence conflicti652 – 6521E → V in BAF84622. 1 Publication
Sequence conflicti667 – 6671V → L in AAA58374. 1 Publication
Sequence conflicti730 – 7301T → A in AAA58374. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L29277 mRNA. Translation: AAA58374.1.
AJ012463 mRNA. Translation: CAA10032.1.
AY572796 Genomic DNA. Translation: AAS66986.1.
AK291933 mRNA. Translation: BAF84622.1.
BC000627 mRNA. Translation: AAH00627.1.
BC014482 mRNA. Translation: AAH14482.1.
AF029311 mRNA. Translation: AAB84254.1.
CCDSiCCDS32656.1. [P40763-1]
CCDS32657.1. [P40763-2]
PIRiA54444.
RefSeqiNP_003141.2. NM_003150.3. [P40763-2]
NP_644805.1. NM_139276.2. [P40763-1]
NP_998827.1. NM_213662.1.
UniGeneiHs.463059.

Genome annotation databases

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

Polymorphism databases

DMDMi48429227.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

STAT3 entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology
STAT3base

STAT3 mutation db

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L29277 mRNA. Translation: AAA58374.1 .
AJ012463 mRNA. Translation: CAA10032.1 .
AY572796 Genomic DNA. Translation: AAS66986.1 .
AK291933 mRNA. Translation: BAF84622.1 .
BC000627 mRNA. Translation: AAH00627.1 .
BC014482 mRNA. Translation: AAH14482.1 .
AF029311 mRNA. Translation: AAB84254.1 .
CCDSi CCDS32656.1. [P40763-1 ]
CCDS32657.1. [P40763-2 ]
PIRi A54444.
RefSeqi NP_003141.2. NM_003150.3. [P40763-2 ]
NP_644805.1. NM_139276.2. [P40763-1 ]
NP_998827.1. NM_213662.1.
UniGenei Hs.463059.

3D structure databases

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

Protein-protein interaction databases

BioGridi 112651. 155 interactions.
DIPi DIP-33584N.
IntActi P40763. 84 interactions.
MINTi MINT-146801.
STRINGi 9606.ENSP00000264657.

Chemistry

BindingDBi P40763.
ChEMBLi CHEMBL4026.

PTM databases

PhosphoSitei P40763.

Polymorphism databases

DMDMi 48429227.

Proteomic databases

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

Protocols and materials databases

DNASUi 6774.
Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

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

Phylogenomic databases

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

Enzyme and pathway databases

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

Miscellaneous databases

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

Gene expression databases

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

Family and domain databases

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

Publicationsi

« 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. SeattleSNPs variation discovery resource
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-143.
  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. "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.
  6. 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.
  7. "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.
  8. "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.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. Cited for: INTERACTION WITH IL23R.
  14. "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.
  15. "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.
  16. "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.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. "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.
  23. "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].
  24. "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.
  25. "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.
  26. "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.
  27. "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.
  28. "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.
  29. "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.
  30. Cited for: INTERACTION WITH ARL2BP, PHOSPHORYLATION AT SERINE RESIDUES, SUBCELLULAR LOCATION.
  31. "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.
  32. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  33. "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].
  34. "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.
  35. "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.
  36. "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.
  37. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  38. "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.
  39. Cited for: FUNCTION, INTERACTION WITH EIF2AK2.
  40. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  41. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  42. 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.
  43. "Dominant-negative mutations in the DNA-binding domain of STAT3 cause hyper-IgE syndrome."
    Minegishi Y., Saito M., Tsuchiya S., Tsuge I., Takada H., Hara T., Kawamura N., Ariga T., Pasic S., Stojkovic O., Metin A., Karasuyama H.
    Nature 448:1058-1062(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS AD-HIES GLN-382; TRP-382; ILE-389; TYR-437 AND VAL-463 DEL, CHARACTERIZATION OF VARIANTS AD-HIES GLN-382; TRP-382; ILE-389; TYR-437 AND VAL-463 DEL.

Entry informationi

Entry nameiSTAT3_HUMAN
AccessioniPrimary (citable) accession number: P40763
Secondary accession number(s): A8K7B8, O14916, Q9BW54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: June 7, 2004
Last modified: September 3, 2014
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Involved in the gp130-mediated signaling pathway.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

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