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UniProtKB/Swiss-Prot entry P40763


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name STAT3_HUMAN
Primary accession number P40763
Secondary accession numbers O14916 Q9BW54
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on June 7, 2004 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 101)
Name and origin of the protein
Protein name Signal transducer and activator of transcription 3
Synonym Acute-phase response factor
Gene name
Name: STAT3
Synonyms: APRF
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT TYR-561.
TISSUE=Placenta;
DOI=10.1016/0092-8674(94)90235-6; PubMed=7512451 [NCBI, ExPASy, EBI, Israel, Japan]
Akira S., Nishio Y., Inoue M., Wang X.-J., Wei S., Matsusaka T., Yoshida K., Sudo T., Naruto M., Kishimoto T.;
"Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91-related transcription factor involved in the gp130-mediated signaling pathway.";
Cell 77:63-71(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1016/S0378-1119(98)00185-1; PubMed=9630560 [NCBI, ExPASy, EBI, Israel, Japan]
Della Pietra L., Bressan A., Pezzotti A., Serlupi-Crescenzi O.;
"Highly conserved amino-acid sequence between murine STAT3 and a revised human STAT3 sequence.";
Gene 213:119-124(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-143.
SeattleSNPs variation discovery resource;
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND DEL-701).
TISSUE=Kidney, and Pancreas;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 564-704.
TISSUE=Liver;
Della Pietra L., Bressan A., Pezzotti A.R., Serlupi-Crescenzi O.;
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[6]
PHOSPHORYLATION AT SERINE RESIDUES.
DOI=10.1126/science.7701321; PubMed=7701321 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang X., Blenis J., Li H.-C., Schindler C., Chen-Kiang S.;
"Requirement of serine phosphorylation for formation of STAT-promoter complexes.";
Science 267:1990-1994(1995).
[7]
INTERACTION WITH NCOA1.
DOI=10.1074/jbc.M111486200; PubMed=11773079 [NCBI, ExPASy, EBI, Israel, Japan]
Giraud S., Bienvenu F., Avril S., Gascan H., Heery D.M., Coqueret O.;
"Functional interaction of STAT3 transcription factor with the coactivator NcoA/SRC1a.";
J. Biol. Chem. 277:8004-8011(2002).
[8]
INTERACTION WITH HCV CORE PROTEIN.
DOI=10.1084/jem.20012127; PubMed=12208879 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshida T., Hanada T., Tokuhisa T., Kosai K., Sata M., Kohara M., Yoshimura A.;
"Activation of STAT3 by the hepatitis C virus core protein leads to cellular transformation.";
J. Exp. Med. 196:641-653(2002).
[9]
INTERACTION WITH IL23R.
PubMed=12023369 [NCBI, ExPASy, EBI, Israel, Japan]
Parham C., Chirica M., Timans J., Vaisberg E., Travis M., Cheung J., Pflanz S., Zhang R., Singh K.P., Vega F., To W., Wagner J., O'Farrell A.-M., McClanahan T.K., Zurawski S., Hannum C., Gorman D., Rennick D.M., Kastelein R.A., de Waal Malefyt R., Moore K.W.;
"A receptor for the heterodimeric cytokine IL-23 is composed of IL-12Rbeta1 and a novel cytokine receptor subunit, IL-23R.";
J. Immunol. 168:5699-5708(2002).
[10]
FUNCTION, AND INTERACTION WITH IL31RA.
DOI=10.1074/jbc.M401122200; PubMed=15194700 [NCBI, ExPASy, EBI, Israel, Japan]
Dreuw A., Radtke S., Pflanz S., Lippok B.E., Heinrich P.C., Hermanns H.M.;
"Characterization of the signaling capacities of the novel gp130-like cytokine receptor.";
J. Biol. Chem. 279:36112-36120(2004).
[11]
INTERACTION WITH TMF1.
DOI=10.1038/sj.onc.1208149; PubMed=15467733 [NCBI, ExPASy, EBI, Israel, Japan]
Perry E., Tsruya R., Levitsky P., Pomp O., Taller M., Weisberg S., Parris W., Kulkarni S., Malovani H., Pawson T., Shpungin S., Nir U.;
"TMF/ARA160 is a BC-box-containing protein that mediates the degradation of Stat3.";
Oncogene 23:8908-8919(2004).
[12]
INTERACTION WITH PELP1.
DOI=10.1158/0008-5472.CAN-04-4664; PubMed=15994929 [NCBI, ExPASy, EBI, Israel, Japan]
Manavathi B., Nair S.S., Wang R.-A., Kumar R., Vadlamudi R.K.;
"Proline-, glutamic acid-, and leucine-rich protein-1 is essential in growth factor regulation of signal transducers and activators of transcription 3 activation.";
Cancer Res. 65:5571-5577(2005).
[13]
INTERACTION WITH SOCS7.
DOI=10.1074/jbc.M411596200; PubMed=15677474 [NCBI, ExPASy, EBI, Israel, Japan]
Martens N., Uzan G., Wery M., Hooghe R., Hooghe-Peters E.L., Gertler A.;
"Suppressor of cytokine signaling 7 inhibits prolactin, growth hormone, and leptin signaling by interacting with STAT5 or STAT3 and attenuating their nuclear translocation.";
J. Biol. Chem. 280:13817-13823(2005).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1074/mcp.M500089-MCP200; PubMed=15951569 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.;
"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules.";
Mol. Cell. Proteomics 4:1240-1250(2005).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[16]
SUBCELLULAR LOCATION.
DOI=10.1073/pnas.0501643102; PubMed=15919823 [NCBI, ExPASy, EBI, Israel, Japan]
Liu L., McBride K.M., Reich N.C.;
"STAT3 nuclear import is independent of tyrosine phosphorylation and mediated by importin-alpha3.";
Proc. Natl. Acad. Sci. U.S.A. 102:8150-8155(2005).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-714 AND SER-727, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-714 AND SER-727, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[21]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[22]
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.
DOI=10.1056/NEJMoa073687; PubMed=17881745 [NCBI, ExPASy, EBI, Israel, Japan]
Holland S.M., DeLeo F.R., Elloumi H.Z., Hsu A.P., Uzel G., Brodsky N., Freeman A.F., Demidowich A., Davis J., Turner M.L., Anderson V.L., Darnell D.N., Welch P.A., Kuhns D.B., Frucht D.M., Malech H.L., Gallin J.I., Kobayashi S.D., Whitney A.R., Voyich J.M., Musser J.M., Woellner C., Schaffer A.A., Puck J.M., Grimbacher B.;
"STAT3 mutations in the hyper-IgE syndrome.";
N. Engl. J. Med. 357:1608-1619(2007).
[23]
VARIANTS AD-HIES GLN-382; TRP-382; ILE-389; TYR-437 AND VAL-463 DEL, AND CHARACTERIZATION OF VARIANTS AD-HIES GLN-382; TRP-382; ILE-389; TYR-437 AND VAL-463 DEL.
DOI=10.1038/nature06096; PubMed=17676033 [NCBI, ExPASy, EBI, Israel, Japan]
Minegishi Y., Saito M., Tsuchiya S., Tsuge I., Takada H., Hara T., Kawamura N., Ariga T., Pasic S., Stojkovic O., Metin A., Karasuyama H.;
"Dominant-negative mutations in the DNA-binding domain of STAT3 cause hyper-IgE syndrome.";
Nature 448:1058-1062(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L29277; AAA58374.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ012463; CAA10032.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY572796; AAS66986.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000627; AAH00627.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC014482; AAH14482.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF029311; AAB84254.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00306436; -.
IPI00784414; -.
PIR A54444; A54444.
RefSeq NP_003141.2; -.
NP_644805.1; -.
NP_998827.1; -.
UniGene Hs.463059
3D structure databases
HSSP P42227; 1BG1. [HSSP ENTRY / PDB]
SMR P40763; 136-703.
ModBase P40763.
Protein-protein interaction databases
IntAct P40763; 12.
PTM databases
PhosphoSite P40763; -.
Enzyme and pathway databases
Pathway_Interaction_DB ifngpathway; IFN-gamma pathway.
il12_stat4pathway; IL12 signaling mediated by STAT4.
il12_2pathway; IL12-mediated signaling events.
il2_1pathway; IL2-mediated signaling events.
il23pathway; IL23-mediated signaling events.
il27pathway; IL27-mediated signaling events.
il6_7pathway; IL6-mediated signaling events.
trkrpathway; Neurotrophic factor-mediated Trk receptor signaling.
pdgfrbpathway; PDGFR-beta signaling pathway.
met_pathway; Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
hdac_classi_pathway; Signaling events mediated by HDAC Class I.
ptp1bpathway; Signaling events mediated by PTP1B.
kitpathway; Signaling events mediated by Stem cell factor receptor (c-Kit).
Reactome REACT_11061; Signalling by NGF.
Organism-specific databases
GeneCards GC17M037718; -.
H-InvDB HIX0013840; -.
HGNC HGNC:11364; STAT3.
GenAtlas STAT3.
HPA CAB003859; -.
HPA001671; -.
MIM 102582; gene. [NCBI / EBI]
147060; phenotype. [NCBI / EBI]
Orphanet 2314; Autosomal dominant hyper IgE syndrome.
PharmGKB PA337; -.
Gene expression databases
ArrayExpress P40763; -.
Bgee P40763; -.
CleanEx HS_STAT3; -.
GermOnline ENSG00000168610; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0005634; Cellular component: nucleus (inferred from direct assay from HGNC).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
GO:0005062; Molecular function: hematopoietin/interferon-class (D200-domain) cytokine receptor signal transducer activity (traceable author statement from ProtInc).
GO:0019901; Molecular function: protein kinase binding (inferred from sequence or structural similarity from UniProtKB).
GO:0003700; Molecular function: transcription factor activity (traceable author statement from ProtInc).
GO:0008134; Molecular function: transcription factor binding (inferred from physical interaction from UniProtKB).
GO:0006928; Biological process: cell motion (traceable author statement from ProtInc).
GO:0032870; Biological process: cellular response to hormone stimulus (inferred from direct assay from UniProtKB).
GO:0070102; Biological process: interleukin-6-mediated signaling pathway (inferred from direct assay from UniProtKB).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0060397; Biological process: JAK-STAT cascade involved in growth hormone signaling pathway (inferred from direct assay from UniProtKB).
GO:0000122; Biological process: negative regulation of transcription from RNA polymerase II promoter (traceable author statement from ProtInc).
GO:0007399; Biological process: nervous system development (traceable author statement from ProtInc).
GO:0032355; Biological process: response to estradiol stimulus (inferred from direct assay from UniProtKB).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR011992; EF-Hand_type.
IPR000980; SH2.
IPR013800; STAT_TF_alpha.
IPR001217; STAT_TF_core.
IPR013801; STAT_TF_DNA-bd.
IPR012345; STAT_TF_DNA-bd_sub.
IPR013799; STAT_TF_prot_interaction.
Graphical view of domain structure.
Gene3D G3DSA:1.10.238.10; EF-Hand_type; 1.
G3DSA:3.30.505.10; SH2; 1.
G3DSA:1.20.1050.20; STAT_alpha; 1.
G3DSA:2.60.40.630; STAT_DNA_bd_sub; 1.
G3DSA:1.10.532.10; STAT_protein_interaction; 1.
PANTHER PTHR11801; STAT; 1.
Pfam PF00017; SH2; 1.
PF01017; STAT_alpha; 1.
PF02864; STAT_bind; 1.
PF02865; STAT_int; 1.
Pfam graphical view of domain structure.
SMART SM00252; SH2; 1.
SMART graphical view of domain structure.
PROSITE PS50001; SH2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P40763; -.
PRIDE P40763; -.
Genome annotation databases
Ensembl ENSG00000168610; Homo sapiens. [Contig view]
GeneID 6774; -.
KEGG hsa:6774; -.
Phylogenomic databases
HOVERGEN P40763; -.
OMA P40763; KSQGDMQ.
Other
NextBio 26438; -.
PMAP-CutDB P40763; -.
SOURCE STAT3; Homo sapiens.
ProtoNet P40763.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Activator; Alternative splicing; Cytoplasm; Disease mutation; DNA-binding; Host-virus interaction; Nucleus; Phosphoprotein; Polymorphism; SH2 domain; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   770  770     Signal transducer and activator of transcription 3. PRO_0000182417
DOMAIN   580   670  91     SH2. 
MOTIF   150   162  13     Essential for nuclear import (By similarity). 
MOD_RES   691   691        Phosphoserine. 
MOD_RES   705   705        Phosphotyrosine. 
MOD_RES   714   714        Phosphothreonine. 
MOD_RES   727   727        Phosphoserine; by NLK. 
VAR_SEQ   701   701        Missing (in isoform Del-701). VSP_010474
VARIANT   32    32  1     Q -> K (in dbSNP:rs1803125 [NCBI]). VAR_018683 
VARIANT   143   143  1     M -> I (in dbSNP:rs17878478 [NCBI]). VAR_018679 [3D]
VARIANT   382   382  1     R -> L (in AD-HIES). VAR_037365 [3D]
VARIANT   382   382  1     R -> Q (in AD-HIES; loss of function). VAR_037366 [3D]
VARIANT   382   382  1     R -> W (in AD-HIES; loss of function). VAR_037367 [3D]
VARIANT   384   384  1     F -> L (in AD-HIES). VAR_037368 [3D]
VARIANT   384   384  1     F -> S (in AD-HIES). VAR_037369 [3D]
VARIANT   389   389  1     T -> I (in AD-HIES; loss of function). VAR_037370 [3D]
VARIANT   423   423  1     R -> Q (in AD-HIES). VAR_037371 [3D]
VARIANT   437   437  1     H -> Y (in AD-HIES; loss of function). VAR_037372 [3D]
VARIANT   463   463  1     Missing (in AD-HIES; loss of function). VAR_037373
VARIANT   561   561  1     F -> Y (in dbSNP:rs1064116 [NCBI]). VAR_037374 [3D]
VARIANT   611   611  1     S -> N (in AD-HIES). VAR_037375 [3D]
VARIANT   621   621  1     F -> V (in AD-HIES). VAR_037376 [3D]
VARIANT   622   622  1     T -> I (in AD-HIES). VAR_037377 [3D]
VARIANT   637   637  1     V -> L (in AD-HIES). VAR_037378 [3D]
VARIANT   637   637  1     V -> M (in AD-HIES). VAR_037379 [3D]
VARIANT   644   644  1     Missing (in AD-HIES). VAR_037380
VARIANT   657   657  1     Y -> C (in AD-HIES). VAR_037381 [3D]
CONFLICT   288   288        Q -> H (in Ref. 1; AAA58374). 
CONFLICT   460   460        P -> S (in Ref. 1; AAA58374). 
CONFLICT   548   548        K -> N (in Ref. 1; AAA58374). 
CONFLICT   667   667        V -> L (in Ref. 1; AAA58374). 
CONFLICT   730   730        T -> A (in Ref. 1; AAA58374). 
Sequence information
Length: 770 AA [This is the length of the unprocessed precursor] Molecular weight: 88068 Da [This is the MW of the unprocessed precursor] CRC64: 6C00632211C8012D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAQWNQLQQL DTRYLEQLHQ LYSDSFPMEL RQFLAPWIES QDWAYAASKE SHATLVFHNL 

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

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

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

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

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

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

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

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

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

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

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

       730        740        750        760        770 
TIDLPMSPRT LDSLMQFGNN GEGAEPSAGG QFESLTFDME LTSECATSPM 

P40763 in FASTA format

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