ID STAT3_HUMAN STANDARD; PRT; 770 AA. AC P40763; O14916; Q9BW54; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2004, sequence version 2. DT 13-JUN-2006, entry version 59. DE Signal transducer and activator of transcription 3 (Acute-phase DE response factor). GN Name=STAT3; Synonyms=APRF; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RC TISSUE=Placenta; RX MEDLINE=94208062; PubMed=7512451; DOI=10.1016/0092-8674(94)90235-6; RA Akira S., Nishio Y., Inoue M., Wang X.-J., Wei S., Matsusaka T., RA Yoshida K., Sudo T., Naruto M., Kishimoto T.; RT "Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91- RT related transcription factor involved in the gp130-mediated signaling RT pathway."; RL Cell 77:63-71(1994). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RX MEDLINE=98296260; PubMed=9630560; DOI=10.1016/S0378-1119(98)00185-1; RA Della Pietra L., Bressan A., Pezzotti A., Serlupi-Crescenzi O.; RT "Highly conserved amino-acid sequence between murine STAT3 and a RT revised human STAT3 sequence."; RL Gene 213:119-124(1998). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-143. RA Rieder M.J., Daniels R.L., da Ponte S.H., Hastings N.C., Ahearn M.O., RA Rajkumar N., Yi Q., Nickerson D.A.; RT "SeattleSNPs. NHLBI HL66682 program for genomic applications, UW- RT FHCRC, Seattle, WA (URL: http://pga.gs.washington.edu)."; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND DEL-701). RC TISSUE=Kidney, and Pancreas; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [5] RP NUCLEOTIDE SEQUENCE OF 564-704. RC TISSUE=Liver; RA Della Pietra L., Bressan A., Pezzotti A.R., Serlupi-Crescenzi O.; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [6] RP PHOSPHORYLATION AT SERINE RESIDUES. RX MEDLINE=95215843; PubMed=7701321; RA Zhang X., Blenis J., Li H.-C., Schindler C., Chen-Kiang S.; RT "Requirement of serine phosphorylation for formation of STAT-promoter RT complexes."; RL Science 267:1990-1994(1995). RN [7] RP INTERACTION WITH NCOA1. RX PubMed=11773079; DOI=10.1074/jbc.M111486200; RA Giraud S., Bienvenu F., Avril S., Gascan H., Heery D.M., Coqueret O.; RT "Functional interaction of STAT3 transcription factor with the RT coactivator NcoA/SRC1a."; RL J. Biol. Chem. 277:8004-8011(2002). RN [8] RP INTERACTION WITH HCV CORE PROTEIN. RX MEDLINE=22198898; PubMed=12208879; DOI=10.1084/jem.20012127; RA Yoshida T., Hanada T., Tokuhisa T., Kosai K., Sata M., Kohara M., RA Yoshimura A.; RT "Activation of STAT3 by the hepatitis C virus core protein leads to RT cellular transformation."; RL J. Exp. Med. 196:641-653(2002). RN [9] RP PHOSPHORYLATION AT TYR-705, AND MASS SPECTROMETRY. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). CC -!- FUNCTION: Transcription factor that binds to the interleukin-6 CC (IL-6)-responsive elements identified in the promoters of various CC acute-phase protein genes. CC -!- PATHWAY: Involved in the gp130-mediated signaling pathway. CC -!- SUBUNIT: Forms a homodimer or a heterodimer with a related family CC member (at least STAT1). Interacts with NCOA1. Interacts with HCV CC core protein. Interacts with STATIP1 (By similarity). CC -!- INTERACTION: CC Q07666:KHDRBS1; NbExp=1; IntAct=EBI-518675, EBI-1364; CC O43318:MAP3K7; NbExp=1; IntAct=EBI-518675, EBI-358684; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Translocated into the CC nucleus in response to phosphorylation. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P40763-1; Sequence=Displayed; CC Name=Del-701; CC IsoId=P40763-2; Sequence=VSP_010474; CC -!- TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver, skeletal CC muscle, kidney and pancreas. CC -!- PTM: Tyrosine phosphorylated in response to IL-6, IL-11, CNTF, CC LIF, CSF-1, EGF, PDGF, IFN-alpha and OSM. Serine phosphorylation CC is important for the formation of stable DNA-binding STAT3 CC homodimers and maximal transcriptional activity. CC -!- SIMILARITY: Belongs to the transcription factor STAT family. CC -!- SIMILARITY: Contains 1 SH2 domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L29277; AAA58374.1; -; mRNA. DR EMBL; AJ012463; CAA10032.1; -; mRNA. DR EMBL; AY572796; AAS66986.1; -; Genomic_DNA. DR EMBL; BC000627; AAH00627.1; -; mRNA. DR EMBL; BC014482; AAH14482.1; -; mRNA. DR EMBL; AF029311; AAB84254.1; -; mRNA. DR PIR; A54444; A54444. DR UniGene; Hs.463059; -. DR HSSP; P42227; 1BG1. DR SMR; P40763; 136-703. DR IntAct; P40763; -. DR TRANSFAC; T01493; -. DR Ensembl; ENSG00000168610; Homo sapiens. DR H-InvDB; HIX0013840; -. DR HGNC; HGNC:11364; STAT3. DR MIM; 102582; gene. DR RZPD-ProtExp; F0658; -. DR RZPD-ProtExp; F0806; -. DR RZPD-ProtExp; IOH12287; -. DR RZPD-ProtExp; IOH14348; -. DR RZPD-ProtExp; IOH4288; -. DR RZPD-ProtExp; RZPDo834B0644; -. DR GO; GO:0005737; C:cytoplasm; TAS. DR GO; GO:0005634; C:nucleus; TAS. DR GO; GO:0005062; F:hematopoietin/interferon-class (D200-domain...; TAS. DR GO; GO:0003700; F:transcription factor activity; TAS. DR GO; GO:0008134; F:transcription factor binding; IPI. DR GO; GO:0006928; P:cell motility; TAS. DR GO; GO:0019221; P:cytokine and chemokine mediated signaling p...; NAS. DR GO; GO:0007259; P:JAK-STAT cascade; TAS. DR GO; GO:0000122; P:negative regulation of transcription from R...; TAS. DR GO; GO:0007399; P:nervous system development; TAS. DR GO; GO:0045449; P:regulation of transcription; IDA. DR GO; GO:0007165; P:signal transduction; TAS. DR InterPro; IPR011992; EF-Hand_type. DR InterPro; IPR008967; P53_like_DNA_bd. DR InterPro; IPR000980; SH2. DR InterPro; IPR001217; STAT. DR InterPro; IPR012345; STAT_DNA_bd_sub. DR PANTHER; PTHR11801; STAT; 1. DR Pfam; PF00017; SH2; 1. DR PROSITE; PS50001; SH2; 1. KW Activator; Alternative splicing; DNA-binding; Host-virus interaction; KW Nuclear protein; Phosphorylation; Polymorphism; SH2 domain; KW Transcription; Transcription regulation. FT CHAIN 1 770 Signal transducer and activator of FT transcription 3. FT /FTId=PRO_0000182417. FT DOMAIN 580 670 SH2. FT MOD_RES 705 705 Phosphotyrosine. FT MOD_RES 727 727 Phosphoserine (By similarity). FT VAR_SEQ 701 701 Missing (in isoform Del-701). FT /FTId=VSP_010474. FT VARIANT 32 32 Q -> K (in dbSNP:1803125). FT /FTId=VAR_018683. FT VARIANT 143 143 M -> I (in dbSNP:17878478). FT /FTId=VAR_018679. FT CONFLICT 288 288 Q -> H (in Ref. 1). FT CONFLICT 460 460 P -> S (in Ref. 1). FT CONFLICT 548 548 K -> N (in Ref. 1). FT CONFLICT 561 561 F -> Y (in Ref. 1). FT CONFLICT 667 667 V -> L (in Ref. 1). FT CONFLICT 730 730 T -> A (in Ref. 1). SQ SEQUENCE 770 AA; 88068 MW; 6C00632211C8012D CRC64; MAQWNQLQQL DTRYLEQLHQ LYSDSFPMEL RQFLAPWIES QDWAYAASKE SHATLVFHNL LGEIDQQYSR FLQESNVLYQ HNLRRIKQFL QSRYLEKPME IARIVARCLW EESRLLQTAA TAAQQGGQAN HPTAAVVTEK QQMLEQHLQD VRKRVQDLEQ KMKVVENLQD DFDFNYKTLK SQGDMQDLNG NNQSVTRQKM QQLEQMLTAL DQMRRSIVSE LAGLLSAMEY VQKTLTDEEL ADWKRRQQIA CIGGPPNICL DRLENWITSL AESQLQTRQQ IKKLEELQQK VSYKGDPIVQ HRPMLEERIV ELFRNLMKSA FVVERQPCMP MHPDRPLVIK TGVQFTTKVR LLVKFPELNY QLKIKVCIDK DSGDVAALRG SRKFNILGTN TKVMNMEESN NGSLSAEFKH LTLREQRCGN GGRANCDASL IVTEELHLIT FETEVYHQGL KIDLETHSLP VVVISNICQM PNAWASILWY NMLTNNPKNV NFFTKPPIGT WDQVAEVLSW QFSSTTKRGL SIEQLTTLAE KLLGPGVNYS GCQITWAKFC KENMAGKGFS FWVWLDNIID LVKKYILALW NEGYIMGFIS KERERAILST KPPGTFLLRF SESSKEGGVT FTWVEKDISG KTQIQSVEPY TKQQLNNMSF AEIIMGYKIM DATNILVSPL VYLYPDIPKE EAFGKYCRPE SQEHPEADPG SAAPYLKTKF ICVTPTTCSN TIDLPMSPRT LDSLMQFGNN GEGAEPSAGG QFESLTFDME LTSECATSPM //