ID STA3_HUMAN STANDARD; PRT; 770 AA. AC P40763; DT 01-FEB-1995 (REL. 31, CREATED) DT 01-FEB-1995 (REL. 31, LAST SEQUENCE UPDATE) DT 01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE) DE SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION 3 (ACUTE-PHASE DE RESPONSE FACTOR). GN STAT3 OR APRF. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RX MEDLINE; 94208062. RA AKIRA S., NISHIO Y., INOUE M., WANG X.-J., WEI S., MATSUSAKA T., RA YOSHIDA K., SUDO T., NARUTO M., KISHIMOTO T.; RL CELL 77:63-71(1994). RN [2] RP PHOSPHORYLATION ON SERINE. RX MEDLINE; 95215843. RA ZHANG X., BLENIS J., LI H.-C., SCHINDLER C., CHEN-KIANG S.; RL SCIENCE 267:1990-1994(1995). 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). CC -!- SUBCELLULAR LOCATION: NUCLEAR; TRANSLOCATED INTO THE NUCLEUS IN CC RESPONSE TO PHOSPHORYLATION. 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 TRANSCIPTIONAL ACTIVITY. CC -!- SIMILARITY: BELONGS TO THE STAT FAMILY OF TRANSCRIPTION FACTORS. CC -!- SIMILARITY: CONTAINS A COPY OF THE 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; G475789; -. DR TRANSFAC; T01493; -. DR MIM; 102582; -. DR PROSITE; PS50001; SH2; 1. KW TRANSCRIPTION REGULATION; DNA-BINDING; NUCLEAR PROTEIN; KW PHOSPHORYLATION; SH2 DOMAIN. FT DOMAIN 580 670 SH2. FT MOD_RES 705 705 PHOSPHORYLATION (BY JAKS) (BY FT SIMILARITY). FT MOD_RES 727 727 PHOSPHORYLATION (BY SIMILARITY). SQ SEQUENCE 770 AA; 88052 MW; CA65BC60 CRC32; 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 IKKLEELHQK VSYKGDPIVQ HRPMLEERIV ELFRNLMKSA FVVERQPCMP MHPDRPLVIK TGVQFTTKVR LLVKFPELNY QLKIKVCIDK DSGDVAALRG SRKFNILGTN TKVMNMEESN NGSLSAEFKH LTLREQRCGN GGRANCDASL IVTEELHLIT FETEVYHQGL KIDLETHSLS VVVISNICQM PNAWASILWY NMLTNNPKNV NFFTKPPIGT WDQVAEVLSW QFSSTTKRGL SIEQLTTLAE KLLGPGVNYS GCQITWANFC KENMAGKGFS YWVWLDNIID LVKKYILALW NEGYIMGFIS KERERAILST KPPGTFLLRF SESSKEGGVT FTWVEKDISG KTQIQSVEPY TKQQLNNMSF AEIIMGYKIM DATNILLSPL VYLYPDIPKE EAFGKYCRPE SQEHPEADPG SAAPYLKTKF ICVTPTTCSN TIDLPMSPRA LDSLMQFGNN GEGAEPSAGG QFESLTFDME LTSECATSPM //