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STAT1_PIG
ID   STAT1_PIG               Reviewed;         757 AA.
AC   Q764M5;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Signal transducer and activator of transcription 1;
GN   Name=STAT1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14681463; DOI=10.1093/nar/gkh037;
RA   Uenishi H., Eguchi T., Suzuki K., Sawazaki T., Toki D., Shinkai H.,
RA   Okumura N., Hamasima N., Awata T.;
RT   "PEDE (Pig EST Data Explorer): construction of a database for ESTs derived
RT   from porcine full-length cDNA libraries.";
RL   Nucleic Acids Res. 32:D484-D488(2004).
RN   [2]
RP   INTERACTION WITH AFRICAN SWINE FEVER VIRUS PROTEIN MGF360-9L (MICROBIAL
RP   INFECTION), AND SUBCELLULAR LOCATION.
RX   PubMed=35076286; DOI=10.1128/mbio.02330-21;
RA   Zhang K., Yang B., Shen C., Zhang T., Hao Y., Zhang D., Liu H., Shi X.,
RA   Li G., Yang J., Li D., Zhu Z., Tian H., Yang F., Ru Y., Cao W.J., Guo J.,
RA   He J., Zheng H., Liu X.;
RT   "MGF360-9L Is a Major Virulence Factor Associated with the African Swine
RT   Fever Virus by Antagonizing the JAK/STAT Signaling Pathway.";
RL   MBio 0:0-0(2022).
CC   -!- FUNCTION: Signal transducer and transcription activator that mediates
CC       cellular responses to interferons (IFNs), cytokine KITLG/SCF and other
CC       cytokines and other growth factors. Following type I IFN (IFN-alpha and
CC       IFN-beta) binding to cell surface receptors, signaling via protein
CC       kinases leads to activation of Jak kinases (TYK2 and JAK1) and to
CC       tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs
CC       dimerize and associate with ISGF3G/IRF-9 to form a complex termed ISGF3
CC       transcription factor, that enters the nucleus. ISGF3 binds to the IFN
CC       stimulated response element (ISRE) to activate the transcription of
CC       IFN-stimulated genes (ISG), which drive the cell in an antiviral state.
CC       In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-
CC       phosphorylated. It then forms a homodimer termed IFN-gamma-activated
CC       factor (GAF), migrates into the nucleus and binds to the IFN gamma
CC       activated sequence (GAS) to drive the expression of the target genes,
CC       inducing a cellular antiviral state. Becomes activated in response to
CC       KITLG/SCF and KIT signaling. May mediate cellular responses to
CC       activated FGFR1, FGFR2, FGFR3 and FGFR4.
CC       {ECO:0000250|UniProtKB:P42224}.
CC   -!- SUBUNIT: Homodimerizes upon IFN-gamma induced phosphorylation.
CC       Heterodimer with STAT2 upon IFN-alpha/beta induced phosphorylation. The
CC       heterodimer STAT1:STAT2 forms the interferon-stimulated gene factor 3
CC       complex (ISGF3) with IRF9. Interacts (phosphorylated at Ser-727) with
CC       PIAS1; the interaction results in release of STAT1 from its target
CC       gene. Interacts with IFNAR1. Interacts with IFNAR2. Found in a complex
CC       with NMI and CREBBP/CBP. Interacts with NMI which is required for
CC       CREBBP/CBP recruitment to the complex. Interacts with PTK2/FAK1.
CC       Interacts with SRC. Interacts with ERBB4 (phosphorylated). Interacts
CC       with PARP9 and DTX3L independently of IFN-beta or IFN-gamma-mediated
CC       STAT1 'Tyr-701' phosphorylation. Interacts with histone
CC       acetyltransferase EP300/p300 in response to INF-gamma stimulation.
CC       Interacts with OTOP1. {ECO:0000250|UniProtKB:P42224,
CC       ECO:0000250|UniProtKB:P42225}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with African swine fever virus
CC       (ASFV) MGF360-9L; this interaction mediates degradation of STAT1
CC       through apoptosis. {ECO:0000269|PubMed:35076286}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:35076286}. Nucleus
CC       {ECO:0000269|PubMed:35076286}. Note=Translocated into the nucleus upon
CC       tyrosine phosphorylation and dimerization, in response to IFN-gamma and
CC       signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4. Monomethylation at
CC       Lys-525 is required for phosphorylation at Tyr-701 and translocation
CC       into the nucleus. Translocates into the nucleus in response to
CC       interferon-beta stimulation. {ECO:0000250|UniProtKB:P42224}.
CC   -!- PTM: Phosphorylated on tyrosine and serine residues in response to a
CC       variety of cytokines/growth hormones including IFN-alpha, IFN-gamma,
CC       PDGF and EGF. Activated KIT promotes phosphorylation on tyrosine
CC       residues and subsequent translocation to the nucleus. Upon EGF
CC       stimulation, phosphorylation on Tyr-701 (lacking in beta form) by JAK1,
CC       JAK2 or TYK2 promotes dimerization and subsequent translocation to the
CC       nucleus. Growth hormone (GH) activates STAT1 signaling only via JAK2.
CC       Tyrosine phosphorylated in response to constitutively activated FGFR1,
CC       FGFR2, FGFR3 and FGFR4. Phosphorylation on Ser-727 by several kinases
CC       including MAPK14, ERK1/2 and CAMKII on IFN-gamma stimulation, regulates
CC       STAT1 transcriptional activity. Phosphorylation on Ser-727 promotes
CC       sumoylation though increasing interaction with PIAS. Phosphorylation on
CC       Ser-727 by PRKCD induces apoptosis in response to DNA-damaging agents.
CC       Phosphorylated on tyrosine residues when PTK2/FAK1 is activated; most
CC       likely this is catalyzed by a SRC family kinase. Dephosphorylation on
CC       tyrosine residues by PTPN2 negatively regulates interferon-mediated
CC       signaling. Upon viral infection or IFN induction, phosphorylation on
CC       Ser-708 occurs much later than phosphorylation on Tyr-701 and is
CC       required for the binding of ISGF3 on the ISREs of a subset of IFN-
CC       stimulated genes IKBKE-dependent. Phosphorylation at Tyr-701 and Ser-
CC       708 are mutually exclusive, phosphorylation at Ser-708 requires
CC       previous dephosphorylation of Tyr-701. {ECO:0000250|UniProtKB:P42224}.
CC   -!- PTM: Sumoylated with SUMO1, SUMO2 and SUMO3. Sumoylation is enhanced by
CC       IFN-gamma-induced phosphorylation on Ser-727, and by interaction with
CC       PIAS proteins. Enhances the transactivation activity.
CC       {ECO:0000250|UniProtKB:P42224}.
CC   -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P42224}.
CC   -!- PTM: Mono-ADP-ribosylated at Glu-657 and Glu-705 by PARP14; ADP-
CC       riboslyation prevents phosphorylation at Tyr-701. However, the role of
CC       ADP-ribosylation in the prevention of phosphorylation has been called
CC       into question and the lack of phosphorylation may be due to sumoylation
CC       of Lys-703. {ECO:0000250|UniProtKB:P42224}.
CC   -!- PTM: Monomethylated at Lys-525 by SETD2; monomethylation is necessary
CC       for phosphorylation at Tyr-701, translocation into the nucleus and
CC       activation of the antiviral defense. {ECO:0000250|UniProtKB:P42224}.
CC   -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Has been shown to be mono-ADP-ribosylated at Glu-657 and Glu-
CC       705 by PARP14 which prevents phosphorylation at Tyr-701 (By
CC       similarity). However, the role of ADP-ribosylation in the prevention of
CC       phosphorylation has been called into question (By similarity). It has
CC       been suggested that the lack of phosphorylation may be due to
CC       sumoylation of Lys-703 (By similarity). {ECO:0000250|UniProtKB:P42224}.
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DR   EMBL; AB116564; BAD06318.1; -; mRNA.
DR   RefSeq; NP_998934.1; NM_213769.1.
DR   AlphaFoldDB; Q764M5; -.
DR   SMR; Q764M5; -.
DR   STRING; 9823.ENSSSCP00000017010; -.
DR   iPTMnet; Q764M5; -.
DR   PaxDb; Q764M5; -.
DR   PeptideAtlas; Q764M5; -.
DR   PRIDE; Q764M5; -.
DR   GeneID; 396655; -.
DR   KEGG; ssc:396655; -.
DR   CTD; 6772; -.
DR   eggNOG; KOG3667; Eukaryota.
DR   InParanoid; Q764M5; -.
DR   OrthoDB; 327469at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR   GO; GO:0008015; P:blood circulation; ISS:UniProtKB.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0006952; P:defense response; IBA:GO_Central.
DR   GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR   GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0010742; P:macrophage derived foam cell differentiation; ISS:UniProtKB.
DR   GO; GO:0072162; P:metanephric mesenchymal cell differentiation; ISS:UniProtKB.
DR   GO; GO:0072136; P:metanephric mesenchymal cell proliferation involved in metanephros development; ISS:UniProtKB.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
DR   GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:UniProtKB.
DR   GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR   GO; GO:0072308; P:negative regulation of metanephric nephron tubule epithelial cell differentiation; ISS:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0032727; P:positive regulation of interferon-alpha production; ISS:UniProtKB.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; ISS:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0051591; P:response to cAMP; ISS:UniProtKB.
DR   GO; GO:0034097; P:response to cytokine; ISS:UniProtKB.
DR   GO; GO:0007584; P:response to nutrient; ISS:UniProtKB.
DR   GO; GO:0043434; P:response to peptide hormone; ISS:UniProtKB.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0060337; P:type I interferon signaling pathway; ISS:UniProtKB.
DR   CDD; cd10372; SH2_STAT1; 1.
DR   Gene3D; 1.10.532.10; -; 1.
DR   Gene3D; 2.60.40.630; -; 1.
DR   Gene3D; 3.30.505.10; -; 1.
DR   Gene3D; 6.10.250.3310; -; 1.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR001217; STAT.
DR   InterPro; IPR038295; STAT1_C_sf.
DR   InterPro; IPR035859; STAT1_SH2.
DR   InterPro; IPR022752; STAT1_TAZ2-bd_C.
DR   InterPro; IPR036535; STAT_N_sf.
DR   InterPro; IPR013800; STAT_TF_alpha.
DR   InterPro; IPR015988; STAT_TF_coiled-coil.
DR   InterPro; IPR013801; STAT_TF_DNA-bd.
DR   InterPro; IPR012345; STAT_TF_DNA-bd_N.
DR   InterPro; IPR013799; STAT_TF_prot_interaction.
DR   PANTHER; PTHR11801; PTHR11801; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF12162; STAT1_TAZ2bind; 1.
DR   Pfam; PF01017; STAT_alpha; 1.
DR   Pfam; PF02864; STAT_bind; 1.
DR   Pfam; PF02865; STAT_int; 1.
DR   SMART; SM00964; STAT_int; 1.
DR   SUPFAM; SSF47655; SSF47655; 1.
DR   SUPFAM; SSF48092; SSF48092; 1.
DR   SUPFAM; SSF49417; SSF49417; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; ADP-ribosylation; Coiled coil; Cytoplasm;
KW   DNA-binding; Host-virus interaction; Isopeptide bond; Methylation; Nucleus;
KW   Phosphoprotein; Reference proteome; SH2 domain; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P42224"
FT   CHAIN           2..757
FT                   /note="Signal transducer and activator of transcription 1"
FT                   /id="PRO_0000182412"
FT   DOMAIN          573..670
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   COILED          136..317
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42224"
FT   MOD_RES         114
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P42224"
FT   MOD_RES         175
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P42224"
FT   MOD_RES         296
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P42224"
FT   MOD_RES         366
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P42224"
FT   MOD_RES         525
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P42224"
FT   MOD_RES         637
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P42224"
FT   MOD_RES         657
FT                   /note="ADP-ribosyl glutamic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P42224"
FT   MOD_RES         665
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P42224"
FT   MOD_RES         701
FT                   /note="Phosphotyrosine; by JAK1, JAK2 or TYK2"
FT                   /evidence="ECO:0000250|UniProtKB:P42224"
FT   MOD_RES         705
FT                   /note="ADP-ribosyl glutamic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P42224"
FT   MOD_RES         708
FT                   /note="Phosphoserine; by IKKE"
FT                   /evidence="ECO:0000250|UniProtKB:P42224"
FT   MOD_RES         727
FT                   /note="Phosphoserine; by MAPK14"
FT                   /evidence="ECO:0000250|UniProtKB:P42224"
FT   CROSSLNK        703
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        703
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P42224"
FT   CROSSLNK        703
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P42224"
SQ   SEQUENCE   757 AA;  88167 MW;  B6093218F2F6A029 CRC64;
     MSQWYELQQL DSKFLEQVHQ LYDDSFPMEI RQYLAQWLEN QDWEHAANDV SFATIRFHDL
     LSQLDDQYSR FSLENNFLLQ HNIRKSKRNL QDNFQEDPIQ MSMIICNCLK EERKILENAQ
     RFNQTQSGNI QSTVMLDKHK ELDSKVRNVK DKVMCIEHEI KTLEDLQDEY DFKCKTLQNR
     EHDTNGVAKN DQKQEQMLLQ KMYLMLDNKR KEVVHKIIEL LNVTELTQKA LINDELVEWK
     RRQQSACIGG PPNACLDQLQ NWFTIVAESL QQVRQQLKKL EELEQKYTYE HDPITKNKQA
     LWDRTFSLFQ QLIQSSFVVE RQPCMPTHPQ RPLVLKTGVQ FTVKLRLLVK LQKLNYNLKV
     KVLFDKDVSE RNTVKGFRKF NILGTHTKVM NMEESTNGSL AAEFRHLQLK EQKNAGARTN
     EGPLIVTEEL HSLSFETQLC QPGLVIDLET TSLPVVVISN VSQLPSGWAS ILWYNMLVAE
     PRNLSFFLNP PCARWSQLSE VLSWQFSSVT KRGLNVDQLN MLGEKLLGPT AGPDGLIPWT
     RFCKENINDK NFPFWLWIES ILELIKKHLL SLWNDGCIVG FISKERERAL LKDQQPGTFL
     LRFSESCREG AITFTWVERS QNGGEPYFHA VEPYTKKELS AVTFPDIIRN YKVMAAENIP
     ENPLKYLYPN IDKDHAFGKY YSRPKEAPEP MELDGPKGTG YIKTELISVS EVHPSRLQTT
     DNLLPMSPEE FDEVSRMVGP VEFDVTWNKF SGTMNLD
 
 
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