Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Signal transducer and activator of transcription 1

 STAT1_PIG               Reviewed;         757 AA.
Q764M5;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
28-MAR-2018, entry version 104.
RecName: Full=Signal transducer and activator of transcription 1;
Name=STAT1;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14681463; DOI=10.1093/nar/gkh037;
Uenishi H., Eguchi T., Suzuki K., Sawazaki T., Toki D., Shinkai H.,
Okumura N., Hamasima N., Awata T.;
"PEDE (Pig EST Data Explorer): construction of a database for ESTs
derived from porcine full-length cDNA libraries.";
Nucleic Acids Res. 32:D484-D488(2004).
-!- FUNCTION: Signal transducer and transcription activator that
mediates cellular responses to interferons (IFNs), cytokine
KITLG/SCF and other cytokines and other growth factors. Following
type I IFN (IFN-alpha and IFN-beta) binding to cell surface
receptors, signaling via protein kinases leads to activation of
Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of
STAT1 and STAT2. The phosphorylated STATs dimerize and associate
with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription
factor, that enters the nucleus. ISGF3 binds to the IFN stimulated
response element (ISRE) to activate the transcription of IFN-
stimulated genes (ISG), which drive the cell in an antiviral
state. In response to type II IFN (IFN-gamma), STAT1 is
tyrosine- and serine-phosphorylated. It then forms a homodimer
termed IFN-gamma-activated factor (GAF), migrates into the nucleus
and binds to the IFN gamma activated sequence (GAS) to drive the
expression of the target genes, inducing a cellular antiviral
state. Becomes activated in response to KITLG/SCF and KIT
signaling. May mediate cellular responses to activated FGFR1,
FGFR2, FGFR3 and FGFR4. {ECO:0000250|UniProtKB:P42224}.
-!- SUBUNIT: Homodimerizes upon IFN-gamma induced phosphorylation.
Heterodimer with STAT2 upon IFN-alpha/beta induced
phosphorylation. The heterodimer STAT1:STAT2 forms the interferon-
stimulated gene factor 3 complex (ISGF3) with IRF9. Interacts
(phosphorylated at Ser-727) with PIAS1 (dimethylated on arginine);
the interaction results in release of STAT1 from its target gene.
Interacts with IFNAR1. Interacts with IFNAR2. Found in a complex
with NMI and CREBBP/CBP. Interacts with NMI which is required for
CREBBP/CBP recruitment to the complex. Interacts with PTK2/FAK1.
Interacts with SRC. Interacts with ERBB4 (phosphorylated).
Interacts with PARP9 and DTX3L independently of IFN-beta or IFN-
gamma-mediated STAT1 'Tyr-701' phosphorylation. Interacts with
histone acetyltransferase EP300/p300 in response to INF-gamma
stimulation. Interacts with OTOP1. {ECO:0000250|UniProtKB:P42224,
ECO:0000250|UniProtKB:P42225}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P42225}.
Nucleus {ECO:0000250|UniProtKB:P42225}. Note=Translocated into the
nucleus upon tyrosine phosphorylation and dimerization, in
response to IFN-gamma and signaling by activated FGFR1, FGFR2,
FGFR3 or FGFR4. Monomethylation at Lys-525 is required for
phosphorylation at Tyr-701 and translocation into the nucleus.
Translocates into the nucleus in response to interferon-beta
stimulation. {ECO:0000250|UniProtKB:P42224}.
-!- PTM: Phosphorylated on tyrosine and serine residues in response to
a variety of cytokines/growth hormones including IFN-alpha, IFN-
gamma, PDGF and EGF. Activated KIT promotes phosphorylation on
tyrosine residues and subsequent translocation to the nucleus.
Upon EGF stimulation, phosphorylation on Tyr-701 (lacking in beta
form) by JAK1, JAK2 or TYK2 promotes dimerization and subsequent
translocation to the nucleus. Growth hormone (GH) activates STAT1
signaling only via JAK2. Tyrosine phosphorylated in response to
constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4.
Phosphorylation on Ser-727 by several kinases including MAPK14,
ERK1/2 and CAMKII on IFN-gamma stimulation, regulates STAT1
transcriptional activity. Phosphorylation on Ser-727 promotes
sumoylation though increasing interaction with PIAS.
Phosphorylation on Ser-727 by PRKCD induces apoptosis in response
to DNA-damaging agents. Phosphorylated on tyrosine residues when
PTK2/FAK1 is activated; most likely this is catalyzed by a SRC
family kinase. Dephosphorylation on tyrosine residues by PTPN2
negatively regulates interferon-mediated signaling. Upon viral
infection or IFN induction, phosphorylation on Ser-708 occurs much
later than phosphorylation on Tyr-701 and is required for the
binding of ISGF3 on the ISREs of a subset of IFN-stimulated genes
IKBKE-dependent. Phosphorylation at Tyr-701 and Ser-708 are
mutually exclusive, phosphorylation at Ser-708 requires previous
dephosphorylation of Tyr-701. {ECO:0000250|UniProtKB:P42224}.
-!- PTM: Sumoylated with SUMO1, SUMO2 and SUMO3. Sumoylation is
enhanced by IFN-gamma-induced phosphorylation on Ser-727, and by
interaction with PIAS proteins. Enhances the transactivation
activity. {ECO:0000250|UniProtKB:P42224}.
-!- PTM: ISGylated. {ECO:0000250|UniProtKB:P42224}.
-!- PTM: Mono-ADP-ribosylated at Glu-657 and Glu-705 by PARP14; ADP-
riboslyation prevents phosphorylation at Tyr-701.
{ECO:0000250|UniProtKB:P42224}.
-!- PTM: Monomethylated at Lys-525 by SETD2; monomethylation is
necessary for phosphorylation at Tyr-701, translocation into the
nucleus and activation of the antiviral defense.
{ECO:0000250|UniProtKB:P42224}.
-!- SIMILARITY: Belongs to the transcription factor STAT family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB116564; BAD06318.1; -; mRNA.
RefSeq; NP_998934.1; NM_213769.1.
UniGene; Ssc.42622; -.
ProteinModelPortal; Q764M5; -.
SMR; Q764M5; -.
STRING; 9823.ENSSSCP00000017010; -.
iPTMnet; Q764M5; -.
PaxDb; Q764M5; -.
PeptideAtlas; Q764M5; -.
PRIDE; Q764M5; -.
GeneID; 396655; -.
KEGG; ssc:396655; -.
CTD; 6772; -.
eggNOG; KOG3667; Eukaryota.
eggNOG; ENOG410XPN8; LUCA.
HOVERGEN; HBG055669; -.
InParanoid; Q764M5; -.
KO; K11220; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
GO; GO:0000983; F:transcription factor activity, RNA polymerase II core promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
GO; GO:0008015; P:blood circulation; ISS:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0007259; P:JAK-STAT cascade; ISS:UniProtKB.
GO; GO:0010742; P:macrophage derived foam cell differentiation; ISS:UniProtKB.
GO; GO:0072162; P:metanephric mesenchymal cell differentiation; ISS:UniProtKB.
GO; GO:0072136; P:metanephric mesenchymal cell proliferation involved in metanephros development; ISS:UniProtKB.
GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:UniProtKB.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:0072308; P:negative regulation of metanephric nephron tubule epithelial cell differentiation; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
GO; GO:0032727; P:positive regulation of interferon-alpha production; ISS:UniProtKB.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0051591; P:response to cAMP; ISS:UniProtKB.
GO; GO:0034097; P:response to cytokine; ISS:UniProtKB.
GO; GO:0007584; P:response to nutrient; ISS:UniProtKB.
GO; GO:0043434; P:response to peptide hormone; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0060337; P:type I interferon signaling pathway; ISS:UniProtKB.
CDD; cd10372; SH2_STAT1; 1.
Gene3D; 1.10.532.10; -; 1.
Gene3D; 1.10.8.1200; -; 1.
Gene3D; 2.60.40.630; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR001217; STAT.
InterPro; IPR038295; STAT1_C_sf.
InterPro; IPR035859; STAT1_SH2.
InterPro; IPR022752; STAT1_TAZ2-bd_C.
InterPro; IPR036535; STAT_N_sf.
InterPro; IPR013800; STAT_TF_alpha.
InterPro; IPR015988; STAT_TF_coiled-coil.
InterPro; IPR013801; STAT_TF_DNA-bd.
InterPro; IPR012345; STAT_TF_DNA-bd_N.
InterPro; IPR013799; STAT_TF_prot_interaction.
PANTHER; PTHR11801; PTHR11801; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF12162; STAT1_TAZ2bind; 1.
Pfam; PF01017; STAT_alpha; 1.
Pfam; PF02864; STAT_bind; 1.
Pfam; PF02865; STAT_int; 1.
SMART; SM00964; STAT_int; 1.
SUPFAM; SSF47655; SSF47655; 1.
SUPFAM; SSF48092; SSF48092; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
2: Evidence at transcript level;
Acetylation; Activator; ADP-ribosylation; Coiled coil;
Complete proteome; Cytoplasm; DNA-binding; Isopeptide bond;
Methylation; Nucleus; Phosphoprotein; Reference proteome; SH2 domain;
Transcription; Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P42224}.
CHAIN 2 757 Signal transducer and activator of
transcription 1.
/FTId=PRO_0000182412.
DOMAIN 573 670 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
COILED 136 317 {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 114 114 N6-methyllysine.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 175 175 N6-methyllysine.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 296 296 N6-methyllysine.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 366 366 N6-methyllysine.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 525 525 N6-methyllysine.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 637 637 N6-methyllysine.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 657 657 ADP-ribosyl glutamic acid.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 665 665 N6-methyllysine.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 701 701 Phosphotyrosine; by JAK1, JAK2 or TYK2.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 705 705 ADP-ribosyl glutamic acid.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 708 708 Phosphoserine; by IKKE.
{ECO:0000250|UniProtKB:P42224}.
MOD_RES 727 727 Phosphoserine; by MAPK14.
{ECO:0000250|UniProtKB:P42224}.
CROSSLNK 703 703 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 703 703 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P42224}.
CROSSLNK 703 703 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P42224}.
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


Related products :

Catalog number Product name Quantity
18-661-15004 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.1 mg
15-288-22758 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.1 mg
15-288-22758 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.05 mg
18-003-44098 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.05 mg Aff Pur
15-288-22780 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.1 mg
15-288-22780 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.05 mg
18-003-43498 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.05 mg Aff Pur
18-003-43847 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.05 mg Aff Pur
FP-0102 Signal transducer and activator of transcription 4. 10 ug
FP-0101 Signal transducer and activator of transcription 3 10 ug
FP-0104 Signal transducer and activator of transcription 5B. 10ug
FP-0102 Signal transducer and activator of transcription 4. 10ug
FP-0101 Signal transducer and activator of transcription 3 10ug
FP-0103 Signal transducer and activator of transcription 5A. 10 ug
FP-0105 Signal transducer and activator of transcription 6 10ug
FP-0104 Signal transducer and activator of transcription 5B. 10 ug
FP-0105 Signal transducer and activator of transcription 6 10 ug
FP-0103 Signal transducer and activator of transcription 5A. 10ug
E02S0211 Rat Signal Transducer And Activator Of Transcription 5B ELISA 96T/kit
E02S0210 Rat Signal Transducer And Activator Of Transcription 5A ELISA 96T/kit
FP-0100 Signal transducer and activator of transcription 2 (p113). 10ug
E02S0206 Rat Signal Transducer And Activator Of Transcription 4 ELISA 96T/kit
pka-315 Recombinant Human Signal Transducer and Activator of Transcription 1 10
EM1378 Signal Transducer And Activator Of Transcription 2 Elisa Kit 96T
E02S0204 Rat Signal Transducer And Activator Of Transcription 3 ELISA 96T/kit


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur