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Interferon gamma (IFN-gamma) (Immune interferon)

 IFNG_HUMAN              Reviewed;         166 AA.
P01579; B5BU88; Q53ZV4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
16-OCT-2019, entry version 222.
RecName: Full=Interferon gamma;
Short=IFN-gamma;
AltName: Full=Immune interferon;
Flags: Precursor;
Name=IFNG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6180322; DOI=10.1038/298859a0;
Gray P.W., Goeddel D.V.;
"Structure of the human immune interferon gene.";
Nature 298:859-863(1982).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6173769; DOI=10.1038/295503a0;
Gray P.W., Leung D.W., Pennica D., Yelverton E., Najarian R.,
Simonsen C.C., Derynck R., Sherwood P.J., Wallace D.M., Berger S.L.,
Levinson A.D., Goeddel D.V.;
"Expression of human immune interferon cDNA in E. coli and monkey
cells.";
Nature 295:503-508(1982).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2860101; DOI=10.1093/oxfordjournals.jbchem.a135039;
Nishi T., Fujita T., Nishi-Takaoka C., Saito A., Matsumoto T.,
Sato M., Oka T., Itoh S., Yip Y.K., Vilcek J., Taniguchi T.;
"Cloning and expression of a novel variant of human interferon-gamma
cDNA.";
J. Biochem. 97:153-159(1985).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6329718; DOI=10.1002/j.1460-2075.1982.tb01277.x;
Taya Y., Devos R., Tavernier J., Cheroutre H., Engler G., Fiers W.;
"Cloning and structure of the human immune interferon-gamma
chromosomal gene.";
EMBO J. 1:953-958(1982).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6176945; DOI=10.1093/nar/10.8.2487;
Devos R., Cheroutre H., Taya Y., Degrave W., van Heuverswyn H.,
Fiers W.;
"Molecular cloning of human immune interferon cDNA and its expression
in eukaryotic cells.";
Nucleic Acids Res. 10:2487-2501(1982).
[6]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-160.
Chikara S.K., Jaiswal P., Sharma G.;
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Blood;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[11]
PROTEIN SEQUENCE OF 24-157, PYROGLUTAMATE FORMATION AT GLN-24, AND
GLYCOSYLATION AT ASN-48 AND ASN-120.
PubMed=6427223;
Rinderknecht E., O'Conner B.H., Rodriguez H.;
"Natural human interferon-gamma. Complete amino acid sequence and
determination of sites of glycosylation.";
J. Biol. Chem. 259:6790-6797(1984).
[12]
PROTEIN SEQUENCE OF 24-161, PYROGLUTAMATE FORMATION AT GLN-24, AND
PROTEOLYTIC PROCESSING OF THE C-TERMINUS.
PubMed=3109913; DOI=10.1111/j.1432-1033.1987.tb13494.x;
Pan Y.C.E., Stern A.S., Familletti P.C., Khan F.R., Chizzonite R.;
"Structural characterization of human interferon gamma. Heterogeneity
of the carboxyl terminus.";
Eur. J. Biochem. 166:145-149(1987).
[13]
STRUCTURE OF CARBOHYDRATES.
PubMed=2504704; DOI=10.1093/oxfordjournals.jbchem.a122762;
Yamamoto S., Hase S., Yamauchi H., Tanimoto T., Ikenaka T.;
"Studies on the sugar chains of interferon-gamma from human
peripheral-blood lymphocytes.";
J. Biochem. 105:1034-1039(1989).
[14]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
PubMed=1902591; DOI=10.1126/science.1902591;
Ealick S.E., Cook W.J., Vijay-Kumar S., Carson M., Nagabhushan T.L.,
Trotta P.P., Bugg C.E.;
"Three-dimensional structure of recombinant human interferon-gamma.";
Science 252:698-702(1991).
[15]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
PubMed=7617032; DOI=10.1038/376230a0;
Walter M.R., Windsor W.T., Nagabhushan T.L., Lundell D.J., Lunn C.A.,
Zauodny P.J., Narula S.K.;
"Crystal structure of a complex between interferon-gamma and its
soluble high-affinity receptor.";
Nature 376:230-235(1995).
[16]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
PubMed=10860730; DOI=10.1006/jmbi.2000.3734;
Landar A., Curry B., Parker M.H., DiGiacomo R., Indelicato S.R.,
Nagabhushan T.L., Rizzi G., Walter M.R.;
"Design, characterization, and structure of a biologically active
single-chain mutant of human IFN-gamma.";
J. Mol. Biol. 299:169-179(2000).
[17]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF COMPLEX WITH RECEPTOR.
PubMed=10986460; DOI=10.1016/s0969-2126(00)00184-2;
Thiel D.J., le Du M.-H., Walter R.L., D'Arcy A., Chene C.,
Fountoulakis M., Garotta G., Winkler F.K., Ealick S.E.;
"Observation of an unexpected third receptor molecule in the crystal
structure of human interferon-gamma receptor complex.";
Structure 8:927-936(2000).
[18]
STRUCTURE BY NMR.
PubMed=1525157; DOI=10.1021/bi00150a009;
Grzesiek S., Doebeli H., Gentz R., Garotta G., Labhardt A.M., Bax A.;
"1H, 13C, and 15N NMR backbone assignments and secondary structure of
human interferon-gamma.";
Biochemistry 31:8180-8190(1992).
[19]
ASSOCIATION WITH APLASTIC ANEMIA.
PubMed=15327519; DOI=10.1111/j.1365-2141.2004.05102.x;
Dufour C., Capasso M., Svahn J., Marrone A., Haupt R., Bacigalupo A.,
Giordani L., Longoni D., Pillon M., Pistorio A., Di Michele P.,
Iori A.P., Pongiglione C., Lanciotti M., Iolascon A.;
"Homozygosis for (12) CA repeats in the first intron of the human IFN-
gamma gene is significantly associated with the risk of aplastic
anaemia in Caucasian population.";
Br. J. Haematol. 126:682-685(2004).
-!- FUNCTION: Produced by lymphocytes activated by specific antigens
or mitogens. IFN-gamma, in addition to having antiviral activity,
has important immunoregulatory functions. It is a potent activator
of macrophages, it has antiproliferative effects on transformed
cells and it can potentiate the antiviral and antitumor effects of
the type I interferons.
-!- SUBUNIT: Homodimer.
-!- INTERACTION:
Q66793:C4R (xeno); NbExp=2; IntAct=EBI-1030767, EBI-15683787;
P15260:IFNGR1; NbExp=3; IntAct=EBI-1030767, EBI-1030755;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Released primarily from activated T
lymphocytes.
-!- PTM: Proteolytic processing produces C-terminal heterogeneity,
with proteins ending alternatively at Gly-150, Met-157 or Gly-161.
{ECO:0000269|PubMed:3109913}.
-!- DISEASE: Aplastic anemia (AA) [MIM:609135]: A form of anemia in
which the bone marrow fails to produce adequate numbers of
peripheral blood elements. It is characterized by peripheral
pancytopenia and marrow hypoplasia. {ECO:0000269|PubMed:15327519}.
Note=Disease susceptibility may be associated with variations
affecting the gene represented in this entry.
-!- PHARMACEUTICAL: Available under the name Actimmune (Genentech).
Used for reducing the frequency and severity of serious infections
associated with chronic granulomatous disease (CGD).
-!- SIMILARITY: Belongs to the type II (or gamma) interferon family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Interferon gamma entry;
URL="https://en.wikipedia.org/wiki/Interferon_gamma";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/ifng/";
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EMBL; X13274; CAA31639.1; -; mRNA.
EMBL; J00219; AAB59534.1; -; Genomic_DNA.
EMBL; X01992; CAA26022.1; -; mRNA.
EMBL; V00543; CAA23804.1; -; mRNA.
EMBL; AY255837; AAP20098.1; -; mRNA.
EMBL; AF375790; AAK53058.1; -; Genomic_DNA.
EMBL; AB451324; BAG70138.1; -; mRNA.
EMBL; AB451453; BAG70267.1; -; mRNA.
EMBL; CH471054; EAW97180.1; -; Genomic_DNA.
EMBL; BC070256; AAH70256.1; -; mRNA.
CCDS; CCDS8980.1; -.
PIR; A93284; IVHUG.
RefSeq; NP_000610.2; NM_000619.2.
PDB; 1EKU; X-ray; 2.90 A; A/B=26-161.
PDB; 1FG9; X-ray; 2.90 A; A/B=24-156.
PDB; 1FYH; X-ray; 2.04 A; A/D=28-156.
PDB; 1HIG; X-ray; 3.50 A; A/B/C/D=24-161.
PDB; 3BES; X-ray; 2.20 A; L=24-161.
PDB; 6E3K; X-ray; 3.25 A; A/B=24-156.
PDB; 6E3L; X-ray; 3.80 A; A/B=24-156.
PDBsum; 1EKU; -.
PDBsum; 1FG9; -.
PDBsum; 1FYH; -.
PDBsum; 1HIG; -.
PDBsum; 3BES; -.
PDBsum; 6E3K; -.
PDBsum; 6E3L; -.
SMR; P01579; -.
BioGrid; 109680; 5.
DIP; DIP-483N; -.
IntAct; P01579; 4.
STRING; 9606.ENSP00000229135; -.
BindingDB; P01579; -.
ChEMBL; CHEMBL3286073; -.
DrugBank; DB05676; Apremilast.
DrugBank; DB14724; Emapalumab.
DrugBank; DB05111; Fontolizumab.
DrugBank; DB10770; Foreskin fibroblast (neonatal).
DrugBank; DB10772; Foreskin keratinocyte (neonatal).
DrugBank; DB01296; Glucosamine.
DrugBank; DB01250; Olsalazine.
DrugBank; DB05110; VIR201.
DrugCentral; P01579; -.
GlyConnect; 287; -.
iPTMnet; P01579; -.
PhosphoSitePlus; P01579; -.
UniCarbKB; P01579; -.
BioMuta; IFNG; -.
DMDM; 124479; -.
MassIVE; P01579; -.
PaxDb; P01579; -.
PeptideAtlas; P01579; -.
PRIDE; P01579; -.
ProteomicsDB; 51389; -.
ABCD; P01579; -.
DNASU; 3458; -.
Ensembl; ENST00000229135; ENSP00000229135; ENSG00000111537.
GeneID; 3458; -.
KEGG; hsa:3458; -.
UCSC; uc001stw.2; human.
CTD; 3458; -.
DisGeNET; 3458; -.
GeneCards; IFNG; -.
HGNC; HGNC:5438; IFNG.
HPA; CAB010344; -.
MalaCards; IFNG; -.
MIM; 147570; gene.
MIM; 609135; phenotype.
neXtProt; NX_P01579; -.
OpenTargets; ENSG00000111537; -.
Orphanet; 88; Idiopathic aplastic anemia.
PharmGKB; PA29674; -.
eggNOG; ENOG410IWSY; Eukaryota.
eggNOG; ENOG410Z8I5; LUCA.
GeneTree; ENSGT00390000007831; -.
HOGENOM; HOG000254784; -.
InParanoid; P01579; -.
KO; K04687; -.
OMA; WKEESDK; -.
OrthoDB; 870903at2759; -.
PhylomeDB; P01579; -.
TreeFam; TF336308; -.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-877312; Regulation of IFNG signaling.
Reactome; R-HSA-8877330; RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs).
Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
SignaLink; P01579; -.
SIGNOR; P01579; -.
EvolutionaryTrace; P01579; -.
GeneWiki; Interferon-gamma; -.
GenomeRNAi; 3458; -.
Pharos; P01579; -.
PMAP-CutDB; P01579; -.
PRO; PR:P01579; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111537; Expressed in 68 organ(s), highest expression level in leukocyte.
Genevisible; P01579; HS.
GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
GO; GO:0005133; F:interferon-gamma receptor binding; TAS:ProtInc.
GO; GO:0002250; P:adaptive immune response; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IGI:MGI.
GO; GO:0048143; P:astrocyte activation; IDA:ARUK-UCL.
GO; GO:0007050; P:cell cycle arrest; IDA:BHF-UCL.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:0006959; P:humoral immune response; IBA:GO_Central.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; IDA:CAFA.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0001774; P:microglial cell activation; IGI:ARUK-UCL.
GO; GO:1900222; P:negative regulation of amyloid-beta clearance; ISS:ARUK-UCL.
GO; GO:0030857; P:negative regulation of epithelial cell differentiation; ISS:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
GO; GO:0032700; P:negative regulation of interleukin-17 production; IDA:BHF-UCL.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:1902948; P:negative regulation of tau-protein kinase activity; IGI:ARUK-UCL.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:CAFA.
GO; GO:0150076; P:neuroinflammatory response; ISS:ARUK-UCL.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; IGI:ARUK-UCL.
GO; GO:0010508; P:positive regulation of autophagy; IDA:UniProtKB.
GO; GO:0060559; P:positive regulation of calcidiol 1-monooxygenase activity; IDA:BHF-UCL.
GO; GO:0032834; P:positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation involved in immune response; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:BHF-UCL.
GO; GO:1901857; P:positive regulation of cellular respiration; ISS:ARUK-UCL.
GO; GO:0045080; P:positive regulation of chemokine biosynthetic process; IDA:ARUK-UCL.
GO; GO:1904798; P:positive regulation of core promoter binding; IDA:CAFA.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IDA:CACAO.
GO; GO:1903543; P:positive regulation of exosomal secretion; HDA:UniProtKB.
GO; GO:0060550; P:positive regulation of fructose 1,6-bisphosphate 1-phosphatase activity; IDA:BHF-UCL.
GO; GO:0060552; P:positive regulation of fructose 1,6-bisphosphate metabolic process; IDA:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0045821; P:positive regulation of glycolytic process; ISS:ARUK-UCL.
GO; GO:0050725; P:positive regulation of interleukin-1 beta biosynthetic process; ISS:ARUK-UCL.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:UniProtKB.
GO; GO:0032747; P:positive regulation of interleukin-23 production; IDA:BHF-UCL.
GO; GO:1904440; P:positive regulation of iron ion import across plasma membrane; ISS:ARUK-UCL.
GO; GO:0051712; P:positive regulation of killing of cells of other organism; IDA:BHF-UCL.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:BHF-UCL.
GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; ISS:ARUK-UCL.
GO; GO:0050769; P:positive regulation of neurogenesis; IGI:ARUK-UCL.
GO; GO:1901216; P:positive regulation of neuron death; IGI:ARUK-UCL.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:BHF-UCL.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISS:ARUK-UCL.
GO; GO:0051173; P:positive regulation of nitrogen compound metabolic process; IGI:ARUK-UCL.
GO; GO:1904783; P:positive regulation of NMDA glutamate receptor activity; ISS:ARUK-UCL.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; IDA:BHF-UCL.
GO; GO:0033141; P:positive regulation of peptidyl-serine phosphorylation of STAT protein; IDA:MGI.
GO; GO:0050766; P:positive regulation of phagocytosis; ISS:ARUK-UCL.
GO; GO:0031334; P:positive regulation of protein complex assembly; IDA:CAFA.
GO; GO:0090312; P:positive regulation of protein deacetylation; IDA:CAFA.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:CAFA.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; HDA:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:CAFA.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:CAFA.
GO; GO:0010870; P:positive regulation of receptor biosynthetic process; ISS:ARUK-UCL.
GO; GO:0034393; P:positive regulation of smooth muscle cell apoptotic process; IDA:BHF-UCL.
GO; GO:2000309; P:positive regulation of tumor necrosis factor (ligand) superfamily member 11 production; IDA:BHF-UCL.
GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; ISS:ARUK-UCL.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; ISS:ARUK-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
GO; GO:0060557; P:positive regulation of vitamin D biosynthetic process; IDA:BHF-UCL.
GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; ISS:ARUK-UCL.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0050796; P:regulation of insulin secretion; IDA:BHF-UCL.
GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0010835; P:regulation of protein ADP-ribosylation; IDA:CAFA.
GO; GO:0045589; P:regulation of regulatory T cell differentiation; TAS:Reactome.
GO; GO:0009615; P:response to virus; IDA:MGI.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR002069; Interferon_gamma.
PANTHER; PTHR11419; PTHR11419; 1.
Pfam; PF00714; IFN-gamma; 1.
PIRSF; PIRSF001936; IFN-gamma; 1.
SUPFAM; SSF47266; SSF47266; 1.
1: Evidence at protein level;
3D-structure; Antiviral defense; Cleavage on pair of basic residues;
Complete proteome; Cytokine; Direct protein sequencing; Glycoprotein;
Growth regulation; Pharmaceutical; Polymorphism;
Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
SIGNAL 1 23 {ECO:0000269|PubMed:3109913,
ECO:0000269|PubMed:6427223}.
CHAIN 24 161 Interferon gamma.
/FTId=PRO_0000016444.
PROPEP 162 166
/FTId=PRO_0000259481.
MOD_RES 24 24 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:3109913,
ECO:0000269|PubMed:6427223}.
CARBOHYD 48 48 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:6427223}.
CARBOHYD 120 120 N-linked (GlcNAc...) asparagine; in
dimeric form.
{ECO:0000269|PubMed:6427223}.
VARIANT 29 29 K -> Q.
/FTId=VAR_004017.
VARIANT 160 160 R -> Q (in dbSNP:rs201359065).
{ECO:0000269|Ref.6}.
/FTId=VAR_004018.
HELIX 27 38 {ECO:0000244|PDB:1FYH}.
TURN 39 41 {ECO:0000244|PDB:1FYH}.
HELIX 43 46 {ECO:0000244|PDB:1FYH}.
HELIX 53 58 {ECO:0000244|PDB:1FYH}.
HELIX 62 81 {ECO:0000244|PDB:1FYH}.
TURN 82 85 {ECO:0000244|PDB:1FYH}.
TURN 87 89 {ECO:0000244|PDB:1FYH}.
HELIX 90 104 {ECO:0000244|PDB:1FYH}.
TURN 105 107 {ECO:0000244|PDB:1FYH}.
HELIX 109 119 {ECO:0000244|PDB:1FYH}.
HELIX 126 142 {ECO:0000244|PDB:1FYH}.
HELIX 146 148 {ECO:0000244|PDB:3BES}.
SEQUENCE 166 AA; 19348 MW; 1514E8F785FD81AA CRC64;
MKYTSYILAF QLCIVLGSLG CYCQDPYVKE AENLKKYFNA GHSDVADNGT LFLGILKNWK
EESDRKIMQS QIVSFYFKLF KNFKDDQSIQ KSVETIKEDM NVKFFNSNKK KRDDFEKLTN
YSVTDLNVQR KAIHELIQVM AELSPAAKTG KRKRSQMLFR GRRASQ


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E0049h ELISA kit Homo sapiens,Human,IFNG,IFN-gamma,Immune interferon,Interferon gamma 96T
U0049h CLIA Homo sapiens,Human,IFNG,IFN-gamma,Immune interferon,Interferon gamma 96T
10-663-45229 Interferon-gamma (IFN-gamma) Porcine - IFN-gamma; Immune interferon N_A 0.05 mg
10-663-45229 Interferon-gamma (IFN-gamma) Porcine - IFN-gamma; Immune interferon N_A 1 mg
10-663-45229 Interferon-gamma (IFN-gamma) Porcine - IFN-gamma; Immune interferon N_A 0.01 mg
orb84812 IFN gamma protein Interferongamma (IFN gamma, also known as Type II interferon or immune interferon) is a cytokine produced primarily by Tlymphocytes and natural killer cells. The protein shares no si 100
orb84828 IFN gamma protein Interferongamma (IFN gamma, also known as Type II interferon or immune interferon) is a cytokine produced primarily by Tlymphocytes and natural killer cells. The protein shares no si 100
orb84830 IFN gamma protein Interferongamma (IFN gamma, also known as Type II interferon or immune interferon) is a cytokine produced primarily by Tlymphocytes and natural killer cells. The protein shares no si 100
10-271-82250 Interferon-gamma Human - IFN-gamma; Immune interferon 0.05 mg
10-663-45189 Interferon-gamma Mouse - IFN-gamma; Immune interferon N_A 0.02 mg
10-271-82250 Interferon-gamma Human - IFN-gamma; Immune interferon 1 mg
10-663-45189 Interferon-gamma Mouse - IFN-gamma; Immune interferon N_A 1 mg
10-663-45189 Interferon-gamma Mouse - IFN-gamma; Immune interferon N_A 0.1 mg
10-663-45190 Interferon-gamma Rat - IFN-gamma; Immune interferon N_A 1 mg
10-663-45190 Interferon-gamma Rat - IFN-gamma; Immune interferon N_A 0.02 mg
10-663-45190 Interferon-gamma Rat - IFN-gamma; Immune interferon N_A 0.1 mg
18-783-78408 RABBIT ANTI HUMAN INTERFERON GAMMA Biotin - INTERFERON GAMMA; IFN-gamma Polyclonal 0.05 mg
20-271-80026 Interferon-gamma - Mouse Anti Human Interferon-gamma; IFN-gamma Monoclonal 0.5 mg
20-271-80026 Interferon-gamma - Mouse Anti Human Interferon-gamma; IFN-gamma Monoclonal 1 mg
18-783-78407 RABBIT ANTI HUMAN INTERFERON GAMMA - INTERFERON GAMMA; IFN-gamma Polyclonal 0.1 mg
20-271-80063 Interferon-gamma - Rat Anti Mouse Interferon-gamma; IFN-gamma Monoclonal 1 mg
20-663-48058 Interferon-gamma - Rat Anti-Mouse Interferon-gamma; IFN-gamma Monoclonal 0.5 mg
Pathways :
WP1836: Interferon gamma signaling
WP1017: Type II interferon signaling (IFNG)
WP866: EBV LMP1 signaling
WP2113: Type III interferon signaling
WP2199: Seed Development
WP1225: estrogen signalling
WP1350: Type II interferon signaling (IFNG)
WP2292: Chemokine signaling pathway
WP537: Translation Factors
WP1722: Th1/Th2
WP1837: Interferon Signaling
WP619: Type II interferon signaling (IFNG)
WP786: Type II interferon signaling (IFNG)
WP2006: Squamous cell TarBase
WP2152: BDNF
WP1224: EBV LMP1 signaling
WP900: Type II interferon signaling (IFNG)
WP1289: Type II interferon signaling (IFNG)
WP32: Translation Factors
WP1654: gamma-Hexachlorocyclohexane degradation
WP585: Interferon type I
WP760: estrogen signalling
WP1993: angiogenesis overview
WP2119: Interferon induced apoptosis
WP1136: Type II interferon signaling (IFNG)

Related Genes :
[IFNG] Interferon gamma (IFN-gamma) (Immune interferon)
[IFNGR1] Interferon gamma receptor 1 (IFN-gamma receptor 1) (IFN-gamma-R1) (CDw119) (Interferon gamma receptor alpha-chain) (IFN-gamma-R-alpha) (CD antigen CD119)
[IRF9 ISGF3G] Interferon regulatory factor 9 (IRF-9) (IFN-alpha-responsive transcription factor subunit) (ISGF3 p48 subunit) (Interferon-stimulated gene factor 3 gamma) (ISGF-3 gamma) (Transcriptional regulator ISGF3 subunit gamma)
[IFNG] Interferon gamma (BoIFNG) (IFN-gamma)
[IFNG] Interferon gamma (IFN-gamma)
[IFNG] Interferon gamma (IFN-gamma)
[Ifng] Interferon gamma (IFN-gamma)
[IFNG] Interferon gamma (IFN-gamma)
[Ifng] Interferon gamma (IFN-gamma)
[IFNG] Interferon gamma (IFN-gamma)
[IFNG] Interferon gamma (IFN-gamma)
[IFNG] Interferon gamma (IFN-gamma)
[IFNG] Interferon gamma (IFN-gamma)
[IFNG] Interferon gamma (IFN-gamma)
[IL18 IGIF IL1F4] Interleukin-18 (IL-18) (Iboctadekin) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[IFNG] Interferon gamma (IFN-gamma)
[Il18 Igif] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[IFNG] Interferon gamma (IFN-gamma)
[IFNG] Interferon gamma (IFN-gamma)
[IFNG] Interferon gamma (IFN-gamma)
[IFNG] Interferon gamma (IFN-gamma)
[IFNG] Interferon gamma (IFN-gamma)
[IFNG] Interferon gamma (IFN-gamma)
[IL18 IGIF] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[Il18 Igif] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[IFN-g IFNG] Interferon gamma (IFN-gamma)
[IL18 IGIF] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[IL18 IGIF] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[IFNG IFN-gamma] Interferon gamma (IFN-gamma)
[IFNG CK820_G0041509] Interferon gamma (IFN-gamma)

Bibliography :
[31629103] Co-expression of Interleukin-17A molecular adjuvant and prophylactic Helicobacter pylori genetic vaccine could cause sterile immunity in Treg suppressed mice.
[31627272] Programmed Death Ligand 1 Indicates Pre-Existing Adaptive Immune Response by Tumor-Infiltrating CD8 T Cells in Non-Small Cell Lung Cancer.
[31626841] Evolution of pathologic T-cell subsets in atopic dermatitis from infancy to adulthood.
[31626125] Serial analysis of cytokine and chemokine profiles and viral load in severe fever with thrombocytopenia syndrome: Case report and review of literature.
[31625070] The therapeutic and protective effects of bee pollen against prenatal methylmercury induced neurotoxicity in rat pups.
[31624262] Targeting the mTOR pathway uncouples the efficacy and toxicity of PD-1 blockade in renal transplantation.
[31622780] Adaptive in vivo device for theranostics of inflammation: real-time monitoring of interferon-γ and aspirin.
[31621209] Effects of pentoxifylline on whole blood IL-2 and IFN-gamma gene expression in normal dogs.
[31620662] Altered metabolism for neuroprotection provided by mesenchymal stem cells.
[31620037] Reduced Expression of Immune Mediators by T-Cell Subpopulations of Combat-Exposed Veterans With Post-Traumatic Stress Disorder.