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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.
22-NOV-2017, entry version 201.
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;
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;
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;
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=2; 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.
UniGene; Hs.856; -.
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.
PDBsum; 1EKU; -.
PDBsum; 1FG9; -.
PDBsum; 1FYH; -.
PDBsum; 1HIG; -.
PDBsum; 3BES; -.
ProteinModelPortal; P01579; -.
SMR; P01579; -.
BioGrid; 109680; 5.
DIP; DIP-483N; -.
IntAct; P01579; 3.
MINT; MINT-1508034; -.
STRING; 9606.ENSP00000229135; -.
BindingDB; P01579; -.
ChEMBL; CHEMBL3286073; -.
DrugBank; DB05676; Apremilast.
DrugBank; DB05111; Fontolizumab.
DrugBank; DB01296; Glucosamine.
DrugBank; DB01250; Olsalazine.
DrugBank; DB05110; VIR201.
iPTMnet; P01579; -.
PhosphoSitePlus; P01579; -.
UniCarbKB; P01579; -.
BioMuta; IFNG; -.
DMDM; 124479; -.
PaxDb; P01579; -.
PeptideAtlas; P01579; -.
PRIDE; P01579; -.
DNASU; 3458; -.
Ensembl; ENST00000229135; ENSP00000229135; ENSG00000111537.
GeneID; 3458; -.
KEGG; hsa:3458; -.
UCSC; uc001stw.2; human.
CTD; 3458; -.
DisGeNET; 3458; -.
EuPathDB; HostDB:ENSG00000111537.4; -.
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; -.
HOVERGEN; HBG056912; -.
InParanoid; P01579; -.
KO; K04687; -.
OMA; WKEESDK; -.
OrthoDB; EOG091G0ZH0; -.
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; -.
PMAP-CutDB; P01579; -.
PRO; PR:P01579; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111537; -.
CleanEx; HS_IFNG; -.
Genevisible; P01579; HS.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
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:0019882; P:antigen processing and presentation; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IGI:MGI.
GO; GO:0002302; P:CD8-positive, alpha-beta T cell differentiation involved in immune response; IEA:Ensembl.
GO; GO:0007050; P:cell cycle arrest; IDA:BHF-UCL.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0071351; P:cellular response to interleukin-18; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
GO; GO:0042832; P:defense response to protozoan; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:Ensembl.
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:0006928; P:movement of cell or subcellular component; TAS:ProtInc.
GO; GO:0030857; P:negative regulation of epithelial cell differentiation; ISS:BHF-UCL.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
GO; GO:0072125; P:negative regulation of glomerular mesangial cell proliferation; IEA:Ensembl.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; IEA:Ensembl.
GO; GO:0032700; P:negative regulation of interleukin-17 production; IDA:BHF-UCL.
GO; GO:0031642; P:negative regulation of myelination; IEA:Ensembl.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:CAFA.
GO; GO:0001781; P:neutrophil apoptotic process; IEA:Ensembl.
GO; GO:0030593; P:neutrophil chemotaxis; IEA:Ensembl.
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 proliferation; ISS:BHF-UCL.
GO; GO:0045080; P:positive regulation of chemokine biosynthetic process; IEA:Ensembl.
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; IDA: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:0050718; P:positive regulation of interleukin-1 beta secretion; IEA:Ensembl.
GO; GO:0045084; P:positive regulation of interleukin-12 biosynthetic process; IEA:Ensembl.
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:0045410; P:positive regulation of interleukin-6 biosynthetic process; IEA:Ensembl.
GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:BHF-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:0031334; P:positive regulation of protein complex assembly; IDA:CAFA.
GO; GO:0090312; P:positive regulation of protein deacetylation; IDA:CAFA.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IDA:CAFA.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA: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:0034393; P:positive regulation of smooth muscle cell apoptotic process; IDA:BHF-UCL.
GO; GO:0032224; P:positive regulation of synaptic transmission, cholinergic; IEA:Ensembl.
GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:2000309; P:positive regulation of tumor necrosis factor (ligand) superfamily member 11 production; IDA:BHF-UCL.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
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:0000060; P:protein import into nucleus, translocation; IDA:UniProtKB.
GO; GO:0050691; P:regulation of defense response to virus by host; IEA:Ensembl.
GO; GO:0060251; P:regulation of glial cell proliferation; IEA:Ensembl.
GO; GO:2000345; P:regulation of hepatocyte proliferation; IEA:Ensembl.
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:0098908; P:regulation of neuronal action potential; IEA:Ensembl.
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:0002026; P:regulation of the force of heart contraction; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0009615; P:response to virus; IDA:MGI.
GO; GO:0050954; P:sensory perception of mechanical stimulus; IEA:Ensembl.
GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
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.
ProDom; PD002435; Interferon_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}.
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}.
HELIX 87 89 {ECO:0000244|PDB:1FYH}.
HELIX 90 105 {ECO:0000244|PDB:1FYH}.
HELIX 109 119 {ECO:0000244|PDB:1FYH}.
HELIX 126 140 {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


 

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