ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P01579


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name IFNG_HUMAN
Primary accession number P01579
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on April 1, 1988 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 106)
Name and origin of the protein
Protein name Interferon gamma [Precursor]
Synonyms IFN-gamma
Immune interferon
Gene name
Name: IFNG
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1038/298859a0; PubMed=6180322 [NCBI, ExPASy, EBI, Israel, Japan]
Gray P.W., Goeddel D.V.;
"Structure of the human immune interferon gene.";
Nature 298:859-863(1982).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1038/295503a0; PubMed=6173769 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1093/nar/10.8.2487; PubMed=6176945 [NCBI, ExPASy, EBI, Israel, Japan]
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 [GENOMIC DNA].
SeattleSNPs program for genomic applications;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Blood;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
PROTEIN SEQUENCE OF 24-157, AND GLYCOSYLATION AT ASN-48 AND ASN-120.
PubMed=6427223 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
PROTEIN SEQUENCE OF 24-161, AND PROTEOLYTIC PROCESSING OF THE C-TERMINUS.
PubMed=3109913 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
STRUCTURE OF CARBOHYDRATES.
PubMed=2504704 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
PubMed=1902591 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
DOI=10.1038/376230a0; PubMed=7617032 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
DOI=10.1006/jmbi.2000.3734; PubMed=10860730 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[14]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF COMPLEX WITH RECEPTOR.
DOI=10.1016/S0969-2126(00)00184-2; PubMed=10986460 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[15]
STRUCTURE BY NMR.
DOI=10.1021/bi00150a009; PubMed=1525157 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[16]
ASSOCIATION WITH APLASTIC ANEMIA.
DOI=10.1111/j.1365-2141.2004.05102.x; PubMed=15327519 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
  • 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.
  • 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.
  • DISEASE: In Caucasians, genetic variation in IFNG is associated with the risk of aplastic anemia (AA) [MIM:609135]. AA is a rare disease in which the reduction of the circulating blood cells results from damage to the stem cell pool in bone marrow. In most patients, the stem cell lesion is caused by an autoimmune attack. T-lymphocytes, activated by an endogenous or exogenous, and most often unknown antigenic stimulus, secrete cytokines, including IFN-gamma, which would in turn be able to suppress hematopoiesis.
  • 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.
  • WEB RESOURCE: Name=Wikipedia; Note=Interferon gamma entry; URL="http://en.wikipedia.org/wiki/Interferon_gamma";.
  • WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/ifng/";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X13274; CAA31639.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J00219; AAB59534.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X01992; CAA26022.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V00543; CAA23804.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF375790; AAK53058.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC070256; AAH70256.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A93284; IVHUG.
RefSeq NP_000610.2; -.
UniGene Hs.856
3D structure databases
PDB
1EKU; X-ray; 2.90 A; A/B=1-161.[ExPASy / RCSB / EBI]
1FG9; X-ray; 2.90 A; A/B=24-156.[ExPASy / RCSB / EBI]
1FYH; X-ray; 2.04 A; A/D=1-156.[ExPASy / RCSB / EBI]
1HIG; X-ray; 3.50 A; A/B/C/D=24-161.[ExPASy / RCSB / EBI]
3BES; X-ray; 2.20 A; L=24-161.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EKU; -.
1FG9; -.
1FYH; -.
1HIG; -.
3BES; -.
ModBase P01579.
Protein-protein interaction databases
DIP DIP:483N; -.
PTM databases
GlycoSuiteDB P01579; -.
PhosphoSite P01579; -.
Organism-specific databases
H-InvDB HIX0036727; -.
HGNC HGNC:5438; IFNG.
GenAtlas IFNG.
HPA CAB010344; -.
MIM 147570; gene. [NCBI / EBI]
609135; phenotype. [NCBI / EBI]
Orphanet 88; Aplastic anaemia.
PharmGKB PA29674; -.
GeneCards P01579.
Gene expression databases
ArrayExpress P01579; -.
CleanEx HS_IFNG; -.
GermOnline ENSG00000111537; Homo sapiens.
Ontologies
GO
GO:0005133; Molecular function: interferon-gamma receptor binding (traceable author statement from ProtInc).
GO:0007050; Biological process: cell cycle arrest (inferred from direct assay from UniProtKB).
GO:0006928; Biological process: cell motion (traceable author statement from ProtInc).
GO:0007166; Biological process: cell surface receptor linked signal transduction (traceable author statement from ProtInc).
GO:0048662; Biological process: negative regulation of smooth muscle cell proliferation (inferred from direct assay from UniProtKB).
GO:0032735; Biological process: positive regulation of interleukin-12 production (inferred from direct assay from UniProtKB).
GO:0051712; Biological process: positive regulation of killing of cells of another organism (inferred from direct assay from UniProtKB).
GO:0045429; Biological process: positive regulation of nitric oxide biosynthetic process (inferred from direct assay from UniProtKB).
GO:0034393; Biological process: positive regulation of smooth muscle cell apoptosis (inferred from direct assay from UniProtKB).
GO:0000060; Biological process: protein import into nucleus, translocation (inferred from direct assay from UniProtKB).
GO:0050796; Biological process: regulation of insulin secretion (inferred from direct assay from UniProtKB).
GO:0042508; Biological process: tyrosine phosphorylation of Stat1 protein (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR012351; 4_helix_cytokine_core.
IPR002069; IFN-gamma.
Graphical view of domain structure.
Gene3D G3DSA:1.20.1250.10; 4_helix_cytokine_core; 1.
PANTHER PTHR11419; IFN-gamma; 1.
Pfam PF00714; IFN-gamma; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001936; IFN-gamma; 1.
ProDom PD002435; IFN-gamma; 1.
[Domain structure / List of seq. sharing at least 1 domain]
BLOCKS P01579.
ProtoNet P01579.
Genome annotation databases
Ensembl ENSG00000111537; Homo sapiens. [Contig view]
GeneID 3458; -.
KEGG hsa:3458; -.
Phylogenomic databases
HOGENOM P01579; -.
HOVERGEN P01579; -.
Other
DrugBank DB01296; Glucosamine.
DB00033; Interferon gamma-1b.
DB00641; Simvastatin.
LinkHub P01579; -.
NextBio 13624; -.
SOURCE IFNG; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Antiviral defense; Cleavage on pair of basic residues; Cytokine; Direct protein sequencing; Glycoprotein; Growth regulation; Pharmaceutical; Polymorphism; Pyrrolidone carboxylic acid; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    23  23      
CHAIN   24   161  138     Interferon gamma. PRO_0000016444
PROPEP   162   166  5      PRO_0000259481
MOD_RES   24    24        Pyrrolidone carboxylic acid. 
CARBOHYD   48    48        N-linked (GlcNAc...). 
CARBOHYD   120   120        N-linked (GlcNAc...); in dimeric form. 
VARIANT   29    29  1     K -> Q. VAR_004017 [3D]
VARIANT   160   160  1     R -> Q. VAR_004018 
HELIX   2    18  17      
HELIX   25    38  14      
HELIX   53    58  6      
HELIX   62    81  20      
TURN   82    85  4      
TURN   87    89  3      
HELIX   90   104  15      
HELIX   109   119  11      
HELIX   126   140  15      
Sequence information
Length: 166 AA [This is the length of the unprocessed precursor] Molecular weight: 19348 Da [This is the MW of the unprocessed precursor] CRC64: 1514E8F785FD81AA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKYTSYILAF QLCIVLGSLG CYCQDPYVKE AENLKKYFNA GHSDVADNGT LFLGILKNWK 

        70         80         90        100        110        120 
EESDRKIMQS QIVSFYFKLF KNFKDDQSIQ KSVETIKEDM NVKFFNSNKK KRDDFEKLTN 

       130        140        150        160 
YSVTDLNVQR KAIHELIQVM AELSPAAKTG KRKRSQMLFR GRRASQ 

P01579 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!