Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P01579 (IFNG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 168. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interferon gamma

Short name=IFN-gamma
Alternative name(s):
Immune interferon
Gene names
Name:IFNG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length166 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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 structure

Homodimer.

Subcellular location

Secreted.

Tissue specificity

Released primarily from activated T lymphocytes.

Post-translational modification

Proteolytic processing produces C-terminal heterogeneity, with proteins ending alternatively at Gly-150, Met-157 or Gly-161.

Involvement in 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.
Note: Disease susceptibility may be associated with variations affecting the gene represented in this entry.

Pharmaceutical use

Available under the name Actimmune (Genentech). Used for reducing the frequency and severity of serious infections associated with chronic granulomatous disease (CGD).

Sequence similarities

Belongs to the type II (or gamma) interferon family.

Ontologies

Keywords
   Biological processAntiviral defense
Growth regulation
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionCytokine
   PTMCleavage on pair of basic residues
Glycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Pharmaceutical
Reference proteome
Gene Ontology (GO)
   Biological_processCD8-positive, alpha-beta T cell differentiation involved in immune response

Inferred from electronic annotation. Source: Ensembl

adaptive immune response

Inferred from Biological aspect of Ancestor. Source: RefGenome

antigen processing and presentation

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from genetic interaction PubMed 7828849. Source: MGI

cell cycle arrest

Inferred from direct assay PubMed 16942485. Source: BHF-UCL

cell surface receptor signaling pathway

Traceable author statement PubMed 10477596. Source: ProtInc

cellular component movement

Traceable author statement PubMed 10477596. Source: ProtInc

cellular response to interleukin-18

Inferred from electronic annotation. Source: Ensembl

cellular response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

defense response to bacterium

Inferred from electronic annotation. Source: Ensembl

defense response to protozoan

Inferred from electronic annotation. Source: Ensembl

defense response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

endoplasmic reticulum unfolded protein response

Inferred from electronic annotation. Source: Ensembl

extrinsic apoptotic signaling pathway

Inferred from direct assay PubMed 16942485. Source: BHF-UCL

humoral immune response

Inferred from Biological aspect of Ancestor. Source: RefGenome

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

negative regulation of growth of symbiont in host

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-17 production

Inferred from direct assay PubMed 18501882. Source: BHF-UCL

negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of metanephric nephron tubule epithelial cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of myelination

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell proliferation

Inferred from direct assay PubMed 16942485. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: BHF-UCL

neutrophil apoptotic process

Inferred from electronic annotation. Source: Ensembl

neutrophil chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation of MHC class II biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of T cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of calcidiol 1-monooxygenase activity

Inferred from direct assay PubMed 9282826. Source: BHF-UCL

positive regulation of cell adhesion

Inferred from electronic annotation. Source: Ensembl

positive regulation of chemokine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of fructose 1,6-bisphosphate 1-phosphatase activity

Inferred from direct assay PubMed 9282826. Source: BHF-UCL

positive regulation of fructose 1,6-bisphosphate metabolic process

Inferred from direct assay PubMed 9282826. Source: BHF-UCL

positive regulation of interleukin-1 beta secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-12 biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-12 production

Inferred from direct assay PubMed 7605994PubMed 8557999. Source: UniProtKB

positive regulation of interleukin-23 production

Inferred from direct assay PubMed 20027291. Source: BHF-UCL

positive regulation of interleukin-6 biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of isotype switching to IgG isotypes

Inferred from electronic annotation. Source: Ensembl

positive regulation of killing of cells of other organism

Inferred from direct assay PubMed 7544003. Source: BHF-UCL

positive regulation of membrane protein ectodomain proteolysis

Inferred from direct assay PubMed 18373975. Source: BHF-UCL

positive regulation of mesenchymal cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric oxide biosynthetic process

Inferred from direct assay PubMed 8383325. Source: BHF-UCL

positive regulation of osteoclast differentiation

Inferred from direct assay PubMed 16220542. Source: BHF-UCL

positive regulation of peptidyl-serine phosphorylation of STAT protein

Non-traceable author statement PubMed 21268089. Source: BHF-UCL

positive regulation of smooth muscle cell apoptotic process

Inferred from direct assay PubMed 16942485. Source: BHF-UCL

positive regulation of synaptic transmission, cholinergic

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of tumor necrosis factor (ligand) superfamily member 11 production

Inferred from direct assay PubMed 16220542. Source: BHF-UCL

positive regulation of tumor necrosis factor production

Inferred from electronic annotation. Source: Ensembl

positive regulation of tyrosine phosphorylation of Stat1 protein

Inferred from direct assay PubMed 15604419. Source: BHF-UCL

positive regulation of vitamin D biosynthetic process

Inferred from direct assay PubMed 9282826. Source: BHF-UCL

protein import into nucleus, translocation

Inferred from direct assay PubMed 15604419. Source: UniProtKB

regulation of insulin secretion

Inferred from direct assay PubMed 8383325. Source: BHF-UCL

regulation of interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

regulation of the force of heart contraction

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to virus

Inferred from direct assay PubMed 16280321. Source: MGI

   Cellular_componentexternal side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular region

Inferred from direct assay PubMed 20041150. Source: BHF-UCL

extracellular space

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functioncytokine activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

interferon-gamma receptor binding

Traceable author statement PubMed 10477596. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.11 Ref.12
Chain24 – 161138Interferon gamma
PRO_0000016444
Propeptide162 – 1665
PRO_0000259481

Amino acid modifications

Modified residue241Pyrrolidone carboxylic acid
Glycosylation481N-linked (GlcNAc...) Ref.11
Glycosylation1201N-linked (GlcNAc...); in dimeric form Ref.11

Natural variations

Natural variant291K → Q.
VAR_004017
Natural variant1601R → Q. Ref.6
VAR_004018

Secondary structure

................... 166
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01579 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 1514E8F785FD81AA

FASTA16619,348
        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 

« Hide

References

« Hide 'large scale' references
[1]"Structure of the human immune interferon gene."
Gray P.W., Goeddel D.V.
Nature 298:859-863(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Expression of human immune interferon cDNA in E. coli and monkey cells."
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.
Nature 295:503-508(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning and expression of a novel variant of human interferon-gamma cDNA."
Nishi T., Fujita T., Nishi-Takaoka C., Saito A., Matsumoto T., Sato M., Oka T., Itoh S., Yip Y.K., Vilcek J., Taniguchi T.
J. Biochem. 97:153-159(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Cloning and structure of the human immune interferon-gamma chromosomal gene."
Taya Y., Devos R., Tavernier J., Cheroutre H., Engler G., Fiers W.
EMBO J. 1:953-958(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Molecular cloning of human immune interferon cDNA and its expression in eukaryotic cells."
Devos R., Cheroutre H., Taya Y., Degrave W., van Heuverswyn H., Fiers W.
Nucleic Acids Res. 10:2487-2501(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]Chikara S.K., Jaiswal P., Sharma G.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-160.
[7]SeattleSNPs variation discovery resource
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
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. expand/collapse author list , 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.
Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Blood.
[11]"Natural human interferon-gamma. Complete amino acid sequence and determination of sites of glycosylation."
Rinderknecht E., O'Conner B.H., Rodriguez H.
J. Biol. Chem. 259:6790-6797(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-157, PYROGLUTAMATE FORMATION AT GLN-24, GLYCOSYLATION AT ASN-48 AND ASN-120.
[12]"Structural characterization of human interferon gamma. Heterogeneity of the carboxyl terminus."
Pan Y.C.E., Stern A.S., Familletti P.C., Khan F.R., Chizzonite R.
Eur. J. Biochem. 166:145-149(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-161, PYROGLUTAMATE FORMATION AT GLN-24, PROTEOLYTIC PROCESSING OF THE C-TERMINUS.
[13]"Studies on the sugar chains of interferon-gamma from human peripheral-blood lymphocytes."
Yamamoto S., Hase S., Yamauchi H., Tanimoto T., Ikenaka T.
J. Biochem. 105:1034-1039(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATES.
[14]"Three-dimensional structure of recombinant human interferon-gamma."
Ealick S.E., Cook W.J., Vijay-Kumar S., Carson M., Nagabhushan T.L., Trotta P.P., Bugg C.E.
Science 252:698-702(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
[15]"Crystal structure of a complex between interferon-gamma and its soluble high-affinity receptor."
Walter M.R., Windsor W.T., Nagabhushan T.L., Lundell D.J., Lunn C.A., Zauodny P.J., Narula S.K.
Nature 376:230-235(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[16]"Design, characterization, and structure of a biologically active single-chain mutant of human IFN-gamma."
Landar A., Curry B., Parker M.H., DiGiacomo R., Indelicato S.R., Nagabhushan T.L., Rizzi G., Walter M.R.
J. Mol. Biol. 299:169-179(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[17]"Observation of an unexpected third receptor molecule in the crystal structure of human interferon-gamma receptor complex."
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.
Structure 8:927-936(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF COMPLEX WITH RECEPTOR.
[18]"1H, 13C, and 15N NMR backbone assignments and secondary structure of human interferon-gamma."
Grzesiek S., Doebeli H., Gentz R., Garotta G., Labhardt A.M., Bax A.
Biochemistry 31:8180-8190(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[19]"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."
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.
Br. J. Haematol. 126:682-685(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH APLASTIC ANEMIA.
+Additional computationally mapped references.

Web resources

Wikipedia

Interferon gamma entry

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13274 mRNA. Translation: CAA31639.1.
J00219 Genomic DNA. Translation: AAB59534.1.
X01992 mRNA. Translation: CAA26022.1.
V00543 mRNA. Translation: CAA23804.1.
AY255837 mRNA. Translation: AAP20098.1.
AF375790 Genomic DNA. Translation: AAK53058.1.
AB451324 mRNA. Translation: BAG70138.1.
AB451453 mRNA. Translation: BAG70267.1.
CH471054 Genomic DNA. Translation: EAW97180.1.
BC070256 mRNA. Translation: AAH70256.1.
CCDSCCDS8980.1.
PIRIVHUG. A93284.
RefSeqNP_000610.2. NM_000619.2.
UniGeneHs.856.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EKUX-ray2.90A/B26-161[»]
1FG9X-ray2.90A/B24-156[»]
1FYHX-ray2.04A/D28-156[»]
1HIGX-ray3.50A/B/C/D24-161[»]
3BESX-ray2.20L24-161[»]
ProteinModelPortalP01579.
SMRP01579. Positions 24-155.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109680. 4 interactions.
DIPDIP-483N.
IntActP01579. 2 interactions.
MINTMINT-1508034.
STRING9606.ENSP00000229135.

Chemistry

DrugBankDB01296. Glucosamine.
DB00033. Interferon gamma-1b.
DB00641. Simvastatin.

PTM databases

PhosphoSiteP01579.
UniCarbKBP01579.

Polymorphism databases

DMDM124479.

Proteomic databases

PaxDbP01579.
PRIDEP01579.

Protocols and materials databases

DNASU3458.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000229135; ENSP00000229135; ENSG00000111537.
GeneID3458.
KEGGhsa:3458.
UCSCuc001stw.1. human.

Organism-specific databases

CTD3458.
GeneCardsGC12M068548.
HGNCHGNC:5438. IFNG.
HPACAB010344.
MIM147570. gene.
609135. phenotype.
neXtProtNX_P01579.
Orphanet88. Idiopathic aplastic anemia.
PharmGKBPA29674.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45353.
HOGENOMHOG000254784.
HOVERGENHBG056912.
InParanoidP01579.
KOK04687.
OrthoDBEOG7VHSZM.
PhylomeDBP01579.
TreeFamTF336308.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP01579.

Gene expression databases

ArrayExpressP01579.
BgeeP01579.
CleanExHS_IFNG.
GenevestigatorP01579.

Family and domain databases

Gene3D1.20.1250.10. 1 hit.
InterProIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR002069. Interferon_gamma.
[Graphical view]
PANTHERPTHR11419. PTHR11419. 1 hit.
PfamPF00714. IFN-gamma. 1 hit.
[Graphical view]
PIRSFPIRSF001936. IFN-gamma. 1 hit.
ProDomPD002435. Interferon_gamma. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF47266. SSF47266. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP01579.
GeneWikiInterferon-gamma.
GenomeRNAi3458.
NextBio13624.
PMAP-CutDBP01579.
PROP01579.
SOURCESearch...

Entry information

Entry nameIFNG_HUMAN
AccessionPrimary (citable) accession number: P01579
Secondary accession number(s): B5BU88, Q53ZV4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: July 9, 2014
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM