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Protein

Interferon gamma

Gene

IFNG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • cytokine activity Source: GO_Central
  • interferon-gamma receptor binding Source: ProtInc

GO - Biological processi

  • adaptive immune response Source: GO_Central
  • apoptotic process Source: MGI
  • cell cycle arrest Source: BHF-UCL
  • cell surface receptor signaling pathway Source: ProtInc
  • defense response to virus Source: UniProtKB-KW
  • extrinsic apoptotic signaling pathway Source: BHF-UCL
  • humoral immune response Source: GO_Central
  • interferon-gamma-mediated signaling pathway Source: CAFA
  • interleukin-12-mediated signaling pathway Source: Reactome
  • negative regulation of epithelial cell differentiation Source: BHF-UCL
  • negative regulation of gene expression Source: UniProtKB
  • negative regulation of interleukin-17 production Source: BHF-UCL
  • negative regulation of smooth muscle cell proliferation Source: BHF-UCL
  • negative regulation of transcription, DNA-templated Source: CAFA
  • negative regulation of transcription by RNA polymerase II Source: BHF-UCL
  • positive regulation of autophagy Source: UniProtKB
  • positive regulation of calcidiol 1-monooxygenase activity Source: BHF-UCL
  • positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation involved in immune response Source: UniProtKB
  • positive regulation of cell proliferation Source: BHF-UCL
  • positive regulation of core promoter binding Source: CAFA
  • positive regulation of epithelial cell migration Source: CACAO
  • positive regulation of exosomal secretion Source: UniProtKB
  • positive regulation of fructose 1,6-bisphosphate 1-phosphatase activity Source: BHF-UCL
  • positive regulation of fructose 1,6-bisphosphate metabolic process Source: BHF-UCL
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of interleukin-12 production Source: UniProtKB
  • positive regulation of interleukin-23 production Source: BHF-UCL
  • positive regulation of killing of cells of other organism Source: BHF-UCL
  • positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
  • positive regulation of nitric oxide biosynthetic process Source: BHF-UCL
  • positive regulation of osteoclast differentiation Source: BHF-UCL
  • positive regulation of peptidyl-serine phosphorylation of STAT protein Source: MGI
  • positive regulation of protein complex assembly Source: CAFA
  • positive regulation of protein deacetylation Source: CAFA
  • positive regulation of protein import into nucleus, translocation Source: CAFA
  • positive regulation of protein localization to plasma membrane Source: UniProtKB
  • positive regulation of protein phosphorylation Source: CAFA
  • positive regulation of protein serine/threonine kinase activity Source: CAFA
  • positive regulation of smooth muscle cell apoptotic process Source: BHF-UCL
  • positive regulation of tumor necrosis factor (ligand) superfamily member 11 production Source: BHF-UCL
  • positive regulation of tyrosine phosphorylation of STAT protein Source: BHF-UCL
  • positive regulation of vitamin D biosynthetic process Source: BHF-UCL
  • protein import into nucleus, translocation Source: UniProtKB
  • regulation of growth Source: UniProtKB-KW
  • regulation of insulin secretion Source: BHF-UCL
  • regulation of interferon-gamma-mediated signaling pathway Source: Reactome
  • regulation of protein ADP-ribosylation Source: CAFA
  • regulation of regulatory T cell differentiation Source: Reactome
  • response to virus Source: MGI

Keywordsi

Molecular functionCytokine
Biological processAntiviral defense, Growth regulation

Enzyme and pathway databases

ReactomeiR-HSA-877300 Interferon gamma signaling
R-HSA-877312 Regulation of IFNG signaling
R-HSA-8877330 RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs)
R-HSA-8950505 Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation
SignaLinkiP01579
SIGNORiP01579

Names & Taxonomyi

Protein namesi
Recommended name:
Interferon gamma
Short name:
IFN-gamma
Alternative name(s):
Immune interferon
Gene namesi
Name:IFNG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000111537.4
HGNCiHGNC:5438 IFNG
MIMi147570 gene
neXtProtiNX_P01579

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Aplastic anemia (AA)1 Publication
Disease susceptibility may be associated with variations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:609135

Pharmaceutical usei

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

Organism-specific databases

DisGeNETi3458
MalaCardsiIFNG
MIMi609135 phenotype
OpenTargetsiENSG00000111537
Orphaneti88 Idiopathic aplastic anemia
PharmGKBiPA29674

Chemistry databases

ChEMBLiCHEMBL3286073
DrugBankiDB05676 Apremilast
DB05111 Fontolizumab
DB01296 Glucosamine
DB01250 Olsalazine
DB05110 VIR201

Polymorphism and mutation databases

BioMutaiIFNG
DMDMi124479

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 232 PublicationsAdd BLAST23
ChainiPRO_000001644424 – 161Interferon gammaAdd BLAST138
PropeptideiPRO_0000259481162 – 1665

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei24Pyrrolidone carboxylic acid2 Publications1
Glycosylationi48N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi120N-linked (GlcNAc...) asparagine; in dimeric form1 Publication1

Post-translational modificationi

Proteolytic processing produces C-terminal heterogeneity, with proteins ending alternatively at Gly-150, Met-157 or Gly-161.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

EPDiP01579
PaxDbiP01579
PeptideAtlasiP01579
PRIDEiP01579

PTM databases

GlyConnecti287
293
iPTMnetiP01579
PhosphoSitePlusiP01579
UniCarbKBiP01579

Miscellaneous databases

PMAP-CutDBiP01579

Expressioni

Tissue specificityi

Released primarily from activated T lymphocytes.

Gene expression databases

BgeeiENSG00000111537
CleanExiHS_IFNG
GenevisibleiP01579 HS

Organism-specific databases

HPAiCAB010344

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

Show more details

GO - Molecular functioni

  • cytokine activity Source: GO_Central
  • interferon-gamma receptor binding Source: ProtInc

Protein-protein interaction databases

BioGridi109680, 5 interactors
DIPiDIP-483N
IntActiP01579, 3 interactors
STRINGi9606.ENSP00000229135

Chemistry databases

BindingDBiP01579

Structurei

Secondary structure

1166
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 38Combined sources12
Turni39 – 41Combined sources3
Helixi43 – 46Combined sources4
Helixi53 – 58Combined sources6
Helixi62 – 81Combined sources20
Turni82 – 85Combined sources4
Helixi87 – 89Combined sources3
Helixi90 – 105Combined sources16
Helixi109 – 119Combined sources11
Helixi126 – 141Combined sources16
Helixi146 – 148Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP01579
SMRiP01579
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01579

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IWSY Eukaryota
ENOG410Z8I5 LUCA
GeneTreeiENSGT00390000007831
HOGENOMiHOG000254784
HOVERGENiHBG056912
InParanoidiP01579
KOiK04687
OMAiWKEESDK
OrthoDBiEOG091G0ZH0
PhylomeDBiP01579
TreeFamiTF336308

Family and domain databases

InterProiView protein in InterPro
IPR009079 4_helix_cytokine-like_core
IPR002069 Interferon_gamma
PANTHERiPTHR11419 PTHR11419, 1 hit
PfamiView protein in Pfam
PF00714 IFN-gamma, 1 hit
PIRSFiPIRSF001936 IFN-gamma, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002435 Interferon_gamma, 1 hit
SUPFAMiSSF47266 SSF47266, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01579-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKYTSYILAF QLCIVLGSLG CYCQDPYVKE AENLKKYFNA GHSDVADNGT
60 70 80 90 100
LFLGILKNWK EESDRKIMQS QIVSFYFKLF KNFKDDQSIQ KSVETIKEDM
110 120 130 140 150
NVKFFNSNKK KRDDFEKLTN YSVTDLNVQR KAIHELIQVM AELSPAAKTG
160
KRKRSQMLFR GRRASQ
Length:166
Mass (Da):19,348
Last modified:April 1, 1988 - v1
Checksum:i1514E8F785FD81AA
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00401729K → Q. 1
Natural variantiVAR_004018160R → Q1 PublicationCorresponds to variant dbSNP:rs201359065Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS8980.1
PIRiA93284 IVHUG
RefSeqiNP_000610.2, NM_000619.2
UniGeneiHs.856

Genome annotation databases

EnsembliENST00000229135; ENSP00000229135; ENSG00000111537
GeneIDi3458
KEGGihsa:3458
UCSCiuc001stw.2 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiIFNG_HUMAN
AccessioniPrimary (citable) accession number: P01579
Secondary accession number(s): B5BU88, Q53ZV4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: April 25, 2018
This is version 206 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Pharmaceutical, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health