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P01579

- IFNG_HUMAN

UniProt

P01579 - IFNG_HUMAN

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Protein

Interferon gamma

Gene

IFNG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- 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

  1. cytokine activity Source: RefGenome
  2. interferon-gamma receptor binding Source: ProtInc

GO - Biological processi

  1. adaptive immune response Source: RefGenome
  2. antigen processing and presentation Source: Ensembl
  3. apoptotic process Source: MGI
  4. CD8-positive, alpha-beta T cell differentiation involved in immune response Source: Ensembl
  5. cell cycle arrest Source: BHF-UCL
  6. cell surface receptor signaling pathway Source: ProtInc
  7. cellular component movement Source: ProtInc
  8. cellular response to interleukin-18 Source: Ensembl
  9. cellular response to lipopolysaccharide Source: Ensembl
  10. cytokine-mediated signaling pathway Source: Reactome
  11. defense response to bacterium Source: Ensembl
  12. defense response to protozoan Source: Ensembl
  13. defense response to virus Source: UniProtKB-KW
  14. endoplasmic reticulum unfolded protein response Source: Ensembl
  15. extrinsic apoptotic signaling pathway Source: BHF-UCL
  16. humoral immune response Source: RefGenome
  17. interferon-gamma-mediated signaling pathway Source: Reactome
  18. negative regulation of epithelial cell differentiation Source: BHF-UCL
  19. negative regulation of growth of symbiont in host Source: Ensembl
  20. negative regulation of interleukin-17 production Source: BHF-UCL
  21. negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis Source: Ensembl
  22. negative regulation of metanephric nephron tubule epithelial cell differentiation Source: Ensembl
  23. negative regulation of myelination Source: Ensembl
  24. negative regulation of smooth muscle cell proliferation Source: BHF-UCL
  25. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  26. neutrophil apoptotic process Source: Ensembl
  27. neutrophil chemotaxis Source: Ensembl
  28. positive regulation of calcidiol 1-monooxygenase activity Source: BHF-UCL
  29. positive regulation of cell adhesion Source: Ensembl
  30. positive regulation of cell proliferation Source: BHF-UCL
  31. positive regulation of chemokine biosynthetic process Source: Ensembl
  32. positive regulation of fructose 1,6-bisphosphate 1-phosphatase activity Source: BHF-UCL
  33. positive regulation of fructose 1,6-bisphosphate metabolic process Source: BHF-UCL
  34. positive regulation of interleukin-12 biosynthetic process Source: Ensembl
  35. positive regulation of interleukin-12 production Source: UniProtKB
  36. positive regulation of interleukin-1 beta secretion Source: Ensembl
  37. positive regulation of interleukin-23 production Source: BHF-UCL
  38. positive regulation of interleukin-6 biosynthetic process Source: Ensembl
  39. positive regulation of isotype switching to IgG isotypes Source: Ensembl
  40. positive regulation of killing of cells of other organism Source: BHF-UCL
  41. positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
  42. positive regulation of mesenchymal cell proliferation Source: Ensembl
  43. positive regulation of MHC class II biosynthetic process Source: Ensembl
  44. positive regulation of neuron differentiation Source: Ensembl
  45. positive regulation of nitric oxide biosynthetic process Source: BHF-UCL
  46. positive regulation of osteoclast differentiation Source: BHF-UCL
  47. positive regulation of peptidyl-serine phosphorylation of STAT protein Source: BHF-UCL
  48. positive regulation of smooth muscle cell apoptotic process Source: BHF-UCL
  49. positive regulation of synaptic transmission, cholinergic Source: Ensembl
  50. positive regulation of T cell proliferation Source: Ensembl
  51. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  52. positive regulation of tumor necrosis factor (ligand) superfamily member 11 production Source: BHF-UCL
  53. positive regulation of tumor necrosis factor production Source: Ensembl
  54. positive regulation of tyrosine phosphorylation of Stat1 protein Source: BHF-UCL
  55. positive regulation of vitamin D biosynthetic process Source: BHF-UCL
  56. protein import into nucleus, translocation Source: UniProtKB
  57. regulation of insulin secretion Source: BHF-UCL
  58. regulation of interferon-gamma-mediated signaling pathway Source: Reactome
  59. regulation of the force of heart contraction Source: Ensembl
  60. response to drug Source: Ensembl
  61. response to virus Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Keywords - Biological processi

Antiviral defense, Growth regulation

Enzyme and pathway databases

ReactomeiREACT_24980. Regulation of IFNG signaling.
REACT_25078. Interferon gamma signaling.
SignaLinkiP01579.

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
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:5438. IFNG.

Subcellular locationi

GO - Cellular componenti

  1. external side of plasma membrane Source: Ensembl
  2. extracellular region Source: BHF-UCL
  3. extracellular space Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

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 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

MIMi609135. phenotype.
Orphaneti88. Idiopathic aplastic anemia.
PharmGKBiPA29674.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23232 PublicationsAdd
BLAST
Chaini24 – 161138Interferon gammaPRO_0000016444Add
BLAST
Propeptidei162 – 1665PRO_0000259481

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241Pyrrolidone carboxylic acid2 Publications
Glycosylationi48 – 481N-linked (GlcNAc...)1 Publication
Glycosylationi120 – 1201N-linked (GlcNAc...); in dimeric form1 Publication

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

PaxDbiP01579.
PRIDEiP01579.

PTM databases

PhosphoSiteiP01579.
UniCarbKBiP01579.

Miscellaneous databases

PMAP-CutDBP01579.

Expressioni

Tissue specificityi

Released primarily from activated T lymphocytes.

Gene expression databases

BgeeiP01579.
CleanExiHS_IFNG.
ExpressionAtlasiP01579. baseline and differential.
GenevestigatoriP01579.

Organism-specific databases

HPAiCAB010344.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi109680. 4 interactions.
DIPiDIP-483N.
IntActiP01579. 2 interactions.
MINTiMINT-1508034.
STRINGi9606.ENSP00000229135.

Structurei

Secondary structure

1
166
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi28 – 3811Combined sources
Helixi43 – 464Combined sources
Helixi53 – 586Combined sources
Helixi62 – 8120Combined sources
Turni82 – 854Combined sources
Turni87 – 893Combined sources
Helixi90 – 10415Combined sources
Helixi109 – 11911Combined sources
Helixi126 – 14015Combined sources
Helixi146 – 1483Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 24-155.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01579.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG45353.
GeneTreeiENSGT00390000007831.
HOGENOMiHOG000254784.
HOVERGENiHBG056912.
InParanoidiP01579.
KOiK04687.
OrthoDBiEOG7VHSZM.
PhylomeDBiP01579.
TreeFamiTF336308.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR002069. Interferon_gamma.
[Graphical view]
PANTHERiPTHR11419. PTHR11419. 1 hit.
PfamiPF00714. IFN-gamma. 1 hit.
[Graphical view]
PIRSFiPIRSF001936. IFN-gamma. 1 hit.
ProDomiPD002435. Interferon_gamma. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 291K → Q.
VAR_004017
Natural varianti160 – 1601R → Q.1 Publication
VAR_004018

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.1. human.

Polymorphism databases

DMDMi124479.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Interferon gamma entry

SeattleSNPs

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 .
CCDSi CCDS8980.1.
PIRi A93284. IVHUG.
RefSeqi NP_000610.2. NM_000619.2.
UniGenei Hs.856.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EKU X-ray 2.90 A/B 26-161 [» ]
1FG9 X-ray 2.90 A/B 24-156 [» ]
1FYH X-ray 2.04 A/D 28-156 [» ]
1HIG X-ray 3.50 A/B/C/D 24-161 [» ]
3BES X-ray 2.20 L 24-161 [» ]
ProteinModelPortali P01579.
SMRi P01579. Positions 24-155.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109680. 4 interactions.
DIPi DIP-483N.
IntActi P01579. 2 interactions.
MINTi MINT-1508034.
STRINGi 9606.ENSP00000229135.

Chemistry

DrugBanki DB01296. Glucosamine.
DB01250. Olsalazine.

PTM databases

PhosphoSitei P01579.
UniCarbKBi P01579.

Polymorphism databases

DMDMi 124479.

Proteomic databases

PaxDbi P01579.
PRIDEi P01579.

Protocols and materials databases

DNASUi 3458.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000229135 ; ENSP00000229135 ; ENSG00000111537 .
GeneIDi 3458.
KEGGi hsa:3458.
UCSCi uc001stw.1. human.

Organism-specific databases

CTDi 3458.
GeneCardsi GC12M068548.
HGNCi HGNC:5438. IFNG.
HPAi CAB010344.
MIMi 147570. gene.
609135. phenotype.
neXtProti NX_P01579.
Orphaneti 88. Idiopathic aplastic anemia.
PharmGKBi PA29674.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG45353.
GeneTreei ENSGT00390000007831.
HOGENOMi HOG000254784.
HOVERGENi HBG056912.
InParanoidi P01579.
KOi K04687.
OrthoDBi EOG7VHSZM.
PhylomeDBi P01579.
TreeFami TF336308.

Enzyme and pathway databases

Reactomei REACT_24980. Regulation of IFNG signaling.
REACT_25078. Interferon gamma signaling.
SignaLinki P01579.

Miscellaneous databases

EvolutionaryTracei P01579.
GeneWikii Interferon-gamma.
GenomeRNAii 3458.
NextBioi 13624.
PMAP-CutDB P01579.
PROi P01579.
SOURCEi Search...

Gene expression databases

Bgeei P01579.
CleanExi HS_IFNG.
ExpressionAtlasi P01579. baseline and differential.
Genevestigatori P01579.

Family and domain databases

Gene3Di 1.20.1250.10. 1 hit.
InterProi IPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR002069. Interferon_gamma.
[Graphical view ]
PANTHERi PTHR11419. PTHR11419. 1 hit.
Pfami PF00714. IFN-gamma. 1 hit.
[Graphical view ]
PIRSFi PIRSF001936. IFN-gamma. 1 hit.
ProDomi PD002435. Interferon_gamma. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF47266. SSF47266. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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.

Entry informationi

Entry nameiIFNG_HUMAN
AccessioniPrimary (citable) accession number: P01579
Secondary accession number(s): B5BU88, Q53ZV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: November 26, 2014
This is version 172 of the entry and version 1 of the sequence. [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

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3