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P01579

- IFNG_HUMAN

UniProt

P01579 - IFNG_HUMAN

Protein

Interferon gamma

Gene

IFNG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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 growth of symbiont in host Source: Ensembl
    19. negative regulation of interleukin-17 production Source: BHF-UCL
    20. negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis Source: BHF-UCL
    21. negative regulation of metanephric nephron tubule epithelial cell differentiation Source: BHF-UCL
    22. negative regulation of myelination Source: Ensembl
    23. negative regulation of smooth muscle cell proliferation Source: BHF-UCL
    24. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    25. neutrophil apoptotic process Source: Ensembl
    26. neutrophil chemotaxis Source: Ensembl
    27. positive regulation of calcidiol 1-monooxygenase activity Source: BHF-UCL
    28. positive regulation of cell adhesion Source: Ensembl
    29. positive regulation of chemokine biosynthetic process Source: Ensembl
    30. positive regulation of fructose 1,6-bisphosphate 1-phosphatase activity Source: BHF-UCL
    31. positive regulation of fructose 1,6-bisphosphate metabolic process Source: BHF-UCL
    32. positive regulation of interleukin-12 biosynthetic process Source: Ensembl
    33. positive regulation of interleukin-12 production Source: UniProtKB
    34. positive regulation of interleukin-1 beta secretion Source: Ensembl
    35. positive regulation of interleukin-23 production Source: BHF-UCL
    36. positive regulation of interleukin-6 biosynthetic process Source: Ensembl
    37. positive regulation of isotype switching to IgG isotypes Source: Ensembl
    38. positive regulation of killing of cells of other organism Source: BHF-UCL
    39. positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
    40. positive regulation of mesenchymal cell proliferation Source: BHF-UCL
    41. positive regulation of MHC class II biosynthetic process Source: Ensembl
    42. positive regulation of neuron differentiation Source: Ensembl
    43. positive regulation of nitric oxide biosynthetic process Source: BHF-UCL
    44. positive regulation of osteoclast differentiation Source: BHF-UCL
    45. positive regulation of peptidyl-serine phosphorylation of STAT protein Source: BHF-UCL
    46. positive regulation of smooth muscle cell apoptotic process Source: BHF-UCL
    47. positive regulation of synaptic transmission, cholinergic Source: Ensembl
    48. positive regulation of T cell proliferation Source: Ensembl
    49. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    50. positive regulation of tumor necrosis factor (ligand) superfamily member 11 production Source: BHF-UCL
    51. positive regulation of tumor necrosis factor production Source: Ensembl
    52. positive regulation of tyrosine phosphorylation of Stat1 protein Source: BHF-UCL
    53. positive regulation of vitamin D biosynthetic process Source: BHF-UCL
    54. protein import into nucleus, translocation Source: UniProtKB
    55. regulation of insulin secretion Source: BHF-UCL
    56. regulation of interferon-gamma-mediated signaling pathway Source: Reactome
    57. regulation of the force of heart contraction Source: Ensembl
    58. response to drug Source: Ensembl
    59. response to virus Source: MGI

    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

    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

    ArrayExpressiP01579.
    BgeeiP01579.
    CleanExiHS_IFNG.
    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 – 3811
    Helixi43 – 464
    Helixi53 – 586
    Helixi62 – 8120
    Turni82 – 854
    Turni87 – 893
    Helixi90 – 10415
    Helixi109 – 11911
    Helixi126 – 14015
    Helixi146 – 1483

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MKYTSYILAF QLCIVLGSLG CYCQDPYVKE AENLKKYFNA GHSDVADNGT    50
    LFLGILKNWK EESDRKIMQS QIVSFYFKLF KNFKDDQSIQ KSVETIKEDM 100
    NVKFFNSNKK KRDDFEKLTN YSVTDLNVQR KAIHELIQVM AELSPAAKTG 150
    KRKRSQMLFR GRRASQ 166
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    DB00033. Interferon gamma-1b.
    DB00641. Simvastatin.

    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.
    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

    ArrayExpressi P01579.
    Bgeei P01579.
    CleanExi HS_IFNG.
    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

    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: October 1, 2014
    This is version 170 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