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P15260

- INGR1_HUMAN

UniProt

P15260 - INGR1_HUMAN

Protein

Interferon gamma receptor 1

Gene

IFNGR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Receptor for interferon gamma. Two receptors bind one interferon gamma dimer.

    GO - Molecular functioni

    1. interferon-gamma receptor activity Source: ProtInc
    2. protein binding Source: IntAct

    GO - Biological processi

    1. cytokine-mediated signaling pathway Source: Reactome
    2. interferon-gamma-mediated signaling pathway Source: Reactome
    3. regulation of interferon-gamma-mediated signaling pathway Source: Reactome
    4. response to virus Source: ProtInc
    5. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Receptor

    Enzyme and pathway databases

    ReactomeiREACT_24980. Regulation of IFNG signaling.
    REACT_25078. Interferon gamma signaling.
    SignaLinkiP15260.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interferon gamma receptor 1
    Short name:
    IFN-gamma receptor 1
    Short name:
    IFN-gamma-R1
    Alternative name(s):
    CDw119
    CD_antigen: CD119
    Gene namesi
    Name:IFNGR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:5439. IFNGR1.

    Subcellular locationi

    GO - Cellular componenti

    1. dendrite Source: Ensembl
    2. endoplasmic reticulum Source: Ensembl
    3. integral component of plasma membrane Source: ProtInc
    4. membrane Source: InterPro
    5. plasma membrane Source: Reactome
    6. postsynaptic density Source: Ensembl
    7. vesicle Source: Ensembl

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Mendelian susceptibility to mycobacterial disease (MSMD) [MIM:209950]: This rare condition confers predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine and environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections, with the exception of Salmonella which infects less than 50% of these individuals. The pathogenic mechanism underlying MSMD is the impairment of interferon-gamma mediated immunity, whose severity determines the clinical outcome. Some patients die of overwhelming mycobacterial disease with lepromatous-like lesions in early childhood, whereas others develop, later in life, disseminated but curable infections with tuberculoid granulomas. MSMD is a genetically heterogeneous disease with autosomal recessive, autosomal dominant or X-linked inheritance.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti77 – 771C → Y in MSMD; fails to bind IFN-gamma. 1 Publication
    VAR_017577
    Natural varianti87 – 871I → T in MSMD; impaired response to IFN-gamma. 1 Publication
    VAR_017578
    Natural varianti99 – 1024Missing in MSMD; fails to bind IFN-gamma.
    VAR_017579

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi209950. phenotype.
    600263. phenotype.
    Orphaneti319581. Autosomal dominant mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR1 deficiency.
    319569. Autosomal recessive mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR1 deficiency.
    99898. Mendelian susceptibility to mycobacterial diseases due to complete IFNgammaR1 deficiency.
    PharmGKBiPA29675.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Add
    BLAST
    Chaini18 – 489472Interferon gamma receptor 1PRO_0000011009Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi34 – 341N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi77 ↔ 851 Publication
    Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi86 – 861N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi122 ↔ 1671 Publication
    Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi195 ↔ 2001 Publication
    Disulfide bondi214 ↔ 2351 Publication
    Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence Analysis
    Modified residuei369 – 3691PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated at Ser/Thr residues.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP15260.
    PaxDbiP15260.
    PRIDEiP15260.

    PTM databases

    PhosphoSiteiP15260.
    UniCarbKBiP15260.

    Expressioni

    Gene expression databases

    ArrayExpressiP15260.
    BgeeiP15260.
    CleanExiHS_IFNGR1.
    GenevestigatoriP15260.

    Organism-specific databases

    HPAiCAB004444.
    HPA029213.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    STAT1P422245EBI-1030755,EBI-1057697

    Protein-protein interaction databases

    BioGridi109681. 8 interactions.
    DIPiDIP-47N.
    IntActiP15260. 6 interactions.
    MINTiMINT-8013365.
    STRINGi9606.ENSP00000356713.

    Structurei

    Secondary structure

    1
    489
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi33 – 386
    Beta strandi40 – 423
    Beta strandi45 – 495
    Beta strandi58 – 658
    Beta strandi69 – 713
    Beta strandi74 – 8613
    Helixi88 – 903
    Beta strandi98 – 1069
    Helixi121 – 1244
    Beta strandi131 – 1366
    Beta strandi138 – 1469
    Helixi149 – 1513
    Beta strandi168 – 17811
    Beta strandi181 – 19111
    Beta strandi197 – 2059
    Beta strandi212 – 22110
    Turni222 – 2243
    Beta strandi234 – 2374

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FG9X-ray2.90C/D/E18-262[»]
    1FYHX-ray2.04B/E18-246[»]
    1JRHX-ray2.80I18-125[»]
    ProteinModelPortaliP15260.
    SMRiP15260. Positions 28-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15260.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini18 – 245228ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini267 – 489223CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei246 – 26621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the type II cytokine receptor family.Curated
    Contains 2 fibronectin type-III domains.Curated

    Keywords - Domaini

    Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG45077.
    HOGENOMiHOG000113074.
    HOVERGENiHBG052128.
    InParanoidiP15260.
    KOiK05132.
    OMAiNSYHSRN.
    PhylomeDBiP15260.
    TreeFamiTF338358.

    Family and domain databases

    Gene3Di2.60.40.10. 2 hits.
    InterProiIPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR021126. Interferon_gamma_pox/mammal.
    IPR008355. Interferon_gamma_rcpt_asu.
    [Graphical view]
    PANTHERiPTHR20859:SF5. PTHR20859:SF5. 1 hit.
    PfamiPF07140. IFNGR1. 1 hit.
    PF01108. Tissue_fac. 1 hit.
    [Graphical view]
    PRINTSiPR01777. INTERFERONGR.
    SUPFAMiSSF49265. SSF49265. 2 hits.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P15260-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MALLFLLPLV MQGVSRAEMG TADLGPSSVP TPTNVTIESY NMNPIVYWEY    50
    QIMPQVPVFT VEVKNYGVKN SEWIDACINI SHHYCNISDH VGDPSNSLWV 100
    RVKARVGQKE SAYAKSEEFA VCRDGKIGPP KLDIRKEEKQ IMIDIFHPSV 150
    FVNGDEQEVD YDPETTCYIR VYNVYVRMNG SEIQYKILTQ KEDDCDEIQC 200
    QLAIPVSSLN SQYCVSAEGV LHVWGVTTEK SKEVCITIFN SSIKGSLWIP 250
    VVAALLLFLV LSLVFICFYI KKINPLKEKS IILPKSLISV VRSATLETKP 300
    ESKYVSLITS YQPFSLEKEV VCEEPLSPAT VPGMHTEDNP GKVEHTEELS 350
    SITEVVTTEE NIPDVVPGSH LTPIERESSS PLSSNQSEPG SIALNSYHSR 400
    NCSESDHSRN GFDTDSSCLE SHSSLSDSEF PPNNKGEIKT EGQELITVIK 450
    APTSFGYDKP HVLVDLLVDD SGKESLIGYR PTEDSKEFS 489
    Length:489
    Mass (Da):54,405
    Last modified:April 1, 1990 - v1
    Checksum:iDCF9E574D8F47400
    GO
    Isoform 2 (identifier: P15260-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-28: MALLFLLPLVMQGVSRAEMGTADLGPSS → MLLKSPENSLLQFQFKYG
         184-196: QYKILTQKEDDCD → KRSCAFSLFSFFI
         197-489: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:186
    Mass (Da):21,542
    Checksum:i13C30A3C31EF0107
    GO

    Polymorphismi

    A genetic variation in the IFNGR1 gene is associated with susceptibility to Helicobacter pylori infection [MIMi:600263].

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti61 – 611V → I.1 Publication
    Corresponds to variant rs17175322 [ dbSNP | Ensembl ].
    VAR_019281
    Natural varianti77 – 771C → Y in MSMD; fails to bind IFN-gamma. 1 Publication
    VAR_017577
    Natural varianti87 – 871I → T in MSMD; impaired response to IFN-gamma. 1 Publication
    VAR_017578
    Natural varianti99 – 1024Missing in MSMD; fails to bind IFN-gamma.
    VAR_017579
    Natural varianti335 – 3351H → P.2 Publications
    Corresponds to variant rs17175350 [ dbSNP | Ensembl ].
    VAR_019282
    Natural varianti467 – 4671L → P.2 Publications
    Corresponds to variant rs1887415 [ dbSNP | Ensembl ].
    VAR_019283

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2828MALLF…LGPSS → MLLKSPENSLLQFQFKYG in isoform 2. 1 PublicationVSP_055589Add
    BLAST
    Alternative sequencei184 – 19613QYKIL…EDDCD → KRSCAFSLFSFFI in isoform 2. 1 PublicationVSP_055590Add
    BLAST
    Alternative sequencei197 – 489293Missing in isoform 2. 1 PublicationVSP_055591Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03143 mRNA. Translation: AAA52731.1.
    AY594694 Genomic DNA. Translation: AAS89302.1.
    BT006814 mRNA. Translation: AAP35460.1.
    AK294252 mRNA. Translation: BAG57548.1.
    AL050337 Genomic DNA. Translation: CAB53062.1.
    CH471051 Genomic DNA. Translation: EAW47931.1.
    CH471051 Genomic DNA. Translation: EAW47932.1.
    BC005333 mRNA. Translation: AAH05333.1.
    CCDSiCCDS5185.1.
    PIRiA31555.
    RefSeqiNP_000407.1. NM_000416.2.
    UniGeneiHs.520414.

    Genome annotation databases

    EnsembliENST00000367739; ENSP00000356713; ENSG00000027697. [P15260-1]
    GeneIDi3459.
    KEGGihsa:3459.
    UCSCiuc003qho.2. human.

    Polymorphism databases

    DMDMi124474.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    IFNGR1base

    IFNGR1 mutation db

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03143 mRNA. Translation: AAA52731.1 .
    AY594694 Genomic DNA. Translation: AAS89302.1 .
    BT006814 mRNA. Translation: AAP35460.1 .
    AK294252 mRNA. Translation: BAG57548.1 .
    AL050337 Genomic DNA. Translation: CAB53062.1 .
    CH471051 Genomic DNA. Translation: EAW47931.1 .
    CH471051 Genomic DNA. Translation: EAW47932.1 .
    BC005333 mRNA. Translation: AAH05333.1 .
    CCDSi CCDS5185.1.
    PIRi A31555.
    RefSeqi NP_000407.1. NM_000416.2.
    UniGenei Hs.520414.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FG9 X-ray 2.90 C/D/E 18-262 [» ]
    1FYH X-ray 2.04 B/E 18-246 [» ]
    1JRH X-ray 2.80 I 18-125 [» ]
    ProteinModelPortali P15260.
    SMRi P15260. Positions 28-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109681. 8 interactions.
    DIPi DIP-47N.
    IntActi P15260. 6 interactions.
    MINTi MINT-8013365.
    STRINGi 9606.ENSP00000356713.

    Chemistry

    ChEMBLi CHEMBL2364171.
    DrugBanki DB00033. Interferon gamma-1b.

    PTM databases

    PhosphoSitei P15260.
    UniCarbKBi P15260.

    Polymorphism databases

    DMDMi 124474.

    Proteomic databases

    MaxQBi P15260.
    PaxDbi P15260.
    PRIDEi P15260.

    Protocols and materials databases

    DNASUi 3459.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367739 ; ENSP00000356713 ; ENSG00000027697 . [P15260-1 ]
    GeneIDi 3459.
    KEGGi hsa:3459.
    UCSCi uc003qho.2. human.

    Organism-specific databases

    CTDi 3459.
    GeneCardsi GC06M137518.
    HGNCi HGNC:5439. IFNGR1.
    HPAi CAB004444.
    HPA029213.
    MIMi 107470. gene.
    209950. phenotype.
    600263. phenotype.
    neXtProti NX_P15260.
    Orphaneti 319581. Autosomal dominant mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR1 deficiency.
    319569. Autosomal recessive mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR1 deficiency.
    99898. Mendelian susceptibility to mycobacterial diseases due to complete IFNgammaR1 deficiency.
    PharmGKBi PA29675.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG45077.
    HOGENOMi HOG000113074.
    HOVERGENi HBG052128.
    InParanoidi P15260.
    KOi K05132.
    OMAi NSYHSRN.
    PhylomeDBi P15260.
    TreeFami TF338358.

    Enzyme and pathway databases

    Reactomei REACT_24980. Regulation of IFNG signaling.
    REACT_25078. Interferon gamma signaling.
    SignaLinki P15260.

    Miscellaneous databases

    ChiTaRSi IFNGR1. human.
    EvolutionaryTracei P15260.
    GeneWikii Interferon_gamma_receptor_1.
    GenomeRNAii 3459.
    NextBioi 13628.
    PROi P15260.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15260.
    Bgeei P15260.
    CleanExi HS_IFNGR1.
    Genevestigatori P15260.

    Family and domain databases

    Gene3Di 2.60.40.10. 2 hits.
    InterProi IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR021126. Interferon_gamma_pox/mammal.
    IPR008355. Interferon_gamma_rcpt_asu.
    [Graphical view ]
    PANTHERi PTHR20859:SF5. PTHR20859:SF5. 1 hit.
    Pfami PF07140. IFNGR1. 1 hit.
    PF01108. Tissue_fac. 1 hit.
    [Graphical view ]
    PRINTSi PR01777. INTERFERONGR.
    SUPFAMi SSF49265. SSF49265. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of the human interferon-gamma receptor."
      Aguet M., Dembic Z., Merlin G.
      Cell 55:273-280(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. SeattleSNPs variation discovery resource
      Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-61; PRO-335 AND PRO-467.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Amygdala.
    5. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Prostate.
    8. "Alignment of disulfide bonds of the extracellular domain of the interferon gamma receptor and investigation of their role in biological activity."
      Stueber D., Friedlein A., Fountoulakis M., Lahm H.-W., Garotta G.
      Biochemistry 32:2423-2430(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS, PARTIAL PROTEIN SEQUENCE, MUTAGENESIS.
    9. "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) OF 26-248.
    10. "Neutralizing epitopes on the extracellular interferon gamma receptor (IFNgammaR) alpha-chain characterized by homolog scanning mutagenesis and X-ray crystal structure of the A6 fab-IFNgammaR1-108 complex."
      Sogabe S., Stuart F., Henke C., Bridges A., Williams G., Birch A., Winkler F.K., Robinson J.A.
      J. Mol. Biol. 273:882-897(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 28-122 IN COMPLEX WITH ANTIBODY.
    11. "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 ING.
    12. "Partial interferon-gamma receptor 1 deficiency in a child with tuberculoid bacillus Calmette-Guerin infection and a sibling with clinical tuberculosis."
      Jouanguy E., Lamhamedi-Cherradi S.-E., Altare F., Fondaneche M.-C., Tuerlinckx D., Blanche S., Emile J.-F., Gaillard J.-L., Schreiber R., Levin M., Fischer A., Hivroz C., Casanova J.-L.
      J. Clin. Invest. 100:2658-2664(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MSMD THR-87.
    13. Cited for: VARIANTS MSMD TYR-77 AND 99-TRP--VAL-102 DEL.
    14. "Genomewide linkage analysis identifies polymorphism in the human interferon-gamma receptor affecting Helicobacter pylori infection."
      Thye T., Burchard G.D., Nilius M., Mueller-Myhsok B., Horstmann R.D.
      Am. J. Hum. Genet. 72:448-453(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO HELICOBACTER PYLORI INFECTION, VARIANTS PRO-335 AND PRO-467.

    Entry informationi

    Entry nameiINGR1_HUMAN
    AccessioniPrimary (citable) accession number: P15260
    Secondary accession number(s): B4DFT7, E1P587, Q53Y96
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    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, Reference proteome

    Documents

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

    External Data

    Dasty 3