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Q9R002

- IFI2_MOUSE

UniProt

Q9R002 - IFI2_MOUSE

Protein

Interferon-activable protein 202

Gene

Ifi202

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Inhibits the transcriptional activity of several transcription factors, including NF-kappa-B p50 and p65, FOS, JUN, E2F1, E2F4, MYOD1 and myogenin. Has anti-apoptotic effects due to inhibition of the transcriptional activity of p53. Binds dsDNA in the cytosol. Is involved in innate immune response and has anti-inflammatory activity. Inhibits caspase activation in response to cytosolic DNA and inhibits the activation of the AIM2 inflammasome, probably by sequestering cytoplasmic DNA and preventing its being bound by AIM2.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei84 – 841Mediates interaction with 53BP1
    Sitei283 – 2831Mediates interaction with 53BP1

    GO - Molecular functioni

    1. double-stranded DNA binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. inflammatory response Source: UniProtKB-KW
    2. innate immune response Source: UniProtKB-KW
    3. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    4. negative regulation of innate immune response Source: UniProtKB

    Keywords - Biological processi

    Immunity, Inflammatory response, Innate immunity

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_196447. IRF3-mediated induction of type I IFN.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interferon-activable protein 202
    Short name:
    Ifi-202
    Alternative name(s):
    Interferon-inducible protein p202
    Lupus susceptibility protein p202
    Gene namesi
    Name:Ifi202
    Synonyms:Ifi202a, Ifi202b
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1347080. Ifi202a.
    MGI:1347083. Ifi202b.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Accumulates first in the cytoplasm, and is translocated to the nucleus after a delay, where it is primarily chromatin-associated.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi48 – 481K → A: Strongly reduces affinity for DNA; when associated with A-53 and W-54. 1 Publication
    Mutagenesisi53 – 531K → A: Strongly reduces affinity for DNA; when associated with A-48 and W-54. 1 Publication
    Mutagenesisi54 – 541G → W: Strongly reduces affinity for DNA; when associated with A-48 and A-53. 1 Publication
    Mutagenesisi76 – 761K → A: Strongly reduces affinity for DNA; when associated with A-79 and A-236. 1 Publication
    Mutagenesisi79 – 791K → A: Strongly reduces affinity for DNA; when associated with A-76 and A-236. 1 Publication
    Mutagenesisi84 – 841H → F: Loss of interaction with 53BP1; when associated with F-283. 1 Publication
    Mutagenesisi166 – 1661S → A: Strongly reduces affinity for DNA; when associated with. 1 Publication
    Mutagenesisi182 – 1854NDKS → ADAA: Strongly reduces affinity for DNA.
    Mutagenesisi187 – 1871T → A: Strongly reduces affinity for DNA; when associated with A-189 and A-198. 1 Publication
    Mutagenesisi189 – 1891K → A: Strongly reduces affinity for DNA; when associated with A-187 and A-198. 1 Publication
    Mutagenesisi198 – 1981K → A: Strongly reduces affinity for DNA; when associated with A-187 and A-189. 1 Publication
    Mutagenesisi222 – 2243HLR → ALA: Strongly reduces affinity for DNA.
    Mutagenesisi226 – 2261G → W: Strongly reduces affinity for DNA; when associated with A-166; A-227 and A-229. 1 Publication
    Mutagenesisi227 – 2271N → A: Strongly reduces affinity for DNA; when associated with A-166; W-226 and A-229. 1 Publication
    Mutagenesisi229 – 2291K → A: Strongly reduces affinity for DNA; when associated with A-166; W-226 and A-227. 1 Publication
    Mutagenesisi236 – 2361N → A: Strongly reduces affinity for DNA; when associated with A-76 and A-79. 1 Publication
    Mutagenesisi283 – 2831H → F: Loss of interaction with 53BP1; when associated with F-84. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 445445Interferon-activable protein 202PRO_0000153719Add
    BLAST

    Post-translational modificationi

    Phosphorylated.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9R002.
    PRIDEiQ9R002.

    PTM databases

    PhosphoSiteiQ9R002.

    Expressioni

    Inductioni

    By beta interferon. By IL6 in splenocytes (at protein level).1 Publication

    Gene expression databases

    BgeeiQ9R002.
    CleanExiMM_IFI202B.
    GenevestigatoriQ9R002.

    Interactioni

    Subunit structurei

    Binds to several transcription factors, including NF-kappa-B p50 and p65, FOS, JUN, E2F1, E2F4, MYOD1 and myogenin. Also binds p53, the hypophosphorylated, growth-inhibitory form of the retinoblastoma protein and the p53-binding protein 1 (53BP1).1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RB1P064005EBI-3043899,EBI-491274From a different organism.
    Rb1P134057EBI-3043899,EBI-971782

    Protein-protein interaction databases

    BioGridi204945. 1 interaction.
    IntActiQ9R002. 4 interactions.
    MINTiMINT-4098521.

    Structurei

    Secondary structure

    1
    445
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni47 – 504
    Beta strandi56 – 583
    Beta strandi62 – 698
    Beta strandi73 – 753
    Turni76 – 794
    Beta strandi80 – 889
    Beta strandi93 – 986
    Helixi101 – 1066
    Beta strandi112 – 12110
    Beta strandi124 – 1274
    Beta strandi132 – 1354
    Helixi138 – 1403
    Helixi146 – 1538
    Helixi158 – 1614
    Beta strandi169 – 18113
    Beta strandi186 – 1916
    Beta strandi196 – 2016
    Turni211 – 2133
    Beta strandi216 – 2249
    Beta strandi226 – 2283
    Beta strandi231 – 2333
    Beta strandi239 – 2424
    Beta strandi253 – 2564
    Beta strandi260 – 2678
    Beta strandi271 – 2744
    Turni275 – 2784
    Beta strandi279 – 2879
    Beta strandi289 – 2979
    Helixi300 – 3067
    Beta strandi311 – 3144
    Beta strandi316 – 3205
    Beta strandi323 – 3264
    Helixi329 – 3313
    Beta strandi332 – 3343
    Helixi356 – 3616
    Beta strandi368 – 37912
    Beta strandi381 – 3899
    Beta strandi395 – 3995
    Helixi401 – 4055
    Beta strandi413 – 42210
    Beta strandi429 – 44113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4JBJX-ray2.69A/B46-242[»]
    4JBKX-ray2.96A/B/C/D46-242[»]
    4L5QX-ray2.23A46-243[»]
    4L5RX-ray1.87C46-243[»]
    4L5SX-ray2.94A/B46-243[»]
    4L5TX-ray3.40A/B/C/D244-445[»]
    4LNQX-ray2.00A/B53-245[»]
    ProteinModelPortaliQ9R002.
    SMRiQ9R002. Positions 46-242, 244-442.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 243198HIN-200 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini244 – 441198HIN-200 2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The HIN-20 domains mediate dsDNA binding via electrostatic interactions.1 Publication

    Sequence similaritiesi

    Belongs to the HIN-200 family.Curated
    Contains 2 HIN-200 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG81691.
    GeneTreeiENSGT00390000013296.
    InParanoidiQ9R002.
    KOiK12971.
    OrthoDBiEOG7ZD1V8.
    TreeFamiTF337385.

    Family and domain databases

    Gene3Di2.40.50.140. 4 hits.
    InterProiIPR004021. HIN200/IF120x.
    IPR012340. NA-bd_OB-fold.
    [Graphical view]
    PfamiPF02760. HIN. 2 hits.
    [Graphical view]
    PROSITEiPS50834. HIN_200. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9R002-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNRNLRSST NSEFSEGQHQ TPSSDSSGHG EDQPQASPGP NKKSHTPKKN    50
    ISKGAVLHEK PMTVMVLTAT EPFNYKEGKE NMFHATVATE SQYYRVKVFN 100
    MDLKEKFTEN KFITISKYFN SSGILEINET ATVSEAAPNQ IIEVPKNIIR 150
    SAKETLKISK IKELDSGTLI YGVFAVEKKK VNDKSITFKI KDNEDNIKVV 200
    WDKKQHNINY EKGDKLQLFS FHLRKGNGKP ILHSGNHSFI KGEKLLKESF 250
    EGDGYHKGPK QVVALKATKL FTYDSIKSKK MFHATVATDT EFFRVMVFEE 300
    NLEKKFIPGN TIALSDYFGM YGSLAIHEYS SVSEVKSQNK EDSSSSDERL 350
    IEHLKICDLH LQTKERLVDG EFKVYRKSTG NNCICYGIWD DTGAMKVVVS 400
    GQLTSVNCEI GNTIRLVCFE LTSNADEWFL RSTRYSYMEV IMPEK 445
    Length:445
    Mass (Da):50,466
    Last modified:July 27, 2011 - v3
    Checksum:i5EA0E93E143C58EA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 153EFS → DLA in AAF04260. (PubMed:10493828)Curated
    Sequence conflicti13 – 153EFS → DLA in AAH55888. (PubMed:15489334)Curated
    Sequence conflicti79 – 791K → N in ABB00055. 1 PublicationCurated
    Sequence conflicti92 – 921Q → K in AAF04260. (PubMed:10493828)Curated
    Sequence conflicti92 – 921Q → K in AAH18233. (PubMed:15489334)Curated
    Sequence conflicti109 – 1091E → G in ABB00055. 1 PublicationCurated
    Sequence conflicti111 – 1111K → Q in AAH18233. (PubMed:15489334)Curated
    Sequence conflicti127 – 1271I → F in ABB00055. 1 PublicationCurated
    Sequence conflicti141 – 1422II → MF in AAA39312. (PubMed:2477366)Curated
    Sequence conflicti141 – 1422II → MF in AAF04260. (PubMed:10493828)Curated
    Sequence conflicti141 – 1422II → MF in ABB00055. 1 PublicationCurated
    Sequence conflicti141 – 1422II → MF in AAH18233. (PubMed:15489334)Curated
    Sequence conflicti141 – 1422II → MF in AAH55888. (PubMed:15489334)Curated
    Sequence conflicti187 – 1871T → I in ABB00055. 1 PublicationCurated
    Sequence conflicti190 – 1901I → V in ABB00055. 1 PublicationCurated
    Sequence conflicti204 – 2041K → E in AAA39312. (PubMed:2477366)Curated
    Sequence conflicti204 – 2041K → E in AAF04260. (PubMed:10493828)Curated
    Sequence conflicti204 – 2041K → E in ABB00055. 1 PublicationCurated
    Sequence conflicti204 – 2041K → E in AAH18233. (PubMed:15489334)Curated
    Sequence conflicti204 – 2041K → E in AAH55888. (PubMed:15489334)Curated
    Sequence conflicti240 – 2401I → V in AAF04260. (PubMed:10493828)Curated
    Sequence conflicti350 – 3501L → P in AAA39312. (PubMed:2477366)Curated
    Sequence conflicti350 – 3501L → P in AAF04260. (PubMed:10493828)Curated
    Sequence conflicti350 – 3501L → P in ABB00055. 1 PublicationCurated
    Sequence conflicti350 – 3501L → P in AAH18233. (PubMed:15489334)Curated
    Sequence conflicti350 – 3501L → P in AAH55888. (PubMed:15489334)Curated
    Sequence conflicti364 – 3641K → E in AAA39312. (PubMed:2477366)Curated
    Sequence conflicti364 – 3641K → E in AAF04260. (PubMed:10493828)Curated
    Sequence conflicti364 – 3641K → E in ABB00055. 1 PublicationCurated
    Sequence conflicti364 – 3641K → E in AAH18233. (PubMed:15489334)Curated
    Sequence conflicti364 – 3641K → E in AAH55888. (PubMed:15489334)Curated
    Sequence conflicti368 – 3681V → F in AAA39312. (PubMed:2477366)Curated
    Sequence conflicti379 – 3791T → S in AAA39312. (PubMed:2477366)Curated
    Sequence conflicti379 – 3791T → S in AAF04260. (PubMed:10493828)Curated
    Sequence conflicti379 – 3791T → S in ABB00055. 1 PublicationCurated
    Sequence conflicti379 – 3791T → S in AAH18233. (PubMed:15489334)Curated
    Sequence conflicti379 – 3791T → S in AAH55888. (PubMed:15489334)Curated
    Sequence conflicti432 – 4321S → A in AAA39312. (PubMed:2477366)Curated
    Sequence conflicti432 – 4321S → A in AAF04260. (PubMed:10493828)Curated
    Sequence conflicti432 – 4321S → A in ABB00055. 1 PublicationCurated
    Sequence conflicti432 – 4321S → A in AAH18233. (PubMed:15489334)Curated
    Sequence conflicti432 – 4321S → A in AAH55888. (PubMed:15489334)Curated

    Polymorphismi

    NZB mice express 10 to 100 fold more Ifi202 in spleen than B6 or NZW mice. This could account for the high susceptibility of NZB mice to systemic lupus.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31418 mRNA. Translation: AAA39312.1.
    AF140672 mRNA. Translation: AAF04260.1.
    DQ222946 mRNA. Translation: ABB00055.1.
    AC170584 Genomic DNA. No translation available.
    BC018233 mRNA. Translation: AAH18233.1.
    BC055888 mRNA. Translation: AAH55888.1.
    CCDSiCCDS35794.1.
    PIRiA34457.
    RefSeqiNP_032353.2. NM_008327.2.
    NP_036070.2. NM_011940.2.
    XP_001473923.2. XM_001473873.3.
    XP_006536966.1. XM_006536903.1.
    UniGeneiMm.218770.

    Genome annotation databases

    EnsembliENSMUST00000000266; ENSMUSP00000000266; ENSMUSG00000026535.
    GeneIDi100044068.
    26388.
    KEGGimmu:100044068.
    mmu:26388.
    UCSCiuc007dsk.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31418 mRNA. Translation: AAA39312.1 .
    AF140672 mRNA. Translation: AAF04260.1 .
    DQ222946 mRNA. Translation: ABB00055.1 .
    AC170584 Genomic DNA. No translation available.
    BC018233 mRNA. Translation: AAH18233.1 .
    BC055888 mRNA. Translation: AAH55888.1 .
    CCDSi CCDS35794.1.
    PIRi A34457.
    RefSeqi NP_032353.2. NM_008327.2.
    NP_036070.2. NM_011940.2.
    XP_001473923.2. XM_001473873.3.
    XP_006536966.1. XM_006536903.1.
    UniGenei Mm.218770.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4JBJ X-ray 2.69 A/B 46-242 [» ]
    4JBK X-ray 2.96 A/B/C/D 46-242 [» ]
    4L5Q X-ray 2.23 A 46-243 [» ]
    4L5R X-ray 1.87 C 46-243 [» ]
    4L5S X-ray 2.94 A/B 46-243 [» ]
    4L5T X-ray 3.40 A/B/C/D 244-445 [» ]
    4LNQ X-ray 2.00 A/B 53-245 [» ]
    ProteinModelPortali Q9R002.
    SMRi Q9R002. Positions 46-242, 244-442.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204945. 1 interaction.
    IntActi Q9R002. 4 interactions.
    MINTi MINT-4098521.

    PTM databases

    PhosphoSitei Q9R002.

    Proteomic databases

    PaxDbi Q9R002.
    PRIDEi Q9R002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000000266 ; ENSMUSP00000000266 ; ENSMUSG00000026535 .
    GeneIDi 100044068.
    26388.
    KEGGi mmu:100044068.
    mmu:26388.
    UCSCi uc007dsk.2. mouse.

    Organism-specific databases

    CTDi 26388.
    MGIi MGI:1347080. Ifi202a.
    MGI:1347083. Ifi202b.

    Phylogenomic databases

    eggNOGi NOG81691.
    GeneTreei ENSGT00390000013296.
    InParanoidi Q9R002.
    KOi K12971.
    OrthoDBi EOG7ZD1V8.
    TreeFami TF337385.

    Enzyme and pathway databases

    Reactomei REACT_196447. IRF3-mediated induction of type I IFN.

    Miscellaneous databases

    ChiTaRSi Ifi202b. mouse.
    NextBioi 304323.
    PROi Q9R002.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9R002.
    CleanExi MM_IFI202B.
    Genevestigatori Q9R002.

    Family and domain databases

    Gene3Di 2.40.50.140. 4 hits.
    InterProi IPR004021. HIN200/IF120x.
    IPR012340. NA-bd_OB-fold.
    [Graphical view ]
    Pfami PF02760. HIN. 2 hits.
    [Graphical view ]
    PROSITEi PS50834. HIN_200. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Interferons as gene activators. Indications for repeated gene duplication during the evolution of a cluster of interferon-activatable genes on murine chromosome 1."
      Choubey D., Snoddy J., Chaturvedi V., Toniato E., Opdenakker G., Thakur A., Samanta H., Engel D.A., Lengyel P.
      J. Biol. Chem. 264:17182-17189(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: AKR.
    2. "Characteristics of three homologous 202 genes (Ifi202a, ifi202b, and ifi202c) from the murine interferon-activatable gene 200 cluster."
      Wang H., Chatterjee G., Meyer J.J., Liu C.J., Manjunath N.A., Bray-Ward P., Lengyel P.
      Genomics 60:281-294(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: 129/Sv.
    3. "Coding cDNA sequence for p202 in New Zealand Black mice."
      Chen J., Choubey D.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: NZB.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "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].
      Strain: Czech II and FVB/N.
      Tissue: Mammary tumor.
    6. "p202, an interferon-inducible modulator of transcription, inhibits transcriptional activation by the p53 tumor suppressor protein, and a segment from the p53-binding protein 1 that binds to p202 overcomes this inhibition."
      Datta B., Li B., Choubey D., Nallur G., Lengyel P.
      J. Biol. Chem. 271:27544-27555(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-84 AND HIS-283.
    7. "Evidence for an interferon-inducible gene, Ifi202, in the susceptibility to systemic lupus."
      Rozzo S.J., Allard J.D., Choubey D., Vyse T.J., Izui S., Peltz G., Kotzin B.L.
      Immunity 15:435-443(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYMORPHISM.
    8. "Interleukin-6 induces expression of Ifi202, an interferon-inducible candidate gene for lupus susceptibility."
      Pramanik R., Jorgensen T.N., Xin H., Kotzin B.L., Choubey D.
      J. Biol. Chem. 279:16121-16127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY IL6.
    9. "Increased expression of Ifi202, an IFN-activatable gene, in B6.Nba2 lupus susceptible mice inhibits p53-mediated apoptosis."
      Xin H., D'Souza S., Jorgensen T.N., Vaughan A.T., Lengyel P., Kotzin B.L., Choubey D.
      J. Immunol. 176:5863-5870(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TP53.
    10. "HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA."
      Roberts T.L., Idris A., Dunn J.A., Kelly G.M., Burnton C.M., Hodgson S., Hardy L.L., Garceau V., Sweet M.J., Ross I.L., Hume D.A., Stacey K.J.
      Science 323:1057-1060(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "Structural basis for termination of AIM2-mediated signaling by p202."
      Ru H., Ni X., Zhao L., Crowley C., Ding W., Hung L.W., Shaw N., Cheng G., Liu Z.J.
      Cell Res. 23:855-858(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 46-242 IN COMPLEX WITH DNA, FUNCTION, DOMAIN, MUTAGENESIS OF LYS-48; LYS-53; GLY-54; LYS-76; LYS-79; SER-166; 182-ASN--SER-185; THR-187; LYS-189; LYS-198; 222-HIS--ARG-224; GLY-226; ASN-227; LYS-229 AND ASN-236, DNA BINDING.

    Entry informationi

    Entry nameiIFI2_MOUSE
    AccessioniPrimary (citable) accession number: Q9R002
    Secondary accession number(s): E9QLD9
    , P15091, Q38JF1, Q7TMN6, Q8VEL7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 97 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3