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O14862

- AIM2_HUMAN

UniProt

O14862 - AIM2_HUMAN

Protein

Interferon-inducible protein AIM2

Gene

AIM2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Involved in innate immune response by recognizing cytosolic double-stranded DNA and inducing caspase-1-activating inflammasome formation in macrophages. Upon binding to DNA is thought to undergo oligomerization and to associate with PYCARD initiating the recruitment of caspase-1 precusrsor and processing of interleukin-1 beta and interleukin-18. Detects cytosolic dsDNA of viral and bacterial origin in a non-sequence-specific manner. Can also trigger PYCARD-dependent, caspase-1-independent cell death that involves caspase-8 By similarity. Tumor suppressor which may act by repressing NF-kappa-B transcriptional activity.By similarity6 Publications

    Enzyme regulationi

    In absence of dsDNA DAPIN and HIN-20 domain can interact inducing a closed conformation; an autoinhibitory mechanism is proposed in which binding to dsDNA liberates the DAPIN domain for homotypic downstream signaling interactions with PYCARD.1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    1. activation of innate immune response Source: UniProtKB
    2. apoptotic process Source: UniProtKB-KW
    3. cellular response to drug Source: MGI
    4. cellular response to interferon-beta Source: Ensembl
    5. immune response Source: ProtInc
    6. inflammatory response Source: UniProtKB-KW
    7. innate immune response Source: Reactome
    8. interleukin-1 beta secretion Source: MGI
    9. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
    10. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
    11. positive regulation of cysteine-type endopeptidase activity Source: UniProtKB
    12. positive regulation of defense response to virus by host Source: UniProtKB
    13. positive regulation of interleukin-1 beta production Source: UniProtKB
    14. positive regulation of interleukin-1 beta secretion Source: UniProtKB
    15. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    16. positive regulation of protein oligomerization Source: UniProtKB
    17. pyroptosis Source: UniProtKB
    18. tumor necrosis factor-mediated signaling pathway Source: UniProtKB

    Keywords - Biological processi

    Apoptosis, Immunity, Inflammatory response, Innate immunity

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_75777. The AIM2 inflammasome.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interferon-inducible protein AIM2
    Alternative name(s):
    Absent in melanoma 2
    Gene namesi
    Name:AIM2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:357. AIM2.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Activated inflammasomes can aggregate in the cytosol as speck-like particles.

    GO - Cellular componenti

    1. AIM2 inflammasome complex Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: Reactome
    4. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141L → A: Fails to activate interleukin-1 beta production. 1 Publication
    Mutagenesisi160 – 1601K → A: Impairs DNA binding; when associated with A-160; A-K162; A-163; A-198; A-204. Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204; A-244; A-251; A-309; A-311; A-355 and A-337. 1 Publication
    Mutagenesisi162 – 1621K → A: Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204. Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204; A-244; A-251; A-309; A-311; A-355 and A-337. 1 Publication
    Mutagenesisi163 – 1631K → A: Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204. Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204; A-244; A-251; A-309; A-311; A-355 and A-337. 1 Publication
    Mutagenesisi165 – 1651F → A: Impairs DNA binding. 1 Publication
    Mutagenesisi198 – 1981K → A: Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204. Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204; A-244; A-251; A-309; A-311; A-355 and A-337. 1 Publication
    Mutagenesisi204 – 2041K → A: Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204. Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204; A-244; A-251; A-309; A-311; A-355 and A-337. 1 Publication
    Mutagenesisi244 – 2441R → A: Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204. Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204; A-244; A-251; A-309; A-311; A-355 and A-337. 1 Publication
    Mutagenesisi251 – 2511K → A: Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204. Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204; A-244; A-251; A-309; A-311; A-355 and A-337. 1 Publication
    Mutagenesisi309 – 3091K → A: Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204. Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204; A-244; A-251; A-309; A-311; A-355 and A-337. 1 Publication
    Mutagenesisi311 – 3111R → A: Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204. Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204; A-244; A-251; A-309; A-311; A-355 and A-337. 1 Publication
    Mutagenesisi335 – 3351K → A: Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204. Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204; A-244; A-251; A-309; A-311; A-355 and A-337. 1 Publication
    Mutagenesisi337 – 3371I → A: Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204. Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204; A-244; A-251; A-309; A-311; A-355 and A-337. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA24651.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 343343Interferon-inducible protein AIM2PRO_0000153726Add
    BLAST

    Proteomic databases

    MaxQBiO14862.
    PaxDbiO14862.
    PRIDEiO14862.

    PTM databases

    PhosphoSiteiO14862.

    Expressioni

    Tissue specificityi

    Expressed in spleen, small intestine, peripheral blood leukocytes, and testis.1 Publication

    Inductioni

    By IFNG/IFN-gamma and IFNB1/IFN-beta.3 Publications

    Gene expression databases

    ArrayExpressiO14862.
    BgeeiO14862.
    CleanExiHS_AIM2.
    GenevestigatoriO14862.

    Organism-specific databases

    HPAiHPA031365.

    Interactioni

    Subunit structurei

    Self-associates; forms homooligomers in response to cytosolic dsDNA and the dsDNA seems to serve as oligomerization platform. Component of the AIM2 inflammasome. Interacts with PYCARD, IFI16, EIF2AK2/PKR and MAPRE1.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-6253193,EBI-6253193
    PYCARDQ9ULZ35EBI-6253193,EBI-751215

    Protein-protein interaction databases

    DIPiDIP-59741N.
    IntActiO14862. 5 interactions.
    STRINGi9606.ENSP00000357112.

    Structurei

    Secondary structure

    343
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 1111
    Helixi14 – 163
    Helixi19 – 2911
    Turni30 – 323
    Helixi37 – 404
    Helixi45 – 5612
    Helixi58 – 7114
    Helixi75 – 9117
    Beta strandi148 – 1503
    Beta strandi154 – 1618
    Beta strandi165 – 1695
    Beta strandi172 – 18211
    Beta strandi187 – 1926
    Helixi195 – 1995
    Beta strandi206 – 2149
    Beta strandi219 – 2213
    Beta strandi225 – 2295
    Helixi240 – 2478
    Helixi252 – 2565
    Beta strandi263 – 27513
    Beta strandi277 – 28610
    Beta strandi289 – 2968
    Helixi300 – 3023
    Beta strandi309 – 31911
    Beta strandi321 – 3277
    Beta strandi333 – 3375

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3RN2X-ray2.55A/B144-343[»]
    3RN5X-ray2.50A/B/C/D144-343[»]
    3VD8X-ray2.07A1-107[»]
    4O7QX-ray1.82A1-93[»]
    ProteinModelPortaliO14862.
    SMRiO14862. Positions 1-97, 147-340.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 8787DAPINPROSITE-ProRule annotationAdd
    BLAST
    Domaini138 – 337200HIN-200PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi206 – 2094Poly-Ile

    Domaini

    The DAPIN domain mediates homotypic interaction with PYCARD (PubMed:19158676, PubMed:19158675).2 Publications
    The HIN-20 domain mediates dsDNA binding via electrostatic interactions.1 Publication

    Sequence similaritiesi

    Belongs to the HIN-200 family.Curated
    Contains 1 DAPIN domain.PROSITE-ProRule annotation
    Contains 1 HIN-200 domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG132015.
    HOGENOMiHOG000033871.
    HOVERGENiHBG006122.
    KOiK12966.
    OMAiFQKLNYM.
    OrthoDBiEOG78H3TT.
    PhylomeDBiO14862.
    TreeFamiTF337385.

    Family and domain databases

    Gene3Di1.10.533.10. 1 hit.
    2.40.50.140. 2 hits.
    InterProiIPR004020. DAPIN.
    IPR011029. DEATH-like_dom.
    IPR004021. HIN200/IF120x.
    IPR012340. NA-bd_OB-fold.
    [Graphical view]
    PfamiPF02760. HIN. 1 hit.
    PF02758. PYRIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF47986. SSF47986. 1 hit.
    PROSITEiPS50824. DAPIN. 1 hit.
    PS50834. HIN_200. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O14862-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESKYKEILL LTGLDNITDE ELDRFKFFLS DEFNIATGKL HTANRIQVAT    50
    LMIQNAGAVS AVMKTIRIFQ KLNYMLLAKR LQEEKEKVDK QYKSVTKPKP 100
    LSQAEMSPAA SAAIRNDVAK QRAAPKVSPH VKPEQKQMVA QQESIREGFQ 150
    KRCLPVMVLK AKKPFTFETQ EGKQEMFHAT VATEKEFFFV KVFNTLLKDK 200
    FIPKRIIIIA RYYRHSGFLE VNSASRVLDA ESDQKVNVPL NIIRKAGETP 250
    KINTLQTQPL GTIVNGLFVV QKVTEKKKNI LFDLSDNTGK MEVLGVRNED 300
    TMKCKEGDKV RLTFFTLSKN GEKLQLTSGV HSTIKVIKAK KKT 343
    Length:343
    Mass (Da):38,954
    Last modified:January 1, 1998 - v1
    Checksum:i92EC418AB28CE1E6
    GO

    Sequence cautioni

    The sequence AAH10940.1 differs from that shown. Reason: Frameshift at position 340.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti253 – 2531N → D in BAF84731. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321E → K.1 Publication
    Corresponds to variant rs2276405 [ dbSNP | Ensembl ].
    VAR_022022
    Natural varianti304 – 3041C → Y.1 Publication
    VAR_043379

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF024714 mRNA. Translation: AAB81613.1.
    AK292042 mRNA. Translation: BAF84731.1.
    AL359753 Genomic DNA. Translation: CAI15088.1.
    BC010940 mRNA. Translation: AAH10940.1. Frameshift.
    CCDSiCCDS1181.1.
    RefSeqiNP_004824.1. NM_004833.1.
    UniGeneiHs.733411.

    Genome annotation databases

    EnsembliENST00000368130; ENSP00000357112; ENSG00000163568.
    GeneIDi9447.
    KEGGihsa:9447.
    UCSCiuc001ftj.1. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF024714 mRNA. Translation: AAB81613.1 .
    AK292042 mRNA. Translation: BAF84731.1 .
    AL359753 Genomic DNA. Translation: CAI15088.1 .
    BC010940 mRNA. Translation: AAH10940.1 . Frameshift.
    CCDSi CCDS1181.1.
    RefSeqi NP_004824.1. NM_004833.1.
    UniGenei Hs.733411.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3RN2 X-ray 2.55 A/B 144-343 [» ]
    3RN5 X-ray 2.50 A/B/C/D 144-343 [» ]
    3VD8 X-ray 2.07 A 1-107 [» ]
    4O7Q X-ray 1.82 A 1-93 [» ]
    ProteinModelPortali O14862.
    SMRi O14862. Positions 1-97, 147-340.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59741N.
    IntActi O14862. 5 interactions.
    STRINGi 9606.ENSP00000357112.

    PTM databases

    PhosphoSitei O14862.

    Proteomic databases

    MaxQBi O14862.
    PaxDbi O14862.
    PRIDEi O14862.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368130 ; ENSP00000357112 ; ENSG00000163568 .
    GeneIDi 9447.
    KEGGi hsa:9447.
    UCSCi uc001ftj.1. human.

    Organism-specific databases

    CTDi 9447.
    GeneCardsi GC01M159032.
    HGNCi HGNC:357. AIM2.
    HPAi HPA031365.
    MIMi 604578. gene.
    neXtProti NX_O14862.
    PharmGKBi PA24651.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG132015.
    HOGENOMi HOG000033871.
    HOVERGENi HBG006122.
    KOi K12966.
    OMAi FQKLNYM.
    OrthoDBi EOG78H3TT.
    PhylomeDBi O14862.
    TreeFami TF337385.

    Enzyme and pathway databases

    Reactomei REACT_75777. The AIM2 inflammasome.

    Miscellaneous databases

    GeneWikii AIM2.
    GenomeRNAii 9447.
    NextBioi 35388.
    PROi O14862.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14862.
    Bgeei O14862.
    CleanExi HS_AIM2.
    Genevestigatori O14862.

    Family and domain databases

    Gene3Di 1.10.533.10. 1 hit.
    2.40.50.140. 2 hits.
    InterProi IPR004020. DAPIN.
    IPR011029. DEATH-like_dom.
    IPR004021. HIN200/IF120x.
    IPR012340. NA-bd_OB-fold.
    [Graphical view ]
    Pfami PF02760. HIN. 1 hit.
    PF02758. PYRIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47986. SSF47986. 1 hit.
    PROSITEi PS50824. DAPIN. 1 hit.
    PS50834. HIN_200. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning a novel member of the human interferon-inducible gene family associated with control of tumorigenicity in a model of human melanoma."
      DeYoung K.L., Ray M.E., Su Y.A., Anzick S.L., Johnstone R.W., Trapani J.A., Meltzer P.S., Trent J.M.
      Oncogene 15:453-457(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION BY IFNG.
    2. "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].
      Tissue: Spleen.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Brain.
    5. "Biochemical and growth regulatory activities of the HIN-200 family member and putative tumor suppressor protein, AIM2."
      Cresswell K.S., Clarke C.J.P., Jackson J.T., Darcy P.K., Trapani J.A., Johnstone R.W.
      Biochem. Biophys. Res. Commun. 326:417-424(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INDUCTION BY IFNG, SUBUNIT.
    6. "AIM2 suppresses human breast cancer cell proliferation in vitro and mammary tumor growth in a mouse model."
      Chen I.-F., Ou-Yang F., Hung J.-Y., Liu J.-C., Wang H., Wang S.-C., Hou M.-F., Hortobagyi G.N., Hung M.-C.
      Mol. Cancer Ther. 5:1-7(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The putative tumor suppressor AIM2 is frequently affected by different genetic alterations in microsatellite unstable colon cancers."
      Woerner S.M., Kloor M., Schwitalle Y., Youmans H., Doeberitz M.K., Gebert J., Dihlmann S.
      Genes Chromosomes Cancer 46:1080-1089(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN COLON CANCER, VARIANTS LYS-32 AND TYR-304.
    8. "An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome."
      Burckstummer T., Baumann C., Bluml S., Dixit E., Durnberger G., Jahn H., Planyavsky M., Bilban M., Colinge J., Bennett K.L., Superti-Furga G.
      Nat. Immunol. 10:266-272(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, DNA-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH PYCARD, MUTAGENESIS OF LEU-14 AND PHE-165.
    9. "AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA."
      Fernandes-Alnemri T., Yu J.W., Datta P., Wu J., Alnemri E.S.
      Nature 458:509-513(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PYCARD, SELF-ASSOCIATION.
    10. "AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC."
      Hornung V., Ablasser A., Charrel-Dennis M., Bauernfeind F., Horvath G., Caffrey D.R., Latz E., Fitzgerald K.A.
      Nature 458:514-518(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, INTERACTION WITH PYCARD.
    11. "Involvement of absent in melanoma 2 in inflammasome activation in macrophages infected with Listeria monocytogenes."
      Tsuchiya K., Hara H., Kawamura I., Nomura T., Yamamoto T., Daim S., Dewamitta S.R., Shen Y., Fang R., Mitsuyama M.
      J. Immunol. 185:1186-1195(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "IFI16 protein mediates the anti-inflammatory actions of the type-I interferons through suppression of activation of caspase-1 by inflammasomes."
      Veeranki S., Duan X., Panchanathan R., Liu H., Choubey D.
      PLoS ONE 6:E27040-E27040(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IFI16.
    13. "Interactome-wide analysis identifies end-binding protein 1 as a crucial component for the speck-like particle formation of activated AIM2 inflammasomes."
      Wang L.J., Hsu C.W., Chen C.C., Liang Y., Chen L.C., Ojcius D.M., Tsang N.M., Hsueh C., Wu C.C., Chang Y.S.
      Mol. Cell. Proteomics 11:1230-1244(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAPRE1.
    14. Cited for: INTERACTION WITH EIF2AK2.
    15. "Structures of the HIN domain:DNA complexes reveal ligand binding and activation mechanisms of the AIM2 inflammasome and IFI16 receptor."
      Jin T., Perry A., Jiang J., Smith P., Curry J.A., Unterholzner L., Jiang Z., Horvath G., Rathinam V.A., Johnstone R.W., Hornung V., Latz E., Bowie A.G., Fitzgerald K.A., Xiao T.S.
      Immunity 36:561-571(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 144-343 IN COMPLEX WITH DOUBLE-STRANDED DNA, ENZYME REGULATION, MUTAGENESIS OF LYS-160; LYS-162; LYS-163; LYS-198; LYS-204; ARG-244; LYS-251; LYS-309; ARG-311; LYS-335 AND ILE-337.

    Entry informationi

    Entry nameiAIM2_HUMAN
    AccessioniPrimary (citable) accession number: O14862
    Secondary accession number(s): A8K7M7, Q5T3V9, Q96FG9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 110 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

    Miscellaneous

    Defects in AIM2 may be a cause of microsatellite unstable colon cancers.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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