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Protein

Interferon-inducible protein AIM2

Gene

AIM2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • double-stranded DNA binding Source: UniProtKB
  • identical protein binding Source: IntAct

GO - Biological processi

  • activation of innate immune response Source: UniProtKB
  • apoptotic process Source: UniProtKB-KW
  • cellular response to drug Source: MGI
  • cellular response to interferon-beta Source: Ensembl
  • immune response Source: ProtInc
  • inflammatory response Source: UniProtKB-KW
  • innate immune response Source: Reactome
  • interleukin-1 beta secretion Source: MGI
  • negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
  • positive regulation of cysteine-type endopeptidase activity Source: UniProtKB
  • positive regulation of defense response to virus by host Source: UniProtKB
  • positive regulation of interleukin-1 beta production Source: UniProtKB
  • positive regulation of interleukin-1 beta secretion Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of protein oligomerization Source: UniProtKB
  • pyroptosis Source: UniProtKB
  • tumor necrosis factor-mediated signaling pathway Source: UniProtKB
Complete GO annotation...

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 Componenti: 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

  • AIM2 inflammasome complex Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiAIM2.

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

BgeeiO14862.
CleanExiHS_AIM2.
ExpressionAtlasiO14862. baseline and differential.
GenevisibleiO14862. HS.

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
itself3EBI-6253193,EBI-6253193
PYCARDQ9ULZ311EBI-6253193,EBI-751215

Protein-protein interaction databases

BioGridi114837. 1 interaction.
DIPiDIP-59741N.
IntActiO14862. 108 interactions.
STRINGi9606.ENSP00000357112.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000013296.
HOGENOMiHOG000033871.
HOVERGENiHBG006122.
InParanoidiO14862.
KOiK12966.
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

        10         20         30         40         50
MESKYKEILL LTGLDNITDE ELDRFKFFLS DEFNIATGKL HTANRIQVAT
60 70 80 90 100
LMIQNAGAVS AVMKTIRIFQ KLNYMLLAKR LQEEKEKVDK QYKSVTKPKP
110 120 130 140 150
LSQAEMSPAA SAAIRNDVAK QRAAPKVSPH VKPEQKQMVA QQESIREGFQ
160 170 180 190 200
KRCLPVMVLK AKKPFTFETQ EGKQEMFHAT VATEKEFFFV KVFNTLLKDK
210 220 230 240 250
FIPKRIIIIA RYYRHSGFLE VNSASRVLDA ESDQKVNVPL NIIRKAGETP
260 270 280 290 300
KINTLQTQPL GTIVNGLFVV QKVTEKKKNI LFDLSDNTGK MEVLGVRNED
310 320 330 340
TMKCKEGDKV RLTFFTLSKN GEKLQLTSGV HSTIKVIKAK KKT
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi114837. 1 interaction.
DIPiDIP-59741N.
IntActiO14862. 108 interactions.
STRINGi9606.ENSP00000357112.

PTM databases

PhosphoSiteiO14862.

Polymorphism and mutation databases

BioMutaiAIM2.

Proteomic databases

MaxQBiO14862.
PaxDbiO14862.
PRIDEiO14862.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9447.
GeneCardsiGC01M159032.
HGNCiHGNC:357. AIM2.
HPAiHPA031365.
MIMi604578. gene.
neXtProtiNX_O14862.
PharmGKBiPA24651.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG132015.
GeneTreeiENSGT00390000013296.
HOGENOMiHOG000033871.
HOVERGENiHBG006122.
InParanoidiO14862.
KOiK12966.
OrthoDBiEOG78H3TT.
PhylomeDBiO14862.
TreeFamiTF337385.

Enzyme and pathway databases

ReactomeiREACT_75777. The AIM2 inflammasome.

Miscellaneous databases

GeneWikiiAIM2.
GenomeRNAii9447.
NextBioi35388.
PROiO14862.
SOURCEiSearch...

Gene expression databases

BgeeiO14862.
CleanExiHS_AIM2.
ExpressionAtlasiO14862. baseline and differential.
GenevisibleiO14862. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 117 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.