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O14862

- AIM2_HUMAN

UniProt

O14862 - AIM2_HUMAN

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Protein

Interferon-inducible protein AIM2

Gene
AIM2
Organism
Homo sapiens (Human)
Status
Reviewed - 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.6 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
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: Chromosome 1

Organism-specific databases

HGNCiHGNC:357. AIM2.

Subcellular locationi

Nucleus. Cytoplasm
Note: Activated inflammasomes can aggregate in the cytosol as speck-like particles.4 Publications

GO - Cellular componenti

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

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.4 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 MAPRE1.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-6253193,EBI-6253193
PYCARDQ9ULZ34EBI-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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8787DAPINAdd
BLAST
Domaini138 – 337200HIN-200Add
BLAST

Compositional bias

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

Domaini

The DAPIN domain mediates homotypic interaction with PYCARD (1 Publication and 1 Publication).
The HIN-20 domain mediates dsDNA binding via electrostatic interactions (1 Publication).

Sequence similaritiesi

Belongs to the HIN-200 family.
Contains 1 DAPIN domain.
Contains 1 HIN-200 domain.

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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti253 – 2531N → D in BAF84731. 1 Publication

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

« 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: September 3, 2014
This is version 109 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

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