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O14862 (AIM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interferon-inducible protein AIM2
Alternative name(s):
Absent in melanoma 2
Gene names
Name:AIM2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Enzyme regulation

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. Ref.15

Subunit structure

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. Ref.5 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14

Subcellular location

Nucleus. Cytoplasm. Note: Activated inflammasomes can aggregate in the cytosol as speck-like particles. Ref.5 Ref.8 Ref.9 Ref.10

Tissue specificity

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

Induction

By IFNG/IFN-gamma and IFNB1/IFN-beta. Ref.1 Ref.5 Ref.8 Ref.15

Domain

The DAPIN domain mediates homotypic interaction with PYCARD (Ref.9 and Ref.10).

The HIN-20 domain mediates dsDNA binding via electrostatic interactions (Ref.15).

Miscellaneous

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

Sequence similarities

Belongs to the HIN-200 family.

Contains 1 DAPIN domain.

Contains 1 HIN-200 domain.

Sequence caution

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

Ontologies

Keywords
   Biological processApoptosis
Immunity
Inflammatory response
Innate immunity
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseTumor suppressor
   LigandDNA-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of innate immune response

Inferred from direct assay Ref.10Ref.9Ref.8. Source: UniProtKB

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to drug

Inferred from direct assay Ref.8. Source: MGI

cellular response to interferon-beta

Inferred from electronic annotation. Source: Ensembl

immune response

Traceable author statement Ref.1. Source: ProtInc

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Traceable author statement. Source: Reactome

interleukin-1 beta secretion

Inferred from mutant phenotype Ref.8. Source: MGI

negative regulation of NF-kappaB transcription factor activity

Inferred from direct assay Ref.6. Source: UniProtKB

nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay Ref.10. Source: UniProtKB

positive regulation of cysteine-type endopeptidase activity

Inferred from direct assay Ref.9Ref.8. Source: UniProtKB

positive regulation of defense response to virus by host

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of interleukin-1 beta production

Inferred from direct assay Ref.10Ref.9Ref.8. Source: UniProtKB

positive regulation of interleukin-1 beta secretion

Inferred from direct assay Ref.8. Source: UniProtKB

positive regulation of protein oligomerization

Inferred from direct assay Ref.9. Source: UniProtKB

pyroptosis

Inferred from direct assay Ref.10Ref.9. Source: UniProtKB

tumor necrosis factor-mediated signaling pathway

Inferred from direct assay Ref.6. Source: UniProtKB

   Cellular_componentAIM2 inflammasome complex

Inferred from direct assay Ref.9Ref.8. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.9. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondouble-stranded DNA binding

Inferred from direct assay Ref.10. Source: UniProtKB

identical protein binding

Inferred from physical interaction Ref.9. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-6253193,EBI-6253193
PYCARDQ9ULZ34EBI-6253193,EBI-751215

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 343343Interferon-inducible protein AIM2
PRO_0000153726

Regions

Domain1 – 8787DAPIN
Domain138 – 337200HIN-200
Compositional bias206 – 2094Poly-Ile

Natural variations

Natural variant321E → K. Ref.7
Corresponds to variant rs2276405 [ dbSNP | Ensembl ].
VAR_022022
Natural variant3041C → Y. Ref.7
VAR_043379

Experimental info

Mutagenesis141L → A: Fails to activate interleukin-1 beta production. Ref.8
Mutagenesis1601K → 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. Ref.15
Mutagenesis1621K → 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. Ref.15
Mutagenesis1631K → 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. Ref.15
Mutagenesis1651F → A: Impairs DNA binding. Ref.8
Mutagenesis1981K → 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. Ref.15
Mutagenesis2041K → 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. Ref.15
Mutagenesis2441R → 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. Ref.15
Mutagenesis2511K → 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. Ref.15
Mutagenesis3091K → 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. Ref.15
Mutagenesis3111R → 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. Ref.15
Mutagenesis3351K → 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. Ref.15
Mutagenesis3371I → 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. Ref.15
Sequence conflict2531N → D in BAF84731. Ref.2

Secondary structure

..................................................... 343
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O14862 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 92EC418AB28CE1E6

FASTA34338,954
        10         20         30         40         50         60 
MESKYKEILL LTGLDNITDE ELDRFKFFLS DEFNIATGKL HTANRIQVAT LMIQNAGAVS 

        70         80         90        100        110        120 
AVMKTIRIFQ KLNYMLLAKR LQEEKEKVDK QYKSVTKPKP LSQAEMSPAA SAAIRNDVAK 

       130        140        150        160        170        180 
QRAAPKVSPH VKPEQKQMVA QQESIREGFQ KRCLPVMVLK AKKPFTFETQ EGKQEMFHAT 

       190        200        210        220        230        240 
VATEKEFFFV KVFNTLLKDK FIPKRIIIIA RYYRHSGFLE VNSASRVLDA ESDQKVNVPL 

       250        260        270        280        290        300 
NIIRKAGETP KINTLQTQPL GTIVNGLFVV QKVTEKKKNI LFDLSDNTGK MEVLGVRNED 

       310        320        330        340 
TMKCKEGDKV RLTFFTLSKN GEKLQLTSGV HSTIKVIKAK KKT 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Novel role of PKR in inflammasome activation and HMGB1 release."
Lu B., Nakamura T., Inouye K., Li J., Tang Y., Lundbaeck P., Valdes-Ferrer S.I., Olofsson P.S., Kalb T., Roth J., Zou Y., Erlandsson-Harris H., Yang H., Ting J.P., Wang H., Andersson U., Antoine D.J., Chavan S.S., Hotamisligil G.S., Tracey K.J.
Nature 488:670-674(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF024714 mRNA. Translation: AAB81613.1.
AK292042 mRNA. Translation: BAF84731.1.
AL359753 Genomic DNA. Translation: CAI15088.1.
BC010940 mRNA. Translation: AAH10940.1. Frameshift.
RefSeqNP_004824.1. NM_004833.1.
UniGeneHs.733411.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3RN2X-ray2.55A/B144-343[»]
3RN5X-ray2.50A/B/C/D144-343[»]
3VD8X-ray2.07A1-110[»]
4O7QX-ray1.82A1-93[»]
ProteinModelPortalO14862.
SMRO14862. Positions 1-97, 147-340.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59741N.
IntActO14862. 5 interactions.
STRING9606.ENSP00000357112.

PTM databases

PhosphoSiteO14862.

Proteomic databases

PaxDbO14862.
PRIDEO14862.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368130; ENSP00000357112; ENSG00000163568.
GeneID9447.
KEGGhsa:9447.
UCSCuc001ftj.1. human.

Organism-specific databases

CTD9447.
GeneCardsGC01M159032.
HGNCHGNC:357. AIM2.
HPAHPA031365.
MIM604578. gene.
neXtProtNX_O14862.
PharmGKBPA24651.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG132015.
HOGENOMHOG000033871.
HOVERGENHBG006122.
KOK12966.
OMAFQKLNYM.
OrthoDBEOG78H3TT.
PhylomeDBO14862.
TreeFamTF337385.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressO14862.
BgeeO14862.
CleanExHS_AIM2.
GenevestigatorO14862.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
2.40.50.140. 2 hits.
InterProIPR004020. DAPIN.
IPR011029. DEATH-like_dom.
IPR004021. HIN200/IF120x.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamPF02760. HIN. 1 hit.
PF02758. PYRIN. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
PROSITEPS50824. DAPIN. 1 hit.
PS50834. HIN_200. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiAIM2.
GenomeRNAi9447.
NextBio35388.
PROO14862.
SOURCESearch...

Entry information

Entry nameAIM2_HUMAN
AccessionPrimary (citable) accession number: O14862
Secondary accession number(s): A8K7M7, Q5T3V9, Q96FG9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM