O14862 (AIM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Interferon-inducible protein AIM2

Alternative name(s):
Absent in melanoma 2

Gene names

Name:

AIM2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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 process	Apoptosis Immunity Inflammatory response Innate immunity
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Disease	Tumor suppressor
Ligand	DNA-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation 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: Compara 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 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_component	AIM2 inflammasome complex Inferred from direct assay Ref.9Ref.8. Source: UniProtKB cytosol Traceable author statement. Source: Reactome mitochondrion Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular_function	double-stranded DNA binding Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-6253193,EBI-6253193
PYCARD	Q9ULZ3	4	EBI-6253193,EBI-751215

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 343

343

Interferon-inducible protein AIM2

PRO_0000153726

Regions

Domain

1 – 87

87

DAPIN

Domain

138 – 337

200

HIN-200

Compositional bias

206 – 209

4

Poly-Ile

Natural variations

Natural variant

32

1

E → K. Ref.7
Corresponds to variant rs2276405 [ dbSNP | Ensembl ].

VAR_022022

Natural variant

304

1

C → Y. Ref.7

VAR_043379

Experimental info

Mutagenesis

14

1

L → A: Fails to activate interleukin-1 beta production. Ref.8

Mutagenesis

160

1

K → 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

Mutagenesis

162

1

K → 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

Mutagenesis

163

1

K → 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

Mutagenesis

165

1

F → A: Impairs DNA binding. Ref.8

Mutagenesis

198

1

K → 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

Mutagenesis

204

1

K → 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

Mutagenesis

244

1

R → 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

Mutagenesis

251

1

K → 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

Mutagenesis

309

1

K → 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

Mutagenesis

311

1

R → 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

Mutagenesis

335

1

K → 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

Mutagenesis

337

1

I → 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 conflict

253

1

N → D in BAF84731. Ref.2

Secondary structure

1

.

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343

Helix Strand Turn

Details...

Helix

1 – 11

11

Helix

14 – 16

3

Helix

19 – 27

9

Beta strand

30 – 32

3

Turn

36 – 38

3

Helix

39 – 42

4

Helix

45 – 56

12

Helix

58 – 71

14

Helix

75 – 93

19

Beta strand

148 – 150

3

Beta strand

154 – 161

8

Beta strand

165 – 169

5

Beta strand

172 – 182

11

Beta strand

187 – 192

6

Helix

195 – 199

5

Beta strand

206 – 214

9

Beta strand

219 – 221

3

Beta strand

225 – 229

5

Helix

240 – 247

8

Helix

252 – 256

5

Beta strand

263 – 275

13

Beta strand

277 – 286

10

Beta strand

289 – 296

8

Helix

300 – 302

3

Beta strand

309 – 319

11

Beta strand

321 – 327

7

Beta strand

333 – 337

5

Sequences

	Sequence		Length	Mass (Da)
	O14862 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 92EC418AB28CE1E6	FASTA	343	38,954
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"Novel role of PKR in inflammasome activation and HMGB1 release." Lu B., Nakamura T., Inouye K., Li J., Tang Y., Lundback 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.

IPI

IPI00844168.

RefSeq

NP_004824.1. NM_004833.1.

UniGene

Hs.733411.

3D structure databases

PDBe
RCSB PDB
PDBj

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	1-110	[»]

ProteinModelPortal

O14862.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59741N.

IntAct

O14862. 5 interactions.

STRING

9606.ENSP00000357112.

PTM databases

PhosphoSite

O14862.

Proteomic databases

PaxDb

O14862.

PRIDE

O14862.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368130; ENSP00000357112; ENSG00000163568.

GeneID

9447.

KEGG

hsa:9447.

UCSC

uc001ftj.1. human.

Organism-specific databases

CTD

9447.

GeneCards

GC01M159032.

HGNC

HGNC:357. AIM2.

HPA

HPA031365.

MIM

604578. gene.

neXtProt

NX_O14862.

PharmGKB

PA24651.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG132015.

HOGENOM

HOG000033871.

HOVERGEN

HBG006122.

KO

K12966.

OMA

EMFHATV.

OrthoDB

EOG4VQ9PK.

PhylomeDB

O14862.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

O14862.

Bgee

O14862.

CleanEx

HS_AIM2.

Genevestigator

O14862.

GermOnline

ENSG00000163568. Homo sapiens.

Family and domain databases

Gene3D

1.10.533.10. 1 hit.
2.40.50.140. 2 hits.

InterPro

IPR004020. DAPIN.
IPR011029. DEATH-like_dom.
IPR004021. HIN200/IF120x.
IPR012340. NA-bd_OB-fold.
[Graphical view]

Pfam

PF02760. HIN. 1 hit.
PF02758. PYRIN. 1 hit.
[Graphical view]

SUPFAM

SSF47986. DEATH_like. 1 hit.

PROSITE

PS50824. DAPIN. 1 hit.
PS50834. HIN_200. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

9447.

NextBio

35388.

SOURCE

Search...

Entry information

Entry name

AIM2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.