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Q9ULZ3

- ASC_HUMAN

UniProt

Q9ULZ3 - ASC_HUMAN

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Protein

Apoptosis-associated speck-like protein containing a CARD

Gene
PYCARD, ASC, CARD5, TMS1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in macrophage pyroptosis, a caspase-1-dependent inflammatory form of cell death and is the major constituent of the ASC pyroptosome which forms upon potassium depletion and rapidly recruits and activates caspase-1. In innate immune response believed to act as an integral adapter in the assembly of the inflammasome which activates caspase-1 leading to processing and secretion of proinflammatory cytokines. The function as activating adapter in different types of inflammasomes is mediated by the DAPIN and CARD domains and their homotypic interactions. Required for recruitment of caspase-1 to inflammasomes containing certain pattern recognition receptors, such as NLRP2, NLRP3, AIM2 and probably IFI16. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in DDX58-triggered proinflammatory responses and inflammasome activation. Isoform 2 may have a regulating effect on the function as inflammasome adapter. Isoform 3 seems to inhibit inflammasome-mediated maturation of interleukin-1 beta. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing.19 Publications

GO - Molecular functioni

  1. cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. protein homodimerization activity Source: HGNC
  4. Pyrin domain binding Source: HGNC

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  2. activation of innate immune response Source: UniProtKB
  3. apoptotic process Source: ProtInc
  4. cellular response to interleukin-1 Source: UniProtKB
  5. cellular response to lipopolysaccharide Source: UniProtKB
  6. cellular response to tumor necrosis factor Source: UniProtKB
  7. defense response to Gram-negative bacterium Source: UniProtKB
  8. defense response to virus Source: UniProtKB
  9. inflammatory response Source: UniProtKB-KW
  10. innate immune response Source: Reactome
  11. interleukin-1 beta production Source: Ensembl
  12. intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
  13. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
  14. macropinocytosis Source: UniProtKB
  15. myeloid dendritic cell activation Source: UniProtKB
  16. myeloid dendritic cell activation involved in immune response Source: UniProtKB
  17. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  18. negative regulation of interferon-beta production Source: UniProtKB
  19. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  20. negative regulation of protein serine/threonine kinase activity Source: UniProtKB
  21. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
  22. positive regulation of actin filament polymerization Source: UniProtKB
  23. positive regulation of activated T cell proliferation Source: UniProtKB
  24. positive regulation of adaptive immune response Source: UniProtKB
  25. positive regulation of antigen processing and presentation of peptide antigen via MHC class II Source: UniProtKB
  26. positive regulation of apoptotic process Source: UniProtKB
  27. positive regulation of chemokine secretion Source: UniProtKB
  28. positive regulation of cysteine-type endopeptidase activity Source: UniProtKB
  29. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: HGNC
  30. positive regulation of defense response to virus by host Source: Ensembl
  31. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  32. positive regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  33. positive regulation of interferon-gamma production Source: UniProtKB
  34. positive regulation of interleukin-10 secretion Source: UniProtKB
  35. positive regulation of interleukin-1 beta secretion Source: HGNC
  36. positive regulation of interleukin-6 production Source: UniProtKB
  37. positive regulation of interleukin-6 secretion Source: UniProtKB
  38. positive regulation of interleukin-8 secretion Source: UniProtKB
  39. positive regulation of JNK cascade Source: UniProtKB
  40. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  41. positive regulation of phagocytosis Source: UniProtKB
  42. positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
  43. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  44. positive regulation of T cell activation Source: UniProtKB
  45. positive regulation of T cell migration Source: UniProtKB
  46. positive regulation of tumor necrosis factor production Source: UniProtKB
  47. regulation of inflammatory response Source: Ensembl
  48. regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  49. regulation of protein stability Source: UniProtKB
  50. regulation of Rac GTPase activity Source: Ensembl
  51. regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
  52. signal transduction Source: UniProtKB
  53. tumor necrosis factor-mediated signaling pathway Source: HGNC
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Immunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_75777. The AIM2 inflammasome.
REACT_75808. The NLRP3 inflammasome.

Names & Taxonomyi

Protein namesi
Recommended name:
Apoptosis-associated speck-like protein containing a CARD
Short name:
hASC
Alternative name(s):
Caspase recruitment domain-containing protein 5
PYD and CARD domain-containing protein
Target of methylation-induced silencing 1
Gene namesi
Name:PYCARD
Synonyms:ASC, CARD5, TMS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:16608. PYCARD.

Subcellular locationi

Cytoplasm. Endoplasmic reticulum. Mitochondrion. Nucleus
Note: Upstream of caspase activation, a redistribution from the cytoplasm to the aggregates occurs. These appear as hollow, perinuclear spherical, ball-like structures. Upon NLRP3 inflammasome activation redistributes to the perinuclear space localizing to endoplasmic reticulum and mitochondria. Localized primarily to the nucleus in resting monocytes/macrophages and rapidly redistributed to the cytoplasm upon pathogen infection. Localized to large cytoplasmic aggregate appearing as a speck containing AIM2, PYCARD, CASP8 and bacterial DNA after infection with Francisella tularensis By similarity.5 Publications

GO - Cellular componenti

  1. AIM2 inflammasome complex Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. endoplasmic reticulum Source: UniProtKB-SubCell
  5. extracellular region Source: Ensembl
  6. IkappaB kinase complex Source: HGNC
  7. mitochondrion Source: UniProtKB
  8. neuronal cell body Source: Ensembl
  9. NLRP1 inflammasome complex Source: UniProtKB
  10. NLRP3 inflammasome complex Source: UniProtKB
  11. nucleolus Source: HPA
  12. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81I → A: Abolishes homooligomerization. 1 Publication
Mutagenesisi12 – 121L → A: Abolishes homooligomerization. 2 Publications
Mutagenesisi12 – 121L → Q: Abolishes promotion of apoptosis and NF-kappa-B activation. 2 Publications
Mutagenesisi13 – 131E → A: Abolishes interaction with PYDC1. 3 Publications
Mutagenesisi13 – 131E → W: Abolishes interaction with NLRP2. 3 Publications
Mutagenesisi15 – 151L → A: Abolishes homooligomerization. 1 Publication
Mutagenesisi19 – 191E → A: Abolishes homooligomerization. 1 Publication
Mutagenesisi20 – 201L → A: Abolishes homooligomerization. 1 Publication
Mutagenesisi21 – 211K → A, E or Q: Abolishes homooligomerization. 1 Publication
Mutagenesisi23 – 231F → A: Abolishes homooligomerization. 1 Publication
Mutagenesisi25 – 251L → A, E, G, K, N or Q: Abolishes homooligomerization. 1 Publication
Mutagenesisi26 – 261K → A or Q: Abolishes homooligomerization. 1 Publication
Mutagenesisi27 – 271L → A: Abolishes homooligomerization. 1 Publication
Mutagenesisi36 – 361Y → A: Abolishes interaction with PYDC1. 1 Publication
Mutagenesisi40 – 401P → A: Abolishes homooligomerization. 1 Publication
Mutagenesisi41 – 411R → A, Q or W: Abolishes homooligomerization. 1 Publication
Mutagenesisi45 – 451L → A: Abolishes homooligomerization. 1 Publication
Mutagenesisi47 – 471M → A, N or Q: Abolishes homooligomerization. 1 Publication
Mutagenesisi48 – 481D → A or K: Abolishes homooligomerization. 2 Publications
Mutagenesisi48 – 481D → A: Abolishes interaction with PYDC1. 2 Publications
Mutagenesisi52 – 521L → A: Abolishes homooligomerization. 1 Publication
Mutagenesisi56 – 561L → A: Abolishes homooligomerization. 1 Publication
Mutagenesisi62 – 621E → A: Abolishes homooligomerization. 1 Publication
Mutagenesisi67 – 671E → A: Abolishes homooligomerization. 1 Publication
Mutagenesisi68 – 681L → A: Abolishes homooligomerization. 1 Publication
Mutagenesisi72 – 721V → A: Abolishes homooligomerization. 1 Publication
Mutagenesisi76 – 761M → A: Abolishes homooligomerization. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA134950175.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 195195Apoptosis-associated speck-like protein containing a CARDPRO_0000064692Add
BLAST

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9ULZ3.
PaxDbiQ9ULZ3.
PRIDEiQ9ULZ3.

PTM databases

PhosphoSiteiQ9ULZ3.

Expressioni

Tissue specificityi

Widely expressed at low levels. Detected in peripheral blood leukocytes, lung, small intestine, spleen, thymus, colon and at lower levels in placenta, liver and kidney. Very low expression in skeletal muscle, heart and brain. Detected in the leukemia cell lines HL-60 and U-937, but not in Jurkat T-cell lymphoma and Daudi Burkitt's lymphoma. Detected in the melanoma cell line WM35, but not in WM793. Not detected in HeLa cervical carcinoma cells and MOLT-4 lymphocytic leukemia cells.

Gene expression databases

ArrayExpressiQ9ULZ3.
BgeeiQ9ULZ3.
CleanExiHS_PYCARD.
GenevestigatoriQ9ULZ3.

Organism-specific databases

HPAiCAB006853.
CAB015948.
HPA049074.

Interactioni

Subunit structurei

Self-associates; enforced oligomerization induces apoptosis, NF-kappa-B regulation and interleukin-1 beta seceretion. Homooligomers can form disk-like particles of approximately 12 nm diameter and approximately 1 nm height. Next to isorm 1 also isoform 2 and isoform 3 may be involved in oligomerization leading to functional regulation. Component of several inflammasomes containing one pattern recognition receptor/sensor, such as NLRP1, NLRP2, NLRP3, AIM2, MEFV or NOD2, and probably NLRC4, NLRP12 or IFI16. Major component of the ASC pyroptosome, a 1-2 um supramolecular assembly (one per macrophage cell) which consists of oligomerized PYCARD dimers and CASP1. Interacts with CASP1 (precursor form); the interaction induces activation of CASP1 leading to the processing of interleukin-1 beta; PYCARD competes with RIPK2 for binding to CASP1. Interacts with NLRP3; the interaction requires the homooligomerization of NLRP3. Interacts with NLRP2, NLRC4, MEFV, CARD16, AIM2, IFI16, NOD2, DDX58, RIPK2, PYDC1, PYDC2, NLRP10, CASP8, CHUK, IKBKB and BAX.23 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AIM2O148624EBI-751215,EBI-6253193
BAXQ078127EBI-751215,EBI-516580
NLRP1Q9C0005EBI-751215,EBI-1220518
NLRP3Q96P204EBI-751215,EBI-6253230
PYDC2Q56P424EBI-751215,EBI-6374418

Protein-protein interaction databases

BioGridi118876. 11 interactions.
DIPiDIP-27618N.
IntActiQ9ULZ3. 21 interactions.
MINTiMINT-206960.
STRINGi9606.ENSP00000247470.

Structurei

Secondary structure

1
195
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1412
Helixi17 – 2610
Turni27 – 293
Beta strandi34 – 363
Helixi41 – 466
Helixi49 – 5810
Helixi62 – 7514
Helixi80 – 9011
Helixi117 – 12610
Helixi129 – 1357
Turni136 – 1405
Helixi143 – 1508
Helixi155 – 16410
Helixi166 – 1683
Helixi171 – 18414
Helixi186 – 1938

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UCPNMR-A1-91[»]
2KN6NMR-A1-195[»]
3J63electron microscopy3.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O1-91[»]
ProteinModelPortaliQ9ULZ3.
SMRiQ9ULZ3. Positions 1-195.

Miscellaneous databases

EvolutionaryTraceiQ9ULZ3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9191DAPINAdd
BLAST
Domaini107 – 19589CARDAdd
BLAST

Domaini

The DAPIN domain mediates homotypic interactions with DAPIN domains of proteins such as of NLRP3, PYDC1 and AIM2 (1 Publication, 1 Publication, 1 Publication and 1 Publication).2 Publications
The CARD domain mediates interaction with CASP1 and NLRC4 (1 Publication and 1 Publication).2 Publications

Sequence similaritiesi

Contains 1 CARD domain.
Contains 1 DAPIN domain.

Phylogenomic databases

eggNOGiNOG39139.
HOGENOMiHOG000034090.
HOVERGENiHBG018739.
InParanoidiQ9ULZ3.
KOiK12799.
OMAiPMDAVDL.
OrthoDBiEOG786H4P.
PhylomeDBiQ9ULZ3.
TreeFamiTF337882.

Family and domain databases

Gene3Di1.10.533.10. 2 hits.
InterProiIPR001315. CARD.
IPR004020. DAPIN.
IPR011029. DEATH-like_dom.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
PF02758. PYRIN. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 2 hits.
PROSITEiPS50209. CARD. 1 hit.
PS50824. DAPIN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9ULZ3-1) [UniParc]FASTAAdd to Basket

Also known as: fASC

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MGRARDAILD ALENLTAEEL KKFKLKLLSV PLREGYGRIP RGALLSMDAL    50
DLTDKLVSFY LETYGAELTA NVLRDMGLQE MAGQLQAATH QGSGAAPAGI 100
QAPPQSAAKP GLHFIDQHRA ALIARVTNVE WLLDALYGKV LTDEQYQAVR 150
AEPTNPSKMR KLFSFTPAWN WTCKDLLLQA LRESQSYLVE DLERS 195
Length:195
Mass (Da):21,627
Last modified:March 1, 2001 - v2
Checksum:i455987286586F46A
GO
Isoform 2 (identifier: Q9ULZ3-2) [UniParc]FASTAAdd to Basket

Also known as: Asc-b, vASC

The sequence of this isoform differs from the canonical sequence as follows:
     93-111: Missing.

Show »
Length:176
Mass (Da):19,969
Checksum:iC4AB645696FA115D
GO
Isoform 3 (identifier: Q9ULZ3-3) [UniParc]FASTAAdd to Basket

Also known as: Asc-c

The sequence of this isoform differs from the canonical sequence as follows:
     26-85: Missing.

Note: No experimental confirmation available.

Show »
Length:135
Mass (Da):15,030
Checksum:iF46DB2DF379E95E9
GO

Sequence cautioni

The sequence BAA91012.1 differs from that shown. Reason: Frameshift at position 4.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei26 – 8560Missing in isoform 3. VSP_004118Add
BLAST
Alternative sequencei93 – 11119Missing in isoform 2. VSP_004119Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB023416 mRNA. Translation: BAA87339.2.
AF184072 Genomic DNA. Translation: AAG01187.1.
AF184073 mRNA. Translation: AAG01188.1.
AF255794 mRNA. Translation: AAF99665.1.
AF310103 mRNA. Translation: AAG30286.1.
AF384665 mRNA. Translation: AAK63850.1.
AK000211 mRNA. Translation: BAA91012.1. Frameshift.
BC004470 mRNA. Translation: AAH04470.1.
BC013569 mRNA. Translation: AAH13569.2.
CCDSiCCDS10708.1. [Q9ULZ3-1]
CCDS10709.1. [Q9ULZ3-2]
RefSeqiNP_037390.2. NM_013258.4. [Q9ULZ3-1]
NP_660183.1. NM_145182.2. [Q9ULZ3-2]
UniGeneiHs.499094.

Genome annotation databases

EnsembliENST00000247470; ENSP00000247470; ENSG00000103490. [Q9ULZ3-1]
ENST00000350605; ENSP00000340441; ENSG00000103490. [Q9ULZ3-2]
GeneIDi29108.
KEGGihsa:29108.
UCSCiuc002ebm.3. human. [Q9ULZ3-2]
uc010cak.3. human. [Q9ULZ3-1]

Polymorphism databases

DMDMi18203507.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB023416 mRNA. Translation: BAA87339.2 .
AF184072 Genomic DNA. Translation: AAG01187.1 .
AF184073 mRNA. Translation: AAG01188.1 .
AF255794 mRNA. Translation: AAF99665.1 .
AF310103 mRNA. Translation: AAG30286.1 .
AF384665 mRNA. Translation: AAK63850.1 .
AK000211 mRNA. Translation: BAA91012.1 . Frameshift.
BC004470 mRNA. Translation: AAH04470.1 .
BC013569 mRNA. Translation: AAH13569.2 .
CCDSi CCDS10708.1. [Q9ULZ3-1 ]
CCDS10709.1. [Q9ULZ3-2 ]
RefSeqi NP_037390.2. NM_013258.4. [Q9ULZ3-1 ]
NP_660183.1. NM_145182.2. [Q9ULZ3-2 ]
UniGenei Hs.499094.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UCP NMR - A 1-91 [» ]
2KN6 NMR - A 1-195 [» ]
3J63 electron microscopy 3.80 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O 1-91 [» ]
ProteinModelPortali Q9ULZ3.
SMRi Q9ULZ3. Positions 1-195.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118876. 11 interactions.
DIPi DIP-27618N.
IntActi Q9ULZ3. 21 interactions.
MINTi MINT-206960.
STRINGi 9606.ENSP00000247470.

PTM databases

PhosphoSitei Q9ULZ3.

Polymorphism databases

DMDMi 18203507.

Proteomic databases

MaxQBi Q9ULZ3.
PaxDbi Q9ULZ3.
PRIDEi Q9ULZ3.

Protocols and materials databases

DNASUi 29108.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000247470 ; ENSP00000247470 ; ENSG00000103490 . [Q9ULZ3-1 ]
ENST00000350605 ; ENSP00000340441 ; ENSG00000103490 . [Q9ULZ3-2 ]
GeneIDi 29108.
KEGGi hsa:29108.
UCSCi uc002ebm.3. human. [Q9ULZ3-2 ]
uc010cak.3. human. [Q9ULZ3-1 ]

Organism-specific databases

CTDi 29108.
GeneCardsi GC16M031212.
H-InvDB HIX0012985.
HGNCi HGNC:16608. PYCARD.
HPAi CAB006853.
CAB015948.
HPA049074.
MIMi 606838. gene.
neXtProti NX_Q9ULZ3.
PharmGKBi PA134950175.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG39139.
HOGENOMi HOG000034090.
HOVERGENi HBG018739.
InParanoidi Q9ULZ3.
KOi K12799.
OMAi PMDAVDL.
OrthoDBi EOG786H4P.
PhylomeDBi Q9ULZ3.
TreeFami TF337882.

Enzyme and pathway databases

Reactomei REACT_75777. The AIM2 inflammasome.
REACT_75808. The NLRP3 inflammasome.

Miscellaneous databases

ChiTaRSi PYCARD. human.
EvolutionaryTracei Q9ULZ3.
GeneWikii PYCARD.
GenomeRNAii 29108.
NextBioi 52169.
PROi Q9ULZ3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9ULZ3.
Bgeei Q9ULZ3.
CleanExi HS_PYCARD.
Genevestigatori Q9ULZ3.

Family and domain databases

Gene3Di 1.10.533.10. 2 hits.
InterProi IPR001315. CARD.
IPR004020. DAPIN.
IPR011029. DEATH-like_dom.
[Graphical view ]
Pfami PF00619. CARD. 1 hit.
PF02758. PYRIN. 1 hit.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 2 hits.
PROSITEi PS50209. CARD. 1 hit.
PS50824. DAPIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "ASC, a novel 22-kDa protein, aggregates during apoptosis of human promyelocytic leukemia HL-60 cells."
    Masumoto J., Taniguchi S., Ayukawa K., Sarvotham H., Kishino T., Niikawa N., Hidaka E., Katsuyama T., Higuchi T., Sagara J.
    J. Biol. Chem. 274:33835-33838(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Leukemia.
  2. "TMS1, a novel proapoptotic caspase recruitment domain protein, is a target of methylation-induced gene silencing in human breast cancers."
    Conway K.E., McConnell B.B., Bowring C.E., Donald C.D., Warren S.T., Vertino P.M.
    Cancer Res. 60:6236-6242(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
    Tissue: Fibroblast.
  3. "A splice variant of ASC regulates IL-1beta release and aggregates differently from intact ASC."
    Matsushita K., Takeoka M., Sagara J., Itano N., Kurose Y., Nakamura A., Taniguchi S.
    Mediators Inflamm. 2009:287387-287387(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2), FUNCTION (ISOFORM 2), MASS SPECTROMETRY (ISOFORM 2).
  4. "Pycard a PYD and CARD containing molecule."
    Martinon F., Hofmann K., Tschopp J.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
  5. "CARD5 protein is a CARD/PYRIN family member that is involved in apoptosis signal transduction."
    Bertin J.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
  6. "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] (ISOFORM 1).
    Tissue: Colon mucosa.
  7. "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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-195 (ISOFORM 1).
    Tissue: Lymph and Pancreas.
  8. "Activation of a caspase-9-mediated apoptotic pathway by subcellular redistribution of the novel caspase recruitment domain protein TMS1."
    McConnell B.B., Vertino P.M.
    Cancer Res. 60:6243-6247(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. Cited for: INTERACTION WITH NLRC4.
  10. "Interaction between pyrin and the apoptotic speck protein (ASC) modulates ASC-induced apoptosis."
    Richards N., Schaner P., Diaz A., Stuckey J., Shelden E., Wadhwa A., Gumucio D.L.
    J. Biol. Chem. 276:39320-39329(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MEFV.
  11. "PYPAF1: a PYRIN-containing APAF1-like protein that assembles with ASC and activates NF-kB."
    Manji G.A., Wang L., Geddes B.J., Brown M., Merriam S., Al-Garawi A., Mak S., Lora J.M., Briskin M., Jurman M., Cao J., DiStefano P.S., Bertin J.
    J. Biol. Chem. 277:11570-11575(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NLRP3, DOMAIN.
  12. "The PYRIN-CARD protein ASC is an activating adaptor for caspase-1."
    Srinivasula S.M., Poyet J.L., Razmara M., Datta P., Zhang Z., Alnemri E.S.
    J. Biol. Chem. 277:21119-21122(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CASP1; NLRC4 AND CARD16.
  13. "The PAAD/PYRIN-family protein ASC is a dual regulator of a conserved step in nuclear factor kappaB activation pathways."
    Stehlik C., Fiorentino L., Dorfleutner A., Bruey J.M., Ariza E.M., Sagara J., Reed J.C.
    J. Exp. Med. 196:1605-1615(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CHUK AND IKBKB.
  14. "The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta."
    Martinon F., Burns K., Tschopp J.
    Mol. Cell 10:417-426(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN NLPR1 INFLAMMASOME.
  15. Cited for: FUNCTION IN APOPTOSIS, INTERACTION WITH CASP8, MUTAGENESIS OF LEU-12.
  16. "The PAAD/PYRIN-only protein POP1/ASC2 is a modulator of ASC-mediated nuclear-factor-kappa B and pro-caspase-1 regulation."
    Stehlik C., Krajewska M., Welsh K., Krajewski S., Godzik A., Reed J.C.
    Biochem. J. 373:101-113(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PYDC1, PHOSPHORYLATION.
  17. "Apoptosis-associated speck-like protein containing a caspase recruitment domain is a regulator of procaspase-1 activation."
    Stehlik C., Lee S.H., Dorfleutner A., Stassinopoulos A., Sagara J., Reed J.C.
    J. Immunol. 171:6154-6163(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CASP1 AND RIPK2.
  18. "NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder."
    Agostini L., Martinon F., Burns K., McDermott M.F., Hawkins P.N., Tschopp J.
    Immunity 20:319-325(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NLRP2 AND NLRP3 INFLAMMASOMES, INTERACTION WITH NLRP2 AND NLRP3, SUBCELLULAR LOCATION.
  19. "PYNOD, a novel Apaf-1/CED4-like protein is an inhibitor of ASC and caspase-1."
    Wang Y., Hasegawa M., Imamura R., Kinoshita T., Kondo C., Konaka K., Suda T.
    Int. Immunol. 16:777-786(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NLRP10.
  20. "Cryopyrin-induced interleukin 1beta secretion in monocytic cells: enhanced activity of disease-associated mutants and requirement for ASC."
    Dowds T.A., Masumoto J., Zhu L., Inohara N., Nunez G.
    J. Biol. Chem. 279:21924-21928(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NLRP3.
  21. "PAN1/NALP2/PYPAF2, an inducible inflammatory mediator that regulates NF-kappaB and caspase-1 activation in macrophages."
    Bruey J.-M., Bruey-Sedano N., Newman R., Chandler S., Stehlik C., Reed J.C.
    J. Biol. Chem. 279:51897-51907(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NLRP2, MUTAGENESIS OF GLU-13.
  22. "ASC is a Bax adaptor and regulates the p53-Bax mitochondrial apoptosis pathway."
    Ohtsuka T., Ryu H., Minamishima Y.A., Macip S., Sagara J., Nakayama K.I., Aaronson S.A., Lee S.W.
    Nat. Cell Biol. 6:121-128(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS, SUBCELLULAR LOCATION, INTERACTION WITH BAX.
  23. "Role of charged and hydrophobic residues in the oligomerization of the PYRIN domain of ASC."
    Moriya M., Taniguchi S., Wu P., Liepinsh E., Otting G., Sagara J.
    Biochemistry 44:575-583(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SELF-ASSOCIATION, MUTAGENESIS OF ILE-8; LEU-12; GLU-13; LEU-15; GLU-19; LEU-20; LYS-21; PHE-23; LEU-25; LYS-26; LEU-27; PRO-40; ARG-41; LEU-45; MET-47; ASP-48; LEU-52; LEU-56; GLU-62; GLU-67; LEU-68; VAL-72 AND MET-76.
  24. "Cryopyrin and pyrin activate caspase-1, but not NF-kappaB, via ASC oligomerization."
    Yu J.W., Wu J., Zhang Z., Datta P., Ibrahimi I., Taniguchi S., Sagara J., Fernandes-Alnemri T., Alnemri E.S.
    Cell Death Differ. 13:236-249(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH INFLAMMASOMES.
  25. "ASC directs NF-kappaB activation by regulating receptor interacting protein-2 (RIP2) caspase-1 interactions."
    Sarkar A., Duncan M., Hart J., Hertlein E., Guttridge D.C., Wewers M.D.
    J. Immunol. 176:4979-4986(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CASP1.
  26. "ASC mediates the induction of multiple cytokines by Porphyromonas gingivalis via caspase-1-dependent and -independent pathways."
    Taxman D.J., Zhang J., Champagne C., Bergstralh D.T., Iocca H.A., Lich J.D., Ting J.P.
    J. Immunol. 177:4252-4256(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  27. "The pyroptosome: a supramolecular assembly of ASC dimers mediating inflammatory cell death via caspase-1 activation."
    Fernandes-Alnemri T., Wu J., Yu J.W., Datta P., Miller B., Jankowski W., Rosenberg S., Zhang J., Alnemri E.S.
    Cell Death Differ. 14:1590-1604(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  28. "Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation."
    Faustin B., Lartigue L., Bruey J.-M., Luciano F., Sergienko E., Bailly-Maitre B., Volkmann N., Hanein D., Rouiller I., Reed J.C.
    Mol. Cell 25:713-724(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NLRP1 INFLAMMASOME.
  29. "Mechanism of ASC-mediated apoptosis: bid-dependent apoptosis in type II cells."
    Hasegawa M., Kawase K., Inohara N., Imamura R., Yeh W.C., Kinoshita T., Suda T.
    Oncogene 26:1748-1756(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS.
  30. "Cellular pyrin domain-only protein 2 is a candidate regulator of inflammasome activation."
    Dorfleutner A., Bryan N.B., Talbott S.J., Funya K.N., Rellick S.L., Reed J.C., Shi X., Rojanasakul Y., Flynn D.C., Stehlik C.
    Infect. Immun. 75:1484-1492(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PYDC2.
  31. "Pyrin-only protein 2 modulates NF-kappaB and disrupts ASC:CLR interactions."
    Bedoya F., Sandler L.L., Harton J.A.
    J. Immunol. 178:3837-3845(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PYDC2.
  32. Cited for: INTERACTION WITH PYDC1, MUTAGENESIS OF GLU-13; TYR-36 AND ASP-48.
  33. "Activation of inflammasomes requires intracellular redistribution of the apoptotic speck-like protein containing a caspase recruitment domain."
    Bryan N.B., Dorfleutner A., Rojanasakul Y., Stehlik C.
    J. Immunol. 182:3173-3182(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  34. Cited for: FUNCTION.
  35. "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 IN AIM2 INFLAMMASOME, INTERACTION WITH AIM2.
  36. "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 IN AIM2 INFLAMMASOME, INTERACTION WITH AIM2.
  37. "Differential splicing of the apoptosis-associated speck like protein containing a caspase recruitment domain (ASC) regulates inflammasomes."
    Bryan N.B., Dorfleutner A., Kramer S.J., Yun C., Rojanasakul Y., Stehlik C.
    J. Inflamm. (Lond.) 7:23-23(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORMS 2 AND 3).
  38. "Recognition of RNA virus by RIG-I results in activation of CARD9 and inflammasome signaling for interleukin 1 beta production."
    Poeck H., Bscheider M., Gross O., Finger K., Roth S., Rebsamen M., Hannesschlager N., Schlee M., Rothenfusser S., Barchet W., Kato H., Akira S., Inoue S., Endres S., Peschel C., Hartmann G., Hornung V., Ruland J.
    Nat. Immunol. 11:63-69(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX58.
  39. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  40. "IFI16 acts as a nuclear pathogen sensor to induce the inflammasome in response to Kaposi Sarcoma-associated herpesvirus infection."
    Kerur N., Veettil M.V., Sharma-Walia N., Bottero V., Sadagopan S., Otageri P., Chandran B.
    Cell Host Microbe 9:363-375(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IFI16.
  41. "The NLR adaptor ASC/PYCARD regulates DUSP10, mitogen-activated protein kinase (MAPK), and chemokine induction independent of the inflammasome."
    Taxman D.J., Holley-Guthrie E.A., Huang M.T., Moore C.B., Bergstralh D.T., Allen I.C., Lei Y., Gris D., Ting J.P.
    J. Biol. Chem. 286:19605-19616(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  42. "Central and overlapping role of cathepsin B and inflammasome adaptor ASC in antigen presenting function of human dendritic cells."
    Guo X., Dhodapkar K.M.
    Hum. Immunol. 73:871-878(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  43. "A role for mitochondria in NLRP3 inflammasome activation."
    Zhou R., Yazdi A.S., Menu P., Tschopp J.
    Nature 469:221-225(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  44. "The death-domain fold of the ASC PYRIN domain, presenting a basis for PYRIN/PYRIN recognition."
    Liepinsh E., Barbals R., Dahl E., Sharipo A., Staub E., Otting G.
    J. Mol. Biol. 332:1155-1163(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-91, FUNCTION OF DAPIN DOMAIN.
  45. "Structure and interdomain dynamics of apoptosis-associated speck-like protein containing a CARD (ASC)."
    de Alba E.
    J. Biol. Chem. 284:32932-32941(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiASC_HUMAN
AccessioniPrimary (citable) accession number: Q9ULZ3
Secondary accession number(s): Q96D12
, Q9BSZ5, Q9HBD0, Q9NXJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: March 1, 2001
Last modified: September 3, 2014
This is version 138 of the entry and version 2 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

In breast tumorigenesis, methylation-mediated silencing may affect genes and proteins that act as positive mediators of cell death.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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