Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Apoptosis-associated speck-like protein containing a CARD

Gene

PYCARD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 pyrin 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.17 Publications

GO - Molecular functioni

  • BMP receptor binding Source: AgBase
  • cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
  • cysteine-type endopeptidase activity involved in apoptotic process Source: GO_Central
  • enzyme binding Source: AgBase
  • identical protein binding Source: IntAct
  • interleukin-6 receptor binding Source: AgBase
  • myosin I binding Source: AgBase
  • protease binding Source: AgBase
  • protein homodimerization activity Source: HGNC
  • Pyrin domain binding Source: HGNC
  • tropomyosin binding Source: AgBase

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • activation of innate immune response Source: UniProtKB
  • apoptotic process Source: ProtInc
  • cellular response to interleukin-1 Source: UniProtKB
  • cellular response to lipopolysaccharide Source: UniProtKB
  • cellular response to tumor necrosis factor Source: UniProtKB
  • defense response to Gram-negative bacterium Source: UniProtKB
  • defense response to virus Source: UniProtKB
  • inflammatory response Source: UniProtKB-KW
  • innate immune response Source: UniProtKB-KW
  • intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
  • macropinocytosis Source: UniProtKB
  • myeloid dendritic cell activation Source: UniProtKB
  • myeloid dendritic cell activation involved in immune response Source: UniProtKB
  • negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • negative regulation of interferon-beta production Source: UniProtKB
  • negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • negative regulation of protein serine/threonine kinase activity Source: UniProtKB
  • positive regulation of actin filament polymerization Source: UniProtKB
  • positive regulation of activated T cell proliferation Source: UniProtKB
  • positive regulation of adaptive immune response Source: UniProtKB
  • positive regulation of antigen processing and presentation of peptide antigen via MHC class II Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of chemokine secretion Source: UniProtKB
  • positive regulation of cysteine-type endopeptidase activity Source: UniProtKB
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: HGNC
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  • positive regulation of interferon-gamma production Source: UniProtKB
  • positive regulation of interleukin-10 secretion Source: UniProtKB
  • positive regulation of interleukin-1 beta secretion Source: HGNC
  • positive regulation of interleukin-6 production Source: UniProtKB
  • positive regulation of interleukin-6 secretion Source: UniProtKB
  • positive regulation of interleukin-8 secretion Source: UniProtKB
  • positive regulation of JNK cascade Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of phagocytosis Source: UniProtKB
  • positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • positive regulation of T cell activation Source: UniProtKB
  • positive regulation of T cell migration Source: UniProtKB
  • positive regulation of tumor necrosis factor production Source: UniProtKB
  • regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  • regulation of protein stability Source: UniProtKB
  • regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
  • signal transduction Source: UniProtKB
  • tumor necrosis factor-mediated signaling pathway Source: HGNC
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Immunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

BioCyciZFISH:ENSG00000103490-MONOMER.
ReactomeiR-HSA-5660668. CLEC7A/inflammasome pathway.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-844456. The NLRP3 inflammasome.
R-HSA-844615. The AIM2 inflammasome.
SIGNORiQ9ULZ3.

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
Proteomesi
  • UP000005640 Componenti: 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).By similarity

GO - Cellular componenti

  • AIM2 inflammasome complex Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • endoplasmic reticulum Source: UniProtKB-SubCell
  • IkappaB kinase complex Source: HGNC
  • mitochondrion Source: UniProtKB
  • NLRP1 inflammasome complex Source: UniProtKB
  • NLRP3 inflammasome complex Source: UniProtKB
  • nucleolus Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi8I → A: Abolishes homooligomerization. 1 Publication1
Mutagenesisi12L → A: Abolishes homooligomerization. 2 Publications1
Mutagenesisi12L → Q: Abolishes promotion of apoptosis and NF-kappa-B activation. 2 Publications1
Mutagenesisi13E → A: Abolishes interaction with PYDC1. 3 Publications1
Mutagenesisi13E → W: Abolishes interaction with NLRP2. 3 Publications1
Mutagenesisi15L → A: Abolishes homooligomerization. 1 Publication1
Mutagenesisi19E → A: Abolishes homooligomerization. 1 Publication1
Mutagenesisi20L → A: Abolishes homooligomerization. 1 Publication1
Mutagenesisi21K → A, E or Q: Abolishes homooligomerization. 1 Publication1
Mutagenesisi23F → A: Abolishes homooligomerization. 1 Publication1
Mutagenesisi25L → A, E, G, K, N or Q: Abolishes homooligomerization. 1 Publication1
Mutagenesisi26K → A or Q: Abolishes homooligomerization. 1 Publication1
Mutagenesisi27L → A: Abolishes homooligomerization. 1 Publication1
Mutagenesisi36Y → A: Abolishes interaction with PYDC1. 1 Publication1
Mutagenesisi40P → A: Abolishes homooligomerization. 1 Publication1
Mutagenesisi41R → A, Q or W: Abolishes homooligomerization. 1 Publication1
Mutagenesisi45L → A: Abolishes homooligomerization. 1 Publication1
Mutagenesisi47M → A, N or Q: Abolishes homooligomerization. 1 Publication1
Mutagenesisi48D → A or K: Abolishes homooligomerization. 2 Publications1
Mutagenesisi48D → A: Abolishes interaction with PYDC1. 2 Publications1
Mutagenesisi52L → A: Abolishes homooligomerization. 1 Publication1
Mutagenesisi56L → A: Abolishes homooligomerization. 1 Publication1
Mutagenesisi62E → A: Abolishes homooligomerization. 1 Publication1
Mutagenesisi67E → A: Abolishes homooligomerization. 1 Publication1
Mutagenesisi68L → A: Abolishes homooligomerization. 1 Publication1
Mutagenesisi72V → A: Abolishes homooligomerization. 1 Publication1
Mutagenesisi76M → A: Abolishes homooligomerization. 1 Publication1

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

DisGeNETi29108.
OpenTargetsiENSG00000103490.
PharmGKBiPA134950175.

Polymorphism and mutation databases

BioMutaiPYCARD.
DMDMi18203507.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000646921 – 195Apoptosis-associated speck-like protein containing a CARDAdd BLAST195

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei195PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9ULZ3.
PaxDbiQ9ULZ3.
PeptideAtlasiQ9ULZ3.
PRIDEiQ9ULZ3.

PTM databases

iPTMnetiQ9ULZ3.
PhosphoSitePlusiQ9ULZ3.

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

BgeeiENSG00000103490.
CleanExiHS_PYCARD.
ExpressionAtlasiQ9ULZ3. baseline and differential.
GenevisibleiQ9ULZ3. HS.

Organism-specific databases

HPAiCAB006853.
CAB015948.
HPA049074.
HPA054496.

Interactioni

Subunit structurei

Self-associates; enforced oligomerization induces apoptosis, NF-kappa-B regulation and interleukin-1 beta secretion. 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
itself6EBI-751215,EBI-751215
AIM2O1486211EBI-751215,EBI-6253193
BAXQ078127EBI-751215,EBI-516580
CASP1P294665EBI-751215,EBI-516667
EXOC5Q8IW245EBI-751215,EBI-10171392
NLRP1Q9C0005EBI-751215,EBI-1220518
NLRP3Q96P208EBI-751215,EBI-6253230
PYDC2Q56P424EBI-751215,EBI-6374418
RIPK1Q135462EBI-751215,EBI-358507

GO - Molecular functioni

  • BMP receptor binding Source: AgBase
  • enzyme binding Source: AgBase
  • identical protein binding Source: IntAct
  • interleukin-6 receptor binding Source: AgBase
  • myosin I binding Source: AgBase
  • protease binding Source: AgBase
  • protein homodimerization activity Source: HGNC
  • Pyrin domain binding Source: HGNC
  • tropomyosin binding Source: AgBase

Protein-protein interaction databases

BioGridi118876. 43 interactors.
DIPiDIP-27618N.
IntActiQ9ULZ3. 46 interactors.
MINTiMINT-206960.
STRINGi9606.ENSP00000247470.

Structurei

Secondary structure

1195
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 14Combined sources12
Helixi17 – 26Combined sources10
Turni27 – 29Combined sources3
Beta strandi34 – 36Combined sources3
Helixi41 – 46Combined sources6
Helixi49 – 58Combined sources10
Helixi62 – 75Combined sources14
Helixi80 – 90Combined sources11
Helixi117 – 126Combined sources10
Helixi129 – 135Combined sources7
Turni136 – 140Combined sources5
Helixi143 – 150Combined sources8
Helixi155 – 164Combined sources10
Helixi166 – 168Combined sources3
Helixi171 – 184Combined sources14
Helixi186 – 193Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5H8OX-ray4.21B115-195[»]
ProteinModelPortaliQ9ULZ3.
SMRiQ9ULZ3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ULZ3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 91PyrinPROSITE-ProRule annotationAdd BLAST91
Domaini107 – 195CARDPROSITE-ProRule annotationAdd BLAST89

Domaini

The CARD domain mediates interaction with CASP1 and NLRC4 (PubMed:14634131 and PubMed:11967258).1 Publication
The pyrin domain mediates homotypic interactions with pyrin domains of proteins such as of NLRP3, PYDC1, PYDC2 and AIM2.6 Publications

Sequence similaritiesi

Contains 1 CARD domain.PROSITE-ProRule annotation
Contains 1 pyrin domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410J02A. Eukaryota.
ENOG4111XEQ. LUCA.
GeneTreeiENSGT00440000033973.
HOGENOMiHOG000034090.
HOVERGENiHBG018739.
InParanoidiQ9ULZ3.
KOiK12799.
OMAiAWNLTCK.
OrthoDBiEOG091G0OWO.
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]
SMARTiSM01289. 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. AlignAdd to basket

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

        10         20         30         40         50
MGRARDAILD ALENLTAEEL KKFKLKLLSV PLREGYGRIP RGALLSMDAL
60 70 80 90 100
DLTDKLVSFY LETYGAELTA NVLRDMGLQE MAGQLQAATH QGSGAAPAGI
110 120 130 140 150
QAPPQSAAKP GLHFIDQHRA ALIARVTNVE WLLDALYGKV LTDEQYQAVR
160 170 180 190
AEPTNPSKMR KLFSFTPAWN WTCKDLLLQA LRESQSYLVE DLERS
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 differs from that shown. Reason: Frameshift at position 4.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00411826 – 85Missing in isoform 3. 1 PublicationAdd BLAST60
Alternative sequenceiVSP_00411993 – 111Missing in isoform 2. 1 PublicationAdd BLAST19

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human. [Q9ULZ3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5H8OX-ray4.21B115-195[»]
ProteinModelPortaliQ9ULZ3.
SMRiQ9ULZ3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118876. 43 interactors.
DIPiDIP-27618N.
IntActiQ9ULZ3. 46 interactors.
MINTiMINT-206960.
STRINGi9606.ENSP00000247470.

PTM databases

iPTMnetiQ9ULZ3.
PhosphoSitePlusiQ9ULZ3.

Polymorphism and mutation databases

BioMutaiPYCARD.
DMDMi18203507.

Proteomic databases

EPDiQ9ULZ3.
PaxDbiQ9ULZ3.
PeptideAtlasiQ9ULZ3.
PRIDEiQ9ULZ3.

Protocols and materials databases

DNASUi29108.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000247470; ENSP00000247470; ENSG00000103490. [Q9ULZ3-1]
ENST00000350605; ENSP00000340441; ENSG00000103490. [Q9ULZ3-2]
GeneIDi29108.
KEGGihsa:29108.
UCSCiuc002ebm.4. human. [Q9ULZ3-1]

Organism-specific databases

CTDi29108.
DisGeNETi29108.
GeneCardsiPYCARD.
H-InvDBHIX0012985.
HGNCiHGNC:16608. PYCARD.
HPAiCAB006853.
CAB015948.
HPA049074.
HPA054496.
MIMi606838. gene.
neXtProtiNX_Q9ULZ3.
OpenTargetsiENSG00000103490.
PharmGKBiPA134950175.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J02A. Eukaryota.
ENOG4111XEQ. LUCA.
GeneTreeiENSGT00440000033973.
HOGENOMiHOG000034090.
HOVERGENiHBG018739.
InParanoidiQ9ULZ3.
KOiK12799.
OMAiAWNLTCK.
OrthoDBiEOG091G0OWO.
PhylomeDBiQ9ULZ3.
TreeFamiTF337882.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000103490-MONOMER.
ReactomeiR-HSA-5660668. CLEC7A/inflammasome pathway.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-844456. The NLRP3 inflammasome.
R-HSA-844615. The AIM2 inflammasome.
SIGNORiQ9ULZ3.

Miscellaneous databases

EvolutionaryTraceiQ9ULZ3.
GeneWikiiPYCARD.
GenomeRNAii29108.
PROiQ9ULZ3.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000103490.
CleanExiHS_PYCARD.
ExpressionAtlasiQ9ULZ3. baseline and differential.
GenevisibleiQ9ULZ3. HS.

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]
SMARTiSM01289. PYRIN. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 2 hits.
PROSITEiPS50209. CARD. 1 hit.
PS50824. DAPIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 163 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

Similar proteinsi

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