ASC_HUMAN - dbPTM
ASC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASC_HUMAN
UniProt AC Q9ULZ3
Protein Name Apoptosis-associated speck-like protein containing a CARD
Gene Name PYCARD
Organism Homo sapiens (Human).
Sequence Length 195
Subcellular Localization Cytoplasm. Endoplasmic reticulum. Mitochondrion. Nucleus. 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 activ
Protein Description 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. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA. [PubMed: 28314590]
Protein Sequence MGRARDAILDALENLTAEELKKFKLKLLSVPLREGYGRIPRGALLSMDALDLTDKLVSFYLETYGAELTANVLRDMGLQEMAGQLQAATHQGSGAAPAGIQAPPQSAAKPGLHFIDQHRAALIARVTNVEWLLDALYGKVLTDEQYQAVRAEPTNPSKMRKLFSFTPAWNWTCKDLLLQALRESQSYLVEDLERS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
21AcetylationNLTAEELKKFKLKLL
HCCHHHHHHHCCHHH
60.4919608861
21UbiquitinationNLTAEELKKFKLKLL
HCCHHHHHHHCCHHH
60.49-
22UbiquitinationLTAEELKKFKLKLLS
CCHHHHHHHCCHHHC
61.43-
46PhosphorylationIPRGALLSMDALDLT
CCCCCEECCCHHHHH
18.5728348404
60PhosphorylationTDKLVSFYLETYGAE
HHHHHHHHHHHHCCH
8.98-
109UbiquitinationAPPQSAAKPGLHFID
CCCHHCCCCCCCCHH
39.0622817900
109 (in isoform 1)Ubiquitination-39.0621890473
137PhosphorylationEWLLDALYGKVLTDE
HHHHHHHHHCCCCHH
19.34-
139UbiquitinationLLDALYGKVLTDEQY
HHHHHHHCCCCHHHH
22.10-
146PhosphorylationKVLTDEQYQAVRAEP
CCCCHHHHHHHHCCC
9.0821552520
164PhosphorylationSKMRKLFSFTPAWNW
HHHHHHHHCCCCCCC
38.3527251275
195PhosphorylationLVEDLERS-------
HHHHHHCC-------
34.8924719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of ASC_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASC_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ASC_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MEFV_HUMANMEFVphysical
11498534
NALP2_HUMANNLRP2physical
15456791
IKKB_HUMANIKBKBphysical
12486103
IKKA_HUMANCHUKphysical
12486103
SQSTM_HUMANSQSTM1physical
22286270
BECN1_HUMANBECN1physical
22286270
RALB_HUMANRALBphysical
22286270
ASC_HUMANPYCARDphysical
23209292
ASC_HUMANPYCARDphysical
25416956
DJC28_HUMANDNAJC28physical
24407287
PPIP1_HUMANPSTPIP1physical
24407287
F184A_HUMANFAM184Aphysical
24407287
PML_HUMANPMLphysical
24407287
INP4B_HUMANINPP4Bphysical
24407287
MAN1_HUMANLEMD3physical
24407287
CP131_HUMANCEP131physical
24407287
ARMC2_HUMANARMC2physical
24407287
MYO1C_HUMANMYO1Cphysical
24407287
IL6RB_HUMANIL6STphysical
24407287
MCM4_HUMANMCM4physical
24407287
TSH2_HUMANTSHZ2physical
24407287
NU107_HUMANNUP107physical
24407287
FSTL5_HUMANFSTL5physical
24407287
NAA15_HUMANNAA15physical
24407287
DRC7_HUMANDRC7physical
24407287
DNLI3_HUMANLIG3physical
24407287
BMPR2_HUMANBMPR2physical
24407287
ENTK_HUMANTMPRSS15physical
24407287
TPM4_HUMANTPM4physical
24407287
ASC_HUMANPYCARDphysical
24407287
RIPK1_HUMANRIPK1physical
25402006
PAK1_HUMANPAK1physical
25402006
IF16_HUMANIFI16physical
26121674
BRCA1_HUMANBRCA1physical
26121674
CASP1_HUMANCASP1physical
26121674
AIM2_HUMANAIM2physical
26121674
ZY11B_HUMANZYG11Bphysical
28514442
CUL2_HUMANCUL2physical
28514442
ARI2_HUMANARIH2physical
29021376

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ASC_HUMAN

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Related Literatures of Post-Translational Modification

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