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PYCARD
Доступные структуры PDB Поиск ортологов: PDBe RCSB Список идентификаторов PDB 1UCP, 2KN6, 3J63, 5H8O
Идентификаторы
Символы	PYCARD, ASC, CARD5, TMS, TMS-1, TMS1, PYD and CARD domain containing
Внешние IDs	MGI: 1931465 HomoloGene: 8307 GeneCards: 29108
Генная онтология Функции • гомодимеризация белка • interleukin-6 receptor binding • BMP receptor binding • связывание с белками плазмы • связывание похожих белков • enzyme binding • cysteine-type endopeptidase activity involved in apoptotic process • Pyrin domain binding • cysteine-type endopeptidase activator activity involved in apoptotic process • myosin I binding • tropomyosin binding • protease binding • ion channel binding • protein dimerization activity • cysteine-type endopeptidase activity Компонент клетки • цитоплазма • NLRP3 inflammasome complex • NLRP1 inflammasome complex • AIM2 inflammasome complex • Ядрышко • Эндоплазматический ретикулум • Митохондрия • IkappaB kinase complex • клеточное ядро • secretory granule lumen • azurophil granule lumen • внеклеточная область • цитозоль • macromolecular complex • neuronal cell body • Golgi membrane Биологический процесс • positive regulation of cysteine-type endopeptidase activity • positive regulation of interleukin-10 secretion • regulation of apoptotic process • intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator • regulation of intrinsic apoptotic signaling pathway • intrinsic apoptotic signaling pathway by p53 class mediator • positive regulation of adaptive immune response • positive regulation of interleukin-6 secretion • defense response to Gram-negative bacterium • immune system process • cellular response to tumor necrosis factor • regulation of tumor necrosis factor-mediated signaling pathway • positive regulation of sequence-specific DNA binding transcription factor activity • tumor necrosis factor-mediated signaling pathway • positive regulation of JNK cascade • negative regulation of interferon-beta production • negative regulation of I-kappaB kinase/NF-kappaB signaling • myeloid dendritic cell activation • positive regulation of T cell activation • defense response to virus • cellular response to interleukin-1 • positive regulation of apoptotic process • positive regulation of tumor necrosis factor production • positive regulation of release of cytochrome c from mitochondria • negative regulation of protein serine/threonine kinase activity • positive regulation of extrinsic apoptotic signaling pathway • positive regulation of interleukin-8 secretion • воспалительная реакция • cellular response to lipopolysaccharide • negative regulation of NF-kappaB transcription factor activity • передача сигнала • Апоптоз • врождённый иммунный ответ • neutrophil degranulation • positive regulation of NF-kappaB transcription factor activity • activation of innate immune response • myeloid dendritic cell activation involved in immune response • positive regulation of antigen processing and presentation of peptide antigen via MHC class II • activation of cysteine-type endopeptidase activity involved in apoptotic process • positive regulation of actin filament polymerization • regulation of protein stability • positive regulation of interferon-gamma production • positive regulation of interleukin-6 production • positive regulation of activated T cell proliferation • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process • macropinocytosis • positive regulation of interleukin-1 beta secretion • positive regulation of phagocytosis • positive regulation of ERK1 and ERK2 cascade • positive regulation of chemokine secretion • positive regulation of T cell migration • positive regulation of defense response to virus by host • intrinsic apoptotic signaling pathway in response to DNA damage • response to bacterium • regulation of autophagy • interleukin-1 beta production • regulation of GTPase activity • regulation of cysteine-type endopeptidase activity involved in apoptotic process • regulation of inflammatory response • protein homooligomerization • activation of cysteine-type endopeptidase activity • negative regulation of cytokine production involved in inflammatory response • Протеолиз Источники:Amigo / QuickGO
Профиль экспрессии РНК
Больше информации
Ортологи
Виды	Человек	Мышь
Entrez	29108	66824
Ensembl	ENSG00000103490	ENSMUSG00000030793
UniProt	Q9ULZ3	Q9EPB4
RefSeq (мРНК)	NM_145183 NM_013258 NM_145182	NM_023258
RefSeq (белок)	NP_037390 NP_660183	NP_075747
Локус (UCSC)	Chr 16: 31.2 – 31.2 Mb	Chr 7: 127.99 – 127.99 Mb
Поиск PubMed
Викиданные
Просмотр/Править (Человек)		Просмотр/Править (Мышь)

PYCARD, или ASC (сокр. от англ. apoptosis-associated speck-like protein containing a CARD, апоптоз-ассоциированный Speck-подобный белок, содержащий CARD) — цитозольный адаптерный белок. Продукт гена человека PYCARD.^[1]

Адаптерный белок включает два домена: N-концевой PYD домен и C-концевой CARD домен. Оба домена входят в большую группу т. н. доменов смерти, состоящих из 6 спиралей, которые опосредуют формирование крупных мультимолекулярных сигнальных комплексов, активирующих каспазу и играющих, таким образом, важную роль в воспалении и апоптозе. В клетках белок ASC находится в цитоплазме, но при активации апоптоза образует сферические белковые агрегаты вблизи клеточного ядра. Существуют две изоформы ASC.^[2]

Взаимодействия

PYCARD взаимодействует с белком MEFV.^[3]

См. также

• Инфламмасома
• NLRP3

Примечания

Литература

• Masumoto J, Taniguchi S, Ayukawa K; et al. (1999). “ASC, a novel 22-kDa protein, aggregates during apoptosis of human promyelocytic leukemia HL-60 cells”. J. Biol. Chem. 274 (48): 33835—8. DOI:10.1074/jbc.274.48.33835. PMID 10567338.
• Lee SK, Na SY, Jung SY; et al. (2000). “Activating protein-1, nuclear factor-kappaB, and serum response factor as novel target molecules of the cancer-amplified transcription coactivator ASC-2”. Mol. Endocrinol. 14 (6): 915—25. DOI:10.1210/me.14.6.915. PMID 10847592.
• Conway KE, McConnell BB, Bowring CE; et al. (2000). “TMS1, a novel proapoptotic caspase recruitment domain protein, is a target of methylation-induced gene silencing in human breast cancers”. Cancer Res. 60 (22): 6236—42. PMID 11103776.
• McConnell BB, Vertino PM (2000). “Activation of a caspase-9-mediated apoptotic pathway by subcellular redistribution of the novel caspase recruitment domain protein TMS1”. Cancer Res. 60 (22): 6243—7. PMID 11103777.
• Martinon F, Hofmann K, Tschopp J (2001). “The pyrin domain: a possible member of the death domain-fold family implicated in apoptosis and inflammation”. Curr. Biol. 11 (4): R118—20. DOI:10.1016/S0960-9822(01)00056-2. PMID 11250163.
• Geddes BJ, Wang L, Huang WJ; et al. (2001). “Human CARD12 is a novel CED4/Apaf-1 family member that induces apoptosis”. Biochem. Biophys. Res. Commun. 284 (1): 77—82. DOI:10.1006/bbrc.2001.4928. PMID 11374873.
• Richards N, Schaner P, Diaz A; et al. (2001). “Interaction between pyrin and the apoptotic speck protein (ASC) modulates ASC-induced apoptosis”. J. Biol. Chem. 276 (42): 39320—9. DOI:10.1074/jbc.M104730200. PMID 11498534.
• Stimson KM, Vertino PM (2002). “Methylation-mediated silencing of TMS1/ASC is accompanied by histone hypoacetylation and CpG island-localized changes in chromatin architecture”. J. Biol. Chem. 277 (7): 4951—8. DOI:10.1074/jbc.M109809200. PMID 11733524.
• Manji GA, Wang L, Geddes BJ; et al. (2002). “PYPAF1, a PYRIN-containing Apaf1-like protein that assembles with ASC and regulates activation of NF-kappa B.”. J. Biol. Chem. 277 (13): 11570—5. DOI:10.1074/jbc.M112208200. PMID 11786556.
• Srinivasula SM, Poyet JL, Razmara M; et al. (2002). “The PYRIN-CARD protein ASC is an activating adaptor for caspase-1”. J. Biol. Chem. 277 (24): 21119—22. DOI:10.1074/jbc.C200179200. PMID 11967258.
• Wang L, Manji GA, Grenier JM; et al. (2002). “PYPAF7, a novel PYRIN-containing Apaf1-like protein that regulates activation of NF-kappa B and caspase-1-dependent cytokine processing”. J. Biol. Chem. 277 (33): 29874—80. DOI:10.1074/jbc.M203915200. PMID 12019269.
• Shiohara M, Taniguchi S, Masumoto J; et al. (2002). “ASC, which is composed of a PYD and a CARD, is up-regulated by inflammation and apoptosis in human neutrophils”. Biochem. Biophys. Res. Commun. 293 (5): 1314—8. DOI:10.1016/S0006-291X(02)00384-4. PMID 12054656.
• Martinon F, Burns K, Tschopp J (2002). “The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta”. Mol. Cell. 10 (2): 417—26. DOI:10.1016/S1097-2765(02)00599-3. PMID 12191486.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899—903. DOI:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Stehlik C, Fiorentino L, Dorfleutner A; et al. (2003). “The PAAD/PYRIN-family protein ASC is a dual regulator of a conserved step in nuclear factor kappaB activation pathways”. J. Exp. Med. 196 (12): 1605—15. DOI:10.1084/jem.20021552. PMC 2196065. PMID 12486103.
• Moriai R, Tsuji N, Kobayashi D; et al. (2003). “A proapoptotic caspase recruitment domain protein gene, TMS1, is hypermethylated in human breast and gastric cancers”. Anticancer Res. 22 (6C): 4163—8. PMID 12553049.
• Dowds TA, Masumoto J, Chen FF; et al. (2003). “Regulation of cryopyrin/Pypaf1 signaling by pyrin, the familial Mediterranean fever gene product”. Biochem. Biophys. Res. Commun. 302 (3): 575—80. DOI:10.1016/S0006-291X(03)00221-3. PMID 12615073.
• Masumoto J, Dowds TA, Schaner P; et al. (2003). “ASC is an activating adaptor for NF-kappa B and caspase-8-dependent apoptosis”. Biochem. Biophys. Res. Commun. 303 (1): 69—73. DOI:10.1016/S0006-291X(03)00309-7. PMID 12646168.
• Stehlik C, Krajewska M, Welsh K; et al. (2003). “The PAAD/PYRIN-only protein POP1/ASC2 is a modulator of ASC-mediated nuclear-factor-kappa B and pro-caspase-1 regulation”. Biochem. J. 373 (Pt 1): 101—13. DOI:10.1042/BJ20030304. PMC 1223462. PMID 12656673.
• Levine JJ, Stimson-Crider KM, Vertino PM (2003). “Effects of methylation on expression of TMS1/ASC in human breast cancer cells”. Oncogene. 22 (22): 3475—88. DOI:10.1038/sj.onc.1206430. PMID 12776200.