TNFAIP3

El factor de necrosis tumoral, proteína 3 inducida por alfa o A20 es una proteína que en humanos está codificada por el gen TNFAIP3 .^[4][5][6]

PDBBúsqueda ortóloga: PDBe RCSB

AliasTNFAIP3, A20, OTUD7C, TNFA1P2, AISBL, TNF alpha induced protein 3, AIFBL1

IDs externosOMIM: 191163 MGI: 1196377 HomoloGene: 4582 GeneCards: TNFAIP3

Función molecular

• DNA binding
• cysteine-type peptidase activity
• zinc ion binding
• metal ion binding
• GO:0050372 ubiquitin-protein transferase activity
• protease binding
• protein self-association
• GO:0070122 peptidase activity
• ligase activity
• kinase binding
• K63-linked polyubiquitin modification-dependent protein binding
• ubiquitin binding
• GO:0001948, GO:0016582 unión a proteína plasmática
• actividad catalítica
• thiol-dependent deubiquitinase
• hydrolase activity
• identical protein binding
• Lys63-specific deubiquitinase activity
• transferase activity

Datos rápidos Estructuras disponibles, PDB ...

TNFAIP3
Estructuras disponibles PDB Búsqueda ortóloga: PDBe RCSB Lista de codigos id de PDB 2EQF, 2EQG, 2VFJ, 3DKB, 3OJ3, 3OJ4, 3VUW, 3VUX, 3VUY, 3ZJD, 3ZJE, 3ZJF, 3ZJG, 4ZRH, 4ZS5
Identificadores
Alias	TNFAIP3, A20, OTUD7C, TNFA1P2, AISBL, TNF alpha induced protein 3, AIFBL1
IDs externos	OMIM: 191163 MGI: 1196377 HomoloGene: 4582 GeneCards: TNFAIP3
Enfermedades genéticamente relacionadas
lupus, psoriasis[1]
Ontología génica Función molecular • DNA binding • cysteine-type peptidase activity • zinc ion binding • metal ion binding • GO:0050372 ubiquitin-protein transferase activity • protease binding • protein self-association • GO:0070122 peptidase activity • ligase activity • kinase binding • K63-linked polyubiquitin modification-dependent protein binding • ubiquitin binding • GO:0001948, GO:0016582 unión a proteína plasmática • actividad catalítica • thiol-dependent deubiquitinase • hydrolase activity • identical protein binding • Lys63-specific deubiquitinase activity • transferase activity Componente celular • citoplasma • citosol • lisosoma • Exosoma (vesícula) • núcleo celular • intracellular membrane-bounded organelle Proceso biológico • regulation of germinal center formation • positive regulation of hepatocyte proliferation • negative regulation of endothelial cell apoptotic process • negative regulation of interleukin-1 beta production • negative regulation of smooth muscle cell proliferation • regulation of vascular wound healing • B-1 B cell homeostasis • protein K48-linked deubiquitination • GO:1903364 positive regulation of protein catabolic process • negative regulation of cyclin-dependent protein serine/threonine kinase activity • regulation of defense response to virus by host • protein deubiquitination involved in ubiquitin-dependent protein catabolic process • negative regulation of toll-like receptor 2 signaling pathway • negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway • regulation of tumor necrosis factor-mediated signaling pathway • negative regulation of interleukin-6 production • negative regulation of B cell activation • negative regulation of toll-like receptor 5 signaling pathway • tolerance induction to lipopolysaccharide • response to muramyl dipeptide • negative regulation of chronic inflammatory response • negative regulation of cell death • negative regulation of I-kappaB kinase/NF-kappaB signaling • proteólisis • establishment of protein localization to vacuole • protein deubiquitination • negative regulation of protein ubiquitination • protein K48-linked ubiquitination • protein K63-linked deubiquitination • negative regulation of CD40 signaling pathway • negative regulation of extrinsic apoptotic signaling pathway via death domain receptors • protein complex oligomerization • protein K11-linked deubiquitination • regulation of inflammatory response • negative regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway • negative regulation of innate immune response • negative regulation of osteoclast proliferation • negative regulation of tumor necrosis factor production • negative regulation of type I interferon production • metabolismo • respuesta inflamatoria • response to molecule of bacterial origin • negative regulation of NF-kappaB transcription factor activity • negative regulation of interleukin-2 production • negative regulation of inflammatory response • negative regulation of toll-like receptor 3 signaling pathway • nucleotide-binding oligomerization domain containing signaling pathway • cellular response to lipopolysaccharide • negative regulation of toll-like receptor 4 signaling pathway • negative regulation of bone resorption • cellular response to hydrogen peroxide • GO:0097285 apoptosis • ubicuitinación de proteínas • cytoskeleton organization • migración celular • positive regulation of Wnt signaling pathway • protein K29-linked deubiquitination • protein K33-linked deubiquitination Fuentes: Amigo / QuickGO
Patrón de la expressión del ARN
Más referencias a datos de expressión
Ortólogos
Especies	Humano	Ratón
Entrez	7128	21929
Ensembl	ENSG00000118503	ENSMUSG00000019850
UniProt	P21580	Q60769
SeqRef (ARNm)	NM_001270507 NM_001270508 NM_006290	NM_001166402 NM_009397
SeqRef (proteina)	NP_001257436 NP_001257437 NP_006281	NP_001159874 NP_033423
Localización (UCSC)	n/a	n/a
Búsqueda en PubMed	[2]	[3]
Wikidata
Ver/Editar Humano		Ver/Editar Ratón

Cerrar

Este gen fue identificado como un gen cuya expresión es inducida por el factor de necrosis tumoral (TNF). La proteína codificada por este gen es una proteína de dedos de zinc que produce una enzima deubiquitinante. Se ha demostrado que inhibe la activación de NF-kappa B así como la apoptosis mediada por TNF. La proteína A20 es antigua, y el homólogo de la proteína se puede encontrar desde los cnidarios (corales, medusas, anémonas) con una composición de dominio de proteína conservada.^[7] Utilizando modelos knockout de TNFAIP3 en ratones y su represor transcripcional (es decir, KCHIP3), se ha demostrado que TNFAIP3 es fundamental para limitar la inflamación al terminar las respuestas de NF-kappa B inducidas por endotoxina y TNF.^[8][9] En resumen, se demostró que la función deubiquitinasa de TNFAIP3 elimina las cadenas de ubiquitina de VE-cadherina para evitar la pérdida de VE-cadherina en las uniones adherentes endoteliales.^[10]