MOUSE:TNAP3

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Species (Taxon ID)	Mus musculus (Mouse). (taxon:10090)
Gene Name(s)	Tnfaip3 ( synonyms: Tnfip3 )
Protein Name(s)	Tumor necrosis factor alpha-induced protein 3 TNF alpha-induced protein 3 Putative DNA-binding protein A20 Zinc finger protein A20
External Links
UniProt Identifier	TNAP3_MOUSE
UniProt Accessions	Q60769, Q3U968,
EMBL	U19463, AK151921,
PIR	I49237,
IntAct	Q60769,
Ensembl	ENSMUST00000019997, ENSMUST00000105527,
Pfam	PF02338, PF01754,

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0001922	B-1 B cell homeostasis	PMID:21088135^[1]	IMP: Inferred from Mutant Phenotype		P
	GO:0002237	response to molecule of bacterial origin	PMID:19912257^[2]	IDA: Inferred from Direct Assay		P
	GO:0002315	marginal zone B cell differentiation	PMID:21088135^[1]	NAS: Non-traceable Author Statement		P
	GO:0002632	negative regulation of granuloma formation	PMID:18006655^[3]	NAS: Non-traceable Author Statement		P
	GO:0002634	regulation of germinal center formation	PMID:21088135^[1]	IMP: Inferred from Mutant Phenotype		P
	GO:0002637	regulation of immunoglobulin production	PMID:21088135^[1]	IC: Inferred by Curator	GO:0001922	P
	GO:0003677	DNA binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR002653	F
	GO:0003677	DNA binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0238	F
	GO:0003824	catalytic activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0511	F
	GO:0004221	ubiquitin thiolesterase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000237289	F
	GO:0004221	ubiquitin thiolesterase activity	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	F
	GO:0004842	ubiquitin-protein ligase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000237289	F
	GO:0004842	ubiquitin-protein ligase activity	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	F
	GO:0004843	ubiquitin-specific protease activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000237289	F
	GO:0004843	ubiquitin-specific protease activity	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	F
	GO:0005515	protein binding	PMID:11390377^[4]	IPI: Inferred from Physical Interaction	UniProtKB:Q99JG7	F
	GO:0005515	protein binding	PMID:18223652^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q2TBA3	F
	GO:0005515	protein binding	PMID:18239685^[6]	IPI: Inferred from Physical Interaction	UniProtKB:Q3UKC1	F
	GO:0005634	nucleus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0539	C
	GO:0005634	nucleus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000237289	C
	GO:0005634	nucleus	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0191	C
	GO:0005737	cytoplasm	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0963	C
	GO:0005737	cytoplasm	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000237289	C
	GO:0005737	cytoplasm	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0086	C
	GO:0005737	cytoplasm	PMID:10385526^[7]	IDA: Inferred from Direct Assay		C
	GO:0005813	centrosome	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000237289	C
	GO:0006915	apoptosis	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0053	P
	GO:0006916	anti-apoptosis	PMID:15962316^[8]	NAS: Non-traceable Author Statement		P
	GO:0008152	metabolic process	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0511	P
	GO:0008233	peptidase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0645	F
	GO:0008234	cysteine-type peptidase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0788	F
	GO:0008270	zinc ion binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR002653	F
	GO:0009611	response to wounding	PMID:20430393^[9]	NAS: Non-traceable Author Statement		P
	GO:0010507	negative regulation of autophagy	PMID:20501938^[10]	NAS: Non-traceable Author Statement		P
	GO:0016579	protein deubiquitination	PMID:18342009^[11]	IDA: Inferred from Direct Assay		P
	GO:0016787	hydrolase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0378	F
	GO:0016874	ligase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0436	F
	GO:0019900	kinase binding	PMID:18342009^[11]	IDA: Inferred from Direct Assay		F
	GO:0032495	response to muramyl dipeptide	PMID:18342009^[11]	IMP: Inferred from Mutant Phenotype		P
	GO:0032691	negative regulation of interleukin-1 beta production	PMID:18006655^[3]	IMP: Inferred from Mutant Phenotype		P
	GO:0032691	negative regulation of interleukin-1 beta production	PMID:18342009^[11]	IMP: Inferred from Mutant Phenotype		P
	GO:0032715	negative regulation of interleukin-6 production	PMID:18006655^[3]	IMP: Inferred from Mutant Phenotype		P
	GO:0032715	negative regulation of interleukin-6 production	PMID:18342009^[11]	IMP: Inferred from Mutant Phenotype		P
	GO:0032715	negative regulation of interleukin-6 production	PMID:21088135^[1]	IMP: Inferred from Mutant Phenotype		P
	GO:0032720	negative regulation of tumor necrosis factor production	PMID:21088135^[1]	IMP: Inferred from Mutant Phenotype		P
	GO:0034115	negative regulation of heterotypic cell-cell adhesion	PMID:18006655^[3]	NAS: Non-traceable Author Statement		P
	GO:0034115	negative regulation of heterotypic cell-cell adhesion	PMID:19252225^[12]	NAS: Non-traceable Author Statement		P
	GO:0034148	negative regulation of toll-like receptor 5 signaling pathway	PMID:19912257^[2]	IDA: Inferred from Direct Assay		P
	GO:0043124	negative regulation of I-kappaB kinase/NF-kappaB cascade	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000237289	P
	GO:0043124	negative regulation of I-kappaB kinase/NF-kappaB cascade	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	P
	GO:0043124	negative regulation of I-kappaB kinase/NF-kappaB cascade	PMID:18342009^[11]	IMP: Inferred from Mutant Phenotype		P
	GO:0043124	negative regulation of I-kappaB kinase/NF-kappaB cascade	PMID:21088135^[1]	IMP: Inferred from Mutant Phenotype		P
	GO:0043154	negative regulation of caspase activity	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	P
	GO:0045088	regulation of innate immune response	PMID:21088135^[1]	IC: Inferred by Curator	GO:0001922	P
	GO:0045732	positive regulation of protein catabolic process	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	P
	GO:0045736	negative regulation of cyclin-dependent protein kinase activity	PMID:15962316^[8]	IDA: Inferred from Direct Assay		P
	GO:0046872	metal ion binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0479	F
	GO:0048662	negative regulation of smooth muscle cell proliferation	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	P
	GO:0050728	negative regulation of inflammatory response	PMID:21088135^[1]	IMP: Inferred from Mutant Phenotype		P
	GO:0050869	negative regulation of B cell activation	PMID:21088135^[1]	IDA: Inferred from Direct Assay		P
	GO:0060548	negative regulation of cell death	PMID:11009421^[13]	IMP: Inferred from Mutant Phenotype		P
	GO:0070429	negative regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway	PMID:18342009^[11]	IMP: Inferred from Mutant Phenotype		P
	GO:0070433	negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway	PMID:18342009^[11]	IDA: Inferred from Direct Assay		P
	GO:0070536	protein K63-linked deubiquitination	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000237289	P
	GO:0070536	protein K63-linked deubiquitination	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	P
	GO:0070936	protein K48-linked ubiquitination	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000237289	P
	GO:0070936	protein K48-linked ubiquitination	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	P
	GO:0071222	cellular response to lipopolysaccharide	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	P
	GO:2000347	positive regulation of hepatocyte proliferation	PMID:15962316^[8]	IDA: Inferred from Direct Assay		P
	GO:0045449	regulation of transcription	PMID:21437236^[14]	IMP: Inferred from Mutant Phenotype		1	Fig 1, Fig2. A20/Tnfaip3 induces transcriptional changes at the basal level and after liver resection.	complete
	GO:0001922	B-1 B cell homeostasis	PMID:21088135^[1]	IMP: Inferred from Mutant Phenotype		P
	GO:0002237	response to molecule of bacterial origin	PMID:19912257^[2]	IDA: Inferred from Direct Assay		P
	GO:0002315	marginal zone B cell differentiation	PMID:21088135^[1]	NAS: Non-traceable Author Statement		P
	GO:0002632	negative regulation of granuloma formation	PMID:18006655^[3]	NAS: Non-traceable Author Statement		P
	GO:0002634	regulation of germinal center formation	PMID:21088135^[1]	IMP: Inferred from Mutant Phenotype		P
	GO:0002637	regulation of immunoglobulin production	PMID:21088135^[1]	IC: Inferred by Curator	GO:0001922	P
	GO:0003677	DNA binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR002653	F
	GO:0003677	DNA binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0238	F
	GO:0003824	catalytic activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0511	F
	GO:0004221	ubiquitin thiolesterase activity	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	F
	GO:0004842	ubiquitin-protein ligase activity	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	F
	GO:0004843	ubiquitin-specific protease activity	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	F
	GO:0005515	protein binding	PMID:18223652^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q2TBA3	F
	GO:0005515	protein binding	PMID:18239685^[6]	IPI: Inferred from Physical Interaction	UniProtKB:Q3UKC1	F
	GO:0005634	nucleus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0539	C
	GO:0005634	nucleus	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0191	C
	GO:0005737	cytoplasm	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0963	C
	GO:0005737	cytoplasm	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0086	C
	GO:0006915	apoptosis	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0053	P
	GO:0006916	anti-apoptosis	PMID:15962316^[8]	NAS: Non-traceable Author Statement		P
	GO:0008152	metabolic process	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0511	P
	GO:0008233	peptidase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0645	F
	GO:0008234	cysteine-type peptidase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0788	F
	GO:0008270	zinc ion binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR002653	F
	GO:0009611	response to wounding	PMID:20430393^[9]	NAS: Non-traceable Author Statement		P
	GO:0010507	negative regulation of autophagy	PMID:20501938^[10]	NAS: Non-traceable Author Statement		P
	GO:0016579	protein deubiquitination	PMID:18342009^[11]	IDA: Inferred from Direct Assay		P
	GO:0016787	hydrolase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0378	F
	GO:0016874	ligase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0436	F
	GO:0019900	kinase binding	PMID:18342009^[11]	IDA: Inferred from Direct Assay		F
	GO:0032495	response to muramyl dipeptide	PMID:18342009^[11]	IMP: Inferred from Mutant Phenotype		P
	GO:0032691	negative regulation of interleukin-1 beta production	PMID:18006655^[3]	IMP: Inferred from Mutant Phenotype		P
	GO:0032691	negative regulation of interleukin-1 beta production	PMID:18342009^[11]	IMP: Inferred from Mutant Phenotype		P
	GO:0032715	negative regulation of interleukin-6 production	PMID:18006655^[3]	IMP: Inferred from Mutant Phenotype		P
	GO:0032715	negative regulation of interleukin-6 production	PMID:18342009^[11]	IMP: Inferred from Mutant Phenotype		P
	GO:0032715	negative regulation of interleukin-6 production	PMID:21088135^[1]	IMP: Inferred from Mutant Phenotype		P
	GO:0032720	negative regulation of tumor necrosis factor production	PMID:21088135^[1]	IMP: Inferred from Mutant Phenotype		P
	GO:0034115	negative regulation of heterotypic cell-cell adhesion	PMID:18006655^[3]	NAS: Non-traceable Author Statement		P
	GO:0034115	negative regulation of heterotypic cell-cell adhesion	PMID:19252225^[12]	NAS: Non-traceable Author Statement		P
	GO:0034148	negative regulation of toll-like receptor 5 signaling pathway	PMID:19912257^[2]	IDA: Inferred from Direct Assay		P
	GO:0043124	negative regulation of I-kappaB kinase/NF-kappaB cascade	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	P
	GO:0043124	negative regulation of I-kappaB kinase/NF-kappaB cascade	PMID:18342009^[11]	IMP: Inferred from Mutant Phenotype		P
	GO:0043124	negative regulation of I-kappaB kinase/NF-kappaB cascade	PMID:21088135^[1]	IMP: Inferred from Mutant Phenotype		P
	GO:0043154	negative regulation of caspase activity	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	P
	GO:0045088	regulation of innate immune response	PMID:21088135^[1]	IC: Inferred by Curator	GO:0001922	P
	GO:0045732	positive regulation of protein catabolic process	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	P
	GO:0045736	negative regulation of cyclin-dependent protein kinase activity	PMID:15962316^[8]	IDA: Inferred from Direct Assay		P
	GO:0046872	metal ion binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0479	F
	GO:0048662	negative regulation of smooth muscle cell proliferation	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	P
	GO:0050728	negative regulation of inflammatory response	PMID:21088135^[1]	IMP: Inferred from Mutant Phenotype		P
	GO:0050869	negative regulation of B cell activation	PMID:21088135^[1]	IDA: Inferred from Direct Assay		P
	GO:0060548	negative regulation of cell death	PMID:11009421^[13]	IMP: Inferred from Mutant Phenotype		P
	GO:0070429	negative regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway	PMID:18342009^[11]	IMP: Inferred from Mutant Phenotype		P
	GO:0070433	negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway	PMID:18342009^[11]	IDA: Inferred from Direct Assay		P
	GO:0070536	protein K63-linked deubiquitination	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	P
	GO:0070936	protein K48-linked ubiquitination	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	P
	GO:0071222	cellular response to lipopolysaccharide	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P21580	P
	GO:2000347	positive regulation of hepatocyte proliferation	PMID:15962316^[8]	IDA: Inferred from Direct Assay		P
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.00 ^1.01 ^1.02 ^1.03 ^1.04 ^1.05 ^1.06 ^1.07 ^1.08 ^1.09 ^1.10 ^1.11 ^1.12 ^1.13 ^1.14 ^1.15 ^1.16 ^1.17 ^1.18 ^1.19 Chu Y et al. (2011) B cells lacking the tumor suppressor TNFAIP3/A20 display impaired differentiation and hyperactivation and cause inflammation and autoimmunity in aged mice. Blood 117: 2227-36 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Oshima N et al. (2010) A20 is an early responding negative regulator of Toll-like receptor 5 signalling in intestinal epithelial cells during inflammation. Clin Exp Immunol 159: 185-98 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 ^3.7 Wolfrum S et al. (2007) The protective effect of A20 on atherosclerosis in apolipoprotein E-deficient mice is associated with reduced expression of NF-kappaB target genes. Proc Natl Acad Sci U S A 104: 18601-6 PubMed GONUTS page
↑ Van Huffel S et al. (2001) Identification of a novel A20-binding inhibitor of nuclear factor-kappa B activation termed ABIN-2. J Biol Chem 276: 30216-23 PubMed GONUTS page
↑ ^5.0 ^5.1 Coornaert B et al. (2008) T cell antigen receptor stimulation induces MALT1 paracaspase-mediated cleavage of the NF-kappaB inhibitor A20. Nat Immunol 9: 263-71 PubMed GONUTS page
↑ ^6.0 ^6.1 Iha H et al. (2008) Inflammatory cardiac valvulitis in TAX1BP1-deficient mice through selective NF-kappaB activation. EMBO J 27: 629-41 PubMed GONUTS page
↑ Heyninck K et al. (1999) The zinc finger protein A20 inhibits TNF-induced NF-kappaB-dependent gene expression by interfering with an RIP- or TRAF2-mediated transactivation signal and directly binds to a novel NF-kappaB-inhibiting protein ABIN. J Cell Biol 145: 1471-82 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 ^8.4 ^8.5 Longo CR et al. (2005) A20 protects mice from lethal radical hepatectomy by promoting hepatocyte proliferation via a p21waf1-dependent mechanism. Hepatology 42: 156-64 PubMed GONUTS page
↑ ^9.0 ^9.1 Damrauer SM et al. (2010) A20 inhibits post-angioplasty restenosis by blocking macrophage trafficking and decreasing adventitial neovascularization. Atherosclerosis 211: 404-8 PubMed GONUTS page
↑ ^10.0 ^10.1 Shi CS & Kehrl JH (2010) TRAF6 and A20 regulate lysine 63-linked ubiquitination of Beclin-1 to control TLR4-induced autophagy. Sci Signal 3: ra42 PubMed GONUTS page
↑ ^11.00 ^11.01 ^11.02 ^11.03 ^11.04 ^11.05 ^11.06 ^11.07 ^11.08 ^11.09 ^11.10 ^11.11 ^11.12 ^11.13 ^11.14 ^11.15 Hitotsumatsu O et al. (2008) The ubiquitin-editing enzyme A20 restricts nucleotide-binding oligomerization domain containing 2-triggered signals. Immunity 28: 381-90 PubMed GONUTS page
↑ ^12.0 ^12.1 Zeng W et al. (2009) A20 overexpression inhibits low shear flow-induced CD14-positive monocyte recruitment to endothelial cells. Biorheology 46: 21-30 PubMed GONUTS page
↑ ^13.0 ^13.1 Lee EG et al. (2000) Failure to regulate TNF-induced NF-kappaB and cell death responses in A20-deficient mice. Science 289: 2350-4 PubMed GONUTS page
↑ Damrauer SM et al. (2011) A20 modulates lipid metabolism and energy production to promote liver regeneration. PLoS One 6: e17715 PubMed GONUTS page

[PMID:21088135-0] 1.00 ^1.01 ^1.02 ^1.03 ^1.04 ^1.05 ^1.06 ^1.07 ^1.08 ^1.09 ^1.10 ^1.11 ^1.12 ^1.13 ^1.14 ^1.15 ^1.16 ^1.17 ^1.18 ^1.19 Chu Y et al. (2011) B cells lacking the tumor suppressor TNFAIP3/A20 display impaired differentiation and hyperactivation and cause inflammation and autoimmunity in aged mice. Blood 117: 2227-36 PubMed GONUTS page

[PMID:19912257-1] 2.0 ^2.1 ^2.2 ^2.3 Oshima N et al. (2010) A20 is an early responding negative regulator of Toll-like receptor 5 signalling in intestinal epithelial cells during inflammation. Clin Exp Immunol 159: 185-98 PubMed GONUTS page

[PMID:18006655-2] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 ^3.7 Wolfrum S et al. (2007) The protective effect of A20 on atherosclerosis in apolipoprotein E-deficient mice is associated with reduced expression of NF-kappaB target genes. Proc Natl Acad Sci U S A 104: 18601-6 PubMed GONUTS page

[PMID:11390377-3] Van Huffel S et al. (2001) Identification of a novel A20-binding inhibitor of nuclear factor-kappa B activation termed ABIN-2. J Biol Chem 276: 30216-23 PubMed GONUTS page

[PMID:18223652-4] 5.0 ^5.1 Coornaert B et al. (2008) T cell antigen receptor stimulation induces MALT1 paracaspase-mediated cleavage of the NF-kappaB inhibitor A20. Nat Immunol 9: 263-71 PubMed GONUTS page

[PMID:18239685-5] 6.0 ^6.1 Iha H et al. (2008) Inflammatory cardiac valvulitis in TAX1BP1-deficient mice through selective NF-kappaB activation. EMBO J 27: 629-41 PubMed GONUTS page

[PMID:10385526-6] Heyninck K et al. (1999) The zinc finger protein A20 inhibits TNF-induced NF-kappaB-dependent gene expression by interfering with an RIP- or TRAF2-mediated transactivation signal and directly binds to a novel NF-kappaB-inhibiting protein ABIN. J Cell Biol 145: 1471-82 PubMed GONUTS page

[PMID:15962316-7] 8.0 ^8.1 ^8.2 ^8.3 ^8.4 ^8.5 Longo CR et al. (2005) A20 protects mice from lethal radical hepatectomy by promoting hepatocyte proliferation via a p21waf1-dependent mechanism. Hepatology 42: 156-64 PubMed GONUTS page

[PMID:20430393-8] 9.0 ^9.1 Damrauer SM et al. (2010) A20 inhibits post-angioplasty restenosis by blocking macrophage trafficking and decreasing adventitial neovascularization. Atherosclerosis 211: 404-8 PubMed GONUTS page

[PMID:20501938-9] 10.0 ^10.1 Shi CS & Kehrl JH (2010) TRAF6 and A20 regulate lysine 63-linked ubiquitination of Beclin-1 to control TLR4-induced autophagy. Sci Signal 3: ra42 PubMed GONUTS page

[PMID:18342009-10] 11.00 ^11.01 ^11.02 ^11.03 ^11.04 ^11.05 ^11.06 ^11.07 ^11.08 ^11.09 ^11.10 ^11.11 ^11.12 ^11.13 ^11.14 ^11.15 Hitotsumatsu O et al. (2008) The ubiquitin-editing enzyme A20 restricts nucleotide-binding oligomerization domain containing 2-triggered signals. Immunity 28: 381-90 PubMed GONUTS page

[PMID:19252225-11] 12.0 ^12.1 Zeng W et al. (2009) A20 overexpression inhibits low shear flow-induced CD14-positive monocyte recruitment to endothelial cells. Biorheology 46: 21-30 PubMed GONUTS page

[PMID:11009421-12] 13.0 ^13.1 Lee EG et al. (2000) Failure to regulate TNF-induced NF-kappaB and cell death responses in A20-deficient mice. Science 289: 2350-4 PubMed GONUTS page

[PMID:21437236-13] Damrauer SM et al. (2011) A20 modulates lipid metabolism and energy production to promote liver regeneration. PLoS One 6: e17715 PubMed GONUTS page

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MOUSE:TNAP3

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