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Protein

Tumor necrosis factor alpha-induced protein 3

Gene

Tnfaip3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, deubiquitinates 'Lys-63'-polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Deubiquitinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation. Deubiquitinates NEMO/IKBKG; the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation. Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin; polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of programmed cell death. Has a role in the function of the lymphoid system. Required for LPS-induced production of proinflammatory cytokines and IFN beta in LPS-tolerized macrophages.6 Publications

Catalytic activityi

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei100 – 1001By similarity
Active sitei103 – 1031NucleophileBy similarity
Active sitei256 – 2561Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri381 – 41636A20-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri464 – 49936A20-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri500 – 53334A20-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri586 – 62136A20-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri636 – 67136A20-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri695 – 73036A20-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri741 – 77535A20-type 7PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • B-1 B cell homeostasis Source: BHF-UCL
  • cellular response to hydrogen peroxide Source: UniProtKB
  • cellular response to lipopolysaccharide Source: BHF-UCL
  • establishment of protein localization to vacuole Source: MGI
  • inflammatory response Source: UniProtKB-KW
  • marginal zone B cell differentiation Source: BHF-UCL
  • negative regulation of autophagy Source: BHF-UCL
  • negative regulation of B cell activation Source: BHF-UCL
  • negative regulation of CD40 signaling pathway Source: BHF-UCL
  • negative regulation of cell death Source: BHF-UCL
  • negative regulation of chronic inflammatory response Source: BHF-UCL
  • negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: BHF-UCL
  • negative regulation of endothelial cell apoptotic process Source: MGI
  • negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
  • negative regulation of granuloma formation Source: BHF-UCL
  • negative regulation of heterotypic cell-cell adhesion Source: BHF-UCL
  • negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • negative regulation of inflammatory response Source: UniProtKB
  • negative regulation of innate immune response Source: UniProtKB
  • negative regulation of interleukin-1 beta production Source: BHF-UCL
  • negative regulation of interleukin-2 production Source: MGI
  • negative regulation of interleukin-6 production Source: BHF-UCL
  • negative regulation of NF-kappaB transcription factor activity Source: MGI
  • negative regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway Source: BHF-UCL
  • negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway Source: BHF-UCL
  • negative regulation of protein ubiquitination Source: MGI
  • negative regulation of smooth muscle cell proliferation Source: BHF-UCL
  • negative regulation of toll-like receptor 3 signaling pathway Source: MGI
  • negative regulation of toll-like receptor 5 signaling pathway Source: BHF-UCL
  • negative regulation of tumor necrosis factor production Source: BHF-UCL
  • positive regulation of cellular protein catabolic process Source: MGI
  • positive regulation of hepatocyte proliferation Source: BHF-UCL
  • positive regulation of protein catabolic process Source: BHF-UCL
  • protein deubiquitination Source: BHF-UCL
  • protein K11-linked deubiquitination Source: UniProtKB
  • protein K48-linked deubiquitination Source: UniProtKB
  • protein K48-linked ubiquitination Source: UniProtKB
  • protein K63-linked deubiquitination Source: UniProtKB
  • regulation of germinal center formation Source: BHF-UCL
  • regulation of immunoglobulin production Source: BHF-UCL
  • regulation of innate immune response Source: BHF-UCL
  • response to molecule of bacterial origin Source: BHF-UCL
  • response to muramyl dipeptide Source: BHF-UCL
  • response to wounding Source: BHF-UCL
  • tolerance induction to lipopolysaccharide Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ligase, Protease, Thiol protease

Keywords - Biological processi

Apoptosis, Inflammatory response, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_289760. Negative regulators of RIG-I/MDA5 signaling.
REACT_301153. NOD1/2 Signaling Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor necrosis factor alpha-induced protein 3 (EC:3.4.19.12, EC:6.3.2.-)
Short name:
TNF alpha-induced protein 3
Alternative name(s):
Putative DNA-binding protein A20
Zinc finger protein A20
Gene namesi
Name:Tnfaip3
Synonyms:Tnfip3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1196377. Tnfaip3.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: MGI
  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • lysosome Source: UniProtKB-SubCell
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Lysosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi100 – 1001D → A: Loss of deubiquitinating activity. 1 Publication
Mutagenesisi103 – 1031C → A: Loss of deubiquitinating activity, does not disassemble TRAF6:UBE2N ubiquitin ligase complex, abolioshes TAX1BP1 interaction with UBE2N. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 775774Tumor necrosis factor alpha-induced protein 3PRO_0000188793Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei451 – 4511PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ60769.
PRIDEiQ60769.

PTM databases

PhosphoSiteiQ60769.

Expressioni

Tissue specificityi

Found in most tissues during development. Strikingly high levels are found in lymphoid organs, including the thymus, spleen, and gut-associated lymphoid tissue. Constitutively expressed in immature and mature thymocyte subpopulations as well as in resting peripheral T-cells; activation of these leads to down-regulation.

Inductioni

By cytokines. TNF-alpha may regulate expression in the thymus. Up-regulated in presence of reactive oxygen species (ROS), like H2O2, in LPS-tolerized macrophages.1 Publication

Gene expression databases

BgeeiQ60769.
CleanExiMM_TNFAIP3.
ExpressionAtlasiQ60769. baseline and differential.
GenevisibleiQ60769. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with TNIP1, TAX1BP1 and TRAF2. Interacts with RNF11, ITCH and TAX1BP1 only after TNF stimulation; these interaction are transient and they are lost after 1 hour of stimulation with TNF (By similarity). Interacts with YWHAZ and YWHAH. Interacts with IKBKG; the interaction is induced by TNF stimulation and by polyubiquitin. Interacts with RIPK1. Interacts with UBE2N; the interaction requires TAX1BP1. Interacts with TRAF6 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Tnip1Q9WUU83EBI-646595,EBI-6126152
Traf2P394293EBI-646595,EBI-520016

Protein-protein interaction databases

BioGridi204243. 16 interactions.
DIPiDIP-41120N.
IntActiQ60769. 6 interactions.
MINTiMINT-97373.
STRINGi10090.ENSMUSP00000019997.

Structurei

3D structure databases

ProteinModelPortaliQ60769.
SMRiQ60769. Positions 3-362, 382-419, 588-620, 743-775.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini92 – 263172OTUPROSITE-ProRule annotationAdd
BLAST
Repeati286 – 317321Add
BLAST
Repeati324 – 356332Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 300243TRAF-bindingBy similarityAdd
BLAST
Regioni157 – 1593Interaction with ubiquitinBy similarity
Regioni190 – 1923Interaction with ubiquitinBy similarity
Regioni224 – 2274Interaction with ubiquitinBy similarity
Regioni286 – 356712 X approximate repeatsAdd
BLAST
Regioni369 – 775407Interaction with TNIP1Add
BLAST
Regioni386 – 44560Interaction with RIPK1By similarityAdd
BLAST
Regioni590 – 64051Required for proteosomal degradation of UBE2N and UBE2D3, TRAF6 deubiquitination, and TAX1BP1 interaction with UBE2NAdd
BLAST
Regioni591 – 775185Sufficient for inhibitory activity of TNF-induced NF-kappa-B activityAdd
BLAST
Regioni682 – 77594Required for lysosomal localization and for TRAF2 lysosomal degradationBy similarityAdd
BLAST

Domaini

The A20-type zinc fingers mediate the ubiquitin ligase activity. The A20-type zinc finger 4 selectively recognizes 'Lys-63'-linked polyubiquitin. The A20-type zinc finger 4-7 are sufficient to bind polyubiquitin (By similarity).By similarity
The OTU domain mediates the deubiquitinase activity.By similarity

Sequence similaritiesi

Belongs to the peptidase C64 family.Curated
Contains 7 A20-type zinc fingers.PROSITE-ProRule annotation
Contains 1 OTU domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri381 – 41636A20-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri464 – 49936A20-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri500 – 53334A20-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri586 – 62136A20-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri636 – 67136A20-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri695 – 73036A20-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri741 – 77535A20-type 7PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG248343.
GeneTreeiENSGT00530000062989.
HOGENOMiHOG000133004.
HOVERGENiHBG059260.
InParanoidiQ60769.
OMAiCETPNCP.
OrthoDBiEOG7JHM57.
TreeFamiTF323312.

Family and domain databases

InterProiIPR003323. OTU_dom.
IPR002653. Znf_A20.
[Graphical view]
PfamiPF02338. OTU. 1 hit.
PF01754. zf-A20. 6 hits.
[Graphical view]
SMARTiSM00259. ZnF_A20. 7 hits.
[Graphical view]
PROSITEiPS50802. OTU. 1 hit.
PS51036. ZF_A20. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q60769-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEQLLPQAL YLSNMRKAVK IRERTPEDIF KPTNGIIYHF KTMHRYTLEM
60 70 80 90 100
FRTCQFCPQF REIIHKALID RSVQASLESQ KKLNWCREVR KLVALKTNGD
110 120 130 140 150
GNCLMHAACQ YMWGVQDTDL VLRKALCSTL KETDTRNFKF RWQLESLKSQ
160 170 180 190 200
EFVETGLCYD TRNWNDEWDN LVKMASADTP AARSGLQYNS LEEIHIFVLS
210 220 230 240 250
NILRRPIIVI SDKMLRSLES GSNFAPLKVG GIYLPLHWPA QECYRYPIVL
260 270 280 290 300
GYDSQHFVPL VTLKDSGPEL RAVPLVNRDR GRFEDLKVHF LTDPENEMKE
310 320 330 340 350
KLLKEYLIVM EIPVQGWDHG TTHLINAAKL DEANLPKEIN LVDDYFELVQ
360 370 380 390 400
HEYKKWQENS DQARRAAHAQ NPLEPSTPQL SLMDIKCETP NCPFFMSVNT
410 420 430 440 450
QPLCHECSER RQKNQSKLPK LNSKLGPEGL PGVGLGSSNW SPEETAGGPH
460 470 480 490 500
SAPPTAPSLF LFSETTAMKC RSPGCPFTLN VQHNGFCERC HARQINASHT
510 520 530 540 550
ADPGKCQACL QDVTRTFNGI CSTCFKRTTA EPSSSLTSSI PASCHQRSKS
560 570 580 590 600
DPSQLIQSLT PHSCHRTGNV SPSGCLSQAA RTPGDRAGTS KCRKAGCMYF
610 620 630 640 650
GTPENKGFCT LCFIEYRENK QSVTASEKAG SPAPRFQNNV PCLGRECGTL
660 670 680 690 700
GSTMFEGYCQ KCFIEAQNQR FHEARRTEEQ LRSSQHRDMP RTTQVASRLK
710 720 730 740 750
CARASCKNIL ACRSEELCME CQHLSQRVGS VAHRGEPTPE EPPKQRCRAP
760 770
ACDHFGNAKC NGYCNECYQF KQMYG
Length:775
Mass (Da):87,654
Last modified:July 27, 2011 - v2
Checksum:i32349928908B3185
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti627 – 6271E → A in AAC52153 (PubMed:7836754).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19463 mRNA. Translation: AAC52153.1.
AK151921 mRNA. Translation: BAE30799.1.
CCDSiCCDS23715.1.
PIRiI49237.
RefSeqiNP_033423.3. NM_009397.3.
XP_006512765.1. XM_006512702.2.
UniGeneiMm.116683.

Genome annotation databases

EnsembliENSMUST00000019997; ENSMUSP00000019997; ENSMUSG00000019850.
ENSMUST00000105527; ENSMUSP00000101167; ENSMUSG00000019850.
GeneIDi21929.
UCSCiuc007ena.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19463 mRNA. Translation: AAC52153.1.
AK151921 mRNA. Translation: BAE30799.1.
CCDSiCCDS23715.1.
PIRiI49237.
RefSeqiNP_033423.3. NM_009397.3.
XP_006512765.1. XM_006512702.2.
UniGeneiMm.116683.

3D structure databases

ProteinModelPortaliQ60769.
SMRiQ60769. Positions 3-362, 382-419, 588-620, 743-775.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204243. 16 interactions.
DIPiDIP-41120N.
IntActiQ60769. 6 interactions.
MINTiMINT-97373.
STRINGi10090.ENSMUSP00000019997.

PTM databases

PhosphoSiteiQ60769.

Proteomic databases

MaxQBiQ60769.
PRIDEiQ60769.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019997; ENSMUSP00000019997; ENSMUSG00000019850.
ENSMUST00000105527; ENSMUSP00000101167; ENSMUSG00000019850.
GeneIDi21929.
UCSCiuc007ena.3. mouse.

Organism-specific databases

CTDi7128.
MGIiMGI:1196377. Tnfaip3.

Phylogenomic databases

eggNOGiNOG248343.
GeneTreeiENSGT00530000062989.
HOGENOMiHOG000133004.
HOVERGENiHBG059260.
InParanoidiQ60769.
OMAiCETPNCP.
OrthoDBiEOG7JHM57.
TreeFamiTF323312.

Enzyme and pathway databases

ReactomeiREACT_289760. Negative regulators of RIG-I/MDA5 signaling.
REACT_301153. NOD1/2 Signaling Pathway.

Miscellaneous databases

NextBioi301520.
PROiQ60769.
SOURCEiSearch...

Gene expression databases

BgeeiQ60769.
CleanExiMM_TNFAIP3.
ExpressionAtlasiQ60769. baseline and differential.
GenevisibleiQ60769. MM.

Family and domain databases

InterProiIPR003323. OTU_dom.
IPR002653. Znf_A20.
[Graphical view]
PfamiPF02338. OTU. 1 hit.
PF01754. zf-A20. 6 hits.
[Graphical view]
SMARTiSM00259. ZnF_A20. 7 hits.
[Graphical view]
PROSITEiPS50802. OTU. 1 hit.
PS51036. ZF_A20. 7 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Lymphoid expression and regulation of A20, an inhibitor of programmed cell death."
    Tewari M., Wolf F.W., Seldin M.F., O'Shea K.S., Dixit V.M., Turka L.A.
    J. Immunol. 154:1699-1706(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The zinc finger protein A20 inhibits TNF-induced NF-B-dependent gene expression by interfering with an RIP- or TRAF2-mediated transactivation signal and directly binds to a novel NF-B-inhibiting protein ABIN."
    Heyninck K., De Valck D., Vanden Berghe W., Van Criekinge W., Contreras R., Fiers W., Haegeman G., Beyaert R.
    J. Cell Biol. 145:1471-1482(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow.
  4. "Functional redundancy of the zinc fingers of A20 for inhibition of NF-kappaB activation and protein-protein interactions."
    Klinkenberg M., Van Huffel S., Heyninck K., Beyaert R.
    FEBS Lett. 498:93-97(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TNIP2; TAX1BP1; IKBKG AND TNIP1.
  5. "The ubiquitin-modifying enzyme A20 is required for termination of Toll-like receptor responses."
    Boone D.L., Turer E.E., Lee E.G., Ahmad R.C., Wheeler M.T., Tsui C., Hurley P., Chien M., Chai S., Hitotsumatsu O., McNally E., Pickart C., Ma A.
    Nat. Immunol. 5:1052-1060(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-100 AND CYS-103.
  6. "The ubiquitin-editing enzyme A20 restricts nucleotide-binding oligomerization domain containing 2-triggered signals."
    Hitotsumatsu O., Ahmad R.C., Tavares R., Wang M., Philpott D., Turer E.E., Lee B.L., Shiffin N., Advincula R., Malynn B.A., Werts C., Ma A.
    Immunity 28:381-390(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "The ubiquitin-editing enzyme A20 requires RNF11 to downregulate NF-kappaB signalling."
    Shembade N., Parvatiyar K., Harhaj N.S., Harhaj E.W.
    EMBO J. 28:513-522(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAX1BP1; RNF11 AND RIPK1.
  8. "Inhibition of NF-kappaB signaling by A20 through disruption of ubiquitin enzyme complexes."
    Shembade N., Ma A., Harhaj E.W.
    Science 327:1135-1139(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UBE2N, MUTAGENESIS OF CYS-103.
  9. "Immune responsive gene 1 (IRG1) promotes endotoxin tolerance by increasing A20 expression in macrophages through ROS."
    Li Y., Zhang P., Wang C., Han C., Meng J., Liu X., Xu S., Li N., Wang Q., Shi X., Cao X.
    J. Biol. Chem. 288:16225-16234(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.

Entry informationi

Entry nameiTNAP3_MOUSE
AccessioniPrimary (citable) accession number: Q60769
Secondary accession number(s): Q3U968
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.