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Q60769 (TNAP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tumor necrosis factor alpha-induced protein 3

Short name=TNF alpha-induced protein 3
EC=3.4.19.12
EC=6.3.2.-
Alternative name(s):
Putative DNA-binding protein A20
Zinc finger protein A20
Gene names
Name:Tnfaip3
Synonyms:Tnfip3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length775 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.4 Ref.5 Ref.7 Ref.9 Ref.10

Catalytic activity

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). Ref.5

Subunit structure

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. Ref.4 Ref.8 Ref.9

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Lysosome By similarity.

Tissue specificity

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.

Induction

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. Ref.10

Domain

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.

The OTU domain mediates the deubiquitinase activity By similarity.

Sequence similarities

Belongs to the peptidase C64 family.

Contains 7 A20-type zinc fingers.

Contains 1 OTU domain.

Ontologies

Keywords
   Biological processApoptosis
Inflammatory response
Ubl conjugation pathway
   Cellular componentCytoplasm
Lysosome
Nucleus
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionHydrolase
Ligase
Protease
Thiol protease
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processB-1 B cell homeostasis

Inferred from mutant phenotype PubMed 21088135. Source: BHF-UCL

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to hydrogen peroxide

Inferred from mutant phenotype Ref.10. Source: UniProtKB

cellular response to lipopolysaccharide

Inferred from sequence or structural similarity. Source: BHF-UCL

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

marginal zone B cell differentiation

Non-traceable author statement PubMed 21088135. Source: BHF-UCL

negative regulation of B cell activation

Inferred from direct assay PubMed 21088135. Source: BHF-UCL

negative regulation of CD40 signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of autophagy

Non-traceable author statement PubMed 20501938. Source: BHF-UCL

negative regulation of cell death

Inferred from mutant phenotype PubMed 11009421. Source: BHF-UCL

negative regulation of chronic inflammatory response

Inferred from mutant phenotype PubMed 18006655. Source: BHF-UCL

negative regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from direct assay PubMed 15962316. Source: BHF-UCL

negative regulation of endothelial cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway via death domain receptors

Non-traceable author statement PubMed 15962316. Source: BHF-UCL

negative regulation of granuloma formation

Non-traceable author statement PubMed 18006655. Source: BHF-UCL

negative regulation of heterotypic cell-cell adhesion

Non-traceable author statement PubMed 18006655PubMed 19252225. Source: BHF-UCL

negative regulation of inflammatory response

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of innate immune response

Inferred from mutant phenotype Ref.10. Source: UniProtKB

negative regulation of interleukin-1 beta production

Inferred from mutant phenotype PubMed 18006655Ref.7. Source: BHF-UCL

negative regulation of interleukin-2 production

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-6 production

Inferred from mutant phenotype PubMed 18006655Ref.7PubMed 21088135. Source: BHF-UCL

negative regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway

Inferred from mutant phenotype Ref.7. Source: BHF-UCL

negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway

Inferred from direct assay Ref.7. Source: BHF-UCL

negative regulation of protein ubiquitination

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of toll-like receptor 3 signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of toll-like receptor 5 signaling pathway

Inferred from direct assay PubMed 19912257. Source: BHF-UCL

negative regulation of tumor necrosis factor production

Inferred from mutant phenotype PubMed 21088135. Source: BHF-UCL

positive regulation of hepatocyte proliferation

Inferred from direct assay PubMed 15962316. Source: BHF-UCL

positive regulation of protein catabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

protein K11-linked deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein K48-linked deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein K48-linked ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein K63-linked deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein deubiquitination

Inferred from direct assay Ref.7. Source: BHF-UCL

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of germinal center formation

Inferred from mutant phenotype PubMed 21088135. Source: BHF-UCL

regulation of immunoglobulin production

Inferred by curator PubMed 21088135. Source: BHF-UCL

regulation of innate immune response

Inferred by curator PubMed 21088135. Source: BHF-UCL

response to molecule of bacterial origin

Inferred from direct assay PubMed 19912257. Source: BHF-UCL

response to muramyl dipeptide

Inferred from mutant phenotype Ref.7. Source: BHF-UCL

response to wounding

Non-traceable author statement PubMed 20430393. Source: BHF-UCL

tolerance induction to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcentrosome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.2. Source: MGI

lysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

kinase binding

Inferred from direct assay Ref.7. Source: BHF-UCL

ubiquitin thiolesterase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Tnip1Q9WUU83EBI-646595,EBI-6126152
Traf2P394293EBI-646595,EBI-520016

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 775774Tumor necrosis factor alpha-induced protein 3
PRO_0000188793

Regions

Domain92 – 263172OTU
Repeat286 – 317321
Repeat324 – 356332
Zinc finger381 – 41636A20-type 1
Zinc finger464 – 49936A20-type 2
Zinc finger500 – 53334A20-type 3
Zinc finger586 – 62136A20-type 4
Zinc finger636 – 67136A20-type 5
Zinc finger695 – 73036A20-type 6
Zinc finger741 – 77535A20-type 7
Region58 – 300243TRAF-binding By similarity
Region157 – 1593Interaction with ubiquitin By similarity
Region190 – 1923Interaction with ubiquitin By similarity
Region224 – 2274Interaction with ubiquitin By similarity
Region286 – 356712 X approximate repeats
Region369 – 775407Interaction with TNIP1
Region386 – 44560Interaction with RIPK1 By similarity
Region590 – 64051Required for proteosomal degradation of UBE2N and UBE2D3, TRAF6 deubiquitination, and TAX1BP1 interaction with UBE2N
Region591 – 775185Sufficient for inhibitory activity of TNF-induced NF-kappa-B activity
Region682 – 77594Required for lysosomal localization and for TRAF2 lysosomal degradation By similarity

Sites

Active site1001 By similarity
Active site1031Nucleophile By similarity
Active site2561Proton acceptor By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue4511Phosphoserine By similarity

Experimental info

Mutagenesis1001D → A: Loss of deubiquitinating activity. Ref.5
Mutagenesis1031C → A: Loss of deubiquitinating activity, does not disassemble TRAF6:UBE2N ubiquitin ligase complex, abolioshes TAX1BP1 interaction with UBE2N. Ref.5 Ref.9
Sequence conflict6271E → A in AAC52153. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q60769 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 32349928908B3185

FASTA77587,654
        10         20         30         40         50         60 
MAEQLLPQAL YLSNMRKAVK IRERTPEDIF KPTNGIIYHF KTMHRYTLEM FRTCQFCPQF 

        70         80         90        100        110        120 
REIIHKALID RSVQASLESQ KKLNWCREVR KLVALKTNGD GNCLMHAACQ YMWGVQDTDL 

       130        140        150        160        170        180 
VLRKALCSTL KETDTRNFKF RWQLESLKSQ EFVETGLCYD TRNWNDEWDN LVKMASADTP 

       190        200        210        220        230        240 
AARSGLQYNS LEEIHIFVLS NILRRPIIVI SDKMLRSLES GSNFAPLKVG GIYLPLHWPA 

       250        260        270        280        290        300 
QECYRYPIVL GYDSQHFVPL VTLKDSGPEL RAVPLVNRDR GRFEDLKVHF LTDPENEMKE 

       310        320        330        340        350        360 
KLLKEYLIVM EIPVQGWDHG TTHLINAAKL DEANLPKEIN LVDDYFELVQ HEYKKWQENS 

       370        380        390        400        410        420 
DQARRAAHAQ NPLEPSTPQL SLMDIKCETP NCPFFMSVNT QPLCHECSER RQKNQSKLPK 

       430        440        450        460        470        480 
LNSKLGPEGL PGVGLGSSNW SPEETAGGPH SAPPTAPSLF LFSETTAMKC RSPGCPFTLN 

       490        500        510        520        530        540 
VQHNGFCERC HARQINASHT ADPGKCQACL QDVTRTFNGI CSTCFKRTTA EPSSSLTSSI 

       550        560        570        580        590        600 
PASCHQRSKS DPSQLIQSLT PHSCHRTGNV SPSGCLSQAA RTPGDRAGTS KCRKAGCMYF 

       610        620        630        640        650        660 
GTPENKGFCT LCFIEYRENK QSVTASEKAG SPAPRFQNNV PCLGRECGTL GSTMFEGYCQ 

       670        680        690        700        710        720 
KCFIEAQNQR FHEARRTEEQ LRSSQHRDMP RTTQVASRLK CARASCKNIL ACRSEELCME 

       730        740        750        760        770 
CQHLSQRVGS VAHRGEPTPE EPPKQRCRAP ACDHFGNAKC NGYCNECYQF KQMYG 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Erratum
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. 6:114-114(2005)
[7]"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.
[8]"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.
[9]"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.
[10]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U19463 mRNA. Translation: AAC52153.1.
AK151921 mRNA. Translation: BAE30799.1.
PIRI49237.
RefSeqNP_033423.3. NM_009397.3.
XP_006512765.1. XM_006512702.1.
UniGeneMm.116683.

3D structure databases

ProteinModelPortalQ60769.
SMRQ60769. Positions 3-362, 382-419, 468-495, 588-620, 641-666, 743-775.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204243. 14 interactions.
DIPDIP-41120N.
IntActQ60769. 6 interactions.
MINTMINT-97373.
STRING10090.ENSMUSP00000101167.

Protein family/group databases

MEROPSC64.003.

PTM databases

PhosphoSiteQ60769.

Proteomic databases

PRIDEQ60769.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000019997; ENSMUSP00000019997; ENSMUSG00000019850.
ENSMUST00000105527; ENSMUSP00000101167; ENSMUSG00000019850.
GeneID21929.
KEGGmmu:21929.
UCSCuc007ena.3. mouse.

Organism-specific databases

CTD7128.
MGIMGI:1196377. Tnfaip3.

Phylogenomic databases

eggNOGNOG248343.
GeneTreeENSGT00530000062989.
HOGENOMHOG000133004.
HOVERGENHBG059260.
InParanoidQ3U968.
KOK11859.
OMACETPNCP.
OrthoDBEOG7JHM57.
TreeFamTF323312.

Gene expression databases

ArrayExpressQ60769.
BgeeQ60769.
CleanExMM_TNFAIP3.
GenevestigatorQ60769.

Family and domain databases

InterProIPR003323. OTU.
IPR002653. Znf_A20.
[Graphical view]
PfamPF02338. OTU. 1 hit.
PF01754. zf-A20. 6 hits.
[Graphical view]
SMARTSM00259. ZnF_A20. 7 hits.
[Graphical view]
PROSITEPS50802. OTU. 1 hit.
PS51036. ZF_A20. 7 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio301520.
PROQ60769.
SOURCESearch...

Entry information

Entry nameTNAP3_MOUSE
AccessionPrimary (citable) accession number: Q60769
Secondary accession number(s): Q3U968
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot