TNAP3_MOUSE - dbPTM
TNAP3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TNAP3_MOUSE
UniProt AC Q60769
Protein Name Tumor necrosis factor alpha-induced protein 3
Gene Name Tnfaip3
Organism Mus musculus (Mouse).
Sequence Length 775
Subcellular Localization Cytoplasm. Nucleus. Lysosome.
Protein Description 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..
Protein Sequence MAEQLLPQALYLSNMRKAVKIRERTPEDIFKPTNGIIYHFKTMHRYTLEMFRTCQFCPQFREIIHKALIDRSVQASLESQKKLNWCREVRKLVALKTNGDGNCLMHAACQYMWGVQDTDLVLRKALCSTLKETDTRNFKFRWQLESLKSQEFVETGLCYDTRNWNDEWDNLVKMASADTPAARSGLQYNSLEEIHIFVLSNILRRPIIVISDKMLRSLESGSNFAPLKVGGIYLPLHWPAQECYRYPIVLGYDSQHFVPLVTLKDSGPELRAVPLVNRDRGRFEDLKVHFLTDPENEMKEKLLKEYLIVMEIPVQGWDHGTTHLINAAKLDEANLPKEINLVDDYFELVQHEYKKWQENSDQARRAAHAQNPLEPSTPQLSLMDIKCETPNCPFFMSVNTQPLCHECSERRQKNQSKLPKLNSKLGPEGLPGVGLGSSNWSPEETAGGPHSAPPTAPSLFLFSETTAMKCRSPGCPFTLNVQHNGFCERCHARQINASHTADPGKCQACLQDVTRTFNGICSTCFKRTTAEPSSSLTSSIPASCHQRSKSDPSQLIQSLTPHSCHRTGNVSPSGCLSQAARTPGDRAGTSKCRKAGCMYFGTPENKGFCTLCFIEYRENKQSVTASEKAGSPAPRFQNNVPCLGRECGTLGSTMFEGYCQKCFIEAQNQRFHEARRTEEQLRSSQHRDMPRTTQVASRLKCARASCKNILACRSEELCMECQHLSQRVGSVAHRGEPTPEEPPKQRCRAPACDHFGNAKCNGYCNECYQFKQMYG
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAEQLLPQA
------CHHHHHHHH		17.16-
81UbiquitinationQASLESQKKLNWCRE
HHHHHHHHHHHHHHH		69.38-
220PhosphorylationKMLRSLESGSNFAPL
HHHHHCCCCCCCCCE		53.4628725479
222PhosphorylationLRSLESGSNFAPLKV
HHHCCCCCCCCCEEE		37.7522942356
376PhosphorylationAQNPLEPSTPQLSLM
HCCCCCCCCCCCEEE		43.2630635358
377PhosphorylationQNPLEPSTPQLSLMD
CCCCCCCCCCCEEEE		26.2730635358
381PhosphorylationEPSTPQLSLMDIKCE
CCCCCCCEEEEEEEC		19.1925266776
437PhosphorylationLPGVGLGSSNWSPEE
CCCCCCCCCCCCHHH		26.0726060331
438PhosphorylationPGVGLGSSNWSPEET
CCCCCCCCCCCHHHC		40.2926060331
441PhosphorylationGLGSSNWSPEETAGG
CCCCCCCCHHHCCCC		27.0426060331
445PhosphorylationSNWSPEETAGGPHSA
CCCCHHHCCCCCCCC		29.0126060331
451PhosphorylationETAGGPHSAPPTAPS
HCCCCCCCCCCCCCC		45.6726060331
455PhosphorylationGPHSAPPTAPSLFLF
CCCCCCCCCCCEEEE		50.5726060331
458PhosphorylationSAPPTAPSLFLFSET
CCCCCCCCEEEEECC		29.3226060331
498PhosphorylationHARQINASHTADPGK
EEEECCCCCCCCCCC		19.5122942356
500PhosphorylationRQINASHTADPGKCQ
EECCCCCCCCCCCHH		30.2022942356
522PhosphorylationRTFNGICSTCFKRTT
HHHCCHHHHHHHCCC		26.7022942356
523PhosphorylationTFNGICSTCFKRTTA
HHCCHHHHHHHCCCC		19.9722942356
528PhosphorylationCSTCFKRTTAEPSSS
HHHHHHCCCCCCCCC		30.8330635358
529PhosphorylationSTCFKRTTAEPSSSL
HHHHHCCCCCCCCCC		32.8122942356
533PhosphorylationKRTTAEPSSSLTSSI
HCCCCCCCCCCCCCC		24.8630635358
534PhosphorylationRTTAEPSSSLTSSIP
CCCCCCCCCCCCCCC		39.8322942356
535PhosphorylationTTAEPSSSLTSSIPA
CCCCCCCCCCCCCCH		39.7522942356
537PhosphorylationAEPSSSLTSSIPASC
CCCCCCCCCCCCHHH		23.5222942356
538PhosphorylationEPSSSLTSSIPASCH
CCCCCCCCCCCHHHH		31.4030635358
539PhosphorylationPSSSLTSSIPASCHQ
CCCCCCCCCCHHHHC		27.6230635358
543PhosphorylationLTSSIPASCHQRSKS
CCCCCCHHHHCCCCC		13.5330635358
548PhosphorylationPASCHQRSKSDPSQL
CHHHHCCCCCCHHHH		29.9127087446
550PhosphorylationSCHQRSKSDPSQLIQ
HHHCCCCCCHHHHHH		56.8727087446
553PhosphorylationQRSKSDPSQLIQSLT
CCCCCCHHHHHHHCC		42.4825266776
558PhosphorylationDPSQLIQSLTPHSCH
CHHHHHHHCCCCCCC		27.5028725479
563PhosphorylationIQSLTPHSCHRTGNV
HHHCCCCCCCCCCCC		16.9028725479
567PhosphorylationTPHSCHRTGNVSPSG
CCCCCCCCCCCCCCC		14.9425619855
571PhosphorylationCHRTGNVSPSGCLSQ
CCCCCCCCCCCHHHH		19.8325521595
573PhosphorylationRTGNVSPSGCLSQAA
CCCCCCCCCHHHHHC		34.3325619855
577PhosphorylationVSPSGCLSQAARTPG
CCCCCHHHHHCCCCC		23.1125619855
616PhosphorylationCTLCFIEYRENKQSV
EEEEEEEECCCCCCC		20.57-
622PhosphorylationEYRENKQSVTASEKA
EECCCCCCCCHHHHC		24.0528285833
628UbiquitinationQSVTASEKAGSPAPR
CCCCHHHHCCCCCCC		56.40-
631PhosphorylationTASEKAGSPAPRFQN
CHHHHCCCCCCCCCC		23.81-
683PhosphorylationRTEEQLRSSQHRDMP
HHHHHHHHHCCCCCC		42.8325266776
684PhosphorylationTEEQLRSSQHRDMPR
HHHHHHHHCCCCCCH		24.4630387612
707UbiquitinationKCARASCKNILACRS
HHHHHHCCHHHHHCC		44.52-
714PhosphorylationKNILACRSEELCMEC
CHHHHHCCHHHHHHH		34.9930387612
730PhosphorylationHLSQRVGSVAHRGEP
HHHHHHHHHHCCCCC		17.1825266776
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of TNAP3_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TNAP3_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TNAP3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SSBP2_MOUSESsbp2physical
20211142
SSBP3_MOUSESsbp3physical
20211142
MED16_MOUSEMed16physical
20211142
TRAF6_MOUSETraf6physical
17703191
TAXB1_MOUSETax1bp1physical
20185725
UB2D3_MOUSEUbe2d3physical
20185725
RIPK1_MOUSERipk1physical
21765415
TAXB1_MOUSETax1bp1physical
21765415
NEMO_MOUSEIkbkgphysical
24859449
UBC_MOUSEUbcphysical
23602765
RIPK1_MOUSERipk1physical
23602765
TNAP3_MOUSETnfaip3physical
23602765
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TNAP3_MOUSE

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Related Literatures of Post-Translational Modification

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