TADBP_MOUSE - dbPTM
TADBP_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TADBP_MOUSE
UniProt AC Q921F2
Protein Name TAR DNA-binding protein 43
Gene Name Tardbp
Organism Mus musculus (Mouse).
Sequence Length 414
Subcellular Localization Nucleus .
Protein Description DNA and RNA-binding protein which regulates transcription and splicing. Involved in the regulation of CFTR splicing. It promotes CFTR exon 9 skipping by binding to the UG repeated motifs in the polymorphic region near the 3'-splice site of this exon. The resulting aberrant splicing is associated with pathological features typical of cystic fibrosis. May also be involved in microRNA biogenesis, apoptosis and cell division. Can repress HIV-1 transcription by binding to the HIV-1 long terminal repeat. Stabilizes the low molecular weight neurofilament (NFL) mRNA through a direct interaction with the 3' UTR..
Protein Sequence MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAVQKTSDLIVLGLPWKTTEQDLKDYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSPDEPLRSRKVFVGRCTEDMTAEELQQFFCQYGEVVDVFIPKPFRAFAFVTFADDKVAQSLCGEDLIIKGISVHISNAEPKHNSNRQLERSGRFGGNPGGFGNQGGFGNSRGGGAGLGNNQGGNMGGGMNFGAFSINPAMMAAAQAALQSSWGMMGMLASQQNQSGPSGNNQSQGSMQREPNQAFGSGNNSYSGSNSGAPLGWGSASNAGSGSGFNGGFGSSMDSKSSGWGM
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
39GlutathionylationTAQFPGACGLRYRNP
EECCCCCCCCEECCH
6.9924333276
50GlutathionylationYRNPVSQCMRGVRLV
ECCHHHHHHHHHEEE
1.2424333276
50S-palmitoylationYRNPVSQCMRGVRLV
ECCHHHHHHHHHEEE
1.2428526873
88PhosphorylationNKRKMDETDASSAVK
CCCCCCCCCHHHHHH
32.3829550500
91PhosphorylationKMDETDASSAVKVKR
CCCCCCHHHHHHHHH
22.9528066266
92PhosphorylationMDETDASSAVKVKRA
CCCCCHHHHHHHHHH
38.5125266776
95UbiquitinationTDASSAVKVKRAVQK
CCHHHHHHHHHHHHH
41.58-
102UbiquitinationKVKRAVQKTSDLIVL
HHHHHHHHCCCEEEE
43.32-
103PhosphorylationVKRAVQKTSDLIVLG
HHHHHHHCCCEEEEC
15.4721454597
104PhosphorylationKRAVQKTSDLIVLGL
HHHHHHCCCEEEECC
37.1421454597
114UbiquitinationIVLGLPWKTTEQDLK
EEECCCCCCCHHHHH
43.56-
114AcetylationIVLGLPWKTTEQDLK
EEECCCCCCCHHHHH
43.568277349
121AcetylationKTTEQDLKDYFSTFG
CCCHHHHHHHHHHHC
59.688277361
137AcetylationVLMVQVKKDLKTGHS
EEEEEEECCCCCCCC
70.238277373
144PhosphorylationKDLKTGHSKGFGFVR
CCCCCCCCCCCCEEE
35.5028285833
155PhosphorylationGFVRFTEYETQVKVM
CEEEEEEEEEHHHEE
22.6325177544
160UbiquitinationTEYETQVKVMSQRHM
EEEEEHHHEEECCCC
23.54-
173S-nitrosocysteineHMIDGRWCDCKLPNS
CCCCCCCCCCCCCCC
4.19-
173S-nitrosylationHMIDGRWCDCKLPNS
CCCCCCCCCCCCCCC
4.1920925432
173GlutathionylationHMIDGRWCDCKLPNS
CCCCCCCCCCCCCCC
4.1924333276
175GlutathionylationIDGRWCDCKLPNSKQ
CCCCCCCCCCCCCCC
4.4024333276
176UbiquitinationDGRWCDCKLPNSKQS
CCCCCCCCCCCCCCC
54.45-
180PhosphorylationCDCKLPNSKQSPDEP
CCCCCCCCCCCCCCC
30.0826239621
181MalonylationDCKLPNSKQSPDEPL
CCCCCCCCCCCCCCH
62.5326320211
181UbiquitinationDCKLPNSKQSPDEPL
CCCCCCCCCCCCCCH
62.53-
183PhosphorylationKLPNSKQSPDEPLRS
CCCCCCCCCCCCHHC
37.7525521595
238UbiquitinationFVTFADDKVAQSLCG
EEEECCHHHHHHHHC
39.76-
242PhosphorylationADDKVAQSLCGEDLI
CCHHHHHHHHCCCEE
18.8526370283
244GlutathionylationDKVAQSLCGEDLIIK
HHHHHHHHCCCEEEE
7.3124333276
244S-palmitoylationDKVAQSLCGEDLIIK
HHHHHHHHCCCEEEE
7.3128526873
266PhosphorylationNAEPKHNSNRQLERS
CCCCCCCCCCCHHHC
32.8622817900
273PhosphorylationSNRQLERSGRFGGNP
CCCCHHHCCCCCCCC
25.5826745281
292PhosphorylationNQGGFGNSRGGGAGL
CCCCCCCCCCCCCCC
32.4523684622
293MethylationQGGFGNSRGGGAGLG
CCCCCCCCCCCCCCC
52.3424129315
379PhosphorylationNSYSGSNSGAPLGWG
CCCCCCCCCCCCCCC
37.7222802335
387PhosphorylationGAPLGWGSASNAGSG
CCCCCCCCCCCCCCC
23.2422802335
389PhosphorylationPLGWGSASNAGSGSG
CCCCCCCCCCCCCCC
28.9822802335
393PhosphorylationGSASNAGSGSGFNGG
CCCCCCCCCCCCCCC
27.6322802335
395PhosphorylationASNAGSGSGFNGGFG
CCCCCCCCCCCCCCC
41.7422802335
403PhosphorylationGFNGGFGSSMDSKSS
CCCCCCCCCCCCCCC
21.8922802335
404PhosphorylationFNGGFGSSMDSKSSG
CCCCCCCCCCCCCCC
27.30-
409PhosphorylationGSSMDSKSSGWGM--
CCCCCCCCCCCCC--
37.73-
410PhosphorylationSSMDSKSSGWGM---
CCCCCCCCCCCC---
42.15-

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 TADBP_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TADBP_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 TADBP_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TADBP_MOUSETardbpphysical
20211142
NACC1_MOUSENacc1physical
23022214
RBBP5_HUMANRBBP5physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TADBP_MOUSE

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Related Literatures of Post-Translational Modification

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