Details for: TARDBP

Gene ID: 23435

Symbol: TARDBP

Ensembl ID: ENSG00000120948

Description: TAR DNA binding protein

Associated with

Other Information

Genular Protein ID: 258416261

Symbol: TADBP_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 7745706

Title: Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs.

PubMed ID: 7745706

DOI: 10.1128/jvi.69.6.3584-3596.1995

PubMed ID: 17481916

Title: TDP43 is a human low molecular weight neurofilament (hNFL) mRNA-binding protein.

PubMed ID: 17481916

DOI: 10.1016/j.mcn.2007.03.007

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 17974005

Title: The full-ORF clone resource of the German cDNA consortium.

PubMed ID: 17974005

DOI: 10.1186/1471-2164-8-399

PubMed ID: 16710414

Title: The DNA sequence and biological annotation of human chromosome 1.

PubMed ID: 16710414

DOI: 10.1038/nature04727

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 17023659

Title: Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis.

PubMed ID: 17023659

DOI: 10.1126/science.1134108

PubMed ID: 11285240

Title: Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping.

PubMed ID: 11285240

DOI: 10.1093/emboj/20.7.1774

PubMed ID: 11470789

Title: Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9.

PubMed ID: 11470789

DOI: 10.1074/jbc.m104236200

PubMed ID: 18957508

Title: Structural determinants of the cellular localization and shuttling of TDP-43.

PubMed ID: 18957508

DOI: 10.1242/jcs.038950

PubMed ID: 19429692

Title: Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo.

PubMed ID: 19429692

DOI: 10.1093/nar/gkp342

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19765185

Title: TDP-43 is recruited to stress granules in conditions of oxidative insult.

PubMed ID: 19765185

DOI: 10.1111/j.1471-4159.2009.06383.x

PubMed ID: 20043239

Title: TDP-43 dimerizes in human cells in culture.

PubMed ID: 20043239

DOI: 10.1007/s10571-009-9489-9

PubMed ID: 20740007

Title: Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS.

PubMed ID: 20740007

DOI: 10.1038/nature09320

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21358640

Title: Characterizing the RNA targets and position-dependent splicing regulation by TDP-43.

PubMed ID: 21358640

DOI: 10.1038/nn.2778

PubMed ID: 23519609

Title: Characterizing TDP-43 interaction with its RNA targets.

PubMed ID: 23519609

DOI: 10.1093/nar/gkt189

PubMed ID: 23398327

Title: TDP-43 associates with stalled ribosomes and contributes to cell survival during cellular stress.

PubMed ID: 23398327

DOI: 10.1111/jnc.12194

PubMed ID: 23541532

Title: Ubiquilin-2 (UBQLN2) binds with high affinity to the C-terminal region of TDP-43 and modulates TDP-43 levels in H4 cells: characterization of inhibition by nucleic acids and 4-aminoquinolines.

PubMed ID: 23541532

DOI: 10.1016/j.bbapap.2013.03.020

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

DOI: 10.1074/mcp.o113.027870

PubMed ID: 24686783

Title: Mutations in the matrin 3 gene cause familial amyotrophic lateral sclerosis.

PubMed ID: 24686783

DOI: 10.1038/nn.3688

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 27123980

Title: USP7 and TDP-43: pleiotropic regulation of cryptochrome protein stability paces the oscillation of the mammalian circadian clock.

PubMed ID: 27123980

DOI: 10.1371/journal.pone.0154263

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 28794432

Title: TDP-43 stabilises the processing intermediates of mitochondrial transcripts.

PubMed ID: 28794432

DOI: 10.1038/s41598-017-06953-y

PubMed ID: 30520513

Title: TDP-43 accelerates deadenylation of target mRNAs by recruiting Caf1 deadenylase.

PubMed ID: 30520513

DOI: 10.1002/1873-3468.13310

PubMed ID: 30464263

Title: TDP-43 and RNA form amyloid-like myo-granules in regenerating muscle.

PubMed ID: 30464263

DOI: 10.1038/s41586-018-0665-2

PubMed ID: 24240615

Title: Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43.

PubMed ID: 24240615

DOI: 10.1038/nsmb.2698

PubMed ID: 24464995

Title: The crystal structure of TDP-43 RRM1-DNA complex reveals the specific recognition for UG- and TG-rich nucleic acids.

PubMed ID: 24464995

DOI: 10.1093/nar/gkt1407

PubMed ID: 28663553

Title: Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation.

PubMed ID: 28663553

DOI: 10.1038/s41467-017-00062-0

PubMed ID: 29438978

Title: A single N-terminal phosphomimic disrupts TDP-43 polymerization, phase separation, and RNA splicing.

PubMed ID: 29438978

DOI: 10.15252/embj.201797452

PubMed ID: 29531287

Title: Atomic-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2.

PubMed ID: 29531287

DOI: 10.1038/s41594-018-0045-5

PubMed ID: 18288693

Title: TDP-43 A315T mutation in familial motor neuron disease.

PubMed ID: 18288693

DOI: 10.1002/ana.21344

PubMed ID: 18438952

Title: TDP-43 mutation in familial amyotrophic lateral sclerosis.

PubMed ID: 18438952

DOI: 10.1002/ana.21392

PubMed ID: 18396105

Title: TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis.

PubMed ID: 18396105

DOI: 10.1016/s1474-4422(08)70071-1

PubMed ID: 18372902

Title: TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis.

PubMed ID: 18372902

DOI: 10.1038/ng.132

PubMed ID: 18309045

Title: TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis.

PubMed ID: 18309045

DOI: 10.1126/science.1154584

PubMed ID: 19350673

Title: TARDBP mutations in motoneuron disease with frontotemporal lobar degeneration.

PubMed ID: 19350673

DOI: 10.1002/ana.21612

PubMed ID: 19224587

Title: High frequency of TARDBP gene mutations in Italian patients with amyotrophic lateral sclerosis.

PubMed ID: 19224587

DOI: 10.1002/humu.20950

PubMed ID: 19655382

Title: Mutation within TARDBP leads to frontotemporal dementia without motor neuron disease.

PubMed ID: 19655382

DOI: 10.1002/humu.21100

PubMed ID: 19695877

Title: Genetic variants in the promoter of TARDBP in sporadic amyotrophic lateral sclerosis.

PubMed ID: 19695877

DOI: 10.1016/j.nmd.2009.07.005

PubMed ID: 19760257

Title: Broad clinical phenotypes associated with TAR-DNA binding protein (TARDBP) mutations in amyotrophic lateral sclerosis.

PubMed ID: 19760257

DOI: 10.1007/s10048-009-0218-9

PubMed ID: 21220647

Title: Large proportion of amyotrophic lateral sclerosis cases in Sardinia due to a single founder mutation of the TARDBP gene.

PubMed ID: 21220647

DOI: 10.1001/archneurol.2010.352

PubMed ID: 21418058

Title: High frequency of the TARDBP p.Ala382Thr mutation in Sardinian patients with amyotrophic lateral sclerosis.

PubMed ID: 21418058

DOI: 10.1111/j.1399-0004.2011.01668.x

PubMed ID: 22456481

Title: Novel TARDBP mutations in Nordic ALS patients.

PubMed ID: 22456481

DOI: 10.1038/jhg.2012.24

PubMed ID: 25678563

Title: Peptidylprolyl isomerase A governs TARDBP function and assembly in heterogeneous nuclear ribonucleoprotein complexes.

PubMed ID: 25678563

DOI: 10.1093/brain/awv005

PubMed ID: 33031745

Title: TDP-43 triggers mitochondrial DNA release via mPTP to activate cGAS/STING in ALS.

PubMed ID: 33031745

DOI: 10.1016/j.cell.2020.09.020

Sequence Information:

  • Length: 414
  • Mass: 44740
  • Checksum: 8E09A1206FB4EF4A
  • Sequence:
  • MSEYIRVTED ENDEPIEIPS EDDGTVLLST VTAQFPGACG LRYRNPVSQC MRGVRLVEGI 
    LHAPDAGWGN LVYVVNYPKD NKRKMDETDA SSAVKVKRAV QKTSDLIVLG LPWKTTEQDL 
    KEYFSTFGEV LMVQVKKDLK TGHSKGFGFV RFTEYETQVK VMSQRHMIDG RWCDCKLPNS 
    KQSQDEPLRS RKVFVGRCTE DMTEDELREF FSQYGDVMDV FIPKPFRAFA FVTFADDQIA 
    QSLCGEDLII KGISVHISNA EPKHNSNRQL ERSGRFGGNP GGFGNQGGFG NSRGGGAGLG 
    NNQGSNMGGG MNFGAFSINP AMMAAAQAAL QSSWGMMGML ASQQNQSGPS GNNQNQGNMQ 
    REPNQAFGSG NNSYSGSNSG AAIGWGSASN AGSGSGFNGG FGSSMDSKSS GWGM

Genular Protein ID: 3111144648

Symbol: Q9H256_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 11181995

Title: The sequence of the human genome.

PubMed ID: 11181995

DOI: 10.1126/science.1058040

Sequence Information:

  • Length: 54
  • Mass: 6433
  • Checksum: A833D9ACDA38BBDD
  • Sequence:
  • MACVNLHWEV MPSKKILIWG SGQNVDYFLM LCSKAYQLKR EYQHLPSLGF EKWN

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.