Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q13148 (TADBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
TAR DNA-binding protein 43

Short name=TDP-43
Gene names
Name:TARDBP
Synonyms:TDP43
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length414 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.12

Subunit structure

Homodimer. Interacts with BRDT By similarity. Binds specifically to pyrimidine-rich motifs of TAR DNA and to single stranded TG repeated sequences. Binds to RNA, specifically to UG repeated sequences with a minimun of six contiguous repeats. Interacts with ATNX2; the interaction is RNA-dependent. Ref.16

Subcellular location

Nucleus. Note: In patients with frontotemporal lobar degeneration and amyotrophic lateral sclerosis, it is absent from the nucleus of affected neurons but it is the primary component of cytoplasmic ubiquitin-positive inclusion bodies. Ref.2 Ref.11

Tissue specificity

Ubiquitously expressed. In particular, expression is high in pancreas, placenta, lung, genital tract and spleen.

Domain

The RRM domains can bind to both DNA and RNA By similarity.

Post-translational modification

Hyperphosphorylated in hippocampus, neocortex, and spinal cord from individuals affected with ALS and FTLDU. Ref.11

Ubiquitinated in hippocampus, neocortex, and spinal cord from individuals affected with ALS and FTLDU. Ref.2 Ref.11

Cleaved to generate C-terminal fragments in hippocampus, neocortex, and spinal cord from individuals affected with ALS and FTLDU.

Involvement in disease

Amyotrophic lateral sclerosis 10 (ALS10) [MIM:612069]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32

Sequence similarities

Contains 2 RRM (RNA recognition motif) domains.

Sequence caution

The sequence ABO32290.1 differs from that shown. Reason: Probable cloning artifact.

The sequence ABO32292.1 differs from that shown. Reason: Probable cloning artifact.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DiseaseAmyotrophic lateral sclerosis
Disease mutation
Neurodegeneration
   DomainRepeat
   LigandDNA-binding
RNA-binding
   Molecular functionRepressor
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process3'-UTR-mediated mRNA stabilization

Inferred from direct assay Ref.2. Source: BHF-UCL

RNA splicing

Inferred from direct assay Ref.12. Source: BHF-UCL

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation by host of viral transcription

Inferred from direct assay Ref.1. Source: BHF-UCL

transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentnucleus

Inferred from direct assay Ref.12Ref.2. Source: BHF-UCL

   Molecular_functionRNA binding

Inferred from direct assay Ref.12. Source: BHF-UCL

double-stranded DNA binding

Inferred from direct assay Ref.1. Source: BHF-UCL

identical protein binding

Inferred from physical interaction PubMed 22193716PubMed 23384725. Source: IntAct

mRNA 3'-UTR binding

Inferred from direct assay Ref.2. Source: BHF-UCL

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.16. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself15EBI-372899,EBI-372899
IRAK2O431872EBI-372899,EBI-447733

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 414414TAR DNA-binding protein 43
PRO_0000081972

Regions

Domain104 – 20097RRM 1
Domain191 – 26272RRM 2
Compositional bias274 – 413140Gly-rich

Amino acid modifications

Modified residue2921Phosphoserine Ref.15

Natural variations

Natural variant901A → V. Ref.24 Ref.25 Ref.32
Corresponds to variant rs80356715 [ dbSNP | Ensembl ].
VAR_045656
Natural variant1691D → G in ALS10. Ref.24
Corresponds to variant rs80356717 [ dbSNP | Ensembl ].
VAR_045657
Natural variant2671N → S in ALS10; also in a patient with frontotemporal dementia. Ref.27 Ref.28
Corresponds to variant rs80356718 [ dbSNP | Ensembl ].
VAR_058611
Natural variant2871G → S in ALS10. Ref.24 Ref.27
Corresponds to variant rs80356719 [ dbSNP | Ensembl ].
VAR_045658
Natural variant2901G → A in ALS10. Ref.23
Corresponds to variant rs121908395 [ dbSNP | Ensembl ].
VAR_045659
Natural variant2941G → A in ALS10. Ref.25 Ref.29
Corresponds to variant rs80356721 [ dbSNP | Ensembl ].
VAR_045660
Natural variant2941G → V in ALS10; a patient with bulbar signs and dementia. Ref.27
VAR_058612
Natural variant2951G → R in ALS10. Ref.27
Corresponds to variant rs80356723 [ dbSNP | Ensembl ].
VAR_058613
Natural variant2951G → S in ALS10; also in patients with frontotemporal lobar degeneration with motor neuron disease. Ref.26 Ref.27
Corresponds to variant rs80356723 [ dbSNP | Ensembl ].
VAR_058614
Natural variant2981G → S in ALS10. Ref.23
Corresponds to variant rs4884357 [ dbSNP | Ensembl ].
VAR_045661
Natural variant3151A → T in ALS10. Ref.21 Ref.24
Corresponds to variant rs80356726 [ dbSNP | Ensembl ].
VAR_045662
Natural variant3311Q → K in ALS10; impedes the development of normal limb and tail buds and increases the number of apoptotic nuclei when expressed in chick embryos; does not affect the interaction with ATNX2. Ref.16 Ref.25
Corresponds to variant rs80356727 [ dbSNP | Ensembl ].
VAR_045663
Natural variant3321S → N in ALS10. Ref.27
Corresponds to variant rs80356728 [ dbSNP | Ensembl ].
VAR_058615
Natural variant3351G → D in ALS10. Ref.27
Corresponds to variant rs80356729 [ dbSNP | Ensembl ].
VAR_058616
Natural variant3371M → V in ALS10; impedes the development of normal limb and tail buds and increases the number of apoptotic nuclei when expressed in chick embryos. Ref.25 Ref.27
Corresponds to variant rs80356730 [ dbSNP | Ensembl ].
VAR_045664
Natural variant3431Q → R in ALS10. Ref.22
Corresponds to variant rs80356731 [ dbSNP | Ensembl ].
VAR_062767
Natural variant3481G → C in ALS10. Ref.24
Corresponds to variant rs80356733 [ dbSNP | Ensembl ].
VAR_045665
Natural variant3571G → R in ALS10. Ref.32
VAR_067499
Natural variant3611R → S in ALS10. Ref.24
Corresponds to variant rs80356735 [ dbSNP | Ensembl ].
VAR_045666
Natural variant3611R → T in ALS10. Ref.32
VAR_067500
Natural variant3791S → C in ALS10. Ref.27
Corresponds to variant rs80356739 [ dbSNP | Ensembl ].
VAR_058617
Natural variant3791S → P in ALS10. Ref.27 Ref.32
Corresponds to variant rs80356738 [ dbSNP | Ensembl ].
VAR_058618
Natural variant3821A → T in ALS10. Ref.24 Ref.27 Ref.30 Ref.31
Corresponds to variant rs11689432 [ dbSNP | Ensembl ].
VAR_045667
Natural variant3901N → D in ALS10. Ref.24
Corresponds to variant rs80356741 [ dbSNP | Ensembl ].
VAR_045668
Natural variant3901N → S in ALS10. Ref.24
Corresponds to variant rs80356742 [ dbSNP | Ensembl ].
VAR_045669
Natural variant3931S → L in ALS10. Ref.27
Corresponds to variant rs80356743 [ dbSNP | Ensembl ].
VAR_058619

Experimental info

Mutagenesis106 – 17570Missing: Completely abolishes RNA binding.
Mutagenesis106 – 1116LIVLGL → DIDLGD: Completely abolishes RNA binding.
Mutagenesis106 – 1116Missing: Completely abolishes RNA binding.
Mutagenesis147 – 1493FGF → LGL: Highly reduces binding to RNA and DNA.
Mutagenesis193 – 25765Missing: Alters but does not abolish RNA binding.
Sequence conflict2001E → G in BAD96474. Ref.5
Sequence conflict2781G → V in BAG35326. Ref.3

Secondary structure

..................................... 414
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13148 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 8E09A1206FB4EF4A

FASTA41444,740
        10         20         30         40         50         60 
MSEYIRVTED ENDEPIEIPS EDDGTVLLST VTAQFPGACG LRYRNPVSQC MRGVRLVEGI 

        70         80         90        100        110        120 
LHAPDAGWGN LVYVVNYPKD NKRKMDETDA SSAVKVKRAV QKTSDLIVLG LPWKTTEQDL 

       130        140        150        160        170        180 
KEYFSTFGEV LMVQVKKDLK TGHSKGFGFV RFTEYETQVK VMSQRHMIDG RWCDCKLPNS 

       190        200        210        220        230        240 
KQSQDEPLRS RKVFVGRCTE DMTEDELREF FSQYGDVMDV FIPKPFRAFA FVTFADDQIA 

       250        260        270        280        290        300 
QSLCGEDLII KGISVHISNA EPKHNSNRQL ERSGRFGGNP GGFGNQGGFG NSRGGGAGLG 

       310        320        330        340        350        360 
NNQGSNMGGG MNFGAFSINP AMMAAAQAAL QSSWGMMGML ASQQNQSGPS GNNQNQGNMQ 

       370        380        390        400        410 
REPNQAFGSG NNSYSGSNSG AAIGWGSASN AGSGSGFNGG FGSSMDSKSS GWGM 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs."
Ou S.-H.I., Wu F., Harrich D., Garcia-Martinez L.F., Gaynor R.B.
J. Virol. 69:3584-3596(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
Tissue: Cervix carcinoma.
[2]"TDP43 is a human low molecular weight neurofilament (hNFL) mRNA-binding protein."
Strong M.J., Volkening K., Hammond R., Yang W., Strong W., Leystra-Lantz C., Shoesmith C.
Mol. Cell. Neurosci. 35:320-327(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[7]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lymph and Testis.
[10]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 122-136 AND 276-293, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[11]"Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis."
Neumann M., Sampathu D.M., Kwong L.K., Truax A.C., Micsenyi M.C., Chou T.T., Bruce J., Schuck T., Grossman M., Clark C.M., McCluskey L.F., Miller B.L., Masliah E., Mackenzie I.R., Feldman H., Feiden W., Kretzschmar H.A., Trojanowski J.Q., Lee V.M.-Y.
Science 314:130-133(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 252-263; 276-293 AND 409-414, SUBCELLULAR LOCATION, PHOSPHORYLATION, UBIQUITINATION.
[12]"Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping."
Buratti E., Doerk T., Zuccato E., Pagani F., Romano M., Baralle F.E.
EMBO J. 20:1774-1784(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9."
Buratti E., Baralle F.E.
J. Biol. Chem. 276:36337-36343(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING, MUTAGENESIS.
[14]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS."
Elden A.C., Kim H.J., Hart M.P., Chen-Plotkin A.S., Johnson B.S., Fang X., Armakola M., Geser F., Greene R., Lu M.M., Padmanabhan A., Clay-Falcone D., McCluskey L., Elman L., Juhr D., Gruber P.J., Rub U., Auburger G. expand/collapse author list , Trojanowski J.Q., Lee V.M., Van Deerlin V.M., Bonini N.M., Gitler A.D.
Nature 466:1069-1075(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATNX2, CHARACTERIZATION OF VARIANT ALS10 LYS-331.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Solution structure of the RNA binding domains of TAR DNA-binding protein-43."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 96-267.
[20]"Solution structure of RRM domain in tar DNA-binding protein-43."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2009) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 193-267.
[21]"TDP-43 A315T mutation in familial motor neuron disease."
Gitcho M.A., Baloh R.H., Chakraverty S., Mayo K., Norton J.B., Levitch D., Hatanpaa K.J., White C.L. III, Bigio E.H., Caselli R., Baker M., Al-Lozi M.T., Morris J.C., Pestronk A., Rademakers R., Goate A.M., Cairns N.J.
Ann. Neurol. 63:535-538(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALS10 THR-315.
[22]"TDP-43 mutation in familial amyotrophic lateral sclerosis."
Yokoseki A., Shiga A., Tan C.F., Tagawa A., Kaneko H., Koyama A., Eguchi H., Tsujino A., Ikeuchi T., Kakita A., Okamoto K., Nishizawa M., Takahashi H., Onodera O.
Ann. Neurol. 63:538-542(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALS10 ARG-343.
[23]"TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis."
Van Deerlin V.M., Leverenz J.B., Bekris L.M., Bird T.D., Yuan W., Elman L.B., Clay D., Wood E.M., Chen-Plotkin A.S., Martinez-Lage M., Steinbart E., McCluskey L., Grossman M., Neumann M., Wu I.-L., Yang W.-S., Kalb R., Galasko D.R. expand/collapse author list , Montine T.J., Trojanowski J.Q., Lee V.M.-Y., Schellenberg G.D., Yu C.-E.
Lancet Neurol. 7:409-416(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALS10 ALA-290 AND SER-298.
[24]"TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis."
Kabashi E., Valdmanis P.N., Dion P., Spiegelman D., McConkey B.J., Vande Velde C., Bouchard J.-P., Lacomblez L., Pochigaeva K., Salachas F., Pradat P.-F., Camu W., Meininger V., Dupre N., Rouleau G.A.
Nat. Genet. 40:572-574(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALS10 GLY-169; SER-287; THR-315; CYS-348; SER-361; THR-382; ASP-390 AND SER-390, VARIANT VAL-90.
[25]"TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis."
Sreedharan J., Blair I.P., Tripathi V.B., Hu X., Vance C., Rogelj B., Ackerley S., Durnall J.C., Williams K.L., Buratti E., Baralle F., de Belleroche J., Mitchell J.D., Leigh P.N., Al-Chalabi A., Miller C.C., Nicholson G., Shaw C.E.
Science 319:1668-1672(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALS10 ALA-294; LYS-331 AND VAL-337, VARIANT VAL-90, CHARACTERIZATION OF VARIANTS ALS10 LYS-331 AND VAL-337.
[26]"TARDBP mutations in motoneuron disease with frontotemporal lobar degeneration."
French clinical and genetic research network on frontotemporal lobar degeneration/frontotemporal lobar degeneration with motoneuron disease
Benajiba L., Le Ber I., Camuzat A., Lacoste M., Thomas-Anterion C., Couratier P., Legallic S., Salachas F., Hannequin D., Decousus M., Lacomblez L., Guedj E., Golfier V., Camu W., Dubois B., Campion D., Meininger V., Brice A.
Ann. Neurol. 65:470-473(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT OF VARIANT ALS10 SER-295 IN FRONTOTEMPORAL LOBAR DEGENERATION WITH MOTOR NEURON DISEASE.
[27]"High frequency of TARDBP gene mutations in Italian patients with amyotrophic lateral sclerosis."
Corrado L., Ratti A., Gellera C., Buratti E., Castellotti B., Carlomagno Y., Ticozzi N., Mazzini L., Testa L., Taroni F., Baralle F.E., Silani V., D'Alfonso S.
Hum. Mutat. 30:688-694(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALS10 SER-267; SER-287; VAL-294; SER-295; ARG-295; ASN-332; ASP-335; VAL-337; PRO-379; CYS-379; THR-382 AND LEU-393.
[28]"Mutation within TARDBP leads to frontotemporal dementia without motor neuron disease."
Borroni B., Bonvicini C., Alberici A., Buratti E., Agosti C., Archetti S., Papetti A., Stuani C., Di Luca M., Gennarelli M., Padovani A.
Hum. Mutat. 30:E974-E983(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT OF VARIANT ALS10 SER-267 IN FRONTOTEMPORAL DEMENTIA.
[29]"Genetic variants in the promoter of TARDBP in sporadic amyotrophic lateral sclerosis."
Luquin N., Yu B., Saunderson R.B., Trent R.J., Pamphlett R.
Neuromuscul. Disord. 19:696-700(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALS10 ALA-294.
[30]"Large proportion of amyotrophic lateral sclerosis cases in Sardinia due to a single founder mutation of the TARDBP gene."
Chio A., Borghero G., Pugliatti M., Ticca A., Calvo A., Moglia C., Mutani R., Brunetti M., Ossola I., Marrosu M.G., Murru M.R., Floris G., Cannas A., Parish L.D., Cossu P., Abramzon Y., Johnson J.O., Nalls M.A. expand/collapse author list , Arepalli S., Chong S., Hernandez D.G., Traynor B.J., Restagno G.
Arch. Neurol. 68:594-598(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALS10 THR-382.
[31]"High frequency of the TARDBP p.Ala382Thr mutation in Sardinian patients with amyotrophic lateral sclerosis."
Orru S., Manolakos E., Orru N., Kokotas H., Mascia V., Carcassi C., Petersen M.B.
Clin. Genet. 81:172-178(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALS10 THR-382.
[32]"Novel TARDBP mutations in Nordic ALS patients."
Chiang H.H., Andersen P.M., Tysnes O.B., Gredal O., Christensen P.B., Graff C.
J. Hum. Genet. 57:316-319(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-90, VARIANTS ALS10 ARG-357; THR-361 AND PRO-379.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U23731 mRNA. Translation: AAA70033.1.
EF434181 mRNA. Translation: ABO32290.1. Sequence problems.
EF434182 mRNA. Translation: ABO32291.1.
EF434183 mRNA. Translation: ABO32292.1. Sequence problems.
AK312416 mRNA. Translation: BAG35326.1.
CR533534 mRNA. Translation: CAG38565.1.
AK222754 mRNA. Translation: BAD96474.1.
AL050265 mRNA. Translation: CAB43367.1.
AL109811 Genomic DNA. Translation: CAI22098.1.
CH471130 Genomic DNA. Translation: EAW71670.1.
BC071657 mRNA. Translation: AAH71657.1.
BC095435 mRNA. Translation: AAH95435.1.
CCDSCCDS122.1.
PIRI38977.
RefSeqNP_031401.1. NM_007375.3.
UniGeneHs.300624.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WF0NMR-A193-267[»]
2CQGNMR-A96-185[»]
4BS2NMR-A102-269[»]
4IUFX-ray2.75A103-179[»]
ProteinModelPortalQ13148.
SMRQ13148. Positions 67-269.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117003. 278 interactions.
DIPDIP-31167N.
IntActQ13148. 23 interactions.
MINTMINT-5002768.
STRING9606.ENSP00000240185.

Chemistry

ChEMBLCHEMBL2362981.

PTM databases

PhosphoSiteQ13148.

Polymorphism databases

DMDM20140568.

Proteomic databases

MaxQBQ13148.
PaxDbQ13148.
PRIDEQ13148.

Protocols and materials databases

DNASU23435.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000240185; ENSP00000240185; ENSG00000120948.
GeneID23435.
KEGGhsa:23435.
UCSCuc001art.3. human.

Organism-specific databases

CTD23435.
GeneCardsGC01P011006.
GeneReviewsTARDBP.
HGNCHGNC:11571. TARDBP.
HPACAB003703.
HPA017284.
MIM605078. gene.
612069. phenotype.
neXtProtNX_Q13148.
Orphanet803. Amyotrophic lateral sclerosis.
275872. Frontotemporal dementia with motor neuron disease.
PharmGKBPA36336.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOVERGENHBG058671.
InParanoidQ13148.
OMAKHNSSRQ.
PhylomeDBQ13148.
TreeFamTF315657.

Gene expression databases

ArrayExpressQ13148.
BgeeQ13148.
CleanExHS_TARDBP.
GenevestigatorQ13148.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTARDBP. human.
EvolutionaryTraceQ13148.
GeneWikiTARDBP.
GenomeRNAi23435.
NextBio45695.
PROQ13148.
SOURCESearch...

Entry information

Entry nameTADBP_HUMAN
AccessionPrimary (citable) accession number: Q13148
Secondary accession number(s): A4GUK4 expand/collapse secondary AC list , A4GUK5, A4GUK6, B2R629, E2PU12, Q53H27, Q6FI92, Q96DJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM