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Q921F2 (TADBP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. 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·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 By similarity.

Subunit structure

Homodimer. 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 BRDT. Ref.4 Ref.5

Subcellular location

Nucleus By similarity.

Domain

The RRM domains can bind to both DNA and RNA.

Post-translational modification

Hyperphosphorylated By similarity.

Ubiquitinated By similarity.

Sequence similarities

Contains 2 RRM (RNA recognition motif) domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 414414TAR DNA-binding protein 43
PRO_0000081973

Regions

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

Amino acid modifications

Modified residue2921Phosphoserine By similarity

Experimental info

Sequence conflict81T → K in BAE32189. Ref.1
Sequence conflict961V → G in BAE32189. Ref.1
Sequence conflict2981G → C in BAE21557. Ref.1

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q921F2 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 2BE6A695EC2CA106

FASTA41444,548
        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 
KDYFSTFGEV LMVQVKKDLK TGHSKGFGFV RFTEYETQVK VMSQRHMIDG RWCDCKLPNS 

       190        200        210        220        230        240 
KQSPDEPLRS RKVFVGRCTE DMTAEELQQF FCQYGEVVDV FIPKPFRAFA FVTFADDKVA 

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

       310        320        330        340        350        360 
NNQGGNMGGG MNFGAFSINP AMMAAAQAAL QSSWGMMGML ASQQNQSGPS GNNQSQGSMQ 

       370        380        390        400        410 
REPNQAFGSG NNSYSGSNSG APLGWGSASN AGSGSGFNGG FGSSMDSKSS GWGM 

« Hide

References

« Hide 'large scale' references
[1]"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: Testis and Thymus.
[2]"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].
Strain: FVB/N.
Tissue: Mammary gland.
[3]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 276-293, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hippocampus.
[4]"The testis-specific double bromodomain-containing protein BRDT forms a complex with multiple spliceosome components and is required for mRNA splicing and 3'-UTR truncation in round spermatids."
Berkovits B.D., Wang L., Guarnieri P., Wolgemuth D.J.
Nucleic Acids Res. 40:7162-7175(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BRDT.
[5]"Structural insights into TDP-43 in nucleic-acid binding and domain interactions."
Kuo P.H., Doudeva L.G., Wang Y.T., Shen C.K., Yuan H.S.
Nucleic Acids Res. 37:1799-1808(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 192-265 IN COMPLEX WITH SINGLE-STRANDED DNA, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK133207 mRNA. Translation: BAE21557.1.
AK153803 mRNA. Translation: BAE32189.1.
BC012873 mRNA. Translation: AAH12873.1.
BC025544 mRNA. Translation: AAH25544.1.
BC027772 mRNA. Translation: AAH27772.1.
BC031126 mRNA. Translation: AAH31126.1.
BC033475 mRNA. Translation: AAH33475.1.
CCDSCCDS38971.1.
RefSeqNP_663531.1. NM_145556.4.
UniGeneMm.22453.
Mm.378962.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3D2WX-ray1.65A192-265[»]
ProteinModelPortalQ921F2.
SMRQ921F2. Positions 67-269.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid231054. 10 interactions.
IntActQ921F2. 3 interactions.
MINTMINT-4136792.
STRING10090.ENSMUSP00000081142.

PTM databases

PhosphoSiteQ921F2.

2D gel databases

REPRODUCTION-2DPAGEQ921F2.

Proteomic databases

MaxQBQ921F2.
PaxDbQ921F2.
PRIDEQ921F2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000084125; ENSMUSP00000081142; ENSMUSG00000041459.
GeneID230908.
KEGGmmu:230908.
UCSCuc008vvg.1. mouse.

Organism-specific databases

CTD23435.
MGIMGI:2387629. Tardbp.

Phylogenomic databases

eggNOGNOG145464.
GeneTreeENSGT00730000110584.
HOGENOMHOG000254792.
HOVERGENHBG058671.
InParanoidQ3V0E7.
OMAKHNSSRQ.
OrthoDBEOG7J70G1.
TreeFamTF315657.

Gene expression databases

ArrayExpressQ921F2.
BgeeQ921F2.
CleanExMM_TARDBP.
GenevestigatorQ921F2.

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

EvolutionaryTraceQ921F2.
NextBio380280.
PROQ921F2.
SOURCESearch...

Entry information

Entry nameTADBP_MOUSE
AccessionPrimary (citable) accession number: Q921F2
Secondary accession number(s): Q3U591, Q3V0E7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 110 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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