Q9D2N4 · DTNA_MOUSE

  • Protein
    Dystrobrevin alpha
  • Gene
    Dtna
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Involved in synapse maturation and required for normal muscle function.

Features

Showing features for binding site.

1746100200300400500600700
TypeIDPosition(s)Description
Binding site243Zn2+ 1 (UniProtKB | ChEBI)
Binding site246Zn2+ 1 (UniProtKB | ChEBI)
Binding site258Zn2+ 2 (UniProtKB | ChEBI)
Binding site261Zn2+ 2 (UniProtKB | ChEBI)
Binding site267Zn2+ 1 (UniProtKB | ChEBI)
Binding site270Zn2+ 1 (UniProtKB | ChEBI)
Binding site280Zn2+ 2 (UniProtKB | ChEBI)
Binding site284Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentaxon
Cellular Componentcell projection
Cellular Componentcytoplasm
Cellular Componentdystrobrevin complex
Cellular Componentextrinsic component of cytoplasmic side of plasma membrane
Cellular Componentplasma membrane
Cellular Componentprotein-containing complex
Cellular Componentsarcolemma
Cellular Componentsynapse
Molecular FunctionPDZ domain binding
Molecular Functionphosphatase binding
Molecular Functionzinc ion binding
Biological Processsynaptic signaling

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Dystrobrevin alpha
  • Short names
    DTN-A
  • Alternative names
    • Alpha-dystrobrevin

Gene names

    • Name
      Dtna
    • Synonyms
      Dtn

Organism names

  • Taxonomic identifier
  • Strains
    • 129/Sv
    • C3H/HeJ
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9D2N4
  • Secondary accessions
    • P97319
    • Q61498
    • Q61499
    • Q9QZZ5
    • Q9WUL9
    • Q9WUM0

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000800371-746Dystrobrevin alpha
Modified residue666Phosphoserine

Post-translational modification

Phosphorylation of isoform 2 on tyrosine kinase substrate domain present in the C-terminus.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in skeletal muscle, heart, lung and brain. Sarcolemma and neuromuscular junction in skeletal muscle. Isoform 2 is restricted to the neuromuscular junction. Isoforms 5 and 6 are only expressed in muscle.

Developmental stage

Expression of alpha-dystrobrevin is up-regulated during differentiation, with isoforms 2, 5 and 6 expressed earliest and isoform 3 and 4 expressed later.

Gene expression databases

Interaction

Subunit

Interacts with dystrophin, utrophin and the syntrophins SNTA1, SNTB1, SNTB2, SNTG1 and SNTG2. Isoforms 5 and 6 do not interact with syntrophin. Isoforms 3 and 4 do not interact with utrophin. Binds dystrobrevin binding protein 1. Interacts with MAGEE1.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9D2N4Dtnbp1 Q91WZ83EBI-296019, EBI-643186

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, zinc finger, coiled coil, compositional bias.

TypeIDPosition(s)Description
Region1-288Interaction with MAGEE1
Zinc finger238-294ZZ-type
Region397-447Syntrophin-binding region
Coiled coil458-557
Region555-577Disordered
Compositional bias557-574Polar residues
Region646-667Disordered
Region684-721Disordered

Domain

The coiled coil domain mediates the interaction with dystrophin and utrophin.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (7)
  • Sequence status
    Complete

This entry describes 7 isoforms produced by Alternative splicing. Additional isoforms seem to exist.

Q9D2N4-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    746
  • Mass (Da)
    84,067
  • Last updated
    2011-02-08 v2
  • Checksum
    6AB7EF3B69250A09
MIEDSGKRGNTMAERRQLFAEMRAQDLDRIRLSTYRTACKLRFVQKKCNLHLVDIWNVIEALRENALNNLDPNIELNVARLEAVLSTIFYQLNKRMPTTHQIHVEQSISLLLNFLLAAFDPEGHGKISVFAVKMALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTLMSDPPPQCLVWLPLLHRLANVENVFHPVECSYCHSESMMGFRYRCQQCHNYQLCQDCFWRGHAGGSHSNQHQMKEYTSWKSPAKKLTNALSKSLSCASSREPLHPMFPDQPEKPLNLAHIVPPRPVTSMNDTLFSHSVPSSGSPFITRSSPPKDSEVEQNKMLARAAPAFLKGRGIQYSLNVADRLADEHVLIGLYVNMLRNDPPCMLESSNRLDEEHRLIARYAARLAAESSSSQPTQQRSAPDISFTIDANKQQRQLIAELENKNREILQEIQRLRVEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEELKQGTQGASSPRSSPSHTISRPIPMPIRSASACPTPTHTPQDSLTGVGGDVQEAFAQSSRRNLRSDLLVAADSITNTMSSLVKELNSEVASETESTVDSEFSRPQFEDLAPSPTSEKAFLAQIHSRKPGYIHGGAASTTHGDMVPEDGDPYTQPEDGNYENESVRQLENELQLEEYLKQKLQDEAYQVSLQG

Q9D2N4-2

  • Name
    2
  • Synonyms
    Alpha-dystrobrevin-1, Alpha-DB1
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q9D2N4-3

  • Name
    3
  • Synonyms
    Alpha-dystrobrevin-2B, Alpha-DB2B
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q9D2N4-4

  • Name
    4
  • Synonyms
    Alpha-dystrobrevin-2A, Alpha-DB2A
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q9D2N4-5

  • Name
    5
  • Synonyms
    Alpha-dystrobrevin-3, Alpha-DB3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q9D2N4-6

  • Name
    6
  • Synonyms
    Alpha-dystrobrevin-3, Alpha-DB3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q9D2N4-7

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1Y7VLZ6A0A1Y7VLZ6_MOUSEDtna73
A0A1Y7VL34A0A1Y7VL34_MOUSEDtna746
A0A1Y7VJN9A0A1Y7VJN9_MOUSEDtna567
A0A1Y7VK79A0A1Y7VK79_MOUSEDtna35
Q8CFR5Q8CFR5_MOUSEDtna682

Features

Showing features for sequence conflict, alternative sequence, compositional bias.

TypeIDPosition(s)Description
Sequence conflict241in Ref. 1; CAA64519
Sequence conflict251in Ref. 5; BAB31746
Sequence conflict259in Ref. 4; AAD33915
Alternative sequenceVSP_004214334in isoform 5 and isoform 7
Alternative sequenceVSP_004215363-419in isoform 2 and isoform 7
Alternative sequenceVSP_004216364-371in isoform 5 and isoform 6
Alternative sequenceVSP_004217372-746in isoform 5 and isoform 6
Sequence conflict416in Ref. 4; AAD33915/AAD33914
Compositional bias557-574Polar residues
Alternative sequenceVSP_004218559-567in isoform 4 and isoform 7
Alternative sequenceVSP_004221559-570in isoform 3
Alternative sequenceVSP_004220560-561in isoform 2
Alternative sequenceVSP_004219568-746in isoform 4 and isoform 7
Alternative sequenceVSP_004222571-746in isoform 3

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X95226
EMBL· GenBank· DDBJ
CAA64518.1
EMBL· GenBank· DDBJ
mRNA
X95227
EMBL· GenBank· DDBJ
CAA64519.1
EMBL· GenBank· DDBJ
mRNA
Z79787
EMBL· GenBank· DDBJ
CAB02145.1
EMBL· GenBank· DDBJ
Genomic DNA
Z79788
EMBL· GenBank· DDBJ
CAB02145.1
EMBL· GenBank· DDBJ
Genomic DNA
Z79789
EMBL· GenBank· DDBJ
CAB02145.1
EMBL· GenBank· DDBJ
Genomic DNA
Z79790
EMBL· GenBank· DDBJ
CAB02145.1
EMBL· GenBank· DDBJ
Genomic DNA
Z79791
EMBL· GenBank· DDBJ
CAB02145.1
EMBL· GenBank· DDBJ
Genomic DNA
Z79792
EMBL· GenBank· DDBJ
CAB02145.1
EMBL· GenBank· DDBJ
Genomic DNA
Z79793
EMBL· GenBank· DDBJ
CAB02145.1
EMBL· GenBank· DDBJ
Genomic DNA
Z79794
EMBL· GenBank· DDBJ
CAB02145.1
EMBL· GenBank· DDBJ
Genomic DNA
Z79795
EMBL· GenBank· DDBJ
CAB02145.1
EMBL· GenBank· DDBJ
Genomic DNA
Z79796
EMBL· GenBank· DDBJ
CAB02145.1
EMBL· GenBank· DDBJ
Genomic DNA
Z79797
EMBL· GenBank· DDBJ
CAB02145.1
EMBL· GenBank· DDBJ
Genomic DNA
AJ009669
EMBL· GenBank· DDBJ
CAA08770.1
EMBL· GenBank· DDBJ
mRNA
AF143544
EMBL· GenBank· DDBJ
AAD33915.1
EMBL· GenBank· DDBJ
mRNA
AF143543
EMBL· GenBank· DDBJ
AAD33914.1
EMBL· GenBank· DDBJ
mRNA
AF143542
EMBL· GenBank· DDBJ
AAD33913.1
EMBL· GenBank· DDBJ
mRNA
AK019477
EMBL· GenBank· DDBJ
BAB31746.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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