ID:SNTB1_HUMAN DESCRIPTION: RecName: Full=Beta-1-syntrophin; AltName: Full=59 kDa dystrophin-associated protein A1 basic component 1; Short=DAPA1B; AltName: Full=BSYN2; AltName: Full=Syntrophin-2; AltName: Full=Tax interaction protein 43; Short=TIP-43; FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. SUBUNIT: Monomer and homodimer (Probable). Interacts with the other members of the syntrophin family SNTA1 and SNTB2; with the sodium channel proteins SCN4A and SCN5A (By similarity). Interacts with the viral HTLV-1 TAX protein and with dystrophin protein DMD and related proteins DTNA and UTRN. INTERACTION: O95477:ABCA1; NbExp=3; IntAct=EBI-295843, EBI-784112; P11532:DMD; NbExp=3; IntAct=EBI-295843, EBI-295827; SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral membrane protein; Cytoplasmic side (By similarity). Cell junction (By similarity). Cytoplasm, cytoskeleton (By similarity). Note=In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions (By similarity). TISSUE SPECIFICITY: Ubiquitous. DOMAIN: The PH 1 domain mediates the oligomerization in a calcium dependent manner (By similarity). DOMAIN: The PDZ domain binds to the last three or four amino acids of ion channels and receptor proteins. The association with dystrophin or related proteins probably leaves the PDZ domain available to recruit proteins to the membrane (By similarity). DOMAIN: The SU domain binds calmodulin in a calcium-dependent manner (By similarity). PTM: Phosphorylated by CaM-kinase II (By similarity). SIMILARITY: Belongs to the syntrophin family. SIMILARITY: Contains 1 PDZ (DHR) domain. SIMILARITY: Contains 2 PH domains. SIMILARITY: Contains 1 SU (syntrophin unique) domain.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q13884
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.