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1Q86VV0_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
DescriptionBreast cancer associated protein brap1.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005737 cytoplasm (IEA)
0005515 protein binding (IEA)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains assigned to SynO:
Endocytosis and intracellular transport involve several mechanistic steps: (1) for the internalisation of cargo molecules.he membrane needs to bend to form a vesicular structure.hich requires membrane curvature and a rearrangement of the cytoskeleton; (2) following its formation.he vesicle has to be pinched off the membrane; (3) the cargo has to be subsequently transported through the cell and the vesicle must fuse with the correct cellular compartment.Members of the Amphiphysin protein family are key regulators in the early steps of endocytosis.nvolved in the formation of clathrin-coated vesicles by promoting the assembly of a protein complex at the plasma membrane and directly assist in the induction of the high curvature of the membrane at the neck of the vesicle. Amphiphysins contain a characteristic domain.nown as the BAR (BinAmphiphysinRvs)-domain.hich is required for their in vivo function and their ability to tubulate membranes . The crystal structure of these proteins suggest the domain forms a crescent-shaped dimer of a three-helix coiled coil with a characteristic set of conserved hydrophobic.romatic and hydrophilic amino acids. Proteins containing this domain have been shown to homodimerise.eterodimerise or.n a few cases.nteract with small GTPases.
Amphiphysins belong to the expanding BAR (Bin-Amphiphysin-Rvsp) family proteins.ll members of which share a highly conserved N-terminal BAR domain.hich has predicted coiled-coil structures required for amphiphysin dimerisation and plasma membrane interaction . Almost all members also share a conserved C-terminal Src homology 3 (SH3) domain.hich mediates their interactions with the GTPase dynamin and the inositol-5-phosphatase synaptojanin 1 in vertebrates and with actin in yeast. The central region of all these proteins is most variable. In mammals.he central region of amphiphysin I and amphiphysin IIa contains a proline-arginine-rich region for endophilin binding and a CLAP domain.or binding to clathrin and AP-2. The interactions mediated by both the central and C-terminal domains arebelieved to be modulated by protein phosphorylation . Amphiphysins are proteins that are thought to be involved in clathrin-mediated endocytosis.ctin function.nd signalling pathways. In vertebrates.mphiphysins may regulate.ut are not essential for clathrin-mediated endocytosis of SVs. However.n Drosophila amphiphysin is not involved at all in SV endocytosis but is required for T-tubule structure and excitation-contraction coupling muscles and plays a role in membrane morphogenesis in developing photoreceptors and a variety of other cells .
InterPro domains unassigned to SynO:
UBA domains are a commonly occurring sequence motif of approximately 45 amino acid residues that are found in diverse proteins involved in the ubiquitin/proteasome pathway.NA excision-repair.nd cell signalling via protein kinases . HHR23A.he human homologue of yeast Rad23A is a nucleotide excision-repair protein that contains both an internal and a C-terminal UBA domain. The fold of the UBA domain consists of a compact three-helical bundle with a right-handed twist.nd have a conserved hydrophobic surface patch for protein-protein interactions. UBA-like domains can be found in other proteins as well.uch as the TS-N domain in the elongation factor Ts (EF-Ts).hich catalyses the recycling of the GTPase EF-Tu required for the binding of aminoacyl-tRNA top the ribosomal A site ; and the C-terminal domain of TAP/NXF1.hich functions in nuclear export through the interaction of its UBA-like domain with FG nucleoporins .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
SequencesProtein: Q86VV0_HUMAN (565 aa)
mRNA: NM_016293
Local Annotation
Synapse Ontology
endocytotic reaction via coated pits
sdb:0119 endocytotic reaction  (Evidence:domains)
clathrin-coat uncoating means clathrin was shed from the budding vesicle membrane.
sdb:0122 clathrin-coat uncoating  (Evidence:domains)
the molecules that link the clathrin lattice to the membrane.
sdb:0259 clathrin adapter  (Evidence:domains)
sdb:0260 coat recruitment  (Evidence:domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 164 residues, 49961089-49961579Exon2: 26 residues, 49964766-49964838Exon3: 29 residues, 49968158-49968239Exon4: 253 residues, 49971641-49972395Exon5: 29 residues, 49975846-49975929Exon6: 27 residues, 49977139-49977215Exon7: 30 residues, 49979253-49979339Exon8: 38 residues, 49979657-49979765Exon9: 34 residues, 49982070-49982166Exon10: 33 residues, 49982736-49982831Exon11: 20 residues, 49983137-49983192Exon12: 29 residues, 49993873-49993954Exon13: 46 residues, 50004072-50004205Exon14: 2 residues, -Jump to Q86VV0_HUMAN  
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Loci Cluster (Details)Loci: 4033 49961089-50004205 ~-43K 8871(-)Loci: 4032 49869231-49897744 ~-29K 8867(POU6F1)(-)Link out to UCSC