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0BIN1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameBIN1
DescriptionMyc box dependent-interacting protein 1 (bridging integrator 1) (amphiphysin-like protein) (amphiphysin ii) (box-dependent myc- interacting protein 1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0015629 actin cytoskeleton (TAS)
0008283 cell proliferation (TAS)
0000074 regulation of progression through cell cycle (TAS)

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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.
  IPR004148:BAR
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 .
  IPR003005:Amphiphysin
InterPro domains unassigned to SynO:
SH3 (src Homology-3) domains are small protein modules containing approximately 50 amino acid residues . They are found in a great variety of intracellular or membrane-associated proteins for example.n a variety of proteins with enzymatic activity.n adaptor proteins that lack catalytic sequences and in cytoskeletal proteins.uch as fodrin and yeast actin binding protein ABP-1. The SH3 domain has a characteristic fold which consists of five or six beta-strands arranged as two tightly packed anti-parallel beta sheets. The linker regions may contain short helices . The surface of the SH2-domain bears a flat.ydrophobic ligand-binding pocket which consists of three shallow grooves defined by conservative aromatic residues in which the ligand adopts an extended left-handed helical arrangement. The ligand binds with low affinity but this may be enhanced by multiple interactions.The region bound by the SH3 domain is in all cases proline-rich and contains PXXP as a core-conserved binding motif. The function of the SH3 domain is not well understood but they may mediate many diverse processes such as increasing local concentration of proteins.ltering their subcellular location and mediating the assembly of large multiprotein complexes .
  IPR001452:Src homology-3
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 .Amphiphysin 2 was the second amphiphysin family member found in mammals.The gene encoding it has been found to be alternatively spliced. Thevarious products have been named: BIN-1.h3P9.RAMP-2 and ALP-1. Theyhave different distribution patterns.ith the largest form (~95 kD) beingexpressed solely in the brain.here it shares a very similar (if notidentical) distribution pattern to amphiphysin 1 .
  IPR003023:Amphiphysin, isoform 2
IPR004148:BAR 
Evalue:-80.6197887582884 
Location:17-269IPR001452:SH3 
Evalue:-12.4089353929735 
Location:523-593IPR003023:AMPHIPHYSIN2 
Evalue:0 
Location:305-321IPR003023:AMPHIPHYSIN2 
Evalue:0 
Location:3-16IPR003023:AMPHIPHYSIN2 
Evalue:0 
Location:490-503IPR003023:AMPHIPHYSIN2 
Evalue:0 
Location:271-284IPR003023:AMPHIPHYSIN2 
Evalue:0 
Location:288-296
SequencesProtein: BIN1_HUMAN (593 aa)
mRNA: NM_139343
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords,domains)
Various stages of the synaptic vesicle cycle, including attachment, prefusion, triggering, recycling and reloading of the vesicles with transmitter.
sdb:0098 synaptic vesicle cycling  (Evidence:keywords,domains)
endocytotic reaction via coated pits
sdb:0119 endocytotic reaction  (Evidence:keywords,domains)
clathrin-coat uncoating means clathrin was shed from the budding vesicle membrane.
sdb:0122 clathrin-coat uncoating  (Evidence:keywords,domains)
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords,domains)
The gaps (approximately 1 micrometer wide) formed between myelin sheath cells along the axons are called Nodes of Ranvier.
sdb:0242 Ranvier node  (Evidence:keywords,domains)
endocytosis may be initiated or blocked by all kinds of signal.
sdb:0257 regulation of endocytosis  (Evidence:keywords,domains)
the molecules that link the clathrin lattice to the membrane.
sdb:0259 clathrin adapter  (Evidence:keywords,domains)
?
sdb:0260 coat recruitment  (Evidence:keywords,domains)
?
sdb:0329 actin in synaptic vesicle cycling  (Evidence:keywords,domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 202 residues, 127522076-127522679Exon2: 36 residues, 127524466-127524568Exon3: 39 residues, 127524847-127524958Exon4: 32 residues, 127525199-127525289Exon5: 45 residues, 127531518-127531647Exon6: 50 residues, 127533056-127533201Exon7: 29 residues, 127536160-127536243Exon8: 27 residues, 127537616-127537692Exon9: 30 residues, 127537978-127538064Exon10: 38 residues, 127542969-127543077Exon11: 34 residues, 127544040-127544136Exon12: 33 residues, 127544598-127544693Exon13: 20 residues, 127544807-127544862Exon14: 29 residues, 127550671-127550752Exon15: 145 residues, 127580905-127581334Exon16: 2 residues, -Jump to Q9BTH3_HUMANExon1: 201 residues, 127522078-127522679Exon2: 36 residues, 127524466-127524568Exon3: 39 residues, 127524847-127524958Exon4: 32 residues, 127525199-127525289Exon5: 38 residues, 127526300-127526408Exon6: 10 residues, 127527467-127527491Exon7: 38 residues, 127527950-127528058Exon8: 45 residues, 127531518-127531647Exon9: 50 residues, 127533056-127533201Exon10: 29 residues, 127536160-127536243Exon11: 27 residues, 127537616-127537692Exon12: 30 residues, 127537978-127538064Exon13: 33 residues, 127542208-127542301Exon14: 38 residues, 127542969-127543077Exon15: 34 residues, 127544040-127544136Exon16: 33 residues, 127544598-127544693Exon17: 20 residues, 127544807-127544862Exon18: 29 residues, 127550671-127550752Exon19: 145 residues, 127580905-127581334Exon20: 2 residues, -Jump to BIN1_HUMANExon1: 201 residues, 127522078-127522679Exon2: 36 residues, 127524466-127524568Exon3: 39 residues, 127524847-127524958Exon4: 32 residues, 127525199-127525289Exon5: 38 residues, 127526300-127526408Exon6: 10 residues, 127527467-127527491Exon7: 38 residues, 127527950-127528058Exon8: 50 residues, 127533056-127533201Exon9: 29 residues, 127536160-127536243Exon10: 27 residues, 127537616-127537692Exon11: 30 residues, 127537978-127538064Exon12: 33 residues, 127542208-127542301Exon13: 38 residues, 127542969-127543077Exon14: 34 residues, 127544040-127544136Exon15: 33 residues, 127544598-127544693Exon16: 20 residues, 127544807-127544862Exon17: 29 residues, 127550671-127550752Exon18: 145 residues, 127580905-127581334Exon19: 2 residues, -Jump to Q9BTH3_HUMANExon1: 201 residues, 127522078-127522679Exon2: 36 residues, 127524466-127524568Exon3: 39 residues, 127524847-127524958Exon4: 32 residues, 127525199-127525289Exon5: 38 residues, 127526300-127526408Exon6: 45 residues, 127531518-127531647Exon7: 50 residues, 127533056-127533201Exon8: 29 residues, 127536160-127536243Exon9: 27 residues, 127537616-127537692Exon10: 30 residues, 127537978-127538064Exon11: 38 residues, 127542969-127543077Exon12: 34 residues, 127544040-127544136Exon13: 33 residues, 127544598-127544693Exon14: 20 residues, 127544807-127544862Exon15: 29 residues, 127550671-127550752Exon16: 145 residues, 127580905-127581334Exon17: 2 residues, -Jump to Q9BTH3_HUMANExon1: 201 residues, 127522078-127522679Exon2: 36 residues, 127524466-127524568Exon3: 39 residues, 127524847-127524958Exon4: 32 residues, 127525199-127525289Exon5: 38 residues, 127526300-127526408Exon6: 50 residues, 127533056-127533201Exon7: 29 residues, 127536160-127536243Exon8: 27 residues, 127537616-127537692Exon9: 30 residues, 127537978-127538064Exon10: 33 residues, 127542208-127542301Exon11: 38 residues, 127542969-127543077Exon12: 34 residues, 127544040-127544136Exon13: 33 residues, 127544598-127544693Exon14: 20 residues, 127544807-127544862Exon15: 29 residues, 127550671-127550752Exon16: 145 residues, 127580905-127581334Exon17: 2 residues, -Jump to Q9BTH3_HUMANExon1: 201 residues, 127522078-127522679Exon2: 36 residues, 127524466-127524568Exon3: 39 residues, 127524847-127524958Exon4: 32 residues, 127525199-127525289Exon5: 38 residues, 127526300-127526408Exon6: 50 residues, 127533056-127533201Exon7: 29 residues, 127536160-127536243Exon8: 27 residues, 127537616-127537692Exon9: 30 residues, 127537978-127538064Exon10: 38 residues, 127542969-127543077Exon11: 34 residues, 127544040-127544136Exon12: 33 residues, 127544598-127544693Exon13: 20 residues, 127544807-127544862Exon14: 29 residues, 127550671-127550752Exon15: 145 residues, 127580905-127581334Exon16: 2 residues, -Jump to Q9BTH3_HUMANExon1: 201 residues, 127522078-127522679Exon2: 36 residues, 127524466-127524568Exon3: 39 residues, 127524847-127524958Exon4: 32 residues, 127525199-127525289Exon5: 45 residues, 127531518-127531647Exon6: 50 residues, 127533056-127533201Exon7: 17 residues, 127534641-127534686Exon8: 29 residues, 127536160-127536243Exon9: 27 residues, 127537616-127537692Exon10: 30 residues, 127537978-127538064Exon11: 38 residues, 127542969-127543077Exon12: 34 residues, 127544040-127544136Exon13: 33 residues, 127544598-127544693Exon14: 20 residues, 127544807-127544862Exon15: 29 residues, 127550671-127550752Exon16: 145 residues, 127580905-127581334Exon17: 2 residues, -Jump to Q9BTH3_HUMANExon1: 201 residues, 127522078-127522679Exon2: 36 residues, 127524466-127524568Exon3: 39 residues, 127524847-127524958Exon4: 32 residues, 127525199-127525289Exon5: 50 residues, 127533056-127533201Exon6: 17 residues, 127534641-127534686Exon7: 29 residues, 127536160-127536243Exon8: 27 residues, 127537616-127537692Exon9: 30 residues, 127537978-127538064Exon10: 38 residues, 127542969-127543077Exon11: 34 residues, 127544040-127544136Exon12: 33 residues, 127544598-127544693Exon13: 20 residues, 127544807-127544862Exon14: 29 residues, 127550671-127550752Exon15: 145 residues, 127580905-127581334Exon16: 2 residues, -Jump to Q9BTH3_HUMANExon1: 201 residues, 127522078-127522679Exon2: 36 residues, 127524466-127524568Exon3: 39 residues, 127524847-127524958Exon4: 32 residues, 127525199-127525289Exon5: 50 residues, 127533056-127533201Exon6: 29 residues, 127536160-127536243Exon7: 27 residues, 127537616-127537692Exon8: 30 residues, 127537978-127538064Exon9: 38 residues, 127542969-127543077Exon10: 34 residues, 127544040-127544136Exon11: 33 residues, 127544598-127544693Exon12: 20 residues, 127544807-127544862Exon13: 29 residues, 127550671-127550752Exon14: 145 residues, 127580905-127581334Exon15: 2 residues, -Jump to Q9BTH3_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4463 127731335-127768222 ~-37K 21224(ERCC3)(-)Loci: 4462 127522076-127581334 ~-59K 21214(-)Link out to UCSC