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0RIMB1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameBZRAP1
DescriptionPeripheral-type benzodiazepine receptor-associated protein 1 (prax-1) (peripheral benzodiazepine receptor interacting protein) (pbr-ip) (rim binding protein 1) (rim-bp1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005739 mitochondrion (IDA)
0030156 benzodiazepine receptor binding (IPI)

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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 unassigned to SynO:
SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organisation. These were first described in the Src cytoplasmic tyrosine kinase . The structure is a partly opened beta barrel.
  IPR011511:Variant SH3
Fibronectins are multi-domain glycoproteins found in a soluble form in plasma.nd in an insoluble form in loose connective tissue and basement membranes . They contain multiple copies of 3 repeat regions (types I.I and III).hich bind to a variety of substances including heparin.ollagen.NA.ctin.ibrin and fibronectin receptors on cell surfaces. The wide variety of these substances means that fibronectins are involved in a number of important functions: e.g..ound healing; cell adhesion; blood coagulation; cell differentiation and migration; maintenance of the cellular cytoskeleton; and tumour metastasis . The role of fibronectin in cell differentiation is demonstrated by the marked reduction in the expression of its gene when neoplastic transformation occurs. Cell attachment has been found to be mediated by the binding of the tetrapeptide RGDS to integrins on the cell surface .lthough related sequences can also display cell adhesion activity.Plasma fibronectin occurs as a dimer of 2 different subunits.inked together by 2 disulphide bonds near the C-terminus. The difference in the 2 chains occurs in the type III repeat region and is caused by alternative splicing of the mRNA from one gene . The observation that.n a given protein.n individual repeat of one of the 3 types (e.g..he first FnIII repeat) shows much less similarity to its subsequent tandem repeats within that protein than to its equivalent repeat between fibronectins from other species.as suggested that the repeating structure of fibronectin arose at an early stage of evolution. It also seems to suggest that the structure is subject to high selective pressure .The fibronectin type III repeat region is an approximately 100 amino acid domain.ifferent tandem repeats of which contain binding sites for DNA.eparin and the cell surface . The superfamily of sequences believed to contain FnIII repeats represents 45 different families.he majority of which are involved in cell surface binding in some manner.r are receptor protein tyrosine kinases.r cytokine receptors.
  IPR003961:Fibronectin, type III
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
Fibronectin is composed of three repeating structural motifs.f which one is the FnIII module. The three modules form a linear sequence of multiple tandem copies connected by short linker peptides. The secondary structure of the FnIII10 module.hich is the only fibronectin module to possess an integrin binding RGD motif.onsists of two beta-sheets containing the antiparallel beta-strands ABE and DCFG.espectively.hich fold up to form a beta-sandwich. The RGD sequence is located in the loop connecting the beta-strands .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008957:Fibronectin, type III-like fold
IPR011511:SH3_2 
Evalue:-19.2518119812012 
Location:1629-1691IPR011511:SH3_2 
Evalue:-18.7958793640137 
Location:1768-1828IPR001452:SH3 
Evalue:-10.7212463990472 
Location:656-719IPR003961:FN3 
Evalue:-3.48148606012211 
Location:882-955IPR003961:fn3 
Evalue:-1.79587996006012 
Location:791-868IPR003961:FN3 
Evalue:0 
Location:978-1076
SequencesProtein: RIMB1_HUMAN (1857 aa)
mRNA: NM_004758
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 406 residues, 53733592-53734807Exon2: 22 residues, 53736697-53736759Exon3: 39 residues, 53737420-53737531Exon4: 26 residues, 53737746-53737818Exon5: 36 residues, 53737899-53738003Exon6: 13 residues, 53738192-53738225Exon7: 26 residues, 53738701-53738773Exon8: 58 residues, 53739159-53739328Exon9: 52 residues, 53739970-53740122Exon10: 35 residues, 53740201-53740301Exon11: 282 residues, 53740900-53741740Exon12: 66 residues, 53742326-53742518Exon13: 82 residues, 53742871-53743111Exon14: 128 residues, 53743195-53743573Exon15: 52 residues, 53743930-53744082Exon16: 279 residues, 53744251-53745082Exon17: 38 residues, 53748382-53748492Exon18: 40 residues, 53748784-53748900Exon19: 59 residues, 53750639-53750812Exon20: 70 residues, 53751449-53751654Exon21: 9 residues, 53752468-53752489Exon22: 19 residues, 53752890-53752941Exon23: 37 residues, 53754667-53754772Exon24: 43 residues, 53755013-53755136Exon25: 32 residues, 53755309-53755399Exon26: 30 residues, 53755657-53755741Exon27: 28 residues, 53755827-53755905Exon28: 66 residues, 53757170-53757362Exon29: 62 residues, 53757893-53758073Exon30: 45 residues, 53758652-53758781Exon31: 38 residues, 53759042-53759150Exon32: 178 residues, 53759947-53760477Exon33: 2 residues, -Jump to RIMB1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3025 53515797-53521810 ~-6K 16281(DLC2)(+)Loci: 4304 53733592-53760477 ~-27K 16290(BZRAP1)(-)Loci: 4305 53852527-53920744 ~-68K 16295(-)Loci: 4306 53952614-53964410 ~-12K 16299(-)Loci: 4303 53435861-53439592 ~-4K 16279(SFRS1)(-)Link out to UCSC