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1O60592_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
NameN/A
DescriptionArg/abl-interacting protein argbp2a.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0015629 actin cytoskeleton (TAS)
0005634 nucleus (TAS)
0008093 cytoskeletal adaptor activity (TAS)
0005200 structural constituent of cytoskeleton (TAS)
0008307 structural constituent of muscle (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 unassigned to SynO:
Phagocytes form the first line of defence against invasion by micro-organisms. Engulfing of bacteria by neutrophils is accompanied by theconsumption of large amounts of oxygen - a so-called respiratory burst.Defects in phagocytosis involving the lack of a respiratory burst giverise to chronic granulomatous disease (CGD).n which patients are pre-disposed to infection.ften from otherwise non-pathogenic bacteria .Regulation of the respiratory burst takes place at the phagocytic vacuole.The process is mediated by NADPH oxidase.hich transports electrons acrossthe plasma membrane to form superoxide (an oxygen molecule with an extraelectron that is toxic to normal cells) in the vacuole interior. Theelectrons are carried across the membrane by a short electron transportchain in the form of an unusual flavocytochrome b .To conserve NADPH and avoid the toxic effects of superoxide.he oxidase remains inactive until it receives an appropriate stimulus. Activationinvolves the participation of a number of cytosolic proteins.ome of which attach to the flavocytochrome. P47phox.67phox and p40phox arespecialised components of phagocytic cells.ll of which contain SH3domains .y means of which they attach to proline-rich regions of otherproteins. Upon activation.47phox and p67phox are phosphorylated and.ith p40phox.ranslocate to the region of the plasma membrane formingthe phagocytic vacuole.here they associates with hydrophilic regionsof the flavocytochrome .
  IPR000108:Neutrophil cytosol factor 2
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
Sorbin is an active peptide present in the digestive tract.here it has pro-absorptive and anti-secretory effects in different parts of the intestine.ncluding the ability to decrease VIP (vasoactive intestinal peptide) and cholera toxin-induced secretion. It is expressed in some intestinal and pancreatic endocrine tumours in humans .Sorbin-homology domains are found in adaptor proteins such as vinexin.AP/ponsin and argBP2.hich regulate various cellular functions.ncluding cell adhesion.ytoskeletal organisation.nd growth factor signalling . In addition to the sorbin domain.hese proteins contain three SH3 (src homology 3) domains. The sorbin homology domain mediates the interaction of vinexin and CAP with flotillin.hich is crucial for the localisation of SH3-binding proteins to the lipid raft. region of the plasma membrane rich in cholesterol and sphingolipids that acts to concentrate certain signalling molecules. The sorbin homology domain of adaptor proteins may mediate interactions with the lipid raft that are crucial to intracellular communication .
  IPR003127:Sorbin-like
Spectrin is an elongated protein that belongs to a family of related molecules (including dystrophin and alpha-actinin) that contain tandemly repeated segments and form resilient cellular meshworks by cross-linking actin filaments . The protein is an alpha-beta heterodimer in which the alpha and beta monomers associate in an anti-parallel fashion . Assembly involves initial contact of complementary nucleation sites on each subunit.ia four tandem repeat regions . Following nucleation.he remainder of the subunits associate rapidly along their full lengths to form a dimer by super-coiling around each other.orming a rope-like.lexible rod . Assembly terminates if either polypeptide is interrupted by protease cleavage. Heterozygotic mutations involving either nucleation site are predicted to affect allele incorporation into the mature membrane skeleton . The structure of a repeat unit of alpha-spectrin has been determined to 1.8A resolution by means of X-ray crystallography . This was shown to comprise an anti-parallel three-helix bundle separated by two loops.hich folds into a left-handed coiled coil . At the interface between tandem repeats.ydrophobic interactions may constrain intersegment flexibility. The interaction between alpha- and beta-subunits is mediated by the association of two helices at the C-terminus of the beta-chain and a single helix from the N-terminus of the alpha-chain. Mutations that affect these critical helix side-chain interactions disrupt spectrin associations that sustain the integrity of erythrocyte membranes giving rise to haemolytic anaemias . These haemolytic syndromes include hereditary elliptocytosis.ts aggravated form hereditary pyropoikilocytosis and hereditary spherocytosis .
  IPR013315:Spectrin alpha chain
IPR003127:Sorb 
Evalue:-39.7212448120117 
Location:113-162IPR001452:SH3 
Evalue:-22.301029995664 
Location:432-487IPR001452:SH3 
Evalue:-18.0506099933551 
Location:507-564IPR001452:SH3_1 
Evalue:-12.958607673645 
Location:610-666IPR000108:P67PHOX 
Evalue:0 
Location:212-229
SequencesProtein: O60592_HUMAN (666 aa)
mRNA: AF049884 NM_003603
Local Annotation
Synapse Ontology
?
sdb:0247 cytoskeleton protein transport  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 749 residues, 186743592-186745836Exon2: 37 residues, 186747826-186747933Exon3: 18 residues, 186752033-186752083Exon4: 69 residues, 186769927-186770128Exon5: 45 residues, 186772978-186773107Exon6: 40 residues, 186773192-186773307Exon7: 17 residues, 186776732-186776779Exon8: 31 residues, 186778210-186778299Exon9: 64 residues, 186784979-186785167Exon10: 18 residues, 186788696-186788746Exon11: 21 residues, 186793502-186793559Exon12: 30 residues, 186796226-186796310Exon13: 40 residues, 186804815-186804930Exon14: 65 residues, 186807614-186807804Exon15: 17 residues, 186809931-186809976Exon16: 24 residues, 186810809-186810876Exon17: 59 residues, 186815571-186815744Exon18: 48 residues, 186820251-186820390Exon19: 20 residues, 186836570-186836626Exon20: 10 residues, 186836944-186836970Exon21: 18 residues, 186848709-186848759Exon22: 48 residues, 186933374-186933514Exon23: 193 residues, 186969811-186970386Exon24: 2 residues, -Jump to O60592_HUMANExon1: 122 residues, 186745473-186745836Exon2: 37 residues, 186747826-186747933Exon3: 18 residues, 186752033-186752083Exon4: 69 residues, 186769927-186770128Exon5: 45 residues, 186772978-186773107Exon6: 40 residues, 186773192-186773307Exon7: 17 residues, 186776732-186776779Exon8: 31 residues, 186778210-186778299Exon9: 64 residues, 186784979-186785167Exon10: 18 residues, 186788696-186788746Exon11: 21 residues, 186793502-186793559Exon12: 30 residues, 186796226-186796310Exon13: 40 residues, 186804815-186804930Exon14: 65 residues, 186807614-186807804Exon15: 17 residues, 186809931-186809976Exon16: 24 residues, 186810809-186810876Exon17: 59 residues, 186815571-186815744Exon18: 48 residues, 186820251-186820390Exon19: 20 residues, 186836570-186836626Exon20: 11 residues, 186836943-186836970Exon21: 18 residues, 186848709-186848759Exon22: 48 residues, 186933374-186933514Exon23: 188 residues, 186969811-186970369Exon24: 2 residues, -Jump to O60592_HUMAN  
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