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0SH3G1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionSh3-containing grb2-like protein 1 (sh3 domain protein 2b) (extra eleven-nineteen leukemia fusion gene) (een) (een fusion partner of mll).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0007417 central nervous system development (TAS)
0007165 signal transduction (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.
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 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
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
SequencesProtein: SH3G1_HUMAN (368 aa)
mRNA: NM_003025
Local Annotation
Synapse Ontology
sdb:0004 Presynaptic compartment  (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)
KO assignmentK00680
  Level 3 annotation:
  Level 2 annotation:
    Butanoate metabolism
    Glycerophospholipid metabolism
     leucine and isoleucine degradation
    Lysine degradation
    Histidine metabolism
    Tyrosine metabolism
    Phenylalanine metabolism
    Limonene and pinene degradation
    Alkaloid biosynthesis II
    Ethylbenzene degradation
    Benzoate degradation via CoA ligation
    1- and 2-Methylnaphthalene degradation
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 476 residues, 4311367-4312793Exon2: 21 residues, 4313325-4313382Exon3: 43 residues, 4313608-4313733Exon4: 36 residues, 4314366-4314470Exon5: 55 residues, 4314716-4314875Exon6: 46 residues, 4315084-4315218Exon7: 50 residues, 4316478-4316622Exon8: 26 residues, 4317497-4317570Exon9: 25 residues, 4317922-4317991Exon10: 52 residues, 4351320-4351471Exon11: 2 residues, -Jump to SH3G1_HUMAN  
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Loci Cluster (Details)Loci: 4354 4311367-4351471 ~-40K 17708(SH3GL1)(-)Loci: 3081 4255690-4274838 ~-19K 17702(+)Link out to UCSC