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0STAM2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSTAM2
DescriptionSignal transducing adapter molecule 2 (stam-2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005515 protein binding (IPI)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The Ubiquitin Interacting Motif (UIM) was first described in the 26S proteasome subunit PSD4/RPN-10 . It is known to bind multiple ubiquitin and was also found in many proteins involved in the endocytic pathway.ncludingthe PSD4/RPN-10/S5a multiubiquitin binding subunit of the 26S proteasome; the VPS27 vacuolar sorting protein; and ataxin-3. protein involved in ataxia disease.
  IPR003903:Ubiquitin interacting motif
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
The VHS domain is a ~140 residues long domain.hose name is derivedfrom its occurrence in VPS-27.rs and STAM. Based on regions surrounding the domain.HS-proteins can be divided into 4 groups : STAM/EAST/Hbp which all share the domain composition VHS-SH3-ITAM and carry one or two ubiquitin-interacting motifs Proteins with a FYVE domain () C-terminal to VHS which also carry one or two ubiquitin-interacting motifs GGA proteins with a domain composition VHS-GAT (GGA and Tom1) homology domain VHS domain alone or in combination with domains other than those listed above The VHS domain is always found at the N-terminus of proteins suggesting that such topology is important for function. The domain is considered to have a general membrane targeting/cargo recognition role in vesicular trafficking .Resolution of the crystal structure of the VHS domain of Drosophila Hrs andhuman Tom1 revealed that it consists of eight helices arranged in a double-layer superhelix. The existence of conserved patches of residues on the domain surface suggests that VHS domains may be involved in protein-protein recognition and docking. Overall.equence similarity is low (approx 25%) amongst domain family members
  IPR002014:VHS
The epsin NH2-terminal homology (ENTH) domain () is a membrane interacting module composed of a superhelix of alpha-helices. It is present at the NH2-terminus of proteins that often contain consensus sequences for binding to clathrin coat components and their accessory factors.nd therefore function as endocytic adaptors. ENTH domain containing proteins have additional roles in signalling and actin regulation and may have yet other actions in the nucleus. The ENTH domain is structurally similar to the VHS domain. The ENTH domain is approximately 150 amino acids long. The ENTH domain forms a compact globular structure.omposed of eight alpha-helices connected by loops of varying length. Three helical hairpins that are stacked consecutively with a right-handed twist determine the general topology of the domain. This stacking gives the ENTH domain a rectangular appearance when viewed face on. The most highly conserved amino acids fall roughly into two classes: internal residues that are involved in packing and therefore are necessary for structural integrity.nd solvent accessible residues that may be involved in protein-protein interactions . VHS domains are found at the N-termini of select proteins involved in intracellular membrane trafficking. The domain consists of eight helices arranged in a superhelix. The surface of the domain has two main features: a basic patch on one side due to several conserved positively charged residues on helix 3 and a negatively charged ridge on the opposite side.ormed by residues on helix 2. Comparison of the two VHS domains and the ENTH domain reveals a conserved surface.omposed of helices 2 and 4.hat is utilized for protein-protein interactions. In addition.HS domain-containing proteins are also often localized to membranes. It has therefore been suggested that the conserved positively charged surface of helix 3 in VHS and ENTH domains plays a role in membrane binding .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008942:ENTH/VHS
IPR002014:VHS 
Evalue:-57.5850266520292 
Location:9-140IPR001452:SH3_1 
Evalue:-24.4317989349365 
Location:205-259IPR003903:UIM 
Evalue:-4.23657178878784 
Location:164-181IPR003110:ITAM_1 
Evalue:0 
Location:0-0
SequencesProtein: STAM2_HUMAN (525 aa)
mRNA: BC028740 NM_005843
Local Annotation
Synapse Ontology
endosome of the presynaptic compartment. A cellular structure that is involved in the transport of proteins in the neuron after the proteins are endocytosed from the outside to the inside of the cell.
sdb:0088 endosome  (Evidence:keywords)
KO assignmentK04705
  Level 3 annotation:
    signal transducing adaptor molecule
  Level 2 annotation:
    Jak-STAT signaling pathway
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 737 residues, 152683352-152685562Exon2: 58 residues, 152688525-152688695Exon3: 53 residues, 152690985-152691139Exon4: 20 residues, 152696873-152696928Exon5: 31 residues, 152697932-152698020Exon6: 30 residues, 152698161-152698247Exon7: 32 residues, 152700271-152700363Exon8: 64 residues, 152708586-152708773Exon9: 25 residues, 152709647-152709717Exon10: 51 residues, 152711921-152712068Exon11: 35 residues, 152712783-152712882Exon12: 27 residues, 152712984-152713060Exon13: 30 residues, 152714904-152714989Exon14: 132 residues, 152740362-152740752Exon15: 2 residues, -Jump to STAM2_HUMANExon1: 107 residues, 152685242-152685562Exon2: 58 residues, 152688525-152688695Exon3: 53 residues, 152690985-152691139Exon4: 20 residues, 152696873-152696928Exon5: 31 residues, 152697932-152698020Exon6: 29 residues, 152698161-152698244Exon7: 33 residues, 152700268-152700363Exon8: 64 residues, 152708586-152708773Exon9: 25 residues, 152709647-152709717Exon10: 51 residues, 152711921-152712068Exon11: 35 residues, 152712783-152712882Exon12: 27 residues, 152712984-152713060Exon13: 30 residues, 152714904-152714989Exon14: 132 residues, 152740362-152740752Exon15: 2 residues, -Jump to STAM2_HUMAN  
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Loci Cluster (Details)Loci: 4468 152683352-152740752 ~-57K 21406(STAM2)(-)Loci: 4467 152402388-152663790 ~-261K 21405(CACNB4)(-)Link out to UCSC