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0ARF6_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameARF6
DescriptionAdp-ribosylation factor 6.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005938 cell cortex (IDA)
0005768 endosome (TAS)
0005886 plasma membrane (IDA)
0005525 GTP binding (TAS)
0007155 cell adhesion (TAS)
0006928 cell motility (TAS)
0030866 cortical actin cytoskeleton organization an... (IMP)
0030838 positive regulation of actin filament polym... (IMP)
0035020 regulation of Rac protein signal transduction (IDA)
0031529 ruffle organization and biogenesis (IDA)
0016192 vesicle-mediated transport (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:
The small ADP ribosylation factor (Arf) GTP-binding proteins are major regulators of vesicle biogenesis in intracellular traffic . They are the founding members of a growing family that includes Arl (Arf-like).rp (Arf-related proteins) and the remotely related Sar (Secretion-associated and Ras-related) proteins. Arf proteins cycle between inactive GDP-bound and active GTP-bound forms that bind selectively to effectors. The classical structural GDP/GTP switch is characterized by conformational changes at the so-called switch 1 and switch 2 regions.hich bind tightly to the gamma-phosphate of GTP but poorly or not at all to the GDP nucleotide. Structural studies of Arf1 and Arf6 have revealed that although these proteins feature the switch 1 and 2 conformational changes.hey depart from other small GTP-binding proteins in that they use an additional.nique switch to propagate structural information from one side of the protein to the other. The GDP/GTP structural cycles of human Arf1 and Arf6 feature a unique conformational change that affects the beta2-beta3 strands connecting switch 1 and switch 2 (interswitch) and also the amphipathic helical N-terminus. In GDP-bound Arf1 and Arf6.he interswitch is retracted and forms a pocket to which the N-terminal helix binds.he latter serving as a molecular hasp to maintain the inactive conformation. In the GTP-bound form of these proteins.he interswitch undergoes a two-residue register shift that pulls switch 1 and switch 2 up.estoring an active conformation that can bind GTP. In this conformation.he interswitch projects out of the protein and extrudes the N-terminal hasp by occluding its binding pocket. ADP-ribosylation factors (ARF) are 20 kDa GTP-binding proteins involved in protein trafficking. They may modulate vesicle budding and uncoating within the Golgi apparatus. ARFs also act as allosteric activators of cholera toxin ADP-ribosyltransferase activity. They are evolutionary conserved and present in all eukaryotes. At least six forms of ARF are present in mammals and three in budding yeast. The ARF family also includes proteins highly related to ARFs but which lack the cholera toxin cofactor activity.hey are collectively known as ARLs (ARF-like). The ARFs are N-terminally myristoylated (the ARLs have not yet been shown to be modified in such a fashion).
  IPR006688:ADP-ribosylation factor
The small ADP ribosylation factor (Arf) GTP-binding proteins are major regulators of vesicle biogenesis in intracellular traffic . They are the founding members of a growing family that includes Arl (Arf-like).rp(Arf-related proteins) and the remotely related Sar (Secretion-associated and Ras-related) proteins. Arf proteins cycle between inactive GDP-bound and active GTP-bound forms that bind selectively to effectors. The classical structural GDP/GTP switch is characterized by conformational changes at the so-called switch 1 and switch 2 regions.hich bind tightly to the gamma-phosphate of GTP but poorly or not at all to the GDP nucleotide. Structural studies of Arf1 and Arf6 have revealed that although these proteins feature the switch 1 and 2 conformational changes.hey depart from other small GTP-binding proteins in that they use an additional.nique switch to propagate structural information from one side of the protein to the other. The GDP/GTP structural cycles of human Arf1 and Arf6 feature a unique conformational change that affects the beta2beta3 strands connecting switch 1 and switch 2 (interswitch) and also the amphipathic helical N-terminus. In GDP-boundArf1 and Arf6.he interswitch is retracted and forms a pocket to which the N-terminal helix binds.he latter serving as a molecular hasp to maintain the inactive conformation. In the GTP-bound form of these proteins.he interswitch undergoes a two-residue register shift that pulls switch 1 and switch 2 up.estoring an active conformation that can bind GTP. In this conformation.he interswitch projects out of the protein and extrudes the N-terminal hasp by occluding its binding pocket.
  IPR006689:ARF/SAR superfamily
Many members of the Ras superfamily of GTPases have been implicated in the regulation of hematopoietic cells.ith roles in growth.urvival.ifferentiation.ytokine production.hemotaxis.esicle-trafficking.nd phagocytosis. The Ras superfamily of proteins now includes over 150 small GTPases (distinguished from the large.eterotrimeric GTPases.he G-proteins). It comprises six subfamilies.he Ras.ho.an.ab.rf.nd Kir/Rem/Rad subfamilies . They exhibit remarkable overall amino acid identities.specially in the regions interacting with the guanine nucleotide exchange factors that catalyze their activation .
  IPR001806:Ras GTPase
Proteins with a small GTP-binding domain include Ras.hoA.ab11.ranslation elongation factor G.ranslation initiation factor IF-2.etratcycline resistance protein TetM.DC42.ra.DP-ribosylation factors.dhF.nd many others . In some proteins the domain occurs more than once. Among them there is a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model.
  IPR005225:Small GTP-binding protein domain
IPR006688:ARF 
Evalue:-132.537602002101 
Location:1-174
SequencesProtein: ARF6_HUMAN (174 aa)
mRNA: NM_001663
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)
?
sdb:0247 cytoskeleton protein transport  (Evidence:keywords)
?
sdb:0329 actin in synaptic vesicle cycling  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 13 residues, 49429588-49429625Exon2: 589 residues, 49429723-49431484Exon3: 2 residues, -Jump to ARF6_HUMAN  
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Loci Cluster (Details)Loci: 2835 49429588-49431484 ~-2K 11111(ARF6)(+)Loci: 2836 49848796-49862418 ~-14K 11116(ATP5S)(+)Loci: 4130 49954996-50069126 ~-114K 11120(MAP4K5)(-)Loci: 2837 50096499-50169140 ~-73K 11121(SPG3A)(+)Loci: 2834 49304536-49319605 ~-15K 11105(KLHDC2)(+)Link out to UCSC