SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
1Q68EM7_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
NameN/A
DescriptionNadrin.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005737 cytoplasm (IEA)
0005524 ATP binding (IEA)
0005515 protein binding (IEA)
0004812 tRNA ligase activity (IEA)
0006418 tRNA aminoacylation for protein translation (IEA)

Warning: fopen(/home/kongl/syndb/www/temp/1543069302.dot) [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
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.
  IPR004148:BAR
InterPro domains unassigned to SynO:
Members of the Rho family of small G proteins transduce signals from plasma-membranereceptors and control cell adhesion.otility and shape by actin cytoskeleton formation.Like all other GTPases.ho proteins act as molecular switches.ith an activeGTP-bound form and an inactive GDP-bound form. The active conformation is promoted byguanine-nucleotide exchange factors.nd the inactive state by GTPase-activating proteins(GAPs) which stimulate the intrinsic GTPase activity of small G proteins.This entry is a Rho/Rac/Cdc42-like GAP domain.hat is found in a wide variety of large.ulti-functional proteins .A number of structure are known for this family .The domain is composed of seven alpha helices.This domain is also known as the breakpoint cluster region-homology (BH) domain.
  IPR000198:RhoGAP
Proteins containing a RhoGAP (Rho GTPase Activating Protein) domain usually function to catalyze the hydrolysis of GTP that is bound to Rho.ac and/or Cdc42.nactivating these regulators of the actin cytoskeleton. The 53 known human RhoGAP domain-containing proteins are the largest known group of Rho GTPase regulators and significantly outnumber the 21 Rho GTPases they presumably regulate. This excess of GAP proteins probably indicates complex regulation of the Rho GTPases and is consistent with the existence of almost as many (48) human Dbl domain-containing Rho GEFs that act antagonistically to the RhoGAP proteins by activating the Rho GTPases. Phylogenetic analysis offers evidence for frequent domain duplication and for duplication of the entire genes containing these GAP domains .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008936:Rho GTPase activation protein
IPR004148:BAR 
Evalue:-83.5686340332031 
Location:1-239IPR000198:RhoGAP 
Evalue:-60.8860566476932 
Location:263-439IPR001412:AA_TRNA_LIGASE_I 
Evalue:0 
Location:784-794
SequencesProtein: Q68EM7_HUMAN (881 aa)
mRNA: NM_001006634
Local Annotation
Synapse Ontology
endocytotic reaction via coated pits
sdb:0119 endocytotic reaction  (Evidence:domains)
clathrin-coat uncoating means clathrin was shed from the budding vesicle membrane.
sdb:0122 clathrin-coat uncoating  (Evidence:domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 290 residues, 24838214-24839082Exon2: 209 residues, 24849605-24850226Exon3: 58 residues, 24854291-24854461Exon4: 80 residues, 24858185-24858419Exon5: 54 residues, 24860808-24860965Exon6: 32 residues, 24862592-24862684Exon7: 40 residues, 24866303-24866417Exon8: 29 residues, 24868225-24868306Exon9: 29 residues, 24871110-24871192Exon10: 39 residues, 24871752-24871864Exon11: 44 residues, 24873424-24873552Exon12: 29 residues, 24878492-24878574Exon13: 25 residues, 24878732-24878801Exon14: 39 residues, 24883018-24883130Exon15: 27 residues, 24887172-24887249Exon16: 39 residues, 24887482-24887594Exon17: 26 residues, 24889328-24889402Exon18: 37 residues, 24896036-24896141Exon19: 15 residues, 24897787-24897827Exon20: 50 residues, 24934030-24934176Exon21: 2 residues, -Jump to Q68EM7_HUMANExon1: 14 residues, 24873513-24873552Exon2: 25 residues, 24878732-24878801Exon3: 39 residues, 24883018-24883130Exon4: 27 residues, 24887172-24887249Exon5: 39 residues, 24887482-24887594Exon6: 26 residues, 24889328-24889402Exon7: 37 residues, 24896036-24896141Exon8: 15 residues, 24897787-24897827Exon9: 19 residues, 24934030-24934083Exon10: 2 residues, -Jump to Q96KS2_HUMAN  
Tune and view alternative isoforms