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
0TOM1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameTOM1
DescriptionTarget of myb protein 1.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005829 cytosol (IDA)
0005769 early endosome (IDA)
0016020 membrane (IDA)
0005515 protein binding (IPI)
0006897 endocytosis (NAS)
0016197 endosome transport (TAS)
0015031 protein transport (NAS)

Warning: fopen(/home/kongl/syndb/www/temp/598018084.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 unassigned to SynO:
The GAT domain is responsible for binding of GGA proteins to several members of the ARF family including ARF1 and ARF3. The GAT domain stabilizes membrane bound ARF1 in its GTP bound state.y interfering with GAP proteins .
  IPR004152:GAT
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:-69.7212463990472 
Location:13-148IPR004152:GAT 
Evalue:-52.4317970275879 
Location:212-312
SequencesProtein: TOM1_HUMAN (492 aa)
mRNA: BC046151 NM_005488
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 assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 38 residues, 34025860-34025973Exon2: 30 residues, 34043869-34043954Exon3: 28 residues, 34047951-34048030Exon4: 52 residues, 34049020-34049170Exon5: 47 residues, 34049488-34049623Exon6: 51 residues, 34049760-34049907Exon7: 41 residues, 34053263-34053380Exon8: 46 residues, 34056339-34056473Exon9: 13 residues, 34058973-34059007Exon10: 33 residues, 34059396-34059490Exon11: 42 residues, 34060320-34060441Exon12: 27 residues, 34064705-34064781Exon13: 22 residues, 34071717-34071777Exon14: 15 residues, 34072922-34072962Exon15: 310 residues, 34073047-34073973Exon16: 2 residues, -Jump to TOM1_HUMANExon1: 19 residues, 34025918-34025973Exon2: 30 residues, 34043869-34043954Exon3: 28 residues, 34047951-34048030Exon4: 52 residues, 34049020-34049170Exon5: 47 residues, 34049488-34049623Exon6: 51 residues, 34049760-34049907Exon7: 41 residues, 34053263-34053380Exon8: 46 residues, 34056339-34056473Exon9: 13 residues, 34058973-34059007Exon10: 33 residues, 34059396-34059490Exon11: 42 residues, 34060320-34060441Exon12: 27 residues, 34064705-34064781Exon13: 22 residues, 34071717-34071777Exon14: 16 residues, 34072922-34072965Exon15: 307 residues, 34073047-34073964Exon16: 2 residues, -Jump to TOM1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3312 34107086-34120194 ~-13K 24618(HMOX1)(+)Loci: 3311 34025860-34073973 ~-48K 24616(TOM1)(+)Link out to UCSC