Protein detail
TBC9B
TBC1 domain family member 9B
Protein symbol TBC9B | UniProt ID | EVMP score 0.50 |
Frequency 5 | Transmembrane count 1 | Protein classification Predicted intracellular proteins |
Basic Information
Protein Names
TBC1 domain family member 9B
Protein Class
Predicted intracellular proteins
Protein Function
Predicted intracellular proteins
Transmembrane
668..688; Helical
Transmembrane Count
1
Ensembl
Entrez Gene Symbol
Gene Synonym
GRAMD9BKIAA0676
Gene Description
TBC1 domain family member 9B
Chromosome
5
Position
179862066-179907897
Frequency
5
EVMP Score
0.50
Fluorescence & Localization
Tissue SpecificgallbladderCell SpecificCholangiocytesSingle-Nuclei Brain Specificoligodendrocyte
Function & Pathway
Protein Function
Predicted intracellular proteins
Cellular Component
Molecular Function
Biological Process
Mediation Categories
Other mediation
Relations & Evidence
Enzyme-Mediated Modification
0 records.
Ligand-Receptor Signaling
7 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| intracellular | intracellular | ComPPI | No | No | No | No | No |
| intracellular | intracellular | OmniPath | No | No | No | No | No |
| transmembrane | transmembrane | UniProt_location | No | No | No | No | No |
| transmembrane | transmembrane | UniProt_topology | No | No | No | No | No |
| transmembrane | transmembrane | UniProt_keyword | No | No | No | No | No |
| transmembrane | transmembrane | Ramilowski_location | No | No | No | No | No |
| transmembrane | transmembrane | OmniPath | No | No | No | No | No |
Regulatory Interaction Network
0 records.
Protein Complex Composition
3 records.
| Component Name | Component Gene Symbols | Component UniProt ID | Stoichiometry | Database | Database IDs | References |
|---|---|---|---|---|---|---|
| CHMCHMLHSPA1BRAB1ARAB32RAB3ARAB4ARAB5ARAB6ARAB7ARABAC1RABGGTBTBC1D9BYIF1A | O95070P0DMV9P20336P20338P20339P20340P24386P26374P51149P53611P62820Q13637Q66K14Q9UI14 | 1:1:1:1:1:1:1:1:1:1:1:1:1:1 | NetworkBlastCompleat | Compleat:HC8849 | ||
| CPT1APIP4P2TBC1D9TBC1D9B | P50416Q66K14Q6ZT07Q8N4L2 | 0:0:0:0 | hu.MAP2 | |||
| TBC1D9TBC1D9B | Q66K14Q6ZT07 | 0:0 | hu.MAP2 |
Isolation & Detection Technology
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| Differential UltracentrifugationSize Exclusion Chromatography | R Sequencing | 1 | 30646616 |
Sequence, Structure & Domains
Sequences
Length
1,250
Mass
140,525
Sequence
MWLSPEEVLVANALWVTERANPFFVLQRRRGHGRGGGLTGLLVGTLDVVLDSSARVAPYRILHQTQDSQVYWTVACGSSRKEITKHWEWLENNLLQTLSIFDSEEDITTFVKGKIHGIIAEENKNLQPQGDEDPGKFKEAELKMRKQFGMPEGEKLVNYYSCSYWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEKNATLLFPESIRVDTRDQELFFSMFLNIGETFKLMEQLANLAMRQLLDSEGFLEDKALPRPIRPHRNISALKRDLDARAKNECYRATFRLPRDERLDGHTSCTLWTPFNKLHIPGQMFISNNYICFASKEEDACHLIIPLREVTIVEKADSSSVLPSPLSISTKSKMTFLFANLKDRDFLVQRISDFLQKTPSKQPGSIGSRKASVVDPSTESSPAPQEGSEQPASPASPLSSRQSFCAQEAPTASQGLLKLFQKNSPMEDLGAKGAKEKMKEESWHIHFFEYGRGVCMYRTAKTRALVLKGIPESLRGELWLLFSGAWNEMVTHPGYYAELVEKSTGKYSLATEEIERDLHRSMPEHPAFQNELGIAALRRVLTAYAFRNPTIGYCQAMNIVTSVLLLYGSEEEAFWLLVALCERMLPDYYNTRVVGALVDQGIFEELTRDFLPQLSEKMQDLGVISSISLSWFLTLFLSVMPFESAVVIVDCFFYEGIKVILQVALAVLDANMEQLLGCSDEGEAMTMLGRYLDNVVNKQSVSPPIPHLRALLSSSDDPPAEVDIFELLKVSYEKFSSLRAEDIEQMRFKQRLKVIQSLEDTAKRSVVRAIPVDIGFSIEELEDLYMVFKAKHLASQYWGCSRTMAGRRDPSLPYLEQYRIDASQFRELFASLTPWACGSHTPLLAGRMFRLLDENKDSLINFKEFVTGMSGMYHGDLTEKLKVLYKLHLPPALSPEEAESALEAAHYFTEDSSSEASPLASDLDLFLPWEAQEALPQEEQEGSGSEERGEEKGTSSPDYRHYLRMWAKEKEAQKETIKDLPKMNQEQFIELCKTLYNMFSEDPMEQDLYHAIATVASLLLRIGEVGKKFSARTGRKPRDCATEEDEPPAPELHQDAARELQPPAAGDPQAKAGGDTHLGKAPQESQVVVEGGSGEGQGSPSQLLSDDETKDDMSMSSYSVVSTGSLQCEDLADDTVLVGGEACSPTARIGGTVDTDWCISFEQILASILTESVLVNFFEKRVDIGLKIKDQKKVERQFSTASDHEQPGVSG
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q66K14-1; Sequence=Displayed; Name=2; IsoId=Q66K14-2; Sequence=VSP_025699
Alternative Sequence
955..971; Missing (in isoform 2)
3D Structural Models
Domain & Motif Annotations
Compositional Bias
414..443; Polar residues; 984..999; Basic and acidic residues
Domain (CC)
The arginine and glutamine fingers are critical for the GTPase-activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site.
Domain (FT)
142..209; GRAM 1; 288..356; GRAM 2; 508..695; Rab-GAP TBC; 879..914; EF-hand
Region
397..443; Disordered; 974..999; Disordered; 1069..1093; Disordered; 1128..1157; Disordered
Clinical Relevance
Antibody