Q66K14 · TBC9B_HUMAN
- ProteinTBC1 domain family member 9B
- GeneTBC1D9B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1250 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 555 | Arginine finger | ||||
Sequence: R | ||||||
Site | 594 | Glutamine finger | ||||
Sequence: Q |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | calcium ion binding | |
Molecular Function | GTPase activator activity |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTBC1 domain family member 9B
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ66K14
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 668-688 | Helical | ||||
Sequence: LSWFLTLFLSVMPFESAVVIV |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_032440 | 240 | in dbSNP:rs1057078 | |||
Sequence: L → P | ||||||
Natural variant | VAR_032441 | 706 | in dbSNP:rs10037618 | |||
Sequence: V → I | ||||||
Natural variant | VAR_036196 | 1086 | in a breast cancer sample; somatic mutation | |||
Sequence: P → Q | ||||||
Natural variant | VAR_032442 | 1119 | in dbSNP:rs30386 | |||
Sequence: K → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,422 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000288501 | 1-1250 | UniProt | TBC1 domain family member 9B | |||
Sequence: MWLSPEEVLVANALWVTERANPFFVLQRRRGHGRGGGLTGLLVGTLDVVLDSSARVAPYRILHQTQDSQVYWTVACGSSRKEITKHWEWLENNLLQTLSIFDSEEDITTFVKGKIHGIIAEENKNLQPQGDEDPGKFKEAELKMRKQFGMPEGEKLVNYYSCSYWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEKNATLLFPESIRVDTRDQELFFSMFLNIGETFKLMEQLANLAMRQLLDSEGFLEDKALPRPIRPHRNISALKRDLDARAKNECYRATFRLPRDERLDGHTSCTLWTPFNKLHIPGQMFISNNYICFASKEEDACHLIIPLREVTIVEKADSSSVLPSPLSISTKSKMTFLFANLKDRDFLVQRISDFLQKTPSKQPGSIGSRKASVVDPSTESSPAPQEGSEQPASPASPLSSRQSFCAQEAPTASQGLLKLFQKNSPMEDLGAKGAKEKMKEESWHIHFFEYGRGVCMYRTAKTRALVLKGIPESLRGELWLLFSGAWNEMVTHPGYYAELVEKSTGKYSLATEEIERDLHRSMPEHPAFQNELGIAALRRVLTAYAFRNPTIGYCQAMNIVTSVLLLYGSEEEAFWLLVALCERMLPDYYNTRVVGALVDQGIFEELTRDFLPQLSEKMQDLGVISSISLSWFLTLFLSVMPFESAVVIVDCFFYEGIKVILQVALAVLDANMEQLLGCSDEGEAMTMLGRYLDNVVNKQSVSPPIPHLRALLSSSDDPPAEVDIFELLKVSYEKFSSLRAEDIEQMRFKQRLKVIQSLEDTAKRSVVRAIPVDIGFSIEELEDLYMVFKAKHLASQYWGCSRTMAGRRDPSLPYLEQYRIDASQFRELFASLTPWACGSHTPLLAGRMFRLLDENKDSLINFKEFVTGMSGMYHGDLTEKLKVLYKLHLPPALSPEEAESALEAAHYFTEDSSSEASPLASDLDLFLPWEAQEALPQEEQEGSGSEERGEEKGTSSPDYRHYLRMWAKEKEAQKETIKDLPKMNQEQFIELCKTLYNMFSEDPMEQDLYHAIATVASLLLRIGEVGKKFSARTGRKPRDCATEEDEPPAPELHQDAARELQPPAAGDPQAKAGGDTHLGKAPQESQVVVEGGSGEGQGSPSQLLSDDETKDDMSMSSYSVVSTGSLQCEDLADDTVLVGGEACSPTARIGGTVDTDWCISFEQILASILTESVLVNFFEKRVDIGLKIKDQKKVERQFSTASDHEQPGVSG | |||||||
Modified residue (large scale data) | 363 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 397 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 397 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 407 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 411 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 411 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 427 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 432 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 432 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 435 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 435 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 439 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 442 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 463 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 463 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 547 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 741 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 752 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 994 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 995 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1138 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1144 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1238 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1239 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1241 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1241 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1249 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q66K14-2 | GABARAPL2 P60520 | 3 | EBI-10217736, EBI-720116 | |
BINARY | Q66K14-2 | L3MBTL2 Q969R5 | 3 | EBI-10217736, EBI-739909 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 142-209 | GRAM 1 | ||||
Sequence: LKMRKQFGMPEGEKLVNYYSCSYWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEKNA | ||||||
Domain | 288-356 | GRAM 2 | ||||
Sequence: ECYRATFRLPRDERLDGHTSCTLWTPFNKLHIPGQMFISNNYICFASKEEDACHLIIPLREVTIVEKAD | ||||||
Region | 397-443 | Disordered | ||||
Sequence: TPSKQPGSIGSRKASVVDPSTESSPAPQEGSEQPASPASPLSSRQSF | ||||||
Domain | 508-695 | Rab-GAP TBC | ||||
Sequence: GIPESLRGELWLLFSGAWNEMVTHPGYYAELVEKSTGKYSLATEEIERDLHRSMPEHPAFQNELGIAALRRVLTAYAFRNPTIGYCQAMNIVTSVLLLYGSEEEAFWLLVALCERMLPDYYNTRVVGALVDQGIFEELTRDFLPQLSEKMQDLGVISSISLSWFLTLFLSVMPFESAVVIVDCFFYEG | ||||||
Domain | 879-914 | EF-hand | ||||
Sequence: HTPLLAGRMFRLLDENKDSLINFKEFVTGMSGMYHG | ||||||
Region | 974-999 | Disordered | ||||
Sequence: LPQEEQEGSGSEERGEEKGTSSPDYR | ||||||
Compositional bias | 980-999 | Basic and acidic residues | ||||
Sequence: EGSGSEERGEEKGTSSPDYR | ||||||
Compositional bias | 1069-1092 | Basic and acidic residues | ||||
Sequence: SARTGRKPRDCATEEDEPPAPELH | ||||||
Region | 1069-1093 | Disordered | ||||
Sequence: SARTGRKPRDCATEEDEPPAPELHQ | ||||||
Region | 1128-1157 | Disordered | ||||
Sequence: VEGGSGEGQGSPSQLLSDDETKDDMSMSSY | ||||||
Compositional bias | 1129-1143 | Polar residues | ||||
Sequence: EGGSGEGQGSPSQLL |
Domain
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q66K14-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length1,250
- Mass (Da)140,525
- Last updated2010-05-18 v3
- Checksum35D9E4914B1D8311
Q66K14-2
- Name2
- Differences from canonical
- 955-971: Missing
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YB58 | H0YB58_HUMAN | TBC1D9B | 65 | ||
H0YB08 | H0YB08_HUMAN | TBC1D9B | 166 | ||
G3V133 | G3V133_HUMAN | TBC1D9B | 409 | ||
E5RIN2 | E5RIN2_HUMAN | TBC1D9B | 100 | ||
A0AAG2TEQ7 | A0AAG2TEQ7_HUMAN | TBC1D9B | 100 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 893 | in Ref. 5; BAD97229 | ||||
Sequence: E → G | ||||||
Alternative sequence | VSP_025699 | 955-971 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 980-999 | Basic and acidic residues | ||||
Sequence: EGSGSEERGEEKGTSSPDYR | ||||||
Compositional bias | 1069-1092 | Basic and acidic residues | ||||
Sequence: SARTGRKPRDCATEEDEPPAPELH | ||||||
Compositional bias | 1129-1143 | Polar residues | ||||
Sequence: EGGSGEGQGSPSQLL | ||||||
Sequence conflict | 1231 | in Ref. 6; CAE46050 | ||||
Sequence: K → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB014576 EMBL· GenBank· DDBJ | BAA31651.1 EMBL· GenBank· DDBJ | mRNA | ||
AC008393 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC010285 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471165 EMBL· GenBank· DDBJ | EAW53780.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471165 EMBL· GenBank· DDBJ | EAW53782.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471165 EMBL· GenBank· DDBJ | EAW53777.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471165 EMBL· GenBank· DDBJ | EAW53779.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC008919 EMBL· GenBank· DDBJ | AAH08919.3 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC080659 EMBL· GenBank· DDBJ | AAH80659.1 EMBL· GenBank· DDBJ | mRNA | ||
AK223509 EMBL· GenBank· DDBJ | BAD97229.1 EMBL· GenBank· DDBJ | mRNA | ||
BX641107 EMBL· GenBank· DDBJ | CAE46050.1 EMBL· GenBank· DDBJ | mRNA |