Q9P2M4 · TBC14_HUMAN
- ProteinTBC1 domain family member 14
- GeneTBC1D14
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids693 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a role in the regulation of starvation-induced autophagosome formation (PubMed:22613832).
Together with the TRAPPIII complex, regulates a constitutive trafficking step from peripheral recycling endosomes to the early Golgi, maintaining the cycling pool of ATG9 required for initiation of autophagy
Together with the TRAPPIII complex, regulates a constitutive trafficking step from peripheral recycling endosomes to the early Golgi, maintaining the cycling pool of ATG9 required for initiation of autophagy
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 | autophagosome | |
Cellular Component | cytosol | |
Cellular Component | Golgi apparatus | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | nucleoplasm | |
Cellular Component | recycling endosome | |
Molecular Function | GTPase activator activity | |
Molecular Function | protein kinase binding | |
Biological Process | autophagy | |
Biological Process | negative regulation of autophagy | |
Biological Process | recycling endosome to Golgi transport | |
Biological Process | regulation of autophagosome assembly |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTBC1 domain family member 14
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9P2M4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: After amino acid starvation, Golgi apparatus-associated protein levels increase compared with fed conditions. May be cycling between the Golgi apparatus and an endosomal pool, redistributing to the Golgi apparatus upon starvation.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_067442 | 41 | in dbSNP:rs34860182 | |||
Sequence: L → V | ||||||
Natural variant | VAR_059856 | 446 | in dbSNP:rs11731231 | |||
Sequence: E → Q | ||||||
Mutagenesis | 472 | Loss of inhibition of autophagosome formation; when associated with A-508. | ||||
Sequence: R → A | ||||||
Mutagenesis | 508 | Loss of inhibition of autophagosome formation; when associated with A-472. | ||||
Sequence: Q → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 814 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, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000208040 | 1-693 | UniProt | TBC1 domain family member 14 | |||
Sequence: MTDGKLSTSTNGVAFMGILDGRPGNPLQNLQHVNLKAPRLLSAPEYGPKLKLRALEDRHSLQSVDSGIPTLEIGNPEPVPCSAVHVRRKQSDSDLIPERAFQSACALPSCAPPAPSSTEREQSVRKSSTFPRTGYDSVKLYSPTSKALTRSDDVSVCSVSSLGTELSTTLSVSNEDILDLVVTSSSSAIVTLENDDDPQFTNVTLSSIKETRGLHQQDCVHEAEEGSKLKILGPFSNFFARNLLARKQSARLDKHNDLGWKLFGKAPLRENAQKDSKRIQKEYEDKAGRPSKPPSPKQNVRKNLDFEPLSTTALILEDRPANLPAKPAEEAQKHRQQYEEMVVQAKKRELKEAQRRKKQLEERCRVEESIGNAVLTWNNEILPNWETMWCSRKVRDLWWQGIPPSVRGKVWSLAIGNELNITHELFDICLARAKERWRSLSTGGSEVENEDAGFSAADREASLELIKLDISRTFPNLCIFQQGGPYHDMLHSILGAYTCYRPDVGYVQGMSFIAAVLILNLDTADAFIAFSNLLNKPCQMAFFRVDHGLMLTYFAAFEVFFEENLPKLFAHFKKNNLTPDIYLIDWIFTLYSKSLPLDLACRIWDVFCRDGEEFLFRTALGILKLFEDILTKMDFIHMAQFLTRLPEDLPAEELFASIATIQMQSRNKKWAQVLTALQKDSREMEKGSPSLRH | |||||||
Modified residue | 91 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 91 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 103 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 128 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 295 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 295 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 439 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 441 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 688 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with ULK1 (PubMed:22613832).
May interact with RAB11A and RAB11B, but does not exhibit any GTPase-activating activity toward these proteins (PubMed:22613832).
Interacts with TRAPPC8 (PubMed:26711178).
May interact with RAB11A and RAB11B, but does not exhibit any GTPase-activating activity toward these proteins (PubMed:22613832).
Interacts with TRAPPC8 (PubMed:26711178).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9P2M4 | NXF1 Q9UBU9 | 3 | EBI-2797718, EBI-398874 | |
BINARY | Q9P2M4 | RAB11B Q15907 | 2 | EBI-2797718, EBI-722234 | |
BINARY | Q9P2M4 | ULK1 O75385 | 4 | EBI-2797718, EBI-908831 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 108-130 | Disordered | ||||
Sequence: PSCAPPAPSSTEREQSVRKSSTF | ||||||
Compositional bias | 115-130 | Polar residues | ||||
Sequence: PSSTEREQSVRKSSTF | ||||||
Compositional bias | 271-291 | Basic and acidic residues | ||||
Sequence: NAQKDSKRIQKEYEDKAGRPS | ||||||
Region | 271-304 | Disordered | ||||
Sequence: NAQKDSKRIQKEYEDKAGRPSKPPSPKQNVRKNL | ||||||
Domain | 401-611 | Rab-GAP TBC | ||||
Sequence: GIPPSVRGKVWSLAIGNELNITHELFDICLARAKERWRSLSTGGSEVENEDAGFSAADREASLELIKLDISRTFPNLCIFQQGGPYHDMLHSILGAYTCYRPDVGYVQGMSFIAAVLILNLDTADAFIAFSNLLNKPCQMAFFRVDHGLMLTYFAAFEVFFEENLPKLFAHFKKNNLTPDIYLIDWIFTLYSKSLPLDLACRIWDVFCRDG |
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9P2M4-1
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
- Length693
- Mass (Da)78,137
- Last updated2008-02-26 v3
- Checksum6E1332D236DE45BD
Q9P2M4-2
- Name2
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB449900 EMBL· GenBank· DDBJ | BAH16643.1 EMBL· GenBank· DDBJ | mRNA | ||
AB037743 EMBL· GenBank· DDBJ | BAA92560.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC092463 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC097382 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC106045 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471131 EMBL· GenBank· DDBJ | EAW82375.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471131 EMBL· GenBank· DDBJ | EAW82376.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471131 EMBL· GenBank· DDBJ | EAW82377.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC041167 EMBL· GenBank· DDBJ | AAH41167.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL833868 EMBL· GenBank· DDBJ | CAD38726.1 EMBL· GenBank· DDBJ | mRNA |