Q9P2M4 · TBC14_HUMAN

  • Protein
    TBC1 domain family member 14
  • Gene
    TBC1D14
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentautophagosome
Cellular Componentcytosol
Cellular ComponentGolgi apparatus
Cellular Componentintracellular membrane-bounded organelle
Cellular Componentnucleoplasm
Cellular Componentrecycling endosome
Molecular FunctionGTPase activator activity
Molecular Functionprotein kinase binding
Biological Processautophagy
Biological Processnegative regulation of autophagy
Biological Processrecycling endosome to Golgi transport
Biological Processregulation of autophagosome assembly

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    TBC1 domain family member 14

Gene names

    • Name
      TBC1D14
    • Synonyms
      KIAA1322

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9P2M4
  • Secondary accessions
    • B9A6L5
    • D3DVT4
    • E9PAZ6
    • Q8IW15
    • Q8NDK3

Proteomes

Organism-specific databases

Subcellular Location

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

Disease & Variants

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variantVAR_06744241in dbSNP:rs34860182
Natural variantVAR_059856446in dbSNP:rs11731231
Mutagenesis472Loss of inhibition of autophagosome formation; when associated with A-508.
Mutagenesis508Loss of inhibition of autophagosome formation; when associated with A-472.

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.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00002080401-693UniProtTBC1 domain family member 14
Modified residue91UniProtPhosphoserine
Modified residue (large scale data)91PRIDEPhosphoserine
Modified residue (large scale data)103PRIDEPhosphoserine
Modified residue (large scale data)128PRIDEPhosphoserine
Modified residue295UniProtPhosphoserine
Modified residue (large scale data)295PRIDEPhosphoserine
Modified residue (large scale data)439PRIDEPhosphoserine
Modified residue (large scale data)441PRIDEPhosphoserine
Modified residue (large scale data)688PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

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).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9P2M4NXF1 Q9UBU93EBI-2797718, EBI-398874
BINARY Q9P2M4RAB11B Q159072EBI-2797718, EBI-722234
BINARY Q9P2M4ULK1 O753854EBI-2797718, EBI-908831

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region108-130Disordered
Compositional bias115-130Polar residues
Compositional bias271-291Basic and acidic residues
Region271-304Disordered
Domain401-611Rab-GAP TBC

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

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.

  • Length
    693
  • Mass (Da)
    78,137
  • Last updated
    2008-02-26 v3
  • Checksum
    6E1332D236DE45BD
MTDGKLSTSTNGVAFMGILDGRPGNPLQNLQHVNLKAPRLLSAPEYGPKLKLRALEDRHSLQSVDSGIPTLEIGNPEPVPCSAVHVRRKQSDSDLIPERAFQSACALPSCAPPAPSSTEREQSVRKSSTFPRTGYDSVKLYSPTSKALTRSDDVSVCSVSSLGTELSTTLSVSNEDILDLVVTSSSSAIVTLENDDDPQFTNVTLSSIKETRGLHQQDCVHEAEEGSKLKILGPFSNFFARNLLARKQSARLDKHNDLGWKLFGKAPLRENAQKDSKRIQKEYEDKAGRPSKPPSPKQNVRKNLDFEPLSTTALILEDRPANLPAKPAEEAQKHRQQYEEMVVQAKKRELKEAQRRKKQLEERCRVEESIGNAVLTWNNEILPNWETMWCSRKVRDLWWQGIPPSVRGKVWSLAIGNELNITHELFDICLARAKERWRSLSTGGSEVENEDAGFSAADREASLELIKLDISRTFPNLCIFQQGGPYHDMLHSILGAYTCYRPDVGYVQGMSFIAAVLILNLDTADAFIAFSNLLNKPCQMAFFRVDHGLMLTYFAAFEVFFEENLPKLFAHFKKNNLTPDIYLIDWIFTLYSKSLPLDLACRIWDVFCRDGEEFLFRTALGILKLFEDILTKMDFIHMAQFLTRLPEDLPAEELFASIATIQMQSRNKKWAQVLTALQKDSREMEKGSPSLRH

Q9P2M4-2

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C9J541C9J541_HUMANTBC1D1456
C9JP26C9JP26_HUMANTBC1D14127
B9A071B9A071_HUMANTBC1D14465
H7BZD7H7BZD7_HUMANTBC1D14200
F5GXK4F5GXK4_HUMANTBC1D14353

Sequence caution

The sequence AAH41167.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence BAA92560.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

Showing features for alternative sequence, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_0414601-280in isoform 2
Compositional bias115-130Polar residues
Compositional bias271-291Basic and acidic residues
Alternative sequenceVSP_041461281in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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