TBCD

Protein identityUniProt · HPA

UniProt accession

Q9BTW9

Gene

TBCD

Ensembl

ENSG00000141556

Chromosome

17

Canonical length

1192 aa

Protein class

Disease related genes, Human disease related genes, Predicted intracellular proteins, Predicted membrane proteins

OverviewNCBI Gene

Cofactor D is one of four proteins (cofactors A, D, E, and C) involved in the pathway leading to correctly folded beta-tubulin from folding intermediates. Cofactors A and D are believed to play a role in capturing and stabilizing beta-tubulin intermediates in a quasi-native confirmation. Cofactor E binds to the cofactor D/beta-tubulin complex; interaction with cofactor C then causes the release of beta-tubulin polypeptides that are committed to the native state. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

1192 residues, UniProt reviewed canonical sequence.

>Q9BTW9|TBCD
     1  MALSDEPAAG GPEEEAEDET LAFGAALEAF GESAETRALL GRLREVHGGG AEREVALERF
    61  RVIMDKYQEQ PHLLDPHLEW MMNLLLDIVQ DQTSPASLVH LAFKFLYIIT KVRGYKTFLR
   121  LFPHEVADVE PVLDLVTIQN PKDHEAWETR YMLLLWLSVT CLIPFDFSRL DGNLLTQPGQ
   181  ARMSIMDRIL QIAESYLIVS DKARDAAAVL VSRFITRPDV KQSKMAEFLD WSLCNLARSS
   241  FQTMQGVITM DGTLQALAQI FKHGKREDCL PYAATVLRCL DGCRLPESNQ TLLRKLGVKL
   301  VQRLGLTFLK PKVAAWRYQR GCRSLAANLQ LLTQGQSEQK PLILTEDDDE DDDVPEGVER
   361  VIEQLLVGLK DKDTVVRWSA AKGIGRMAGR LPRALADDVV GSVLDCFSFQ ETDKAWHGGC
   421  LALAELGRRG LLLPSRLVDV VAVILKALTY DEKRGACSVG TNVRDAACYV CWAFARAYEP
   481  QELKPFVTAI SSALVIAAVF DRDINCRRAA SAAFQENVGR QGTFPHGIDI LTTADYFAVG
   541  NRSNCFLVIS VFIAGFPEYT QPMIDHLVTM KISHWDGVIR ELAARALHNL AQQAPEFSAT
   601  QVFPRLLSMT LSPDLHMRHG SILACAEVAY ALYKLAAQEN RPVTDHLDEQ AVQGLKQIHQ
   661  QLYDRQLYRG LGGQLMRQAV CVLIEKLSLS KMPFRGDTVI DGWQWLINDT LRHLHLISSH
   721  SRQQMKDAAV SALAALCSEY YMKEPGEADP AIQEELITQY LAELRNPEEM TRCGFSLALG
   781  ALPGFLLKGR LQQVLTGLRA VTHTSPEDVS FAESRRDGLK AIARICQTVG VKAGAPDEAV
   841  CGENVSQIYC ALLGCMDDYT TDSRGDVGTW VRKAAMTSLM DLTLLLARSQ PELIEAHTCE
   901  RIMCCVAQQA SEKIDRFRAH AASVFLTLLH FDSPPIPHVP HRGELEKLFP RSDVASVNWS
   961  APSQAFPRIT QLLGLPTYRY HVLLGLVVSL GGLTESTIRH STQSLFEYMK GIQSDPQALG
  1021  SFSGTLLQIF EDNLLNERVS VPLLKTLDHV LTHGCFDIFT TEEDHPFAVK LLALCKKEIK
  1081  NSKDIQKLLS GIAVFCEMVQ FPGDVRRQAL LQLCLLLCHR FPLIRKTTAS QVYETLLTYS
  1141  DVVGADVLDE VVTVLSDTAW DAELAVVREQ RNRLCDLLGV PRPQLVPQPG AC

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against TBCD can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Cell surface

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.24

Highest tissue expression

57 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about TBCD.

Disease | AllUniProt

Conditions TBCD is implicated in, by any mechanism.

• Encephalopathy, progressive, early-onset, with brain atrophy and thin corpus callosum (PEBAT) MIM:617193

Disease | GeneticClinVar

94 pathogenic / likely-pathogenic of 1,436 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Early-onset progressive diffuse brain atrophy-microcephaly-muscle weakness-optic atrophy syndrome
• TBCD-related disorder
• Hepatocellular carcinoma
• Inborn genetic diseases
• Nonpapillary renal cell carcinoma

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.49

gnomAD pLI

0

gnomAD missense Z

1.82

DepMap mean gene effect

-1.2

DepMap dependency class

common

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 7% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• adherens junction assembly
• bicellular tight junction assembly
• cell morphogenesis involved in neuron differentiation
• microtubule cytoskeleton organization
• mitotic cell cycle
• negative regulation of cell-substrate adhesion
• negative regulation of microtubule polymerization
• post-chaperonin tubulin folding pathway
• protein folding
• tubulin complex assembly

Molecular functions

• beta-tubulin binding
• GTPase activator activity
• protein-folding chaperone binding

Cellular components

• adherens junction
• bicellular tight junction
• centrosome
• cytoplasm
• lateral plasma membrane
• microtubule

Protein domainsUniProt · Pfam · InterPro

• Armadillo-like helical
• Armadillo-type fold
• Tubulin-folding cofactor D, C-terminal domain
• Tubulin-folding cofactor D
• Tubulin-folding cofactor D, ARM repeats
• Tubulin folding cofactor D C terminal
• Tubulin-specific chaperone D-like, ARM repeat
• Tubulin-specific chaperone D-like, ARM repeats

KeywordsUniProt

• Cell junction
• Cell membrane
• Chaperone
• Cytoplasm
• Cytoskeleton
• GTPase activation
• Membrane
• Neurodegeneration
• Repeat
• Tight junction

InteractionsUniProt · HPA

Protein binding partners of TBCD in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• ARL2
• PPP2CB
• TBCE