Variant position: 229 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1192 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human VLVSRFITRPDVKQSKMAEF LDWSLCNL---------ARSSFQTMQGVIT
Mouse VLVSKFITRPDVKQRKMASF LDWSLCTL---------AHSS
Bovine VLVSKFVTRPDVKQKKMASF LDWSLCTL---------ARSS
Chicken VLVSKFIVRPDVRQKRMADF LDWTLSML---------SKSS
Caenorhabditis elegans LVIAHCLSRTD-GIPKVLSF LSRLLDSI-----------KT
Slime mold ELLSKLLNRPDMKFEQ-KQF IKWCTNSIQLISNNNNNNNQN
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
1 – 1192 Tubulin-specific chaperone D
1 – 1008 Missing. In isoform 2.
1 – 546 Missing. In isoform 3.
Biallelic mutations in TBCD, encoding the tubulin folding cofactor D, perturb microtubule dynamics and cause early-onset encephalopathy.
Flex E.; Niceta M.; Cecchetti S.; Thiffault I.; Au M.G.; Capuano A.; Piermarini E.; Ivanova A.A.; Francis J.W.; Chillemi G.; Chandramouli B.; Carpentieri G.; Haaxma C.A.; Ciolfi A.; Pizzi S.; Douglas G.V.; Levine K.; Sferra A.; Dentici M.L.; Pfundt R.R.; Le Pichon J.B.; Farrow E.; Baas F.; Piemonte F.; Dallapiccola B.; Graham J.M. Jr.; Saunders C.J.; Bertini E.; Kahn R.A.; Koolen D.A.; Tartaglia M.;
Am. J. Hum. Genet. 99:962-973(2016)
Cited for: FUNCTION; SUBCELLULAR LOCATION; INTERACTION WITH BETA TUBULIN; INVOLVEMENT IN PEBAT; VARIANTS PEBAT ARG-229; MET-374; GLN-377; THR-626; MET-994; MET-1105 AND LEU-1122; CHARACTERIZATION OF VARIANTS PEBAT MET-374; GLN-377; THR-626 AND LEU-1122;
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.