Variant position: 305 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 367 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 AYMNFYYKSTEGWSIGNVLL DFTGGSFSLLQMFLQSYNNDQ
Mouse AYMNFYYKSTKGWSIGGVLL DFTGGSFSLLQMFLQSYNNDQ
Bovine AYMNFHYKSTEGWSIGNVLL DFTGGSFSLLQMFLQSYNNDQ
Caenorhabditis elegans AYFNYTRKSTVGWSIGNIML DFTGGTLDILQMILQAVNVND
Drosophila ALMNYRRKSTSGWSIGNILL DFTGGTLSMLQMILNAHNYDD
Slime mold AYLNFKNKSTSGWSVHNVLL DFSGGVLSLLQMFLDVADSGN
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
23 – 367 Cystinosin
298 – 318 Helical
263 – 328 PQ-loop 2
305 – 305 H(+); protonated following cystine-binding
305 – 305 D -> E. Abolished steady-state transport current.
305 – 305 D -> N. Abolished transient cxurrents. Abolished steady-state transport current.
309 – 309 G -> CS. Gain-of-function mutant that shows higher transport of cystine.
312 – 312 S -> N. Gain-of-function mutant that shows higher transport of cystine.
Severity of phenotype in cystinosis varies with mutations in the CTNS gene: predicted effect on the model of cystinosin.
Attard M.; Jean G.; Forestier L.; Cherqui S.; van 't Hoff W.; Broyer M.; Antignac C.; Town M.;
Hum. Mol. Genet. 8:2507-2514(1999)
Cited for: VARIANTS CTNS PHE-139; ASP-205 DEL; SER-270 DEL; TYR-305; ARG-308; PRO-338; ARG-339; 343-ILE--ASP-346 DEL AND ASN-346; VARIANT ILE-42; VARIANT CTNSJAN PRO-CYS-SER-154 INS;
Molecular pathogenesis of cystinosis: effect of CTNS mutations on the transport activity and subcellular localization of cystinosin.
Kalatzis V.; Nevo N.; Cherqui S.; Gasnier B.; Antignac C.;
Hum. Mol. Genet. 13:1361-1371(2004)
Cited for: FUNCTION; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS CTNS VAL-110; PHE-133; PHE-139; PHE-141; PRO-158; ASP-169; SER-177; ARG-182; ASN-205; ASP-205 DEL; ARG-222; SER-270 DEL; LYS-288; ASN-298; TYR-305; ARG-308; PRO-338; ARG-339; 343-ILE--ASP-346 DEL; ASP-346--349-PHE DEL AND ASP-VAL-GLU-PHE-349 INS; CHARACTERIZATION OF VARIANT CTNSJAN 67-ILE--PRO-73 DEL; PRO-CYS-SER-154 INS; LEU-200; ARG-280; LYS-323 AND ASN-346; CHARACTERIZATION OF VARIANT CTNSANN ARG-197; CHARACTERIZATION OF VARIANT ILE-42 AND ILE-260;
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.