Variant position: 323 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 LLDFTGGSFSLLQMFLQSYN NDQWTLIFGDPTKFGLGVFSI
Mouse LLDFTGGSFSLLQMFLQSYN NDQWTLIFGDPTKFGLGVFTI
Bovine LLDFTGGSFSLLQMFLQSYN NDQWTLIFGDPTKFGLGIFSI
Caenorhabditis elegans MLDFTGGTLDILQMILQAVN VNDWSAFYANPVKFGLGFVSI
Drosophila LLDFTGGTLSMLQMILNAHN YDDWVSIFGDPTKFGLGLFSV
Slime mold LLDFSGGVLSLLQMFLDVAD SGNWNIFTGDPVKLGLSLFSI
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
319 – 335 Lumenal
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.
335 – 335 K -> Q. Abolished steady-state transport current. Decreased midpoint potential. Impaired dielectric distance. Accelerated the time course.
Mutations of CTNS causing intermediate cystinosis.
Thoene J.; Lemons R.; Anikster Y.; Mullet J.; Paelicke K.; Lucero C.; Gahl W.A.; Schneider J.; Shu S.G.; Campbell H.T.;
Mol. Genet. Metab. 67:283-293(1999)
Cited for: VARIANTS CTNSJAN ARG-280 AND LYS-323;
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;
Two novel CTNS mutations in cystinosis patients in Thailand.
Yeetong P.; Tongkobpetch S.; Kingwatanakul P.; Deekajorndech T.; Bernardini I.M.; Suphapeetiporn K.; Gahl W.A.; Shotelersuk V.;
Cited for: VARIANTS CTNS ASP-309 AND LYS-323;
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