Variant position: 280 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 TTWLQFLFCFSYIKLAVTLV KYFPQAYMNFYYKSTEGWSIG
Mouse TTWLQFLFCFSYIKLIITLI KYFPQAYMNFYYKSTKGWSIG
Bovine TTWLQFLFCFSYIKLAVTLV KYFPQAYMNFHYKSTEGWSIG
Caenorhabditis elegans IQLLSFVTSLSYIKMAVTCC KYFPQAYFNYTRKSTVGWSIG
Drosophila IHWLDFLYYCSYVKLTITII KYVPQALMNYRRKSTSGWSIG
Slime mold FTWLWVINYYSYVKLFITFI KYIPQAYLNFKNKSTSGWSVH
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
262 – 282 Helical
263 – 328 PQ-loop 2
270 – 270 S -> T. Gain-of-function mutant that shows higher transport of cystine.
274 – 274 L -> F. Gain-of-function mutant that shows higher transport of cystine.
280 – 288 Missing. In delta(A) mutant; abolished localization to the lysosome; when associated with deletion of 362-G--L-366.
281 – 281 Y -> F. Decreased midpoint potential. 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;
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.