Variant position: 447 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 563 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 TKFLSSSPHLPPSS---YF--NASG RAYPDVAALSDGYWVVSNRVP
Chimpanzee TKFLSSSPHLPPSS---YF--NASG RAYPDVAALSDGYWVV
Mouse AQFLKSSSHLPPSS---YF--NASG RAYPDVAALSDGYWVV
Rat AQFLKSSSHLPPSS---YF--NASG RAYPDVAALSDGYWVV
Bovine TRYLSSSPHLPPSS---YF--NASG RAYPDVAALSDGYWVV
Zebrafish RAYLKSVQSLPPQT---YF--NTTG RAYPDLAALSDNYWVV
Slime mold SSYIEWLNG-SLSS---FY--NQSG RGFPDISSFSENVVIL
Baker's yeast -----------------YYCGDAAG RK----KDFSDSDIKF
Fission yeast RNWMDDIKGLGLSAEHGSFVRKPHS TTWINLAELLDMSWKK
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.
Mutational analysis of the defective protease in classic late-infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
Sleat D.E.; Gin R.M.; Sohar I.; Wisniewski K.; Sklower-Brooks S.; Pullarkat R.K.; Palmer D.N.; Lerner T.J.; Boustany R.-M.N.; Uldall P.; Siakotos A.N.; Donnelly R.J.; Lobel P.;
Am. J. Hum. Genet. 64:1511-1523(1999)
Cited for: VARIANTS CLN2 ARG-77; ASN-287; LYS-343; ARG-365; TYR-365; ASP-385; GLU-389; HIS-422; HIS-447; GLU-454 AND LEU-475; VARIANT ARG-100;
Expression and analysis of CLN2 variants in CHO cells: Q100R represents a polymorphism, and G389E and R447H represent loss-of-function mutations.
Lin L.; Lobel P.;
Hum. Mutat. 18:165-165(2001)
Cited for: CHARACTERIZATION OF VARIANTS ARG-100; GLU-389 AND HIS-447;
Functional consequences and rescue potential of pathogenic missense mutations in tripeptidyl peptidase I.
Walus M.; Kida E.; Golabek A.A.;
Hum. Mutat. 31:710-721(2010)
Cited for: VARIANT CLN2 SER-544; CHARACTERIZATION OF VARIANTS CLN2 ARG-77; GLN-127; LEU-202; CYS-206; MET-277; VAL-284; SER-286; ASN-287; LYS-343; ARG-365; HIS-422; HIS-447; LEU-475 AND SER-544;
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.