Sequence information
Variant position: 432 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 476 The length of the canonical sequence.
Location on the sequence:
GNGSGSSSSGGSSGGSGFCA
V RANGLYPVANNRNAFWHCVN
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 GNGSGSSSSGGSSGGSGFCAV RANGLYPVANNRNAFWHCVN
Mouse GSGSGGGSSGGSSGGSGFCAD KADGLYPVADDRNAFWQCIN
Rat GSGSGGGSSGGGSEGSGFCAG KADGLYPVADDRNAFWHCIN
Bovine GNESGSGNKSSSSEGRGYCAG KADGLYPVADNRNAFWNCVN
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
Chain
22 – 476
Acidic mammalian chitinase
Domain
427 – 476
Chitin-binding type-2
Literature citations
Isolation and mapping of a human lung-specific gene, TSA1902, encoding a novel chitinase family member.
Saito A.; Ozaki K.; Fujiwara T.; Nakamura Y.; Tanigami A.;
Gene 239:325-331(1999)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3); VARIANTS VAL-339 AND GLY-432;
Differential enzymatic activity of common haplotypic versions of the human acidic mammalian chitinase protein.
Seibold M.A.; Reese T.A.; Choudhry S.; Salam M.T.; Beckman K.; Eng C.; Atakilit A.; Meade K.; Lenoir M.; Watson H.G.; Thyne S.; Kumar R.; Weiss K.B.; Grammer L.C.; Avila P.; Schleimer R.P.; Fahy J.V.; Rodriguez-Santana J.; Rodriguez-Cintron W.; Boot R.G.; Sheppard D.; Gilliland F.D.; Locksley R.M.; Burchard E.G.;
J. Biol. Chem. 284:19650-19658(2009)
Cited for: VARIANTS ASP-45; ASN-47; MET-61; ARG-102; ARG-125; VAL-339; SER-354 AND GLY-432; CATALYTIC ACTIVITY; FUNCTION; CHARACTERIZATION OF VARIANTS ASP-45; ASN-47 AND MET-61;
Disclaimer:
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.