Variant position: 604 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 2768 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 AISVPEDVARDLGDVMETVL SSQTCEQTPERLFVPSCTTEG
Mouse AVSVPEDIARDLGDVMEMVF SAQACKQMPGKFFVPSCTAGG
Rat AVSVPEDRARDLGDVMEMVF SAQACKQTSGRFFVPSCTAEG
Bovine AISVPEDIARDLGDVMEMVF SSQGCGQAPGSLFVPACTAEG
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
20 – 2768 Thyroglobulin
Primary structure of human thyroglobulin deduced from the sequence of its 8448-base complementary DNA.
Malthiery Y.; Lissitzky S.;
Eur. J. Biochem. 165:491-498(1987)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS ASP-604; ASP-653; GLN-985 DEL; TYR-1043; THR-1059; GLY-1312; ARG-1437; HIS-1463; THR-1936; GLU-2091; LEU-2149; ARG-2170 AND HIS-2242;
Sequence of the 5'-end quarter of the human-thyroglobulin messenger ribonucleic acid and of its deduced amino-acid sequence.
Malthiery Y.; Lissitzky S.;
Eur. J. Biochem. 147:53-58(1985)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-730; VARIANTS ASP-604 AND ASP-653;
Two novel cysteine substitutions (C1263R and C1995S) of thyroglobulin cause a defect in intracellular transport of thyroglobulin in patients with congenital goiter and the variant type of adenomatous goiter.
Hishinuma A.; Takamatsu J.; Ohyama Y.; Yokozawa T.; Kanno Y.; Kuma K.; Yoshida S.; Matsuura N.; Ieiri T.;
J. Clin. Endocrinol. Metab. 84:1438-1444(1999)
Cited for: VARIANTS TDH3 ARG-1264 AND SER-1996; VARIANTS HIS-135; ASP-604; ASP-653; ALA-734; GLU-830; GLN-985 DEL; VAL-1028; TYR-1043; THR-1059; ARG-1437; HIS-1463; ASN-1838; THR-1936; TRP-1999; GLU-2091; LEU-2149; ARG-2170; HIS-2242; ARG-2501 AND GLN-2530;
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