UniProtKB/Swiss-Prot P08123: Variant p.Gln1354His

Collagen alpha-2(I) chain
Gene: COL1A2
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Variant information Variant position:

1354 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B The variants are classified into three categories: LP/P, LB/B and US.

LP/P: likely pathogenic or pathogenic.
LB/B: likely benign or benign.
US: uncertain significance

Residue change:

From Glutamine (Q) to Histidine (H) at position 1354 (Q1354H, p.Gln1354His). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties:

Similar physico-chemical property. Both residues are medium size and polar. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

0 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:

Lowest score: -4 (low probability of substitution).
Highest score: 11 (high probability of substitution).

More information can be found on the following page
Other resources:

Links to websites of interest for the variant.

Variant rs418570 [ dbSNP | Ensembl ]

Sequence information Variant position:

1354 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

1366 The length of the canonical sequence.
Location on the sequence:

NKPSRLPFLDIAPLDIGGAD Q EFFVDIGPVCFK 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                         NKPSRLPFLDIAPLDIGGADQEFFVDIGPVCFK

                              NKPSRLPILDIAPLDIGDADQEFRVDVGPVCFK

Mouse                         NKPSRLPFLDIAPLDIGGADQEFRVEVGPVCFK

Rat                           NKPSRLPFLDIAPLDIGGTNQEFRVEVGPVCFK

Bovine                        NKPSRLPILDIAPLDIGGADQEIRLNIGPVCFK

Chicken                       NKPSRLPILDIAPLDIGGADQEFGLHIGPVCFK

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
Propeptide	1120 – 1366	C-terminal propeptide
Domain	1133 – 1366	Fibrillar collagen NC1
Disulfide bond	1203 – 1364

Literature citations
Organization of the human pro-alpha 2(I) collagen gene.
de Wet W.J.; Bernard M.P.; Benson-Chanda V.; Chu M.-L.; Dickson L.A.; Weil D.; Ramirez F.;
J. Biol. Chem. 262:16032-16036(1987)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANTS ASN-249; THR-276; VAL-483; ALA-549; HIS-678; GLY-743; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354; The human type I collagen mutation database.
Dalgleish R.;
Nucleic Acids Res. 25:181-187(1997)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; REVIEW ON OI VARIANTS; VARIANTS ALA-549; HIS-678 AND HIS-1354; Analysis of the COL1A1 and COL1A2 genes by PCR amplification and scanning by conformation-sensitive gel electrophoresis identifies only COL1A1 mutations in 15 patients with osteogenesis imperfecta type I: identification of common sequences of null-allele mutations.
Korkko J.M.; Ala-Kokko L.; De Paepe A.; Nuytinck L.; Earley J.J.; Prockop D.J.;
Am. J. Hum. Genet. 62:98-110(1998)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS ILE-270; VAL-483; HIS-678; GLY-743; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354; Structure of a cDNA for the pro alpha 2 chain of human type I procollagen. Comparison with chick cDNA for pro alpha 2(I) identifies structurally conserved features of the protein and the gene.
Bernard M.P.; Myers J.C.; Chu M.-L.; Ramirez F.; Eikenberry E.F.; Prockop D.J.;
Biochemistry 22:1139-1145(1983)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 623-1366; VARIANTS HIS-678; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354; Growth-dependent modulation of type I collagen production and mRNA levels in cultured human skin fibroblasts.
Maekelae J.K.; Vuorio T.; Vuorio E.;
Biochim. Biophys. Acta 1049:171-176(1990)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 960-1356; VARIANT HIS-1354; Analysis of the 3' end of the human pro-alpha 2(I) collagen gene. Utilization of multiple polyadenylation sites in cultured fibroblasts.
Myers J.C.; Dickson L.A.; de Wet W.J.; Bernard M.P.; Chu M.-L.; Di Liberto M.; Pepe G.; Sangiorgi F.O.; Ramirez F.;
J. Biol. Chem. 258:10128-10135(1983)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1319-1366; VARIANT HIS-1354; Osteogenesis imperfecta: cloning of a pro-alpha 2(I) collagen gene with a frameshift mutation.
Pihlajaniemi T.; Dickson L.A.; Pope F.M.; Korhonen V.R.; Nicholls A.; Prockop D.J.; Myers J.C.;
J. Biol. Chem. 259:12941-12944(1984)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1319-1366; VARIANT HIS-1354;

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