UniProtKB/Swiss-Prot P02461: Variant p.His1353Gln

Collagen alpha-1(III) chain
Gene: COL3A1
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Variant information Variant position:

1353 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 Histidine (H) to Glutamine (Q) at position 1353 (H1353Q, p.His1353Gln). 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 rs1516446 [ dbSNP | Ensembl ]

Sequence information Variant position:

1353 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

1466 The length of the canonical sequence.
Location on the sequence:

DGGFQFSYGNPELPEDVLDV H LAFLRLLSSRASQNITYHCK 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                         DGGFQFSYGNPELPEDVLDVHLAFLRLLSSRASQNITYHCK

Mouse                         NGGFQFSYGPPDLPEDVVDVQLAFLRLLSSRASQNITYHCK

Rat                           NGGFQFSYGNPDLPEDVLDVQLAFLRLLSSRASQNITYHCK

Bovine                        -----------------------------------------

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	1222 – 1466	C-terminal propeptide
Domain	1232 – 1466	Fibrillar collagen NC1
Disulfide bond	1302 – 1464
Helix	1347 – 1360

Literature citations
Structure of cDNA clones coding for the entire prepro alpha 1 (III) chain of human type III procollagen. Differences in protein structure from type I procollagen and conservation of codon preferences.
Ala-Kokko L.; Kontusaari S.; Baldwin C.T.; Kuivaniemi H.; Prockop D.J.;
Biochem. J. 260:509-516(1989)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANT GLN-1353; Genomic organization of the human COL3A1 and COL5A2 genes: COL5A2 has evolved differently than the other minor fibrillar collagen genes.
Valkkila M.; Melkoniemi M.; Kvist L.; Kuivaniemi H.; Tromp G.; Ala-Kokko L.;
Matrix Biol. 20:357-366(2001)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1); VARIANT GLN-1353; Submission
Mural R.J.; Istrail S.; Sutton G.G.; Florea L.; Halpern A.L.; Mobarry C.M.; Lippert R.; Walenz B.; Shatkay H.; Dew I.; Miller J.R.; Flanigan M.J.; Edwards N.J.; Bolanos R.; Fasulo D.; Halldorsson B.V.; Hannenhalli S.; Turner R.; Yooseph S.; Lu F.; Nusskern D.R.; Shue B.C.; Zheng X.H.; Zhong F.; Delcher A.L.; Huson D.H.; Kravitz S.A.; Mouchard L.; Reinert K.; Remington K.A.; Clark A.G.; Waterman M.S.; Eichler E.E.; Adams M.D.; Hunkapiller M.W.; Myers E.W.; Venter J.C.;
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]; VARIANT GLN-1353; The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
The MGC Project Team;
Genome Res. 14:2121-2127(2004)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2); VARIANT GLN-1353; Human pro alpha 1(III) collagen: cDNA sequence for the 3' end.
Mankoo B.S.; Dalgleish R.;
Nucleic Acids Res. 16:2337-2337(1988)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 950-1466 (ISOFORM 1); VARIANT GLN-1353; Isolation of cDNA and genomic clones encoding human pro-alpha 1 (III) collagen. Partial characterization of the 3' end region of the gene.
Chu M.-L.; Weil D.; de Wet W.J.; Bernard M.P.; Sippola M.; Ramirez F.;
J. Biol. Chem. 260:4357-4363(1985)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1122-1466 (ISOFORMS 1/2); VARIANT GLN-1353; Natural variation in four human collagen genes across an ethnically diverse population.
Chan T.F.; Poon A.; Basu A.; Addleman N.R.; Chen J.; Phong A.; Byers P.H.; Klein T.E.; Kwok P.Y.;
Genomics 91:307-314(2008)
Cited for: VARIANTS THR-679; THR-698; VAL-1205 AND GLN-1353;

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