Home  |  Contact

UniProtKB/Swiss-Prot P02452: Variant p.Gly530Ser

Collagen alpha-1(I) chain
Gene: COL1A1
Variant information

Variant position:  530
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LP/P [Disclaimer]
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 Glycine (G) to Serine (S) at position 530 (G530S, p.Gly530Ser).
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:  Change from glycine (G) to small size and polar (S)
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

Variant description:  In OI2, OI3 and OI4; mild to lethal form.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  530
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  1464
The length of the canonical sequence.

Location on the sequence:   ERGSPGPAGPKGSPGEAGRP  G EAGLPGAKGLTGSPGSPGPD
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                         ERGSPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPD

                              ERGSPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPD

Mouse                         ERGAPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPD

Rat                           ERGSPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPD

Bovine                        ERGAPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPD

Chicken                       ERGSPGAVGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPD

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.

TypePositionsDescription
Chain 162 – 1218 Collagen alpha-1(I) chain
Region 179 – 1192 Triple-helical region
Modified residue 514 – 514 4-hydroxyproline
Modified residue 523 – 523 4-hydroxyproline
Modified residue 529 – 529 4-hydroxyproline
Modified residue 535 – 535 4-hydroxyproline
Modified residue 544 – 544 4-hydroxyproline
Modified residue 547 – 547 4-hydroxyproline


Literature citations

Moderately severe osteogenesis imperfecta associated with substitutions of serine for glycine in the alpha 1(I) chain of type I collagen.
Marini J.C.; Lewis M.B.; Chen K.J.;
Am. J. Med. Genet. 45:241-245(1993)
Cited for: VARIANT OI3 SER-530;

An RT-PCR-SSCP screening strategy for detection of mutations in the gene encoding the alpha 1 chain of type I collagen: application to four patients with osteogenesis imperfecta.
Mackay K.; Byers P.H.; Dalgleish R.;
Hum. Mol. Genet. 2:1155-1160(1993)
Cited for: VARIANTS OI2 SER-425 AND SER-530; VARIANT OI4 SER-560; VARIANT OI3 SER-719; VARIANT ALA-823;

Serine for glycine substitutions in type I collagen in two cases of type IV osteogenesis imperfecta (OI). Additional evidence for a regional model of OI pathophysiology.
Marini J.C.; Lewis M.B.; Wang Q.; Chen K.J.; Orrison B.M.;
J. Biol. Chem. 268:2667-2673(1993)
Cited for: VARIANT OI4 SER-530;

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.