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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P12107: Variant p.Gly1516Val

Collagen alpha-1(XI) chain
Gene: COL11A1
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Variant information Variant position: help 1516 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Glycine (G) to Valine (V) at position 1516 (G1516V, p.Gly1516Val). 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: help Change from glycine (G) to medium size and hydrophobic (V) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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: help In STL2; overlapping phenotype with Marshall syndrome. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 1516 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1806 The length of the canonical sequence.
Location on the sequence: help PLGPPGPPGLPGPQGPKGNK G STGPAGQKGDSGLPGPPGSP 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         PLGPPGPPGLPGPQGPKGNKGSTGPAGQKGDSGLPGPPGSP

Mouse                         PIGPPGPPGLPGPAGPKGNKGSSGPTGQKGDSGMPGPPGPP

Rat                           PIGPPGPPGLPGPAGPKGNKGSSGPTGQKGDSGMPGPPGPP
Sequence annotation in neighborhood: help 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 512 – 1563 Collagen alpha-1(XI) chain
Domain 1483 – 1541 Collagen-like 8
Region 527 – 1563 Disordered
Region 529 – 1542 Triple-helical region



Literature citations
Splicing mutations of 54-bp exons in the COL11A1 gene cause Marshall syndrome, but other mutations cause overlapping Marshall/Stickler phenotypes.
Annunen S.; Koerkkoe J.; Czarny M.; Warman M.L.; Brunner H.G.; Kaeaeriaeinen H.; Mulliken J.B.; Tranebjaerg L.; Brooks D.G.; Cox G.F.; Cruysberg J.R.; Curtis M.A.; Davenport S.L.H.; Friedrich C.A.; Kaitila I.; Krawczynski M.R.; Latos-Bielenska A.; Mukai S.; Olsen B.R.; Shinno N.; Somer M.; Vikkula M.; Zlotogora J.; Prockop D.J.; Ala-Kokko L.;
Am. J. Hum. Genet. 65:974-983(1999)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; ALTERNATIVE SPLICING (ISOFORMS A; B AND C); VARIANTS STL2/MARSHALL SYNDROME ARG-676; 921-GLN--PRO-926 DEL; 1313-PHE--GLY-1315 DEL; LEU-1323; VAL-1516 AND PRO-1535; Stickler syndrome and the vitreous phenotype: mutations in COL2A1 and COL11A1.
Richards A.J.; McNinch A.; Martin H.; Oakhill K.; Rai H.; Waller S.; Treacy B.; Whittaker J.; Meredith S.; Poulson A.; Snead M.P.;
Hum. Mutat. 31:E1461-E1471(2010)
Cited for: VARIANTS STL2 VAL-565; ARG-1027; 1110-VAL--PRO-1118 DEL; ASP-1513 AND VAL-1516;
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.