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UniProtKB/Swiss-Prot P08185: Variant p.Asp389Asn

Corticosteroid-binding globulin
Gene: SERPINA6
Variant information

Variant position:  389
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Aspartate (D) to Asparagine (N) at position 389 (D389N, p.Asp389Asn).
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 medium size and acidic (D) to medium size and polar (N)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  1
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 CBG deficiency; Lyon; decreased cortisol-binding affinity.
Any additional useful information about the variant.

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



Sequence information

Variant position:  389
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  405
The length of the canonical sequence.

Location on the sequence:   NLTSKPIILRFNQPFIIMIF  D HFTWSSLFLARVMNPV
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                         NLTSKPIILRFNQPFIIMIFDHFTWSSLFLARVMNPV--------------------------

Mouse                         HLPSESFTLKYNRPFIFLAFDKYTWSSLMMSQVMNPA

Rat                           HLRSEPLDIKFNKPFILLLFDKFTWSSLMMSQVVNPA

Pig                           HAAPKPVTVHFNRPFIVMVFDHFTWSSLFLGKIVNLT

Bovine                        SAAPGPLTLRFNRPFIIMIFDDFTWSSLFLGKVVNPT

Rabbit                        QLVSEPLTLNFNRPFLILIFDDFTWSSLFLGKVVIPA

Sheep                         TAAPGPLTLRFNRPFIIMIFDDFTWSSLFLGKVVNPT

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 23 – 405 Corticosteroid-binding globulin
Binding site 390 – 390 Corticosteroid
Binding site 393 – 393 Corticosteroid
Glycosylation 369 – 369 N-linked (GlcNAc...) asparagine
Beta strand 383 – 389


Literature citations

Novel human corticosteroid-binding globulin variant with low cortisol-binding affinity.
Emptoz-Bonneton A.; Cousin P.; Seguchi K.; Avvakumov G.V.; Bully C.; Hammond G.L.; Pugeat M.;
J. Clin. Endocrinol. Metab. 85:361-367(2000)
Cited for: VARIANT CBG DEFICIENCY ASN-389;

Haploinsufficiency of the SERPINA6 gene is associated with severe muscle fatigue: A de novo mutation in corticosteroid-binding globulin deficiency.
Buss C.; Schuelter U.; Hesse J.; Moser D.; Phillips D.I.; Hellhammer D.; Meyer J.;
J. Neural Transm. 114:563-569(2007)
Cited for: VARIANT CBG DEFICIENCY ASN-389;

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.