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UniProtKB/Swiss-Prot P30203: Variant p.Ser351Asn

T-cell differentiation antigen CD6
Gene: CD6
Variant information

Variant position:  351
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Polymorphism
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 Serine (S) to Asparagine (N) at position 351 (S351N, p.Ser351Asn).
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 small size and polar (S) 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:  Adds an additional glycosylation site and impairs interaction with ALCAM.
Any additional useful information about the variant.

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



Sequence information

Variant position:  351
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  668
The length of the canonical sequence.

Location on the sequence:   NGEELTLSNCSWRFNNSNLC  S QSLAARVLCSASRSLHNLST
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                         NGEELTLSNCSWRFNNSNLCSQSLAARVLCSASRSLHNLST

Mouse                         KGQEPALSTCSWRFNNSNLCSQSRAARVVCSGSQRHLNLST

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 18 – 668 T-cell differentiation antigen CD6
Topological domain 18 – 402 Extracellular
Domain 265 – 361 SRCR 3
Glycosylation 339 – 339 N-linked (GlcNAc...) asparagine
Glycosylation 345 – 345 N-linked (GlcNAc...) asparagine
Glycosylation 368 – 368 N-linked (GlcNAc...) asparagine
Disulfide bond 303 – 360
Alternative sequence 259 – 359 Missing. In isoform 7.
Alternative sequence 261 – 383 Missing. In isoform 6.
Mutagenesis 346 – 346 N -> A. Strongly reduces interaction with ALCAM.
Mutagenesis 349 – 349 L -> A. Reduces interaction with ALCAM.
Mutagenesis 352 – 352 Q -> A. Reduces interaction with ALCAM.
Mutagenesis 353 – 353 S -> A. Reduces interaction with ALCAM.
Beta strand 350 – 352


Literature citations

Structures of CD6 and its ligand CD166 give insight into their interaction.
Chappell P.E.; Garner L.I.; Yan J.; Metcalfe C.; Hatherley D.; Johnson S.; Robinson C.V.; Lea S.M.; Brown M.H.;
Structure 23:1426-1436(2015)
Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 1-364; DISULFIDE BONDS; GLYCOSYLATION AT ASN-28 ASN-49 AND ASN-229; IDENTIFICATION BY MASS SPECTROMETRY; INTERACTION WITH ALCAM; CHARACTERIZATION OF VARIANT ASN-351; MUTAGENESIS OF ASP-291; GLU-293; TYR-295; GLU-298; ARG-314; TYR-327; SER-329; ASN-346; LEU-349; GLN-352 AND SER-353;

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.