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UniProtKB/Swiss-Prot B2RUZ4: Variant p.Met51Lys

Small integral membrane protein 1
Gene: SMIM1
Variant information

Variant position:  51
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 Methionine (M) to Lysine (K) at position 51 (M51K, p.Met51Lys).
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 hydrophobic (M) to large size and basic (K)
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

Polymorphism:  SMIM1 is responsible for the Vel blood group system (VEL) [MIM:615264]. The Vel antigen is present on red blood cells from all people except rare Vel-negative individuals who can form antibodies to Vel in response to transfusion or pregnancy. These antibodies may cause severe hemolytic reactions in blood recipients. In most cases, Vel-negative individuals are homozygous for a 17 nucleotide frameshift deletion in exon 3. In some cases, Vel-negative are heterozygous for the 17 nucleotide frameshift deletion and a missense variant at position 51.
Additional information on the polymorphism described.

Variant description:  Polymorphism found in Vel-negative population; heterozygous with the 17 nucleotide frameshift deletion.
Any additional useful information about the variant.

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

Sequence information

Variant position:  51
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  78
The length of the canonical sequence.

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.




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.

Chain 1 – 78 Small integral membrane protein 1
Transmembrane 47 – 67 Helical; Signal-anchor for type II membrane protein
Mutagenesis 35 – 35 C -> S. No effect on cell surface expression of the Vel antigen; when associated with S-43.
Mutagenesis 43 – 43 C -> S. No effect on cell surface expression of the Vel antigen; when associated with S-35.

Literature citations

SMIM1 underlies the Vel blood group and influences red blood cell traits.
Cvejic A.; Haer-Wigman L.; Stephens J.C.; Kostadima M.; Smethurst P.A.; Frontini M.; van den Akker E.; Bertone P.; Bielczyk-Maczynska E.; Farrow S.; Fehrmann R.S.; Gray A.; de Haas M.; Haver V.G.; Jordan G.; Karjalainen J.; Kerstens H.H.; Kiddle G.; Lloyd-Jones H.; Needs M.; Poole J.; Soussan A.A.; Rendon A.; Rieneck K.; Sambrook J.G.; Schepers H.; Sillje H.H.; Sipos B.; Swinkels D.; Tamuri A.U.; Verweij N.; Watkins N.A.; Westra H.J.; Stemple D.; Franke L.; Soranzo N.; Stunnenberg H.G.; Goldman N.; van der Harst P.; van der Schoot C.E.; Ouwehand W.H.; Albers C.A.;
Nat. Genet. 45:542-545(2013)

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.