UniProtKB/Swiss-Prot Q92982: Variant p.Ala110Asp

Ninjurin-1
Gene: NINJ1
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Variant information Variant position:

110 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B 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 Alanine (A) to Aspartate (D) at position 110 (A110D, p.Ala110Asp). 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 hydrophobic (A) to medium size and acidic (D) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-2 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
Other resources:

Links to websites of interest for the variant.

Variant rs2275848 [ dbSNP | Ensembl ]

Sequence information Variant position:

110 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

152 The length of the canonical sequence.
Location on the sequence:

LQIGVGVLLIFLVKYDLNNP A KHAKLDFLNNLATGLVFIIV 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                         LQIGVGVLLIFLVKYDLNNPAKHAKLDFLNNLATGLVFIIV

Mouse                         LQIGVGVLLIFLVKYDLNNPAKHAKLDFLNNLATGLVFIIV

Rat                           LQIGVGVLLIFLVKYDLNNPAKHAKLDFLNNLATGLVFIIV

Zebrafish                     LQIIVGILLIFIVKWNLNDSSKHYILNLLENIVTALVFIVV

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.

Type	Positions	Description
Chain	1 – 152	Ninjurin-1
Topological domain	104 – 113	Cytoplasmic
Mutagenesis	90 – 90	L -> W. Strongly reduced ability to mediate plasma membrane rupture.
Mutagenesis	91 – 91	Q -> A. Strongly reduced ability to homooligomerize and mediate plasma membrane rupture (cytolysis).
Mutagenesis	93 – 93	G -> L. Reduced ability to mediate plasma membrane rupture.
Mutagenesis	95 – 95	G -> L. Strongly reduced ability to homooligomerize and mediate plasma membrane rupture (cytolysis).
Mutagenesis	103 – 103	K -> E. Strongly reduced ability to mediate plasma membrane rupture.
Mutagenesis	111 – 111	K -> E. Strongly reduced ability to mediate plasma membrane rupture.
Mutagenesis	114 – 114	K -> E. Slightly reduced ability to mediate plasma membrane rupture.
Mutagenesis	121 – 121	L -> F. Does not affect ability to homooligomerize and mediate plasma membrane rupture (cytolysis).
Mutagenesis	121 – 121	L -> W. Does not affect ability to homooligomerize, but shows reduced ability to mediate plasma membrane rupture (cytolysis).
Mutagenesis	123 – 123	T -> L. Strongly reduced ability to homooligomerize and mediate plasma membrane rupture (cytolysis).
Mutagenesis	124 – 124	G -> L. Reduced ability to mediate plasma membrane rupture.
Mutagenesis	125 – 125	L -> W. Strongly reduced ability to mediate plasma membrane rupture.
Mutagenesis	128 – 128	I -> F. Slightly reduced ability to mediate plasma membrane rupture.

Literature citations
Ninjurin, a novel adhesion molecule, is induced by nerve injury and promotes axonal growth.
Araki T.; Milbrandt J.;
Neuron 17:353-361(1996)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; FUNCTION; TISSUE SPECIFICITY; INDUCTION; VARIANT ASP-110; The human homologue of the ninjurin gene maps to the candidate region of hereditary sensory neuropathy type I (HSNI).
Chadwick B.P.; Heath S.K.; Williamson J.; Obermayr F.; Patel L.; Sheer D.; Frischauf A.-M.;
Genomics 47:58-63(1998)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]; VARIANT ASP-110; The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
The MGC Project Team;
Genome Res. 14:2121-2127(2004)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]; VARIANT ASP-110;

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.