UniProtKB/Swiss-Prot O15232: Variant p.Glu252Lys

Matrilin-3
Gene: MATN3
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Variant information Variant position:

252 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 Glutamate (E) to Lysine (K) at position 252 (E252K, p.Glu252Lys). 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 (E) 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
Variant description:

Secreted normally as the wild-type. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs52826764 [ dbSNP | Ensembl ]

Sequence information Variant position:

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

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

MMASEPLEEHVFYVETYGVI E KLSSRFQETFCALDPCVLGT 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                         MMASEPLEEHVFYVETYGVIEKLSSRFQETFCALDPCVLGT

Mouse                         MMASKPLEEHVFYVETYGVIEKLSARFQETFCALDQCMLGT

Chicken                       IMASEPLDEHVFYVETYGVIEKLTSKFRETFCAANTCALGT

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	29 – 486	Matrilin-3
Domain	83 – 258	VWFA

Literature citations
Novel and recurrent mutations clustered in the von Willebrand factor A domain of MATN3 in multiple epiphyseal dysplasia.
Mabuchi A.; Haga N.; Maeda K.; Nakashima E.; Manabe N.; Hiraoka H.; Kitoh H.; Kosaki R.; Nishimura G.; Ohashi H.; Ikegawa S.;
Hum. Mutat. 24:439-440(2004)
Cited for: VARIANTS EDM5 SER-105; MET-120 AND TRP-121; VARIANTS SER-11; LYS-252 AND MET-303; Missense mutations in the beta strands of the single A-domain of matrilin-3 result in multiple epiphyseal dysplasia.
Jackson G.C.; Barker F.S.; Jakkula E.; Czarny-Ratajczak M.; Maekitie O.; Cole W.G.; Wright M.J.; Smithson S.F.; Suri M.; Rogala P.; Mortier G.R.; Baldock C.; Wallace A.; Elles R.; Ala-Kokko L.; Briggs M.D.;
J. Med. Genet. 41:52-59(2004)
Cited for: VARIANTS EDM5 MET-120; TRP-121; LYS-134; ASN-192 AND ASP-219; VARIANTS LYS-252 AND MET-303; Multiple epiphyseal dysplasia mutations in MATN3 cause misfolding of the A-domain and prevent secretion of mutant matrilin-3.
Cotterill S.L.; Jackson G.C.; Leighton M.P.; Wagener R.; Maekitie O.; Cole W.G.; Briggs M.D.;
Hum. Mutat. 26:557-565(2005)
Cited for: VARIANTS EDM5 TRP-121; LYS-195 AND ASN-218; VARIANT LYS-252; CHARACTERIZATION OF VARIANTS MET-120; TRP-121; LYS-134; ASN-192; ASP-194 AND ASP-219; CHARACTERIZATION OF VARIANT LYS-252;

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.