UniProtKB/Swiss-Prot P32004: Variant p.Arg184Gln

Neural cell adhesion molecule L1
Gene: L1CAM
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Variant information Variant position:

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

LP/P [Disclaimer] 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 Arginine (R) to Glutamine (Q) at position 184 (R184Q, p.Arg184Gln). 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 large size and basic (R) to medium size and polar (Q) 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 HYCX; severe; reduced axon arborization; partial loss of localization at the cell surface; retention in the endoplasmic reticulum; in neurons, restricted to cell bodies and proximal segments of processes; loss of axon guidance and of proper synapse formation, when assayed in a heterologous system. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs137852521 [ dbSNP | Ensembl ]

Sequence information Variant position:

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

1257 The length of the canonical sequence.
Location on the sequence:

AEPLRIYWMNSKILHIKQDE R VTMGQNGNLYFANVLTSDNH 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                         AEPLRIYWMNSKILHIKQDERVTMGQNGNLYFANVLTSDNH

Mouse                         AAPPRIYWMNSKIFDIKQDERVSMGQNGDLYFANVLTSDNH

Rat                           AAPLRIYWMNSKILHIKQDERVSMGQNGDLYFANVLTSDNH

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	20 – 1257	Neural cell adhesion molecule L1
Topological domain	20 – 1120	Extracellular
Domain	139 – 226	Ig-like C2-type 2
Glycosylation	203 – 203	N-linked (GlcNAc...) asparagine
Disulfide bond	158 – 209

Literature citations
Genotype-phenotype correlations in L1 syndrome: a guide for genetic counselling and mutation analysis.
Vos Y.J.; de Walle H.E.; Bos K.K.; Stegeman J.A.; Ten Berge A.M.; Bruining M.; van Maarle M.C.; Elting M.W.; den Hollander N.S.; Hamel B.; Fortuna A.M.; Sunde L.E.; Stolte-Dijkstra I.; Schrander-Stumpel C.T.; Hofstra R.M.;
J. Med. Genet. 47:169-175(2010)
Cited for: INVOLVEMENT IN L1 SYNDROME; VARIANTS 26-TYR--GLU-1257 DEL; ASN-37; MET-38; 66-GLN--GLU-1257 DEL; 109-GLN--GLU-1257 DEL; 133-GLU--GLU-1257 DEL; 138-TRP--GLU-1257 DEL; ILE-172; GLY-184; 187-MET--VAL-198 DEL; ASP-254; ARG-276; PRO-313; 366-TRP--GLU-1257 DEL; LYS-369; 423-GLN--GLU-1257 DEL; ARG-480; ASN-516; TYR-516; HIS-525; MET-627; PRO-645; 662-TRP--GLU-1257 DEL; SER-714; ARG-754; 760-ARG--GLU-1257 DEL; 789-GLN--GLU-1257 DEL; 811-TYR--GLU-1257 DEL; 891-TYR--GLU-1257 DEL; 901-ARG--GLU-1257 DEL; 1064-SER--GLU-1257 DEL; ASN-1071 DEL AND GLN-1080; VARIANTS MASA SER-179; TYR-202; ARG-335 AND MET-752; VARIANTS HYCX SER-179; GLN-184; ARG-335; PRO-415 AND MET-752; X-linked spastic paraplegia (SPG1), MASA syndrome and X-linked hydrocephalus result from mutations in the L1 gene.
Jouet M.; Rosenthal A.; Armstrong G.; Macfarlane J.; Stevenson R.; Paterson J.; Metzenberg A.; Ionasescu V.; Temple K.; Kenwrick S.;
Nat. Genet. 7:402-407(1994)
Cited for: INVOLVEMENT IN MASA; INVOLVEMENT IN HYCX; VARIANTS HYCX GLN-184 AND ARG-452; VARIANT MASA GLN-210; CRASH syndrome: clinical spectrum of corpus callosum hypoplasia, retardation, adducted thumbs, spastic paraparesis and hydrocephalus due to mutations in one single gene, L1.
Fransen E.; Lemmon V.; van Camp G.; Vits L.; Coucke P.; Willems P.J.;
Eur. J. Hum. Genet. 3:273-284(1995)
Cited for: VARIANTS HYCX GLN-184; TYR-264; ARG-452 AND LEU-1194; VARIANTS MASA GLN-210; ASN-598 AND LEU-1194; Nine novel L1 CAM mutations in families with X-linked hydrocephalus.
Macfarlane J.R.; Du J.-S.; Pepys M.E.; Ramsden S.; Donnai D.; Charlton R.; Garrett C.; Tolmie J.; Yates J.R.W.; Berry C.; Goudie D.; Moncla A.; Lunt P.; Hodgson S.; Jouet M.; Kenwrick S.;
Hum. Mutat. 9:512-518(1997)
Cited for: VARIANTS HYCX GLN-184; 439-VAL--THR-443 DEL; CYS-784 AND 936-LEU--LEU-948 DEL; L1 syndrome mutations impair neuronal L1 function at different levels by divergent mechanisms.
Schaefer M.K.; Nam Y.C.; Moumen A.; Keglowich L.; Bouche E.; Kueffner M.; Bock H.H.; Rathjen F.G.; Raoul C.; Frotscher M.;
Neurobiol. Dis. 40:222-237(2010)
Cited for: CHARACTERIZATION OF VARIANTS HYCX GLN-184 AND LEU-1036; FUNCTION; SUBCELLULAR LOCATION; Differential effects of human L1CAM mutations on complementing guidance and synaptic defects in Drosophila melanogaster.
Kudumala S.; Freund J.; Hortsch M.; Godenschwege T.A.;
PLoS ONE 8:E76974-E76974(2013)
Cited for: CHARACTERIZATION OF VARIANT VAL-120; CHARACTERIZATION OF VARIANTS MASA GLN-210 AND LYS-309; CHARACTERIZATION OF VARIANTS HYCX GLN-184; TYR-264 AND CYS-1070; MUTAGENESIS OF 1147-LYS--VAL-1153;

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.