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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P32004: Variant p.Cys264Tyr

Neural cell adhesion molecule L1
Gene: L1CAM
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Variant information Variant position: help 264 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Cysteine (C) to Tyrosine (Y) at position 264 (C264Y, p.Cys264Tyr). 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: help Change from medium size and polar (C) to large size and aromatic (Y) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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
Variant description: help In HYCX; severe; loss of localization to the cell surface; retention in the endoplasmic reticulum; loss of axon guidance, when assayed in a heterologous system. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 264 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1257 The length of the canonical sequence.
Location on the sequence: help FPTNSSSHLVALQGQPLVLE C IAEGFPTPTIKWLRPSGPMP 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         FPTNSSSHLVALQGQPLVLECIAEGFPTPTIKWLRPSGPMP

Mouse                         FPTNSSSRLVALQGQSLILECIAEGFPTPTIKWLHPSDPMP

Rat                           FPTNSSSHLVALQGQSLILECIAEGFPTPTIKWLHPSDPMP
Sequence annotation in neighborhood: help 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 20 – 1257 Neural cell adhesion molecule L1
Topological domain 20 – 1120 Extracellular
Domain 240 – 328 Ig-like C2-type 3
Glycosylation 247 – 247 N-linked (GlcNAc...) asparagine
Disulfide bond 264 – 312



Literature citations
A missense mutation confirms the L1 defect in X-linked hydrocephalus (HSAS).
Jouet M.; Rosenthal A.; Macfarlane J.; Kenwrick S.; Donnai D.;
Nat. Genet. 4:331-331(1993)
Cited for: VARIANT HYCX TYR-264; 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; The C264Y missense mutation in the extracellular domain of L1 impairs protein trafficking in vitro and in vivo.
Ruenker A.E.; Bartsch U.; Nave K.A.; Schachner M.;
J. Neurosci. 23:277-286(2003)
Cited for: CHARACTERIZATION OF VARIANT HYCX TYR-264; SUBCELLULAR LOCATION; GLYCOSYLATION; 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.