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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P29965: Variant p.Leu155Pro

CD40 ligand
Gene: CD40LG
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Variant information Variant position: help 155 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 Leucine (L) to Proline (P) at position 155 (L155P, p.Leu155Pro). 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 Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 HIGM1. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 155 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 261 The length of the canonical sequence.
Location on the sequence: help TSVLQWAEKGYYTMSNNLVT L ENGKQLTVKRQGLYYIYAQV 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                         TSVLQWAEKGYYTMSNNLVTLENGKQLTVKRQGLYYIYAQV

                              ASVLRWAPKGYYTISSNLVSLENGKQLAVKRQGLYYVYAQV

Rhesus macaque                TSVLQWAEKGYYTMSNNLVTLENGKQLTVKRQGLYYIYAQV

Mouse                         ASVLQWAKKGYYTMKSNLVMLENGKQLTVKREGLYYVYTQV

Rat                           ASVLQWAKKGYYTMKSNLVVLENGRQLTVKREGLYYVYTQV

Pig                           ASVLQWAPKGYYTLSTNLVTLENGRQLAVKRQGIYYIYAQV

Bovine                        TSVLQWAPKGYYTLSNNLVTLENGKQLAVKRQGFYYIYTQV

Cat                           ASVLQWAPKGYYTISSNLVTLENGKQLAVKRQGLYYIYAQV

Chicken                       VRVLKWMTTS-YAPTSSLISYHEGK-LKVEKAGLYYIYSQV
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 1 – 261 CD40 ligand, membrane form
Chain 113 – 261 CD40 ligand, soluble form
Topological domain 47 – 261 Extracellular
Domain 122 – 261 THD
Mutagenesis 170 – 170 Y -> E. Decreases ITGA5:ITGB1 binding, B-cell activation, activation of NF-kappa-B signaling, and anti-apoptotic signaling; in soluble form. Slightly decreases CD40 binding; in soluble form.
Beta strand 153 – 156



Literature citations
CD40 ligand gene defects responsible for X-linked hyper-IgM syndrome.
Allen R.C.; Armitage R.J.; Conley M.E.; Rosenblatt H.; Jenkins N.A.; Copeland N.G.; Bedell M.A.; Edelhoff S.; Disteche C.M.; Simoneaux D.K.; Fanslow W.C.; Belmont J.W.; Spriggs M.K.;
Science 259:990-993(1993)
Cited for: VARIANTS HIGM1 PRO-155; ASN-211 AND VAL-227; A single strand conformation polymorphism study of CD40 ligand. Efficient mutation analysis and carrier detection for X-linked hyper IgM syndrome.
Lin Q.; Rohrer J.; Allen R.C.; Larche M.; Greene J.M.; Shigeoka A.O.; Gatti R.A.; Derauf D.C.; Belmont J.W.; Conley M.E.;
J. Clin. Invest. 97:196-201(1996)
Cited for: VARIANTS HIGM1 PRO-155 AND VAL-227; VARIANT ARG-219;
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.