Home  |  Contact

UniProtKB/Swiss-Prot P21583: Variant p.Leu104Val

Kit ligand
Gene: KITLG
Variant information

Variant position:  104
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  US
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 Leucine (L) to Valine (V) at position 104 (L104V, p.Leu104Val).
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:  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:  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:  Found in a patient with Waardenburg syndrome type 2 (WS2) and hearing loss; unknown pathological significance; reduces secretion.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  104
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  273
The length of the canonical sequence.

Location on the sequence:   LLDKFSNISEGLSNYSIIDK  L VNIVDDLVECVKENSSKDLK
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                         LLDKFSNIS---EGLSNYSIIDKLVNIVDDLVECVKENSSKD-LK

                              LLDKFSNIS---EGLSNYSIIDKLVKIVDDLVECTEGYSFE

Mouse                         LLDKFSNIS---EGLSNYSIIDKLGKIVDDLVLCMEENAPK

Rat                           LLDKFSNIS---EGLSNYSIIDKLGKIVDDLVACMEENAPK

Pig                           LLDKFSNIS---EGLSNYSIIDKLVKIVDDLVECMEEHSFE

Bovine                        LLDKFSNIS---EGLSNYCIIDKLVKIVDDLVECMEEHSSE

Goat                          LLDKFSNIS---EGLSNYSIIDKLVKIVDDLVECMEEHSFE

Cat                           LLDKFSNIS---EGLSNYSIIDKLVKIVDDLVECVEGHSSE

Horse                         LLEKFSNIS---EGLSNYSIIDKLVKIVDDLVECMEEHSSE

Chicken                       LLQKFSDISDMSDVLSNYSIINNLTRIINDLMACLAFDKNK

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.

TypePositionsDescription
Chain 26 – 273 Kit ligand
Chain 26 – 190 Soluble KIT ligand
Topological domain 26 – 214 Extracellular
Site 97 – 97 Not glycosylated
Glycosylation 90 – 90 N-linked (GlcNAc...) asparagine; partial
Glycosylation 118 – 118 N-linked (GlcNAc...) asparagine; partial
Disulfide bond 29 – 114
Disulfide bond 68 – 163
Helix 97 – 114


Literature citations

Allelic Mutations of KITLG, Encoding KIT Ligand, Cause Asymmetric and Unilateral Hearing Loss and Waardenburg Syndrome Type 2.
Zazo Seco C.; Serrao de Castro L.; van Nierop J.W.; Morin M.; Jhangiani S.; Verver E.J.; Schraders M.; Maiwald N.; Wesdorp M.; Venselaar H.; Spruijt L.; Oostrik J.; Schoots J.; van Reeuwijk J.; Lelieveld S.H.; Huygen P.L.; Insenser M.; Admiraal R.J.; Pennings R.J.; Hoefsloot L.H.; Arias-Vasquez A.; de Ligt J.; Yntema H.G.; Jansen J.H.; Muzny D.M.; Huls G.; van Rossum M.M.; Lupski J.R.; Moreno-Pelayo M.A.; Kunst H.P.; Kremer H.;
Am. J. Hum. Genet. 97:647-660(2015)
Cited for: VARIANT DCUA 67-HIS-CYS-68 DELINS ARG; CHARACTERIZATION OF VARIANT DCUA 67-HIS-CYS-68 DELINS ARG; INVOLVEMENT IN DCUA; VARIANT VAL-104; CHARACTERIZATION OF VARIANT VAL-104; SUBCELLULAR LOCATION (ISOFORM 2);

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.