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UniProtKB/Swiss-Prot P10912: Variant p.Glu242Asp

Growth hormone receptor
Gene: GHR
Variant information

Variant position:  242
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 Glutamate (E) to Aspartate (D) at position 242 (E242D, p.Glu242Asp).
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 acidic.
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  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:  Found in a patient with idiopathic short stature; unknown pathological significance.
Any additional useful information about the variant.

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



Sequence information

Variant position:  242
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  638
The length of the canonical sequence.

Location on the sequence:   VDKEYEVRVRSKQRNSGNYG  E FSEVLYVTLPQMSQFTCEED
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                         VDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMS-QFT-CEED

                              LDKEYEVRVRTRQRNTEKYGKFSEVLLITFPQMN-PSA-CE

                              LDKEYEVRVRSRQRNSEKYGEFSEALYVTLPQMS-PFA-CE

Rhesus macaque                VDKEYEVLVRSKRRNSRNYGEFSEVLYVTLPQMN-QFT-CE

Mouse                         MDKEHEVRVRSRQRSFEKYSEFSEVLRVIFPQTN-ILEACE

Rat                           LDKEHEVRVRSRQRSFEKYSEFSEVLRVTFPQMD-TLAACE

Pig                           LDKEYEVRVRSRQRNSEKYGEFSEVLYVTLPQMS-PFA-CE

Bovine                        LDKEYEVRVRTRQRNTEKYGKFSEVLLITFPQMN-PSA-CE

Rabbit                        LDKEYEVRVRSRQRSSEKYGEFSEVLYVTLPQMS-PFT-CE

Sheep                         LDKEYEVRVRTRQRNTEKYGKFSEVLLITFPQMN-PSA-CE

Chicken                       MGRDYEIRVRSRQRTSEKFGEFSEILYVSFTQAGIEFVHCA

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 19 – 638 Growth hormone receptor
Chain 19 – 256 Growth hormone-binding protein
Topological domain 19 – 264 Extracellular
Domain 151 – 254 Fibronectin type-III
Motif 240 – 244 WSXWS motif
Mutagenesis 260 – 260 E -> A. No change in shedding activity: No change in hormone binding.
Mutagenesis 261 – 261 E -> A. No change in shedding activity: No change in hormone binding.
Mutagenesis 262 – 262 D -> A. No change in shedding activity: No change in hormone binding.
Beta strand 240 – 243


Literature citations

Mutations of the growth hormone receptor in children with idiopathic short stature.
Goddard A.D.; Covello R.; Luoh S.-M.; Clackson T.; Attie K.M.; Gesundheit N.; Rundle A.C.; Wells J.A.; Carlsson L.M.S.;
N. Engl. J. Med. 333:1093-1098(1995)
Cited for: VARIANTS GHIP LYS-62 AND CYS-179; VARIANTS HIS-229 AND ASP-242;

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.