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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P10912: Variant p.Asp170His

Growth hormone receptor
Gene: GHR
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Variant information Variant position: help 170 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 Aspartate (D) to Histidine (H) at position 170 (D170H, p.Asp170His). 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 acidic (D) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In LARS; abolishes receptor homodimerization. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 170 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 638 The length of the canonical sequence.
Location on the sequence: help DPPIALNWTLLNVSLTGIHA D IQVRWEAPRNADIQKGWMVL 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                         DPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVL

                              DPPVGLNWTLLNISLTEIHADILVKWEPPPNTDVKMGWIIL

                              DPPIGLNWTLLNISLTGIHADIQVRWEPPPNADVQKGWIVL

Rhesus macaque                DPPIALNWTLLNVSLTGIHADILVRWEAPPNADIQKGWMVL

Mouse                         DPPIGLNWTLLNISLTGIRGDIQVSWQPPPNADVLKGWIIL

Rat                           DPPIGLNWTLLNISLPGIRGDIQVSWQPPPSADVLKGWIIL

Pig                           DPPIGLNWTLLNISLTGIHADIQVRWEPPPNADVQKGWIVL

Bovine                        DPPVGLNWTLLNISLTEIHADILVKWEPPPNTDVKMGWIIL

Rabbit                        DPPIGLNWTLLNVSLTGIHADIQVRWEPPPNADVQKGWIVL

Sheep                         DPPVGLNWTLLNISLTEIHADILVKWEPPPNTDVKMGWIIL

Chicken                       DPPVHLNWTLLNTSQTGIHGDIQVRWDPPPTADVQKGWITL
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 19 – 638 Growth hormone receptor
Chain 19 – 256 Growth hormone-binding protein
Topological domain 19 – 264 Extracellular
Domain 151 – 254 Fibronectin type-III
Glycosylation 156 – 156 N-linked (GlcNAc...) asparagine
Glycosylation 161 – 161 N-linked (GlcNAc...) asparagine
Beta strand 167 – 176



Literature citations
A single amino acid substitution in the exoplasmic domain of the human growth hormone (GH) receptor confers familial GH resistance (Laron syndrome) with positive GH-binding activity by abolishing receptor homodimerization.
Duquesnoy P.; Sobrier M.-L.; Duriez B.; Dastot F.; Buchanan C.R.; Savage M.O.; Preece M.A.; Craescu C.T.; Blouquit Y.; Goossens M.; Amselem S.;
EMBO J. 13:1386-1395(1994)
Cited for: VARIANT LARS HIS-170; Four contiguous amino acid substitutions, identified in patients with Laron syndrome, differently affect the binding affinity and intracellular trafficking of the growth hormone receptor.
Wojcik J.; Berg M.A.; Esposito N.; Geffner M.E.; Sakati N.; Reiter E.O.; Dower S.; Francke U.; Postel-Vinay M.-C.; Finidori J.;
J. Clin. Endocrinol. Metab. 83:4481-4489(1998)
Cited for: VARIANTS LARS HIS-170; THR-171; PRO-172 AND GLY-173; CHARACTERIZATION OF VARIANTS LARS THR-171; PRO-172 AND GLY-173;
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.