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UniProtKB/Swiss-Prot P01308: Variant p.Arg89His

Insulin
Gene: INS
Variant information

Variant position:  89
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Arginine (R) to Histidine (H) at position 89 (R89H, p.Arg89His).
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:  Change from large size and basic (R) to medium size and polar (H)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  0
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:  In HPRI; impairs post-translational cleavage.
Any additional useful information about the variant.

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



Sequence information

Variant position:  89
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  110
The length of the canonical sequence.

Location on the sequence:   GGGPGAGSLQPLALEGSLQK  R GIVEQCCTSICSLYQLENYC
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                         GGGPGAGSLQPLALEGSLQKRGIVEQCCTSICSLYQLENYC

Gorilla                       GGGPGAGSLQPLALEGSLQKRGIVEQCCTSICSLYQLENYC

                              AGAPGEGGLQPLALEGALQKRGIVEQCCTSICSLYQLENYC

Chimpanzee                    GGGPGAGSLQPLALEGSLQKRGIVEQCCTSICSLYQLENYC

Pig                           GG--GLGGLQALALEGPPQKRGIVEQCCTSICSLYQLENYC

Bovine                        AGGPGAGGL-----EGPPQKRGIVEQCCASVCSLYQLENYC

Rabbit                        GGGPGAGGLQPSALELALQKRGIVEQCCTSICSLYQLENYC

Goat                          ---------------------GIVEQCCAGVCSLYQLENYC

Sheep                         AGGPGAGGL-----EGPPQKRGIVEQCCAGVCSLYQLENYC

Cat                           GEAPGAGGLQPSALEAPLQKRGIVEQCCASVCSLYQLEHYC

Horse                         GGGPGLGGLQPLALAGPQQXXGIVEQCCTGICSLYQLENYC

Chicken                       GE---AGVLPFQQEEYEKVKRGIVEQCCHNTCSLYQLENYC

Zebrafish                     AQETEVADFAFKDHAELIRKRGIVEQCCHKPCSIFELQNYC

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
Disulfide bond 31 – 96 Interchain (between B and A chains)
Disulfide bond 43 – 109 Interchain (between B and A chains)


Literature citations

Two unrelated patients with familial hyperproinsulinemia due to a mutation substituting histidine for arginine at position 65 in the proinsulin molecule: identification of the mutation by direct sequencing of genomic deoxyribonucleic acid amplified by polymerase chain reaction.
Barbetti F.; Raben N.; Kadowaki T.; Cama A.; Accili D.; Gabbay K.H.; Merenich J.A.; Taylor S.I.; Roth J.;
J. Clin. Endocrinol. Metab. 71:164-169(1990)
Cited for: VARIANT HPRI HIS-89;

Posttranslational cleavage of proinsulin is blocked by a point mutation in familial hyperproinsulinemia.
Shibasaki Y.; Kawakami T.; Kanazawa Y.; Akanuma Y.; Takaku F.;
J. Clin. Invest. 76:378-380(1985)
Cited for: VARIANT HPRI HIS-89;

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.