UniProtKB/SwissProt variant VAR

Variant information

Variant position:

137

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

Type of variant:

Disease [Disclaimer]

The variants are classified into three categories: Disease, Polymorphism and Unclassified.

Disease: Variants implicated in disease according to literature reports.
Polymorphism: Variants not reported to be implicated in disease.
Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:

From Arginine (R) to Histidine (H) at position 137 (R137H, p.Arg137His).

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 XNDI; fails to activate the adenylyl cyclase system.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs104894756 [ dbSNP | Ensembl ]

Sequence information

Variant position:

137

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

Protein sequence length:

371

The length of the canonical sequence.

Location on the sequence:

YLQMVGMYASSYMILAMTLD R HRAICRPMLAYRHGSGAHWN

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                         YLQMVGMYASSYMILAMTLDRHRAICRPMLAYRHGSGAHWN

                              YLQMVGMYASSYMILAMTLDRHRAICRPMLAYRHGGGARWN

Mouse                         YLQMVGMYASSYMILAMTLDRHRAICRPMLAYRHGGGARWN

Rat                           YLQMVGMYASSYMILAMTLDRHRAICRPMLAYRHGGGARWN

Pig                           YLQMVGMYASSYMILAMTLDRHRAICRPMLAYRHGGGARWN

Bovine                        YLQMVGMYASSYMILAMTLDRHRAICRPMLAHRHGGGTHWN

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.

Type	Positions	Description
Chain	1 – 371	Vasopressin V2 receptor
Topological domain	136 – 159	Cytoplasmic

Literature citations

Nephrogenic diabetes insipidus. A V2 vasopressin receptor unable to stimulate adenylyl cyclase.
Rosenthal W.; Antaramian A.; Gilbert S.; Birnbaumer M.;
J. Biol. Chem. 268:13030-13033(1993)
Cited for: VARIANT XNDI HIS-137;

Nature and recurrence of AVPR2 mutations in X-linked nephrogenic diabetes insipidus.
Bichet D.G.; Birnbaumer M.; Lonergan M.; Arthus M.-F.; Rosenthal W.; Goodyer P.; Nivet H.; Benoit S.; Giampietro P.; Simonetti S.; Fish A.; Whitley C.B.; Jaeger P.; Gertner J.; New M.; Dibona F.J.; Kaplan B.S.; Robertson G.L.; Hendy G.N.; Fujiwara T.M.; Morgan K.;
Am. J. Hum. Genet. 55:278-286(1994)
Cited for: VARIANTS XNDI MET-88; CYS-106; ARG-112; TRP-113; PHE-126; SER-128; HIS-137; SER-164; LEU-167; CYS-181; CYS-202 AND PRO-285;

Mutational analyses of AVPR2 gene in three Japanese families with X-linked nephrogenic diabetes insipidus: two recurrent mutations, R137H and deltaV278, caused by the hypermutability at CpG dinucleotides.
Shoji Y.; Takahashi T.; Suzuki Y.; Suzuki T.; Komatsu K.; Hirono H.; Shoji Y.; Yokoyama T.; Kito H.; Takada G.;
Hum. Mutat. Suppl. 1:S278-S283(1998)
Cited for: VARIANTS XNDI HIS-137; VAL-277 DEL AND PRO-309;

V2 vasopressin receptor dysfunction in nephrogenic diabetes insipidus caused by different molecular mechanisms.
Schoeneberg T.; Schulz A.; Biebermann H.; Grueters A.; Grimm T.; Huebschmann K.; Filler G.; Gudermann T.; Schultz G.;
Hum. Mutat. 12:196-205(1998)
Cited for: VARIANTS XNDI HIS-137 AND CYS-181;

Novel mutations underlying nephrogenic diabetes insipidus in Arab families.
Carroll P.; Al-Mojalli H.; Al-Abbad A.; Al-Hassoun I.; Al-Hamed M.; Al-Amr R.; Butt A.I.; Meyer B.F.;
Genet. Med. 8:443-447(2006)
Cited for: VARIANTS XNDI ASP-122 AND HIS-137;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P30518: Variant p.Arg137His