UniProtKB/Swiss-Prot P41220: Variant p.Gln78His

Regulator of G-protein signaling 2
Gene: RGS2
Feedback?

Variant information Variant position:

78 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B 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 Glutamine (Q) to Histidine (H) at position 78 (Q78H, p.Gln78His). 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 polar. 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:

Found in hypertensive patients; likely benign; no effect on down-regulation of angiotensin-activated signaling pathway. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs1665572116 [ dbSNP | Ensembl ]

Sequence information Variant position:

78 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

211 The length of the canonical sequence.
Location on the sequence:

PKTGKKSKQQAFIKPSPEEA Q LWSEAFDELLASKYGLAAFR 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                         PKTGKKSKQQAFIKPSPEEAQLWSEAFDELLASKYGLAAFR

Mouse                         PKTGKKSKQQTFIKPSPEEAQLWAEAFDELLASKYGLAAFR

Rat                           PKTGKKSKQQTFIKPSPEEALLWAEAFDELLASKYGLAAFR

Pig                           PKTGKKSKPQTFIKPSPEEAQLWAEAFDELLASKYGLAAFR

Bovine                        PKTGKKSKQQTFIKPSPEEAQLWSEAFDELLASKYGLAAFR

Caenorhabditis elegans        --------------PTYEIVFGWSQSFENLMKHRAGQKYFA

Baker's yeast                 ------------------------KGHHERMRSPYTIQKFY

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 – 211	Regulator of G-protein signaling 2
Mutagenesis	79 – 79	L -> A. Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with E-86; L-87; S-90; K-102; F-105; I-110; E-111 and L-114.
Mutagenesis	86 – 86	E -> A. Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; L-87; S-90; K-102; F-105; I-110; E-111 and L-114.
Mutagenesis	87 – 87	L -> A. Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; S-90; K-102; F-105; I-110; E-111 and L-114.
Mutagenesis	90 – 90	S -> A. Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; K-102; F-105; I-110; E-111 and L-114.
Helix	74 – 79

Literature citations
Human missense mutations in regulator of G protein signaling 2 affect the protein function through multiple mechanisms.
Phan H.T.N.; Sjoegren B.; Neubig R.R.;
Mol. Pharmacol. 92:451-458(2017)
Cited for: FUNCTION; SUBCELLULAR LOCATION; INTERACTION WITH GNAQ; CHARACTERIZATION OF VARIANTS ARG-2; LEU-2; GLY-3; VAL-4; VAL-5; ASN-18; ASP-23; TYR-40; HIS-44; LYS-50; LEU-55; HIS-78; GLY-99; VAL-110; HIS-188 AND ARG-196; Genetic variations of regulator of G-protein signaling 2 in hypertensive patients and in the general population.
Yang J.; Kamide K.; Kokubo Y.; Takiuchi S.; Tanaka C.; Banno M.; Miwa Y.; Yoshii M.; Horio T.; Okayama A.; Tomoike H.; Kawano Y.; Miyata T.;
J. Hypertens. 23:1497-1505(2005)
Cited for: VARIANTS ARG-2; LEU-2; VAL-5; HIS-44 AND HIS-78;

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.