UniProtKB/Swiss-Prot P41220: Variant p.Ile110Val

Regulator of G-protein signaling 2
Gene: RGS2
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Variant information Variant position:

110 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 Isoleucine (I) to Valine (V) at position 110 (I110V, p.Ile110Val). 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 hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

3 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:

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 rs146862218 [ dbSNP | Ensembl ]

Sequence information Variant position:

110 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:

SKYGLAAFRAFLKSEFCEEN I EFWLACEDFKKTKSPQKLSS 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                         SKYGLAAFRAFLKSEFCEENIEFWLACEDFKKTKSPQKLSS

Mouse                         SKYGLAAFRAFLKSEFCEENIEFWLACEDFKKTKSPQKLSS

Rat                           SKYGLAAFRAFLKSEFCEENIEFWLACEDFKKTKSPQKLSS

Pig                           SKYGLAAFRAFLKSEFCEENIEFWLACEDFKKTKSPQKLSS

Bovine                        SKYGLAAFRAFLKSEFCEENIEFWLACEDFKKTKSPQKLSS

Caenorhabditis elegans        HRAGQKYFAEFLKGEYSDENILFWQACEELKREKNAEKIEE

Baker's yeast                 SPYTIQKFYKFLKRAHCEENLEFFEKAHQFLQLKQNRSISE

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
Domain	83 – 199	RGS
Region	79 – 116	Necessary to inhibit protein synthesis
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.
Mutagenesis	102 – 102	K -> A. Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; F-105; I-110; E-111 and L-114.
Mutagenesis	105 – 105	F -> A. Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; I-110; E-111 and L-114.
Mutagenesis	106 – 106	C -> S. Changes specificity and confers GNAI1 binding; when associated with D-184. Strongly increases affinity for GNAI1 and GNAI3; when associated with D-184 and K-191.
Mutagenesis	110 – 110	I -> A. Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; F-105; E-111 and L-114.
Mutagenesis	111 – 111	E -> A. Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; F-105; I-110 and L-114.
Mutagenesis	114 – 114	L -> A. Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; F-105; I-110 and E-111.
Helix	108 – 120

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; Analysis of protein-coding genetic variation in 60,706 humans.
Lek M.; Karczewski K.J.; Minikel E.V.; Samocha K.E.; Banks E.; Fennell T.; O'Donnell-Luria A.H.; Ware J.S.; Hill A.J.; Cummings B.B.; Tukiainen T.; Birnbaum D.P.; Kosmicki J.A.; Duncan L.E.; Estrada K.; Zhao F.; Zou J.; Pierce-Hoffman E.; Berghout J.; Cooper D.N.; Deflaux N.; DePristo M.; Do R.; Flannick J.; Fromer M.; Gauthier L.; Goldstein J.; Gupta N.; Howrigan D.; Kiezun A.; Kurki M.I.; Moonshine A.L.; Natarajan P.; Orozco L.; Peloso G.M.; Poplin R.; Rivas M.A.; Ruano-Rubio V.; Rose S.A.; Ruderfer D.M.; Shakir K.; Stenson P.D.; Stevens C.; Thomas B.P.; Tiao G.; Tusie-Luna M.T.; Weisburd B.; Won H.H.; Yu D.; Altshuler D.M.; Ardissino D.; Boehnke M.; Danesh J.; Donnelly S.; Elosua R.; Florez J.C.; Gabriel S.B.; Getz G.; Glatt S.J.; Hultman C.M.; Kathiresan S.; Laakso M.; McCarroll S.; McCarthy M.I.; McGovern D.; McPherson R.; Neale B.M.; Palotie A.; Purcell S.M.; Saleheen D.; Scharf J.M.; Sklar P.; Sullivan P.F.; Tuomilehto J.; Tsuang M.T.; Watkins H.C.; Wilson J.G.; Daly M.J.; MacArthur D.G.;
Nature 536:285-291(2016)
Cited for: VARIANTS ARG-2; LEU-2; GLY-3; VAL-4; VAL-5; ASN-18; ASP-23; TYR-40; HIS-44; LYS-50; LEU-55; GLY-99; VAL-110; HIS-188 AND ARG-196;

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.