UniProtKB/Swiss-Prot Q9UQM7: Variant p.Glu183Val

Calcium/calmodulin-dependent protein kinase type II subunit alpha
Gene: CAMK2A
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Variant information Variant position:

183 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 Glutamate (E) to Valine (V) at position 183 (E183V, p.Glu183Val). 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 medium size and acidic (E) to medium size and hydrophobic (V) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-2 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 MRD53; increased ubiquitin-mediated proteasomal degradation with a dominant negative effect on wild-type protein; decreased localization to dendritic spines; no effect on holoenzyme assembly; loss of interaction with SHANK3; loss of interaction with GRIN2B; loss of interaction with CACNB2; loss of interaction with LRRC7; loss of interaction with GRM5; decreased protein serine/threonine kinase activity with a dominant negative effect on wild-type protein; decreased autophosphorylation; changed dendritic spine development; decreased neuronal migration. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs1554122129 [ dbSNP | Ensembl ]

Sequence information Variant position:

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

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

VEGEQQAWFGFAGTPGYLSP E VLRKDPYGKPVDLWACGVIL 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                         VEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVIL

Mouse                         VEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVIL

Rat                           VEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVIL

Drosophila                    VQGDHQAWFGFAGTPGYLSPEVLKKEPYGKSVDIWACGVIL

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 – 478	Calcium/calmodulin-dependent protein kinase type II subunit alpha
Domain	13 – 271	Protein kinase
Helix	182 – 186

Literature citations
Mutation Disrupts Dendritic Morphology and Synaptic Transmission, and Causes ASD-Related Behaviors.
Stephenson J.R.; Wang X.; Perfitt T.L.; Parrish W.P.; Shonesy B.C.; Marks C.R.; Mortlock D.P.; Nakagawa T.; Sutcliffe J.S.; Colbran R.J.;
J. Neurosci. 37:2216-2233(2017)
Cited for: FUNCTION; INTERACTION WITH CACNB2; GRIN2B; GRM5; LRRC7 AND SHANK3; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANT MRD53 VAL-183; De Novo Mutations in Protein Kinase Genes CAMK2A and CAMK2B Cause Intellectual Disability.
Kuery S.; van Woerden G.M.; Besnard T.; Proietti Onori M.; Latypova X.; Towne M.C.; Cho M.T.; Prescott T.E.; Ploeg M.A.; Sanders S.; Stessman H.A.F.; Pujol A.; Distel B.; Robak L.A.; Bernstein J.A.; Denomme-Pichon A.S.; Lesca G.; Sellars E.A.; Berg J.; Carre W.; Busk O.L.; van Bon B.W.M.; Waugh J.L.; Deardorff M.; Hoganson G.E.; Bosanko K.B.; Johnson D.S.; Dabir T.; Holla O.L.; Sarkar A.; Tveten K.; de Bellescize J.; Braathen G.J.; Terhal P.A.; Grange D.K.; van Haeringen A.; Lam C.; Mirzaa G.; Burton J.; Bhoj E.J.; Douglas J.; Santani A.B.; Nesbitt A.I.; Helbig K.L.; Andrews M.V.; Begtrup A.; Tang S.; van Gassen K.L.I.; Juusola J.; Foss K.; Enns G.M.; Moog U.; Hinderhofer K.; Paramasivam N.; Lincoln S.; Kusako B.H.; Lindenbaum P.; Charpentier E.; Nowak C.B.; Cherot E.; Simonet T.; Ruivenkamp C.A.L.; Hahn S.; Brownstein C.A.; Xia F.; Schmitt S.; Deb W.; Bonneau D.; Nizon M.; Quinquis D.; Chelly J.; Rudolf G.; Sanlaville D.; Parent P.; Gilbert-Dussardier B.; Toutain A.; Sutton V.R.; Thies J.; Peart-Vissers L.E.L.M.; Boisseau P.; Vincent M.; Grabrucker A.M.; Dubourg C.; Tan W.H.; Verbeek N.E.; Granzow M.; Santen G.W.E.; Shendure J.; Isidor B.; Pasquier L.; Redon R.; Yang Y.; State M.W.; Kleefstra T.; Cogne B.; Petrovski S.; Retterer K.; Eichler E.E.; Rosenfeld J.A.; Agrawal P.B.; Bezieau S.; Odent S.; Elgersma Y.; Mercier S.;
Am. J. Hum. Genet. 101:768-788(2017)
Cited for: INVOLVEMENT IN MRD53; VARIANTS MRD53 SER-98; ASP-109; VAL-112; VAL-183; LEU-212; LEU-235; ARG-282 AND PRO-286; CHARACTERIZATION OF VARIANTS MRD53 ALA-98; ASP-109; ALA-138; VAL-183; LEU-212; LEU-235; ARG-282 AND PRO-286; FUNCTION; MUTAGENESIS OF LYS-42 AND THR-286;

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.