UniProtKB/SwissProt variant VAR

Variant information

Variant position:

296

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 Glycine (G) to Serine (S) at position 296 (G296S, p.Gly296Ser).

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 glycine (G) to small size and polar (S)

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 ASD2; decreased function resulting in reduced myocardial genes expression; fails to downregulate endothelial and endocardial genes.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs104894073 [ dbSNP | Ensembl ]

Sequence information

Variant position:

296

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

Protein sequence length:

442

The length of the canonical sequence.

Location on the sequence:

TTTTTLWRRNAEGEPVCNAC G LYMKLHGVPRPLAMRKEGIQ

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                         TTTTTLWRRNAEGEPVCNACGLYMKLHGVPRPLAMRKEGIQ

                              TTTTTLWRRNAEGEPVCNACGLYMKLHGVPRPLAMRKEGIQ

Mouse                         TTTTTLWRRNAEGEPVCNACGLYMKLHGVPRPLAMRKEGIQ

Rat                           TTTTTLWRRNAEGEPVCNACGLYMKLHGVPRPLAMRKEGIQ

Xenopus laevis                TTTTTLWRRNAEGEPVCNACGLYMKLHGVPRPLAMKKEGIQ

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 – 442	Transcription factor GATA-4
Modified residue	300 – 300	N6-methyllysine; by EZH2
Helix	293 – 301

Literature citations

Disease model of GATA4 mutation reveals transcription factor cooperativity in human cardiogenesis.
Ang Y.S.; Rivas R.N.; Ribeiro A.J.; Srivas R.; Rivera J.; Stone N.R.; Pratt K.; Mohamed T.M.; Fu J.D.; Spencer C.I.; Tippens N.D.; Li M.; Narasimha A.; Radzinsky E.; Moon-Grady A.J.; Yu H.; Pruitt B.L.; Snyder M.P.; Srivastava D.;
Cell 167:1734-1749(2016)
Cited for: FUNCTION; CHARACTERIZATION OF VARIANT ASD2 SER-296;

GATA4 mutations cause human congenital heart defects and reveal an interaction with TBX5.
Garg V.; Kathiriya I.S.; Barnes R.; Schluterman M.K.; King I.N.; Butler C.A.; Rothrock C.R.; Eapen R.S.; Hirayama-Yamada K.; Joo K.; Matsuoka R.; Cohen J.C.; Srivastava D.;
Nature 424:443-447(2003)
Cited for: VARIANT ASD2 SER-296;

Phenotypes with GATA4 or NKX2.5 mutations in familial atrial septal defect.
Hirayama-Yamada K.; Kamisago M.; Akimoto K.; Aotsuka H.; Nakamura Y.; Tomita H.; Furutani M.; Imamura S.; Takao A.; Nakazawa M.; Matsuoka R.;
Am. J. Med. Genet. A 135:47-52(2005)
Cited for: VARIANTS ASD2 PHE-52 AND SER-296;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P43694: Variant p.Gly296Ser