UniProtKB/Swiss-Prot Q9NS23: Variant p.Ala137Ser

Ras association domain-containing protein 1
Gene: RASSF1
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Variant information Variant position:

137 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 Alanine (A) to Serine (S) at position 137 (A137S, p.Ala137Ser). 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 small size and hydrophobic (A) to small size and polar (S) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

1 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:

Prevents G1 cell cycle arrest; reduced protein phosphorylation. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs2073498 [ dbSNP | Ensembl ]

Sequence information Variant position:

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

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

VERDTNVDEPVEWETPDLSQ A EIEQKIKEYNAQINSNLFMS 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                         VERDTNVDEPVEWETPDLSQAEIEQKIKEYNAQINSNLFMS

Mouse                         LERDTNVDEAVERETPDLSQAETEQKIKDYNGQINSNLFMS

Caenorhabditis elegans        VERYVKEDTPFEW-TDEYKEMDLERKIHSYNS-LAKGMEIT

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	2 – 344	Ras association domain-containing protein 1
Alternative sequence	1 – 155	Missing. In isoform B.
Alternative sequence	84 – 149	RLSADCKFTCHYRCRALVCLDCCGPRDLGWEPAVERDTNVDEPVEWETPDLSQAEIEQKIKEYNAQ -> QQGRFLHRLHQGSAEAGAPCLCALQQEATLLAGCPAGPRTGHKCQAPHFLLPAQGCCQAPACAVTHKGT. In isoform G.
Alternative sequence	93 – 344	Missing. In isoform F.
Alternative sequence	123 – 123	V -> VPILQ. In isoform E.

Literature citations
Epigenetic inactivation of RASSF1A in lung and breast cancers and malignant phenotype suppression.
Burbee D.G.; Forgacs E.; Zochbauer-Muller S.; Shivakumar L.; Fong K.; Gao B.; Randle D.; Kondo M.; Virmani A.; Bader S.; Sekido Y.; Latif F.; Milchgrub S.; Toyooka S.; Gazdar A.F.; Lerman M.I.; Zabarovsky E.; White M.; Minna J.D.;
J. Natl. Cancer Inst. 93:691-699(2001)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; C; D; E; F AND G); FUNCTION; TISSUE SPECIFICITY; VARIANTS GLN-21; CYS-53; GLU-133; SER-137 AND CYS-329; The RASSF1A tumor suppressor blocks cell cycle progression and inhibits cyclin D1 accumulation.
Shivakumar L.; Minna J.; Sakamaki T.; Pestell R.; White M.A.;
Mol. Cell. Biol. 22:4309-4318(2002)
Cited for: FUNCTION; VARIANT PHE-135; CHARACTERIZATION OF VARIANTS PHE-135 AND SER-137;

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.