UniProtKB/SwissProt variant VAR

Histone deacetylase 8
Gene: HDAC8
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Variant information Variant position:

320 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 Arginine (R) at position 320 (G320R, p.Gly320Arg). 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 large size and basic (R) 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 CDLS5. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs398122909 [ dbSNP | Ensembl ]

Sequence information Variant position:

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

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

ILGGGGYNLANTARCWTYLT G VILGKTLSSEIPDHEFFTAY 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                         ILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAY

Mouse                         ILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAY

Rat                           ILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAY

Bovine                        ILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAY

Xenopus laevis                ILGGGGYHLPNTARCWTYLTALIVGRTLSSEIPDHEFFTEY

Xenopus tropicalis            ILGGGGYHLPNTARCWTYLTALIVGRTLSSEIPDHEFFTEY

Zebrafish                     LLGGGGYNLANTARCWTYLTGTVLGQTLSSEIPDHEFFTEY

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 – 377	Histone deacetylase 8
Region	14 – 324	Histone deacetylase
Binding site	306 – 306
Alternative sequence	147 – 377	Missing. In isoform 8.
Alternative sequence	159 – 377	Missing. In isoform 7.
Alternative sequence	257 – 377	Missing. In isoform 6.
Alternative sequence	273 – 377	Missing. In isoform 5.
Mutagenesis	306 – 306	Y -> F. Loss of catalytic activity. Complete loss of catalytic activity; when associated with A-101.
Helix	308 – 323

Literature citations
HDAC8 mutations in Cornelia de Lange syndrome affect the cohesin acetylation cycle.
Deardorff M.A.; Bando M.; Nakato R.; Watrin E.; Itoh T.; Minamino M.; Saitoh K.; Komata M.; Katou Y.; Clark D.; Cole K.E.; De Baere E.; Decroos C.; Di Donato N.; Ernst S.; Francey L.J.; Gyftodimou Y.; Hirashima K.; Hullings M.; Ishikawa Y.; Jaulin C.; Kaur M.; Kiyono T.; Lombardi P.M.; Magnaghi-Jaulin L.; Mortier G.R.; Nozaki N.; Petersen M.B.; Seimiya H.; Siu V.M.; Suzuki Y.; Takagaki K.; Wilde J.J.; Willems P.J.; Prigent C.; Gillessen-Kaesbach G.; Christianson D.W.; Kaiser F.J.; Jackson L.G.; Hirota T.; Krantz I.D.; Shirahige K.;
Nature 489:313-317(2012)
Cited for: FUNCTION; CATALYTIC ACTIVITY; VARIANTS CDLS5 ARG-180; MET-311; ARG-320 AND ARG-334;

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.

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9BY41: Variant p.Gly320Arg