UniProtKB/Swiss-Prot Q8IWE4: Variant p.Gly2Ser

DCN1-like protein 3
Gene: DCUN1D3
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Variant information Variant position:

2 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

US 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 2 (G2S, p.Gly2Ser). 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 a cancer; uncertain significance. Any additional useful information about the variant.

Sequence information Variant position:

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

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

M G QCVTKCKNPSSTLGSKNGDR 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                         MGQCV------------TKCKNPSSTLGSKNGDR

Mouse                         MGQCV------------TKCKN

Rat                           MGQCV------------TKCKN

Bovine                        MGQCV------------TKCKN

Xenopus laevis                MGQCV------------TKCKN

Xenopus tropicalis            MGQCV------------TKCKN

Drosophila                    MGNCLKCFQSAAEQSMPTNASS

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
Initiator methionine	1 – 1	Removed
Chain	2 – 304	DCN1-like protein 3
Region	1 – 86	Disordered
Compositional bias	1 – 21	Polar residues
Lipidation	2 – 2	N-myristoyl glycine
Mutagenesis	1 – 26	Missing. No effect on CAND1-, CUL1-, CUL3- and RBX1-binding.
Mutagenesis	2 – 2	G -> A. No effect on CAND1-, CUL1-, CUL3- and RBX1-binding. Loss of localization at the cell membrane. Loss of function of inhibition of DCUN1D1-mediated CUL1 neddylation. Loss of myristoylation. Loss of myristoylation; when associated with A-4. Loss of myristoylation; when associated with A-8. Loss of palmitoylation. Affects cell membrane localization, and localizes throughout the cytoplasm. Does not relocalizes CUL3 to the cell membrane.
Mutagenesis	4 – 4	C -> A. Does not affect myristoylation; when associated with A-8. Loss of myristoylation; when associated with A-2. Loss of palmitoylation; when associated with A-8. Reduces cell membrane localization.
Mutagenesis	8 – 8	C -> A. Does not affect myristoylation; when associated with A-4. Loss of myristoylation; when associated with A-2. Loss of palmitoylation; when associated with A-4. Reduces cell membrane localization.

Literature citations
SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity of SCCRO (DCUN1D1).
Huang G.; Stock C.; Bommelje C.C.; Weeda V.B.; Shah K.; Bains S.; Buss E.; Shaha M.; Rechler W.; Ramanathan S.Y.; Singh B.;
J. Biol. Chem. 289:34728-34742(2014)
Cited for: FUNCTION; INTERACTION WITH CAND1; CUL1; CUL3 AND RBX1; LACK OF INTERACTION WITH UBE2M; SUBCELLULAR LOCATION; TISSUE SPECIFICITY; MUTAGENESIS OF 1-MET--ASN-26; GLY-2; ASP-241; ALA-265 AND ASP-271; VARIANTS SER-2 AND PHE-239;

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.