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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q8IWE4: Variant p.Ser239Phe

DCN1-like protein 3
Gene: DCUN1D3
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Variant information Variant position: help 239 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Serine (S) to Phenylalanine (F) at position 239 (S239F, p.Ser239Phe). 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: help Change from small size and polar (S) to large size and aromatic (F) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In a cancer; uncertain significance. Any additional useful information about the variant.


Sequence information Variant position: help 239 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 304 The length of the canonical sequence.
Location on the sequence: help PVLDQWLNFLTENPSGIKGI S RDTWNMFLNFTQVIGPDLSN 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human                         PVLDQWLNFLTENPSGIKGISRDTWNMFLNFTQVIGPDLSN

Mouse                         PVLDQWLNFLTENPSGIKGISRDTWNMFLNFTQVIGPDLSN

Rat                           PVLDQWLNFLTENPSGIKGISRDTWNMFLNFTQVIGPDLSN

Bovine                        PVLDQWLNFLTENPSGIKGISRDTWNMFLNFTQVIGPDLSN

Xenopus laevis                LILDQWLEFLTENPSGIKGISRDTWNMFLNFTQVIGPDLSN

Xenopus tropicalis            LILDQWLDFLTENPSGIKGISRDTWNMFLNFTQVIGPDLSN

Drosophila                    DLFSNWIHFLEKHPN-IRRIPKDTWNMYLNFTEQC--DIQN

Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 2 – 304 DCN1-like protein 3
Domain 86 – 278 DCUN1
Mutagenesis 241 – 241 D -> A. Loss of interaction with CUL1, CUL2, CUL3, CULA4, CULA5, CAND1 and RBX1; when associated with R-265 and A-271. Does not affect both nucleus and cytoplasm localization; when associated with R-265 and A-271. Loss of interaction with CUL3; when associated with R-265 and A-271.
Mutagenesis 241 – 241 D -> N. Loss of CAND1-, CUL1-, CUL3- and RBX1-binding. Loss of function of inhibition of DCUN1D1-mediated CUL1 neddylation, but no effect on localization at the cell membrane; when associated with R-265 and N-271.



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.