UniProtKB/Swiss-Prot O95163: Variant p.Pro1158Leu

Elongator complex protein 1
Gene: ELP1
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Variant information Variant position:

1158 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 Proline (P) to Leucine (L) at position 1158 (P1158L, p.Pro1158Leu). 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:

Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-3 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:

Reduced interaction with ELP2; does not affect interaction with ELP3; does not affect dimerization. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs1538660 [ dbSNP | Ensembl ]

Sequence information Variant position:

1158 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

1332 The length of the canonical sequence.
Location on the sequence:

LLVVRELKEQAQQAGLDDEV P HGQESDLFSETSSVVSGSEM 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                         LLVVRELKEQAQQAGLDDEVPHGQESDLFSETSSVVSGSEM

Mouse                         LQVVRALRRQAPQVHVDHEVAHGPESDLFSETSSIMSGSEM

Rat                           LKVVRELKSQRPRVHVDHEVAHGRETDLFSETSSIRSGSEM

Rabbit                        LLEVRELKERAQQVDLDDEMPHGQEADLFSETSSIVSGSEM

Xenopus laevis                LSVVREMKEKARLGLLDEDVTGCAEADLFSDTSSIMTASDA

Drosophila                    LLDIRRNQAKSGEGYIDTDV-NLKEVDLLSDTTSLHSSQ--

Baker's yeast                 LRELRAKKEENPYAFYGQETE--QADDVSVAPSETSTQESF

Fission yeast                 ILVLREKKKEDPISWMEGTMEDQTPDDISLASTSLSTNRSL

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 – 1332	Elongator complex protein 1
Region	885 – 1332	Mediates dimerization
Region	1150 – 1208	Disordered
Modified residue	1171 – 1171	Phosphoserine
Modified residue	1174 – 1174	Phosphoserine

Literature citations
The full-ORF clone resource of the German cDNA consortium.
Bechtel S.; Rosenfelder H.; Duda A.; Schmidt C.P.; Ernst U.; Wellenreuther R.; Mehrle A.; Schuster C.; Bahr A.; Bloecker H.; Heubner D.; Hoerlein A.; Michel G.; Wedler H.; Koehrer K.; Ottenwaelder B.; Poustka A.; Wiemann S.; Schupp I.;
BMC Genomics 8:399-399(2007)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 961-1332; VARIANTS SER-1072 AND LEU-1158; Dimerization of elongator protein 1 is essential for Elongator complex assembly.
Xu H.; Lin Z.; Li F.; Diao W.; Dong C.; Zhou H.; Xie X.; Wang Z.; Shen Y.; Long J.;
Proc. Natl. Acad. Sci. U.S.A. 112:10697-10702(2015)
Cited for: X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) OF 715-1332; SUBUNIT; IDENTIFICATION IN THE ELONGATOR COMPLEX; DIMERIZATION REGION; CHARACTERIZATION OF VARIANTS PRO-696; LEU-914; SER-1072 AND LEU-1158; MUTAGENESIS OF ARG-1011;

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.