UniProtKB/Swiss-Prot Q14457: Variant p.Ala103Val

Beclin-1
Gene: BECN1
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Variant information Variant position:

103 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 Valine (V) at position 103 (A103V, p.Ala103Val). 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 medium size and hydrophobic (V) 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

Sequence information Variant position:

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

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

IPPARMMSTESANSFTLIGE A SDGGTMENLSRRLKVTGDLF 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                         IP----PARMMSTESANSFTLIGEASDGGTM---------------EN---------LSRRLKVTGDLF

Mouse                         IP----PARMMSTESANSFTLIGEASDGGTM----------

Rat                           IP----PARMMSTESANSFTLIGEASDGGTM----------

Pig                           IP----PARMMSTESANSFTLIGEASDGGTM----------

Bovine                        IP----PARMMSTESANSFTLIGEASDGGTM----------

Chicken                       IP----PARMMSTESANSFTLIGEASDGGTM----------

Xenopus laevis                IP----PARMMSTESATSFTLIGEASDGGTM----------

Xenopus tropicalis            IP----PARMMSTESATSFTLIGEASDGGTM----------

Zebrafish                     IP----PARMMSAESTNSFTLIGEASDGGTM----------

Drosophila                    VP----PYRLTDSINGTGFMLV---SDGRDN----------

Baker's yeast                 TSNSREDQRYGNANGNDNKKANSDTSDGTSTFRDHDEEEQE

Fission yeast                 VP----PPEL-RTPTLDSFVVLPAAKDGYEE----------

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 – 450	Beclin-1
Modified residue	90 – 90	Phosphoserine; by AMPK
Modified residue	93 – 93	Phosphoserine; by AMPK
Modified residue	96 – 96	Phosphoserine; by AMPK
Modified residue	119 – 119	Phosphothreonine; by DAPK1
Mutagenesis	90 – 90	S -> A. Complete loss of phosphorylation. Complete loss of phosphorylation and defective autophagic function; when associated with Ala-93.
Mutagenesis	93 – 93	S -> A. Partial loss of phosphorylation. Complete loss of phosphorylation and defective autophagic function; when associated with Ala-90.
Mutagenesis	112 – 112	L -> A. Weakly decreases interaction with MUHV-4 M11, greatly decreases interaction with BCL2L1 isoform Bcl-X(L).
Mutagenesis	116 – 116	L -> A. Decreases interaction with BCL2L1 isoform Bcl-X(L).
Mutagenesis	117 – 117	K -> A. Weakly decreases interaction with MUHV-4 M11, greatly decreases interaction with BCL2L1 isoform Bcl-X(L).
Mutagenesis	117 – 117	K -> R. Does not affect ubiquitination by the DCX(AMBRA1) complex.
Mutagenesis	120 – 120	G -> E. Decreases interaction with MUHV-4 M11, disrupts interaction with BCL2L1 isoform Bcl-X(L).
Mutagenesis	121 – 121	D -> A. No effect on interaction with MUHV-4 M11, disrupts interaction with BCL2L1 isoform Bcl-X(L).
Mutagenesis	123 – 123	F -> A. Weakly decreases interaction with MUHV-4 M11, disrupts interaction with BCL2 and decreases interaction with BCL2L1 isoform Bcl-X(L). Reduces interaction with BCL2L10.

Literature citations
No reference for the current variant in UniProtKB/Swiss-Prot.

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.