UniProtKB/SwissProt variant VAR

Small COPII coat GTPase SAR1B
Gene: SAR1B
Feedback?

Variant information Variant position:

137 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 Aspartate (D) to Asparagine (N) at position 137 (D137N, p.Asp137Asn). 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 medium size and acidic (D) to medium size and polar (N) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

1 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 CMRD; reduced affinity for GDP/GTP. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs28942109 [ dbSNP | Ensembl ]

Sequence information Variant position:

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

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

SLMTDETIANVPILILGNKI D RPEAISEERLREMFGLYGQT 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                         SLMTDETIANVPILILGNKIDRPEAISEERLREMFGLYGQT

Mouse                         SLMTDETIANVPILILGNKIDRPEAISEERLREMFGLYGQT

Rat                           SLMTDETIANVPILILGNKIDRPEAISEERLREMFGLYGQT

Pig                           SLMTDETVANVPILILGNKIDRPEAISEERLREMFGLYGQT

Bovine                        SLMTDETVANVPILILGNKIDRPEAISEERLREMFGLYGQT

Slime mold                    DILGDEHLSQSPLLILGSKCDAKGHHNRENLIDLLDI----

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 – 198	Small COPII coat GTPase SAR1B
Binding site	134 – 134
Binding site	134 – 134
Binding site	135 – 135
Binding site	135 – 135
Binding site	137 – 137
Binding site	137 – 137
Mutagenesis	122 – 122	E -> A. Loss of interaction with MIOS. Loss of localization to lysosomal membrane. Loss of function in negative regulation of TORC1 signaling.
Mutagenesis	141 – 141	A -> D. Loss of leucine binding. Constitutive negative regulation of TORC1 signaling.
Mutagenesis	144 – 144	E -> A. Loss of leucine binding. Constitutive negative regulation of TORC1 signaling.

Literature citations
Mutations in a Sar1 GTPase of COPII vesicles are associated with lipid absorption disorders.
Jones B.; Jones E.L.; Bonney S.A.; Patel H.N.; Mensenkamp A.R.; Eichenbaum-Voline S.; Rudling M.; Myrdal U.; Annesi G.; Naik S.; Meadows N.; Quattrone A.; Islam S.A.; Naoumova R.P.; Angelin B.; Infante R.; Levy E.; Roy C.C.; Freemont P.S.; Scott J.; Shoulders C.C.;
Nat. Genet. 34:29-31(2003)
Cited for: VARIANTS CMRD ARG-37; ASN-137 AND ARG-179; TISSUE SPECIFICITY;

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 Q9Y6B6: Variant p.Asp137Asn