UniProtKB/Swiss-Prot P10645: Variant p.Arg392Gln

Chromogranin-A
Gene: CHGA
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Variant information Variant position:

392 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 Arginine (R) to Glutamine (Q) at position 392 (R392Q, p.Arg392Gln). 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 large size and basic (R) to medium size and polar (Q) 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:

No effect on plasmin-mediated proteolytic processing; decrease in ability to inhibit nicotine-evoked catecholamine secretion in vitro. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs9658669 [ dbSNP | Ensembl ]

Sequence information Variant position:

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

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

MKLSFRARAYGFRGPGPQLR R GWRPSSREDSLEAGLPLQVR 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                         MKLSFRARAYGFRGPGPQLRRGWRPSSREDSLEAGLPLQVR

Mouse                         MKLSFRTRAYGFRDPGPQLRRGWRPSSREDSVEA------R

Rat                           MKLSFRARAYGFRDPGPQLRRGWRPSSREDSVEA------R

Bovine                        MRLSFRARGYGFRGPGLQLRRGWRPNSREDSVEAGLPLQVR

Horse                         MKLSFRARAYGFRGPGLQLRRGWRPSSREDSIEAGLPPPVR

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	19 – 457	Chromogranin-A
Region	88 – 440	Disordered
Modified residue	372 – 372	Methionine sulfoxide
Modified residue	398 – 398	Phosphoserine
Modified residue	402 – 402	Phosphoserine

Literature citations
The catecholamine release-inhibitory 'catestatin' fragment of chromogranin a: naturally occurring human variants with different potencies for multiple chromaffin cell nicotinic cholinergic responses.
Mahata S.K.; Mahata M.; Wen G.; Wong W.B.; Mahapatra N.R.; Hamilton B.A.; O'Connor D.T.;
Mol. Pharmacol. 66:1180-1191(2004)
Cited for: VARIANTS SER-382; LEU-388 AND GLN-392; CHARACTERIZATION OF VARIANTS SER-382; LEU-388 AND GLN-392; FUNCTION (CATESTATIN); Proteolytic cleavage of human chromogranin a containing naturally occurring catestatin variants: differential processing at catestatin region by plasmin.
Biswas N.; Vaingankar S.M.; Mahata M.; Das M.; Gayen J.R.; Taupenot L.; Torpey J.W.; O'Connor D.T.; Mahata S.K.;
Endocrinology 149:749-757(2008)
Cited for: VARIANTS SER-382; LEU-388 AND GLN-392; CHARACTERIZATION OF VARIANTS SER-382; LEU-388 AND GLN-392; PROTEOLYTIC PROCESSING;

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.