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UniProtKB/Swiss-Prot P08686: Variant p.Arg356Gln

Steroid 21-hydroxylase
Gene: CYP21A2
Variant information

Variant position:  356
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 Arginine (R) to Glutamine (Q) at position 356 (R356Q, p.Arg356Gln).
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:  In AH3; simple virilizing form; mild; 0.65% activity.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  356
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  494
The length of the canonical sequence.

Location on the sequence:   YKDRARLPLLNATIAEVLRL  R PVVPLALPHRTTRPSSISGY
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                         YKDRARLPLLNATIAEVLRLRPVVPLALPHRTTRPSSISGY

                              YRDPTRLPLLSATVAEVLRLRPVVPLALPHCTTRPSSISGY

Mouse                         YRNRMQLPLLMATIAEVLRLRPVVPLALPHRATRASSISGY

Rat                           YKNRMQLPLLMATIAEVLRLRPVVPMALPHRATKASSISGY

Pig                           YKDRARLPLLNATIAEVLRLRPVVPLALPHRATRPSSIFGY

Bovine                        YKDRARLPLLNATIAEVLRLRPVVPLALPHRTTRPSSIFGY

Cat                           LKDPSRLPLLTATIAEVLRLRPVVPLALPHRTTRHSSILGY

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.

TypePositionsDescription
Chain 1 – 494 Steroid 21-hydroxylase
Region 342 – 358 Steroid-binding


Literature citations

A cluster of missense mutations at Arg356 of human steroid 21-hydroxylase may impair redox partner interaction.
Lajic S.; Levo A.; Nikoshkov A.; Lundberg Y.; Partanen J.; Wedell A.;
Hum. Genet. 99:704-709(1997)
Cited for: VARIANTS AH3 PRO-356 AND GLN-356;

Identification of CYP21 mutations, one novel, by single strand conformational polymorphism (SSCP) analysis.
Witchel S.F.; Smith R.; Suda-Hartman M.;
Hum. Mutat. 13:172-172(1999)
Cited for: VARIANTS AH3 TYR-169; LEU-281 AND GLN-356;

Detection and assignment of CYP21 mutations using peptide mass signature genotyping.
Zeng X.; Witchel S.F.; Dobrowolski S.F.; Moulder P.V.; Jarvik J.W.; Telmer C.A.;
Mol. Genet. Metab. 82:38-47(2004)
Cited for: VARIANTS AH3 LEU-30; ASN-172; ASN-236; GLU-237; LYS-239; LEU-281; SER-291; GLN-356; TRP-356; TYR-365; SER-453; LEU-479 AND PRO-483; VARIANT ARG-102;

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.