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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P16435: Variant p.Ala284Pro

NADPH--cytochrome P450 reductase
Gene: POR
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Variant information Variant position: help 284 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Alanine (A) to Proline (P) at position 284 (A284P, p.Ala284Pro). 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: help Change from small size and hydrophobic (A) to medium size and hydrophobic (P) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In ABS1 and DISPORD; significant reduction of activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 284 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 677 The length of the canonical sequence.
Location on the sequence: help GRLKSYENQKPPFDAKNPFL A AVTTNRKLNQGTERHLMHLE 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human                         GR--LKSYENQKP-------PFDAKNPFLAAVTTNRKLNQG-TERHLMHLE

Mouse                         GR--LKSYENQKP-------PFDAKNPFLAAVTTNRKLNQG

Rat                           GR--LKSYENQKP-------PFDAKNPFLAAVTANRKLNQG

Pig                           GR--LKSYENQKP-------PFDAKNPFLAVVTTNRKLNQG

Bovine                        GR--LKSYENQKP-------PFDAKNPFLAVVTTNRKLNQG

Rabbit                        GR--LKSYENQKP-------PFDAKNPFLATVTTNRKLNQG

Drosophila                    AR--LHSIQNQRP-------PFDAKNPFLAPIKVNRELHKG

Slime mold                    KP---KLSTDNKV-------IYDMKNPYYAEVLENRELHSN

Baker's yeast                 SAHYLPSHQLNRNADGIQLGPFDLSQPYIAPIVKSRELFSS

Fission yeast                 SRQQLKGNVASKA-------PRSQANPFFSSPVRSLELFKS

Sequence annotation in neighborhood: help 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 2 – 677 NADPH--cytochrome P450 reductase
Topological domain 43 – 677 Cytoplasmic
Domain 279 – 521 FAD-binding FR-type
Binding site 298 – 298
Beta strand 282 – 291



Literature citations
Congenital adrenal hyperplasia caused by mutant P450 oxidoreductase and human androgen synthesis: analytical study.
Arlt W.; Walker E.A.; Draper N.; Ivison H.E.; Ride J.P.; Hammer F.; Chalder S.M.; Borucka-Mankiewicz M.; Hauffa B.P.; Malunowicz E.M.; Stewart P.M.; Shackleton C.H.L.;
Lancet 363:2128-2135(2004)
Cited for: VARIANTS DISPORD ASP-178; PRO-284; HIS-454 AND TYR-566; CHARACTERIZATION OF VARIANTS DISPORD ASP-178; PRO-284; HIS-454 AND TYR-566; Mutant P450 oxidoreductase causes disordered steroidogenesis with and without Antley-Bixler syndrome.
Flueck C.E.; Tajima T.; Pandey A.V.; Arlt W.; Okuhara K.; Verge C.F.; Jabs E.W.; Mendonca B.B.; Fujieda K.; Miller W.L.;
Nat. Genet. 36:228-230(2004)
Cited for: VARIANTS ABS1 PRO-284; HIS-454 AND GLU-489; VARIANTS DISPORD TYR-566 AND PHE-605; CHARACTERIZATION OF VARIANTS ABS1 PRO-284; HIS-454 AND GLU-489; CHARACTERIZATION OF VARIANTS DISPORD TYR-566 AND PHE-605;
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.