Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P22830: Variant p.Cys406Ser

Ferrochelatase, mitochondrial
Gene: FECH
Feedback?
Variant information Variant position: help 406 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 Cysteine (C) to Serine (S) at position 406 (C406S, p.Cys406Ser). 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 medium size and polar (C) to small size and polar (S) 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 EPP1; enzyme almost inactive. Any additional useful information about the variant.


Sequence information Variant position: help 406 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 423 The length of the canonical sequence.
Location on the sequence: help HSHIQSNELCSKQLTLSCPL C VNPVCRETKSFFTSQQL 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                         HSHIQSNE-LCSKQLTLSCPLCV--NPVCRETKSFFTSQQL-

Chimpanzee                    HSHIQSNE-LCSKQLTLSCPLCV--NPVCRETKSFFTS

Mouse                         HSHIQSNK-LCSTQLSLNCPLCV--NPVCRKTKSFFTS

Bovine                        HSHLQSKE-RCSTQLTLSCPLCV--NPTCRETKSFFTS

Chicken                       CSHIQSNE-ICSKQLTLCCPLCV--NPVCRETKAFFTN

Xenopus laevis                LSHMKSSE-ICSKQLSLRCPMCV--NPVCGEAKSFFTK

Drosophila                    ADHLKSQQ-AVNPKFLMRCPMCS--NPKCRESKSWYRQ

Slime mold                    NTHLKSNKTIHSNQYHLKCPGCKDDSTFCRTISNPIQA

Baker's yeast                 KSHLQSNQ-LYSNQLPLDFALGKSNDPV-KDLSLVFGN

Fission yeast                 AEHLKAKV-PYSRQFTQRCPGCT--SESCAERINFFQD
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 55 – 423 Ferrochelatase, mitochondrial
Binding site 403 – 403
Binding site 406 – 406
Binding site 411 – 411
Modified residue 415 – 415 N6-acetyllysine; alternate
Modified residue 415 – 415 N6-succinyllysine; alternate
Mutagenesis 395 – 395 C -> S. No loss of activity.
Mutagenesis 403 – 403 C -> DH. Loss of activity.
Mutagenesis 406 – 406 C -> DHS. Loss of activity.
Mutagenesis 411 – 411 C -> HS. Loss of activity.
Mutagenesis 417 – 417 F -> L. Decreased activity.
Mutagenesis 417 – 417 F -> YW. Greatly reduced activity.



Literature citations
Mutations in the iron-sulfur cluster ligands of the human ferrochelatase lead to erythropoietic protoporphyria.
Schneider-Yin X.; Gouya L.; Dorsey M.; Ruefenacht U.; Deybach J.-C.; Ferreira G.C.;
Blood 96:1545-1549(2000)
Cited for: VARIANTS EPP1 SER-406; TYR-406 AND 408-ASN--CYS-411 DELINS LYS-SER-VAL-GLY; CHARACTERIZATION OF VARIANTS EPP1 SER-406; TYR-406 AND 408-ASN--CYS-411 DELINS LYS-SER-VAL-GLY;
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.