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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q00597: Variant p.Leu554Pro

Fanconi anemia group C protein
Gene: FANCC
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Variant information Variant position: help 554 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 Leucine (L) to Proline (P) at position 554 (L554P, p.Leu554Pro). 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 Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 FANCC; loss of activity; loss of CDK1-binding and IFNG-induced STAT1-binding; abnormal EIF2AK2 activation and augmented cell death. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 554 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 558 The length of the canonical sequence.
Location on the sequence: help NRLGIESPRSEKLARELLKE L RTQV 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                         NRLGIESPRSEKLARELLKELRTQV-------

Mouse                         QHLCVEA--SRKLARDLLKELQAQV

Rat                           HHLCVEA--SRKLARELLKDLQAQV

Bovine                        DHLCVEAHRSRKLARELLTELREQA
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 1 – 558 Fanconi anemia group C protein



Literature citations
Cloning of cDNAs for Fanconi's anaemia by functional complementation.
Strathdee C.A.; Gavish H.; Shannon W.R.; Buchwald M.;
Nature 356:763-767(1992)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; INVOLVEMENT IN FANCC; VARIANT FANCC PRO-554; The Fanconi anemia polypeptide, FAC, binds to the cyclin-dependent kinase, cdc2.
Kupfer G.M.; Yamashita T.; Naf D.; Suliman A.; Asano S.; D'Andrea A.D.;
Blood 90:1047-1054(1997)
Cited for: INTERACTION WITH CDK1; SUBCELLULAR LOCATION; DEVELOPMENTAL STAGE; INVOLVEMENT IN FANCC; CHARACTERIZATION OF VARIANT FANCC PRO-554; The Fanconi anemia complementation group C gene product: structural evidence of multifunctionality.
Pang Q.; Christianson T.A.; Keeble W.; Diaz J.; Faulkner G.R.; Reifsteck C.; Olson S.; Bagby G.C.;
Blood 98:1392-1401(2001)
Cited for: FUNCTION; INTERACTION WITH STAT1; CHARACTERIZATION OF VARIANT FANCC PRO-554; MUTAGENESIS OF PHE-64; THR-66; SER-249; GLU-251; THR-529 AND TYR-531; The Fanconi anemia proteins functionally interact with the protein kinase regulated by RNA (PKR).
Zhang X.; Li J.; Sejas D.P.; Rathbun K.R.; Bagby G.C.; Pang Q.;
J. Biol. Chem. 279:43910-43919(2004)
Cited for: IDENTIFICATION IN A COMPLEX WITH EIF2AK2; FANCA; FANCG AND HSP70; CHARACTERIZATION OF VARIANT FANCC PRO-554; A Leu554-to-Pro substitution completely abolishes the functional complementing activity of the Fanconi anemia (FACC) protein.
Gavish H.; Dos Santos C.C.; Buchwald M.;
Hum. Mol. Genet. 2:123-126(1993)
Cited for: CHARACTERIZATION OF VARIANT FANCC PRO-554; Mutation analysis of the Fanconi anemia gene FACC.
Verlander P.C.; Lin J.D.; Udono M.U.; Zhang Q.; Gibson R.A.; Mathew C.G.; Auerbach A.D.;
Am. J. Hum. Genet. 54:595-601(1994)
Cited for: VARIANTS FANCC VAL-195 AND PRO-554; VARIANTS PHE-26 AND GLU-139;
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.