FANCC_HUMAN
ID FANCC_HUMAN Reviewed; 558 AA.
AC Q00597; B1ALR8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Fanconi anemia group C protein;
DE Short=Protein FACC;
GN Name=FANCC; Synonyms=FAC, FACC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN FANCC, AND VARIANT FANCC
RP PRO-554.
RC TISSUE=Lymphoid tissue;
RX PubMed=1574115; DOI=10.1038/356763a0;
RA Strathdee C.A., Gavish H., Shannon W.R., Buchwald M.;
RT "Cloning of cDNAs for Fanconi's anaemia by functional complementation.";
RL Nature 356:763-767(1992).
RN [2]
RP ERRATUM OF PUBMED:1574115, AND SEQUENCE REVISION TO 179-192.
RX PubMed=1641028; DOI=10.1038/358434a0;
RA Strathdee C.A., Gavish H., Shannon W.R., Buchwald M.;
RL Nature 358:434-434(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8490620; DOI=10.1093/hmg/2.1.35;
RA Gibson R.A., Buchwald M., Roberts R.G., Mathew C.G.;
RT "Characterisation of the exon structure of the Fanconi anaemia group C gene
RT by vectorette PCR.";
RL Hum. Mol. Genet. 2:35-38(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-80; GLU-139 AND
RP MET-449.
RG NIEHS SNPs program;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=7517562; DOI=10.1073/pnas.91.14.6712;
RA Yamashita T., Barber D.L., Zhu Y., Wu N., D'Andrea A.D.;
RT "The Fanconi anemia polypeptide FACC is localized to the cytoplasm.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6712-6716(1994).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=8058745; DOI=10.1073/pnas.91.17.7975;
RA Youssoufian H.;
RT "Localization of Fanconi anemia C protein to the cytoplasm of mammalian
RT cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:7975-7979(1994).
RN [10]
RP INTERACTION WITH CDK1, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP INVOLVEMENT IN FANCC, AND CHARACTERIZATION OF VARIANT FANCC PRO-554.
RX PubMed=9242535;
RA Kupfer G.M., Yamashita T., Naf D., Suliman A., Asano S., D'Andrea A.D.;
RT "The Fanconi anemia polypeptide, FAC, binds to the cyclin-dependent kinase,
RT cdc2.";
RL Blood 90:1047-1054(1997).
RN [11]
RP INTERACTION WITH ZBTB32.
RX PubMed=10572087;
RA Hoatlin M.E., Zhi Y., Ball H., Silvey K., Melnick A., Stone S., Arai S.,
RA Hawe N., Owen G., Zelent A., Licht J.D.;
RT "A novel BTB/POZ transcriptional repressor protein interacts with the
RT Fanconi anemia group C protein and PLZF.";
RL Blood 94:3737-3747(1999).
RN [12]
RP FUNCTION, INTERACTION WITH STAT1, CHARACTERIZATION OF VARIANT FANCC
RP PRO-554, AND MUTAGENESIS OF PHE-64; THR-66; SER-249; GLU-251; THR-529 AND
RP TYR-531.
RX PubMed=11520787; DOI=10.1182/blood.v98.5.1392;
RA Pang Q., Christianson T.A., Keeble W., Diaz J., Faulkner G.R.,
RA Reifsteck C., Olson S., Bagby G.C.;
RT "The Fanconi anemia complementation group C gene product: structural
RT evidence of multifunctionality.";
RL Blood 98:1392-1401(2001).
RN [13]
RP IDENTIFICATION IN A COMPLEX WITH FANCA; FANCE; FANCF; FANCG AND FANCL.
RX PubMed=12724401; DOI=10.1128/mcb.23.10.3417-3426.2003;
RA Meetei A.R., Sechi S., Wallisch M., Yang D., Young M.K., Joenje H.,
RA Hoatlin M.E., Wang W.;
RT "A multiprotein nuclear complex connects Fanconi anemia and Bloom
RT syndrome.";
RL Mol. Cell. Biol. 23:3417-3426(2003).
RN [14]
RP IDENTIFICATION IN A COMPLEX WITH EIF2AK2; FANCA; FANCG AND HSP70, AND
RP CHARACTERIZATION OF VARIANT FANCC PRO-554.
RX PubMed=15299030; DOI=10.1074/jbc.m403884200;
RA Zhang X., Li J., Sejas D.P., Rathbun K.R., Bagby G.C., Pang Q.;
RT "The Fanconi anemia proteins functionally interact with the protein kinase
RT regulated by RNA (PKR).";
RL J. Biol. Chem. 279:43910-43919(2004).
RN [15]
RP IDENTIFICATION IN A COMPLEX WITH FANCA; FANCB; FANCE; FANCF; FANCG AND
RP FANCL.
RX PubMed=15502827; DOI=10.1038/ng1458;
RA Meetei A.R., Levitus M., Xue Y., Medhurst A.L., Zwaan M., Ling C.,
RA Rooimans M.A., Bier P., Hoatlin M., Pals G., de Winter J.P., Wang W.,
RA Joenje H.;
RT "X-linked inheritance of Fanconi anemia complementation group B.";
RL Nat. Genet. 36:1219-1224(2004).
RN [16]
RP IDENTIFICATION IN A COMPLEX WITH FANCA; FANCB; FANCE; FANCF; FANCG; FANCL
RP AND FANCM.
RX PubMed=16116422; DOI=10.1038/ng1626;
RA Meetei A.R., Medhurst A.L., Ling C., Xue Y., Singh T.R., Bier P.,
RA Steltenpool J., Stone S., Dokal I., Mathew C.G., Hoatlin M., Joenje H.,
RA de Winter J.P., Wang W.;
RT "A human ortholog of archaeal DNA repair protein Hef is defective in
RT Fanconi anemia complementation group M.";
RL Nat. Genet. 37:958-963(2005).
RN [17]
RP IDENTIFICATION IN THE FA COMPLEX.
RX PubMed=22266823; DOI=10.1038/nsmb.2222;
RA Kim H., Yang K., Dejsuphong D., D'Andrea A.D.;
RT "Regulation of Rev1 by the Fanconi anemia core complex.";
RL Nat. Struct. Mol. Biol. 19:164-170(2012).
RN [18]
RP CHARACTERIZATION OF VARIANT FANCC PRO-554.
RX PubMed=8499901; DOI=10.1093/hmg/2.2.123;
RA Gavish H., Dos Santos C.C., Buchwald M.;
RT "A Leu554-to-Pro substitution completely abolishes the functional
RT complementing activity of the Fanconi anemia (FACC) protein.";
RL Hum. Mol. Genet. 2:123-126(1993).
RN [19]
RP VARIANT GLU-139.
RX PubMed=8348157; DOI=10.1038/ng0693-202;
RA Whitney M.A., Saito H., Jakops P.M., Gibson R.A., Moses R.E., Grompe M.;
RT "A common mutation in the FACC gene causes Fanconi anaemia in Ashkenazi
RT Jews.";
RL Nat. Genet. 4:202-205(1993).
RN [20]
RP VARIANTS FANCC VAL-195 AND PRO-554, AND VARIANTS PHE-26 AND GLU-139.
RX PubMed=8128956;
RA Verlander P.C., Lin J.D., Udono M.U., Zhang Q., Gibson R.A., Mathew C.G.,
RA Auerbach A.D.;
RT "Mutation analysis of the Fanconi anemia gene FACC.";
RL Am. J. Hum. Genet. 54:595-601(1994).
RN [21]
RP VARIANTS PHE-190; VAL-312; MET-449 AND ARG-465, AND VARIANT FANCC ARG-496.
RX PubMed=8844212;
RX DOI=10.1002/(sici)1098-1004(1996)8:2<140::aid-humu6>3.0.co;2-f;
RA Gibson R.A., Morgan N.V., Goldstein L.H., Pearson I.C., Kesterton I.P.,
RA Foot N.J., Jansen S., Havenga C., Pearson T., de Ravel T.J., Cohn R.J.,
RA Marques I.M., Dokal I., Roberts I., Marsh J., Ball S., Milner R.D.,
RA Llerena J.C. Jr., Samochatova E., Mohan S.P., Vasudevan P., Birjandi F.,
RA Hajianpour A., Murer-Orlando M., Mathew C.G.;
RT "Novel mutations and polymorphisms in the Fanconi anemia group C gene.";
RL Hum. Mutat. 8:140-148(1996).
CC -!- FUNCTION: DNA repair protein that may operate in a postreplication
CC repair or a cell cycle checkpoint function. May be implicated in
CC interstrand DNA cross-link repair and in the maintenance of normal
CC chromosome stability. Upon IFNG induction, may facilitate STAT1
CC activation by recruiting STAT1 to IFNGR1.
CC {ECO:0000269|PubMed:11520787}.
CC -!- SUBUNIT: Belongs to the multisubunit FA complex composed of FANCA,
CC FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM. This complex
CC may also include HSP70. The complex is not found in FA patients.
CC Interacts with ZBTB32. Upon IFNG induction, interacts with STAT1.
CC Interacts with CDK1. Interacts with EIF2AK2; interaction between FA
CC variants and EIF2AK2 may lead to augmented EIF2AK2 activation and cell
CC death. {ECO:0000269|PubMed:10572087, ECO:0000269|PubMed:11520787,
CC ECO:0000269|PubMed:12724401, ECO:0000269|PubMed:15299030,
CC ECO:0000269|PubMed:15502827, ECO:0000269|PubMed:16116422,
CC ECO:0000269|PubMed:22266823, ECO:0000269|PubMed:9242535}.
CC -!- INTERACTION:
CC Q00597; P14625: HSP90B1; NbExp=4; IntAct=EBI-81625, EBI-359129;
CC Q00597; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-81625, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=The major form is
CC nuclear. The minor form is cytoplasmic.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DEVELOPMENTAL STAGE: Expression increases during S phase, is maximal at
CC the G2/M transition, and declines during M phase (at protein level).
CC {ECO:0000269|PubMed:9242535}.
CC -!- DISEASE: Fanconi anemia complementation group C (FANCC) [MIM:227645]: A
CC disorder affecting all bone marrow elements and resulting in anemia,
CC leukopenia and thrombopenia. It is associated with cardiac, renal and
CC limb malformations, dermal pigmentary changes, and a predisposition to
CC the development of malignancies. At the cellular level it is associated
CC with hypersensitivity to DNA-damaging agents, chromosomal instability
CC (increased chromosome breakage) and defective DNA repair.
CC {ECO:0000269|PubMed:11520787, ECO:0000269|PubMed:15299030,
CC ECO:0000269|PubMed:1574115, ECO:0000269|PubMed:8128956,
CC ECO:0000269|PubMed:8499901, ECO:0000269|PubMed:8844212,
CC ECO:0000269|PubMed:9242535}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FACCID101.html";
CC -!- WEB RESOURCE: Name=Fanconi Anemia Mutation Database;
CC URL="https://www2.rockefeller.edu/fanconi/genes/jumpc";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/fancc/";
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DR EMBL; X66894; CAA47348.1; -; mRNA.
DR EMBL; X66893; CAA47347.1; -; mRNA.
DR EMBL; L02664; AAA53104.1; -; Genomic_DNA.
DR EMBL; L02651; AAA53104.1; JOINED; Genomic_DNA.
DR EMBL; L02652; AAA53104.1; JOINED; Genomic_DNA.
DR EMBL; L02653; AAA53104.1; JOINED; Genomic_DNA.
DR EMBL; L02654; AAA53104.1; JOINED; Genomic_DNA.
DR EMBL; L02655; AAA53104.1; JOINED; Genomic_DNA.
DR EMBL; L02656; AAA53104.1; JOINED; Genomic_DNA.
DR EMBL; L02657; AAA53104.1; JOINED; Genomic_DNA.
DR EMBL; L02658; AAA53104.1; JOINED; Genomic_DNA.
DR EMBL; L02659; AAA53104.1; JOINED; Genomic_DNA.
DR EMBL; L02660; AAA53104.1; JOINED; Genomic_DNA.
DR EMBL; L02661; AAA53104.1; JOINED; Genomic_DNA.
DR EMBL; L02662; AAA53104.1; JOINED; Genomic_DNA.
DR EMBL; L02663; AAA53104.1; JOINED; Genomic_DNA.
DR EMBL; AY220878; AAO26042.1; -; Genomic_DNA.
DR EMBL; AL157384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471174; EAW92626.1; -; Genomic_DNA.
DR EMBL; BC015748; AAH15748.1; -; mRNA.
DR CCDS; CCDS35071.1; -.
DR PIR; S21733; S21733.
DR RefSeq; NP_000127.2; NM_000136.2.
DR RefSeq; NP_001230672.1; NM_001243743.1.
DR RefSeq; XP_011516667.1; XM_011518365.2.
DR PDB; 7KZP; EM; 3.10 A; C=1-558.
DR PDB; 7KZQ; EM; 4.20 A; C=1-558.
DR PDB; 7KZR; EM; 4.20 A; C=1-558.
DR PDB; 7KZS; EM; 4.20 A; C=1-558.
DR PDB; 7KZT; EM; 4.20 A; C=1-558.
DR PDB; 7KZV; EM; 4.20 A; C=1-558.
DR PDBsum; 7KZP; -.
DR PDBsum; 7KZQ; -.
DR PDBsum; 7KZR; -.
DR PDBsum; 7KZS; -.
DR PDBsum; 7KZT; -.
DR PDBsum; 7KZV; -.
DR AlphaFoldDB; Q00597; -.
DR SMR; Q00597; -.
DR BioGRID; 108473; 86.
DR ComplexPortal; CPX-6263; Fanconi anemia ubiquitin ligase complex.
DR CORUM; Q00597; -.
DR DIP; DIP-32846N; -.
DR IntAct; Q00597; 34.
DR MINT; Q00597; -.
DR STRING; 9606.ENSP00000289081; -.
DR iPTMnet; Q00597; -.
DR PhosphoSitePlus; Q00597; -.
DR BioMuta; FANCC; -.
DR DMDM; 1706762; -.
DR EPD; Q00597; -.
DR MassIVE; Q00597; -.
DR MaxQB; Q00597; -.
DR PaxDb; Q00597; -.
DR PeptideAtlas; Q00597; -.
DR PRIDE; Q00597; -.
DR ProteomicsDB; 57860; -.
DR Antibodypedia; 4496; 442 antibodies from 35 providers.
DR DNASU; 2176; -.
DR Ensembl; ENST00000289081.8; ENSP00000289081.3; ENSG00000158169.13.
DR Ensembl; ENST00000375305.6; ENSP00000364454.1; ENSG00000158169.13.
DR GeneID; 2176; -.
DR KEGG; hsa:2176; -.
DR MANE-Select; ENST00000289081.8; ENSP00000289081.3; NM_000136.3; NP_000127.2.
DR UCSC; uc004avh.4; human.
DR CTD; 2176; -.
DR DisGeNET; 2176; -.
DR GeneCards; FANCC; -.
DR GeneReviews; FANCC; -.
DR HGNC; HGNC:3584; FANCC.
DR HPA; ENSG00000158169; Tissue enhanced (liver).
DR MalaCards; FANCC; -.
DR MIM; 227645; phenotype.
DR MIM; 613899; gene.
DR neXtProt; NX_Q00597; -.
DR OpenTargets; ENSG00000158169; -.
DR Orphanet; 84; Fanconi anemia.
DR PharmGKB; PA27997; -.
DR VEuPathDB; HostDB:ENSG00000158169; -.
DR eggNOG; ENOG502QSB8; Eukaryota.
DR GeneTree; ENSGT00390000016390; -.
DR HOGENOM; CLU_035819_0_0_1; -.
DR InParanoid; Q00597; -.
DR OMA; RWHHRAS; -.
DR OrthoDB; 1546359at2759; -.
DR PhylomeDB; Q00597; -.
DR TreeFam; TF330803; -.
DR PathwayCommons; Q00597; -.
DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR SignaLink; Q00597; -.
DR SIGNOR; Q00597; -.
DR BioGRID-ORCS; 2176; 62 hits in 1082 CRISPR screens.
DR ChiTaRS; FANCC; human.
DR GeneWiki; Fanconi_anemia,_complementation_group_C; -.
DR GenomeRNAi; 2176; -.
DR Pharos; Q00597; Tbio.
DR PRO; PR:Q00597; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q00597; protein.
DR Bgee; ENSG00000158169; Expressed in pancreatic ductal cell and 117 other tissues.
DR ExpressionAtlas; Q00597; baseline and differential.
DR Genevisible; Q00597; HS.
DR GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0043240; C:Fanconi anaemia nuclear complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0048854; P:brain morphogenesis; IEA:Ensembl.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR GO; GO:0007281; P:germ cell development; IEA:Ensembl.
DR GO; GO:0036297; P:interstrand cross-link repair; IC:ComplexPortal.
DR GO; GO:0002262; P:myeloid cell homeostasis; IEA:Ensembl.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:ComplexPortal.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:Ensembl.
DR InterPro; IPR000686; FANCC.
DR PANTHER; PTHR16798; PTHR16798; 1.
DR Pfam; PF02106; Fanconi_C; 1.
DR PIRSF; PIRSF018417; FACC_protein; 1.
DR PRINTS; PR00494; FANCONICGENE.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disease variant; DNA damage; DNA repair;
KW Fanconi anemia; Nucleus; Reference proteome.
FT CHAIN 1..558
FT /note="Fanconi anemia group C protein"
FT /id="PRO_0000087184"
FT VARIANT 26
FT /note="S -> F (in dbSNP:rs1800361)"
FT /evidence="ECO:0000269|PubMed:8128956"
FT /id="VAR_005225"
FT VARIANT 80
FT /note="I -> T (in dbSNP:rs4647419)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_016339"
FT VARIANT 139
FT /note="G -> E (in dbSNP:rs1800362)"
FT /evidence="ECO:0000269|PubMed:8128956,
FT ECO:0000269|PubMed:8348157, ECO:0000269|Ref.4"
FT /id="VAR_005226"
FT VARIANT 190
FT /note="L -> F (in dbSNP:rs1800364)"
FT /evidence="ECO:0000269|PubMed:8844212"
FT /id="VAR_005227"
FT VARIANT 195
FT /note="D -> V (in FANCC; dbSNP:rs1800365)"
FT /evidence="ECO:0000269|PubMed:8128956"
FT /id="VAR_005228"
FT VARIANT 312
FT /note="I -> V (in dbSNP:rs1800366)"
FT /evidence="ECO:0000269|PubMed:8844212"
FT /id="VAR_005229"
FT VARIANT 449
FT /note="V -> M (in dbSNP:rs1800367)"
FT /evidence="ECO:0000269|PubMed:8844212, ECO:0000269|Ref.4"
FT /id="VAR_005230"
FT VARIANT 465
FT /note="Q -> R (in dbSNP:rs1800368)"
FT /evidence="ECO:0000269|PubMed:8844212"
FT /id="VAR_005231"
FT VARIANT 496
FT /note="L -> R (in FANCC; dbSNP:rs121917785)"
FT /evidence="ECO:0000269|PubMed:8844212"
FT /id="VAR_005232"
FT VARIANT 554
FT /note="L -> P (in FANCC; loss of activity; loss of CDK1-
FT binding and IFNG-induced STAT1-binding; abnormal EIF2AK2
FT activation and augmented cell death; dbSNP:rs104886458)"
FT /evidence="ECO:0000269|PubMed:11520787,
FT ECO:0000269|PubMed:15299030, ECO:0000269|PubMed:1574115,
FT ECO:0000269|PubMed:8128956, ECO:0000269|PubMed:8499901,
FT ECO:0000269|PubMed:9242535"
FT /id="VAR_005233"
FT MUTAGEN 64
FT /note="F->A: No loss of protection from cross-linking
FT agent-induced toxicity. No effect on IFNG-induced STAT1-
FT binding."
FT /evidence="ECO:0000269|PubMed:11520787"
FT MUTAGEN 66
FT /note="T->A: No effect on protective function from
FT mitomycin C-genotoxicity."
FT /evidence="ECO:0000269|PubMed:11520787"
FT MUTAGEN 249
FT /note="S->A: No effect on protective function from
FT mitomycin C-genotoxicity. Loss of IFNG-induced STAT1-
FT binding."
FT /evidence="ECO:0000269|PubMed:11520787"
FT MUTAGEN 251
FT /note="E->A: No effect on protective function from
FT mitomycin C-genotoxicity. Loss of IFNG-induced STAT1-
FT binding."
FT /evidence="ECO:0000269|PubMed:11520787"
FT MUTAGEN 529
FT /note="T->A: No effect on protective function from
FT mitomycin C-genotoxicity."
FT /evidence="ECO:0000269|PubMed:11520787"
FT MUTAGEN 531
FT /note="Y->A: No effect on protective function from
FT mitomycin C-genotoxicity. No effect on IFNG-induced STAT1-
FT binding."
FT /evidence="ECO:0000269|PubMed:11520787"
FT CONFLICT 294
FT /note="Missing (in Ref. 3; AAA53104)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="Missing (in Ref. 1; CAA47348/CAA47347)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 558 AA; 63429 MW; C9DDFFAC725D050C CRC64;
MAQDSVDLSC DYQFWMQKLS VWDQASTLET QQDTCLHVAQ FQEFLRKMYE ALKEMDSNTV
IERFPTIGQL LAKACWNPFI LAYDESQKIL IWCLCCLINK EPQNSGQSKL NSWIQGVLSH
ILSALRFDKE VALFTQGLGY APIDYYPGLL KNMVLSLASE LRENHLNGFN TQRRMAPERV
ASLSRVCVPL ITLTDVDPLV EALLICHGRE PQEILQPEFF EAVNEAILLK KISLPMSAVV
CLWLRHLPSL EKAMLHLFEK LISSERNCLR RIECFIKDSS LPQAACHPAI FRVVDEMFRC
ALLETDGALE IIATIQVFTQ CFVEALEKAS KQLRFALKTY FPYTSPSLAM VLLQDPQDIP
RGHWLQTLKH ISELLREAVE DQTHGSCGGP FESWFLFIHF GGWAEMVAEQ LLMSAAEPPT
ALLWLLAFYY GPRDGRQQRA QTMVQVKAVL GHLLAMSRSS SLSAQDLQTV AGQGTDTDLR
APAQQLIRHL LLNFLLWAPG GHTIAWDVIT LMAHTAEITH EIIGFLDQTL YRWNRLGIES
PRSEKLAREL LKELRTQV
