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 27-MAR-2024, entry version 203. 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="https://atlasgeneticsoncology.org/gene/101/FACC"; 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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-23085; -. DR EMDB; EMD-23086; -. DR EMDB; EMD-23087; -. DR EMDB; EMD-23088; -. DR EMDB; EMD-23089; -. DR EMDB; EMD-23090; -. DR SMR; Q00597; -. DR BioGRID; 108473; 90. DR ComplexPortal; CPX-6263; Fanconi anemia ubiquitin ligase complex. DR CORUM; Q00597; -. DR DIP; DIP-32846N; -. DR IntAct; Q00597; 37. DR MINT; Q00597; -. DR STRING; 9606.ENSP00000289081; -. DR GlyGen; Q00597; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q00597; -. DR PhosphoSitePlus; Q00597; -. DR BioMuta; FANCC; -. DR DMDM; 1706762; -. DR EPD; Q00597; -. DR MassIVE; Q00597; -. DR MaxQB; Q00597; -. DR PaxDb; 9606-ENSP00000289081; -. DR PeptideAtlas; Q00597; -. DR ProteomicsDB; 57860; -. DR Pumba; Q00597; -. DR Antibodypedia; 4496; 470 antibodies from 35 providers. DR DNASU; 2176; -. DR Ensembl; ENST00000289081.8; ENSP00000289081.3; ENSG00000158169.14. DR Ensembl; ENST00000375305.6; ENSP00000364454.1; ENSG00000158169.14. 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 AGR; HGNC:3584; -. 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; 2918906at2759; -. 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 Reactome; R-HSA-9833482; PKR-mediated signaling. DR SignaLink; Q00597; -. DR SIGNOR; Q00597; -. DR BioGRID-ORCS; 2176; 76 hits in 1165 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 119 other cell types or tissues. DR ExpressionAtlas; Q00597; baseline and differential. 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; NAS: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: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:SF0; FANCONI ANEMIA GROUP C PROTEIN; 1. DR PANTHER; PTHR16798; FANCONI ANEMIA GROUP C PROTEIN FANCC; 1. DR Pfam; PF02106; Fanconi_C; 1. DR PIRSF; PIRSF018417; FACC_protein; 1. DR PRINTS; PR00494; FANCONICGENE. DR Genevisible; Q00597; HS. 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 FT CDK1-binding and IFNG-induced STAT1-binding; abnormal FT EIF2AK2 activation and augmented cell death; FT 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 FT STAT1-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 FT STAT1-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 FT STAT1-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 FT STAT1-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 //