FANCE_HUMAN
ID FANCE_HUMAN Reviewed; 536 AA.
AC Q9HB96; A8K907; Q4ZGH2;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Fanconi anemia group E protein;
DE Short=Protein FACE;
GN Name=FANCE; Synonyms=FACE;
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], AND INVOLVEMENT IN FANCE.
RX PubMed=11001585; DOI=10.1016/s0002-9297(07)62959-0;
RA de Winter J.P., Leveille F., van Berkel C.G.M., Rooimans M.A.,
RA van der Weel L., Steltenpool J., Demuth I., Morgan N.V., Alon N.,
RA Bosnoyan-Collins L., Lightfoot J., Leegwater P.A., Waisfisz Q., Komatsu K.,
RA Arwert F., Pronk J.C., Mathew C.G., Digweed M., Buchwald M., Joenje H.;
RT "Isolation of a cDNA representing the Fanconi anemia complementation group
RT E gene.";
RL Am. J. Hum. Genet. 67:1306-1308(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-89; LEU-204; ARG-340;
RP GLN-343 AND THR-502.
RG NIEHS SNPs program;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12093742; DOI=10.1093/emboj/cdf355;
RA Pace P., Johnson M., Tan W.M., Mosedale G., Sng C., Hoatlin M.E.,
RA de Winter J.P., Joenje H., Gergely F., Patel K.J.;
RT "FANCE: the link between Fanconi anaemia complex assembly and activity.";
RL EMBO J. 21:3414-3423(2002).
RN [8]
RP INTERACTION WITH FANCC AND FANCD2.
RX PubMed=12649160; DOI=10.1182/blood-2002-11-3517;
RA Gordon S.M., Buchwald M.;
RT "Fanconi anemia protein complex: mapping protein interactions in the yeast
RT 2- and 3-hybrid systems.";
RL Blood 102:136-141(2003).
RN [9]
RP IDENTIFICATION IN A COMPLEX WITH FANCA; FANCC; 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 [10]
RP IDENTIFICATION IN A COMPLEX WITH FANCA; FANCB; FANCC; 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 [11]
RP IDENTIFICATION IN A COMPLEX WITH FANCA; FANCB; FANCC; 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 [12]
RP FUNCTION IN DNA REPAIR, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-346
RP AND SER-374, MUTAGENESIS OF THR-346 AND SER-374, AND UBIQUITINATION.
RX PubMed=17296736; DOI=10.1128/mcb.02357-06;
RA Wang X., Kennedy R.D., Ray K., Stuckert P., Ellenberger T., D'Andrea A.D.;
RT "Chk1-mediated phosphorylation of FANCE is required for the Fanconi
RT anemia/BRCA pathway.";
RL Mol. Cell. Biol. 27:3098-3108(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP VARIANT FANCE GLN-184.
RX PubMed=17924555; DOI=10.1002/humu.20625;
RA Ameziane N., Errami A., Leveille F., Fontaine C., de Vries Y.,
RA van Spaendonk R.M., de Winter J.P., Pals G., Joenje H.;
RT "Genetic subtyping of Fanconi anemia by comprehensive mutation screening.";
RL Hum. Mutat. 29:159-166(2008).
CC -!- FUNCTION: As part of the Fanconi anemia (FA) complex functions in DNA
CC cross-links repair. Required for the nuclear accumulation of FANCC and
CC provides a critical bridge between the FA complex and FANCD2.
CC {ECO:0000269|PubMed:12093742, ECO:0000269|PubMed:17296736}.
CC -!- SUBUNIT: Belongs to the multisubunit FA complex composed of FANCA,
CC FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM. The complex is
CC not found in FA patients. Interacts with FANCC and FANCD2.
CC {ECO:0000269|PubMed:12649160, ECO:0000269|PubMed:12724401,
CC ECO:0000269|PubMed:15502827, ECO:0000269|PubMed:16116422,
CC ECO:0000269|PubMed:22266823}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12093742,
CC ECO:0000269|PubMed:17296736}.
CC -!- PTM: Phosphorylated. Phosphorylation by CHEK1 at Thr-346 and Ser-374
CC regulates its function in DNA cross-links repair.
CC {ECO:0000269|PubMed:17296736}.
CC -!- PTM: Ubiquitinated. Phosphorylation by CHEK1 induces polyubiquitination
CC and degradation. {ECO:0000269|PubMed:17296736}.
CC -!- DISEASE: Fanconi anemia complementation group E (FANCE) [MIM:600901]: 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:11001585, ECO:0000269|PubMed:17924555}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FANCEID293.html";
CC -!- WEB RESOURCE: Name=Fanconi Anemia Mutation Database;
CC URL="https://www2.rockefeller.edu/fanconi/genes/jumpe";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/fance/";
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DR EMBL; AF265210; AAG16743.1; -; mRNA.
DR EMBL; DQ020173; AAY26395.1; -; Genomic_DNA.
DR EMBL; AK292522; BAF85211.1; -; mRNA.
DR EMBL; AL022721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03830.1; -; Genomic_DNA.
DR EMBL; BC046359; AAH46359.1; -; mRNA.
DR CCDS; CCDS4805.1; -.
DR RefSeq; NP_068741.1; NM_021922.2.
DR PDB; 2ILR; X-ray; 2.00 A; A=273-536.
DR PDB; 7KZP; EM; 3.10 A; E=1-536.
DR PDB; 7KZQ; EM; 4.20 A; E=1-536.
DR PDB; 7KZR; EM; 4.20 A; E=1-536.
DR PDB; 7KZS; EM; 4.20 A; E=1-536.
DR PDB; 7KZT; EM; 4.20 A; E=1-536.
DR PDB; 7KZV; EM; 4.20 A; E=1-536.
DR PDBsum; 2ILR; -.
DR PDBsum; 7KZP; -.
DR PDBsum; 7KZQ; -.
DR PDBsum; 7KZR; -.
DR PDBsum; 7KZS; -.
DR PDBsum; 7KZT; -.
DR PDBsum; 7KZV; -.
DR AlphaFoldDB; Q9HB96; -.
DR SMR; Q9HB96; -.
DR BioGRID; 108475; 35.
DR ComplexPortal; CPX-6263; Fanconi anemia ubiquitin ligase complex.
DR CORUM; Q9HB96; -.
DR DIP; DIP-32845N; -.
DR IntAct; Q9HB96; 13.
DR MINT; Q9HB96; -.
DR STRING; 9606.ENSP00000229769; -.
DR iPTMnet; Q9HB96; -.
DR PhosphoSitePlus; Q9HB96; -.
DR BioMuta; FANCE; -.
DR DMDM; 45476978; -.
DR EPD; Q9HB96; -.
DR jPOST; Q9HB96; -.
DR MassIVE; Q9HB96; -.
DR MaxQB; Q9HB96; -.
DR PaxDb; Q9HB96; -.
DR PeptideAtlas; Q9HB96; -.
DR PRIDE; Q9HB96; -.
DR ProteomicsDB; 81510; -.
DR TopDownProteomics; Q9HB96; -.
DR Antibodypedia; 4446; 200 antibodies from 30 providers.
DR DNASU; 2178; -.
DR Ensembl; ENST00000229769.3; ENSP00000229769.2; ENSG00000112039.5.
DR GeneID; 2178; -.
DR KEGG; hsa:2178; -.
DR MANE-Select; ENST00000229769.3; ENSP00000229769.2; NM_021922.3; NP_068741.1.
DR UCSC; uc003oko.2; human.
DR CTD; 2178; -.
DR DisGeNET; 2178; -.
DR GeneCards; FANCE; -.
DR GeneReviews; FANCE; -.
DR HGNC; HGNC:3586; FANCE.
DR HPA; ENSG00000112039; Low tissue specificity.
DR MalaCards; FANCE; -.
DR MIM; 600901; phenotype.
DR MIM; 613976; gene.
DR neXtProt; NX_Q9HB96; -.
DR OpenTargets; ENSG00000112039; -.
DR Orphanet; 84; Fanconi anemia.
DR PharmGKB; PA28000; -.
DR VEuPathDB; HostDB:ENSG00000112039; -.
DR eggNOG; ENOG502QQV6; Eukaryota.
DR GeneTree; ENSGT00390000000705; -.
DR HOGENOM; CLU_037283_0_0_1; -.
DR InParanoid; Q9HB96; -.
DR OMA; PQICQRN; -.
DR OrthoDB; 575714at2759; -.
DR PhylomeDB; Q9HB96; -.
DR TreeFam; TF330720; -.
DR PathwayCommons; Q9HB96; -.
DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
DR SignaLink; Q9HB96; -.
DR SIGNOR; Q9HB96; -.
DR BioGRID-ORCS; 2178; 56 hits in 1080 CRISPR screens.
DR EvolutionaryTrace; Q9HB96; -.
DR GeneWiki; FANCE; -.
DR GenomeRNAi; 2178; -.
DR Pharos; Q9HB96; Tbio.
DR PRO; PR:Q9HB96; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9HB96; protein.
DR Bgee; ENSG00000112039; Expressed in buccal mucosa cell and 121 other tissues.
DR ExpressionAtlas; Q9HB96; baseline and differential.
DR Genevisible; Q9HB96; HS.
DR GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
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; NAS:UniProtKB.
DR GO; GO:0036297; P:interstrand cross-link repair; IC:ComplexPortal.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:ComplexPortal.
DR CDD; cd07439; FANCE_c-term; 1.
DR InterPro; IPR039685; FANCE.
DR InterPro; IPR021025; Fanconi_anaemia_gr_E_prot_C.
DR PANTHER; PTHR32094; PTHR32094; 1.
DR Pfam; PF11510; FA_FANCE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; DNA damage; DNA repair; Fanconi anemia;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..536
FT /note="Fanconi anemia group E protein"
FT /id="PRO_0000087187"
FT REGION 150..371
FT /note="Interaction with FANCC"
FT /evidence="ECO:0000269|PubMed:12649160"
FT REGION 171..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 346
FT /note="Phosphothreonine; by CHEK1"
FT /evidence="ECO:0000269|PubMed:17296736"
FT MOD_RES 374
FT /note="Phosphoserine; by CHEK1"
FT /evidence="ECO:0000269|PubMed:17296736"
FT VARIANT 89
FT /note="R -> L (in dbSNP:rs45600543)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_023372"
FT VARIANT 184
FT /note="P -> Q (in FANCE; uncertain pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:17924555"
FT /id="VAR_038022"
FT VARIANT 204
FT /note="S -> L (in dbSNP:rs7761870)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_023373"
FT VARIANT 340
FT /note="G -> R (in dbSNP:rs45524646)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_023374"
FT VARIANT 343
FT /note="R -> Q (in dbSNP:rs45467798)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_023375"
FT VARIANT 502
FT /note="A -> T (in dbSNP:rs9462088)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_023376"
FT MUTAGEN 346
FT /note="T->A: Non-phosphorylatable by CHEK1, not
FT polyubiquitinated and unable to complement the mitomycin C
FT hypersensitivity of cells lacking FANCE; when associated
FT with A-374."
FT /evidence="ECO:0000269|PubMed:17296736"
FT MUTAGEN 374
FT /note="S->A: Non-phosphorylatable by CHEK1, not
FT polyubiquitinated and unable to complement the mitomycin C
FT hypersensitivity of cells lacking FANCE; when associated
FT with A-346."
FT /evidence="ECO:0000269|PubMed:17296736"
FT HELIX 282..299
FT /evidence="ECO:0007829|PDB:2ILR"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:2ILR"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:2ILR"
FT HELIX 321..331
FT /evidence="ECO:0007829|PDB:2ILR"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:2ILR"
FT HELIX 338..350
FT /evidence="ECO:0007829|PDB:2ILR"
FT HELIX 357..374
FT /evidence="ECO:0007829|PDB:2ILR"
FT HELIX 381..393
FT /evidence="ECO:0007829|PDB:2ILR"
FT HELIX 395..408
FT /evidence="ECO:0007829|PDB:2ILR"
FT HELIX 414..425
FT /evidence="ECO:0007829|PDB:2ILR"
FT HELIX 431..443
FT /evidence="ECO:0007829|PDB:2ILR"
FT HELIX 448..458
FT /evidence="ECO:0007829|PDB:2ILR"
FT HELIX 466..477
FT /evidence="ECO:0007829|PDB:2ILR"
FT HELIX 487..499
FT /evidence="ECO:0007829|PDB:2ILR"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:2ILR"
FT HELIX 506..516
FT /evidence="ECO:0007829|PDB:2ILR"
FT STRAND 518..523
FT /evidence="ECO:0007829|PDB:2ILR"
FT HELIX 524..534
FT /evidence="ECO:0007829|PDB:2ILR"
SQ SEQUENCE 536 AA; 58711 MW; 0E94D8C469C791A5 CRC64;
MATPDAGLPG AEGVEPAPWA QLEAPARLLL QALQAGPEGA RRGLGVLRAL GSRGWEPFDW
GRLLEALCRE EPVVQGPDGR LELKPLLLRL PRICQRNLMS LLMAVRPSLP ESGLLSVLQI
AQQDLAPDPD AWLRALGELL RRDLGVGTSM EGASPLSERC QRQLQSLCRG LGLGGRRLKS
PQAPDPEEEE NRDSQQPGKR RKDSEEEAAS PEGKRVPKRL RCWEEEEDHE KERPEHKSLE
SLADGGSASP IKDQPVMAVK TGEDGSNLDD AKGLAESLEL PKAIQDQLPR LQQLLKTLEE
GLEGLEDAPP VELQLLHECS PSQMDLLCAQ LQLPQLSDLG LLRLCTWLLA LSPDLSLSNA
TVLTRSLFLG RILSLTSSAS RLLTTALTSF CAKYTYPVCS ALLDPVLQAP GTGPAQTELL
CCLVKMESLE PDAQVLMLGQ ILELPWKEET FLVLQSLLER QVEMTPEKFS VLMEKLCKKG
LAATTSMAYA KLMLTVMTKY QANITETQRL GLAMALEPNT TFLRKSLKAA LKHLGP
