ID FANCG_HUMAN Reviewed; 622 AA. AC O15287; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 215. DE RecName: Full=Fanconi anemia group G protein; DE Short=Protein FACG; DE AltName: Full=DNA repair protein XRCC9; GN Name=FANCG; Synonyms=XRCC9; 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]. RX PubMed=9256465; DOI=10.1073/pnas.94.17.9232; RA Liu N., Lamerdin J.E., Tucker J.D., Zhou Z.-Q., Walter C.A., Albala J.S., RA Busch D.B., Thompson L.H.; RT "The human XRCC9 gene corrects chromosomal instability and mutagen RT sensitivities in CHO UV40 cells."; RL Proc. Natl. Acad. Sci. U.S.A. 94:9232-9237(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX PubMed=9806548; DOI=10.1038/3093; RA De Winter J.P., Waisfisz Q., Rooimans M.A., Van Berkel C.G.M., RA Bosnoyan-Collins L., Alon N., Carreau M., Bender O., Demuth I., RA Schindler D., Pronk J.C., Arwert F., Hoehn H., Digweed M., Buchwald M., RA Joenje H.; RT "The Fanconi anaemia group G gene FANCG is identical with XRCC9."; RL Nat. Genet. 20:281-283(1998). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-294; ILE-297; SER-330; RP LEU-378; GLU-430; GLN-513 AND PHE-603. RG NIEHS SNPs program; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney, and Uterus; 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 [6] RP CHARACTERIZATION. RX PubMed=10373536; DOI=10.1128/mcb.19.7.4866; RA Garcia-Higuera I., Kuang Y., Naf D., Wasik J., D'Andrea A.D.; RT "Fanconi anemia proteins FANCA, FANCC, and FANCG/XRCC9 interact in a RT functional nuclear complex."; RL Mol. Cell. Biol. 19:4866-4873(1999). RN [7] RP IDENTIFICATION IN A COMPLEX WITH FANCA; FANCC; FANCE; FANCF 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 [8] RP IDENTIFICATION IN A COMPLEX WITH EIF2AK2; FANCA; FANCC AND HSP70. 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 [9] RP IDENTIFICATION IN A COMPLEX WITH FANCA; FANCB; FANCC; FANCE; FANCF 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 [10] RP IDENTIFICATION IN A COMPLEX WITH FANCA; FANCB; FANCC; FANCE; FANCF; 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 [11] RP INTERACTION WITH BRCA2; FANCD2 AND XRCC3, PHOSPHORYLATION AT SER-7, AND RP MUTAGENESIS OF SER-7; SER-383 AND SER-387. RX PubMed=18212739; DOI=10.1038/sj.onc.1211034; RA Wilson J.B., Yamamoto K., Marriott A.S., Hussain S., Sung P., Hoatlin M.E., RA Mathew C.G., Takata M., Thompson L.H., Kupfer G.M., Jones N.J.; RT "FANCG promotes formation of a newly identified protein complex containing RT BRCA2, FANCD2 and XRCC3."; RL Oncogene 27:3641-3652(2008). RN [12] RP IDENTIFICATION IN THE FA COMPLEX. RX PubMed=22343915; DOI=10.1182/blood-2011-10-385963; RA Ali A.M., Pradhan A., Singh T.R., Du C., Li J., Wahengbam K., Grassman E., RA Auerbach A.D., Pang Q., Meetei A.R.; RT "FAAP20: a novel ubiquitin-binding FA nuclear core-complex protein required RT for functional integrity of the FA-BRCA DNA repair pathway."; RL Blood 119:3285-3294(2012). RN [13] RP IDENTIFICATION IN THE FA COMPLEX. RX PubMed=22705371; DOI=10.1016/j.molcel.2012.05.026; RA Yan Z., Guo R., Paramasivam M., Shen W., Ling C., Fox D. III, Wang Y., RA Oostra A.B., Kuehl J., Lee D.Y., Takata M., Hoatlin M.E., Schindler D., RA Joenje H., de Winter J.P., Li L., Seidman M.M., Wang W.; RT "A ubiquitin-binding protein, FAAP20, links RNF8-mediated ubiquitination to RT the Fanconi anemia DNA repair network."; RL Mol. Cell 47:61-75(2012). RN [14] 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 [15] RP VARIANT FANCG PRO-71. RX PubMed=11093276; DOI=10.1038/sj.ejhg.5200552; RA Demuth I., Wlodarski M., Tipping A.J., Morgan N.V., de Winter J.P., RA Thiel M., Grasl S., Schindler D., D'Andrea A.D., Altay C., Kayserili H., RA Zatterale A., Kunze J., Ebell W., Mathew C.G., Joenje H., Sperling K., RA Digweed M.; RT "Spectrum of mutations in the Fanconi anaemia group G gene, FANCG/XRCC9."; RL Eur. J. Hum. Genet. 8:861-868(2000). RN [16] RP VARIANT [LARGE SCALE ANALYSIS] THR-607. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [17] RP VARIANT FANCG PRO-71, INTERACTION WITH HES1, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF GLY-546. RX PubMed=18550849; DOI=10.1182/blood-2008-04-152710; RA Tremblay C.S., Huang F.F., Habi O., Huard C.C., Godin C., Levesque G., RA Carreau M.; RT "HES1 is a novel interactor of the Fanconi anemia core complex."; RL Blood 112:2062-2070(2008). 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. Candidate tumor suppressor gene. 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. In complex with FANCF, FANCA and FANCL, but CC not with FANCC, nor FANCE, interacts with HES1; this interaction may be CC essential for the stability and nuclear localization of FA core complex CC proteins. The complex with FANCC and FANCG may also include EIF2AK2 and CC HSP70. When phosphorylated at Ser-7, forms a complex with BRCA2, FANCD2 CC and XRCC3. {ECO:0000269|PubMed:12724401, ECO:0000269|PubMed:15299030, CC ECO:0000269|PubMed:15502827, ECO:0000269|PubMed:16116422, CC ECO:0000269|PubMed:18212739, ECO:0000269|PubMed:18550849, CC ECO:0000269|PubMed:22266823, ECO:0000269|PubMed:22343915, CC ECO:0000269|PubMed:22705371}. CC -!- INTERACTION: CC O15287; Q92870-2: APBB2; NbExp=3; IntAct=EBI-81610, EBI-21535880; CC O15287; P54252: ATXN3; NbExp=3; IntAct=EBI-81610, EBI-946046; CC O15287; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-81610, EBI-10175300; CC O15287; P08684: CYP3A4; NbExp=3; IntAct=EBI-81610, EBI-3928618; CC O15287; G5E9A7: DMWD; NbExp=3; IntAct=EBI-81610, EBI-10976677; CC O15287; O15360: FANCA; NbExp=13; IntAct=EBI-81610, EBI-81570; CC O15287; O15360-3: FANCA; NbExp=5; IntAct=EBI-81610, EBI-21315382; CC O15287; Q9NPI8: FANCF; NbExp=4; IntAct=EBI-81610, EBI-81589; CC O15287; P14136: GFAP; NbExp=3; IntAct=EBI-81610, EBI-744302; CC O15287; Q53GS7: GLE1; NbExp=3; IntAct=EBI-81610, EBI-1955541; CC O15287; P04792: HSPB1; NbExp=3; IntAct=EBI-81610, EBI-352682; CC O15287; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-81610, EBI-1055254; CC O15287; O60333-2: KIF1B; NbExp=3; IntAct=EBI-81610, EBI-10975473; CC O15287; O14901: KLF11; NbExp=3; IntAct=EBI-81610, EBI-948266; CC O15287; P19404: NDUFV2; NbExp=3; IntAct=EBI-81610, EBI-713665; CC O15287; P29474: NOS3; NbExp=3; IntAct=EBI-81610, EBI-1391623; CC O15287; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-81610, EBI-2811583; CC O15287; P16284: PECAM1; NbExp=3; IntAct=EBI-81610, EBI-716404; CC O15287; Q13393: PLD1; NbExp=3; IntAct=EBI-81610, EBI-2827556; CC O15287; Q99633: PRPF18; NbExp=3; IntAct=EBI-81610, EBI-2798416; CC O15287; P60891: PRPS1; NbExp=3; IntAct=EBI-81610, EBI-749195; CC O15287; P20339: RAB5A; NbExp=3; IntAct=EBI-81610, EBI-399437; CC O15287; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-81610, EBI-5235340; CC O15287; Q13813: SPTAN1; NbExp=4; IntAct=EBI-81610, EBI-351450; CC O15287; P51687: SUOX; NbExp=3; IntAct=EBI-81610, EBI-3921347; CC O15287; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-81610, EBI-11955057; CC O15287; Q8N7U7-2: TPRX1; NbExp=3; IntAct=EBI-81610, EBI-14115717; CC O15287; P08670: VIM; NbExp=3; IntAct=EBI-81610, EBI-353844; CC O15287; O76024: WFS1; NbExp=3; IntAct=EBI-81610, EBI-720609; CC O15287; Q86UD4: ZNF329; NbExp=3; IntAct=EBI-81610, EBI-7233259; CC O15287; P14079: tax; Xeno; NbExp=3; IntAct=EBI-81610, EBI-9675698; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18550849}. Cytoplasm CC {ECO:0000269|PubMed:18550849}. Note=The major form is nuclear. The CC minor form is cytoplasmic. CC -!- TISSUE SPECIFICITY: Highly expressed in testis and thymus. Found in CC lymphoblasts. CC -!- DISEASE: Fanconi anemia complementation group G (FANCG) [MIM:614082]: 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:11093276, ECO:0000269|PubMed:18550849}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- WEB RESOURCE: Name=Fanconi Anemia Mutation Database; CC URL="https://www2.rockefeller.edu/fanconi/genes/jumpg"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/295/FANCG"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/fancg/"; 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; U70310; AAB80802.1; -; mRNA. DR EMBL; AJ007669; CAA07602.1; -; mRNA. DR EMBL; AY795970; AAV40841.1; -; Genomic_DNA. DR EMBL; AC004472; AAC07981.1; -; Genomic_DNA. DR EMBL; AL353795; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000032; AAH00032.1; -; mRNA. DR EMBL; BC011623; AAH11623.1; -; mRNA. DR CCDS; CCDS6574.1; -. DR PIR; T02244; T02244. DR RefSeq; NP_004620.1; NM_004629.1. DR PDB; 7KZP; EM; 3.10 A; G/H=1-622. DR PDB; 7KZQ; EM; 4.20 A; G/H=1-622. DR PDB; 7KZR; EM; 4.20 A; G/H=1-622. DR PDB; 7KZS; EM; 4.20 A; G/H=1-622. DR PDB; 7KZT; EM; 4.20 A; G/H=1-622. DR PDB; 7KZV; EM; 4.20 A; G/H=1-622. DR PDBsum; 7KZP; -. DR PDBsum; 7KZQ; -. DR PDBsum; 7KZR; -. DR PDBsum; 7KZS; -. DR PDBsum; 7KZT; -. DR PDBsum; 7KZV; -. DR AlphaFoldDB; O15287; -. 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; O15287; -. DR BioGRID; 108484; 109. DR ComplexPortal; CPX-6263; Fanconi anemia ubiquitin ligase complex. DR CORUM; O15287; -. DR IntAct; O15287; 81. DR MINT; O15287; -. DR STRING; 9606.ENSP00000367910; -. DR MoonDB; O15287; Predicted. DR iPTMnet; O15287; -. DR PhosphoSitePlus; O15287; -. DR BioMuta; FANCG; -. DR EPD; O15287; -. DR jPOST; O15287; -. DR MassIVE; O15287; -. DR PaxDb; 9606-ENSP00000367910; -. DR PeptideAtlas; O15287; -. DR ProteomicsDB; 48561; -. DR Pumba; O15287; -. DR Antibodypedia; 25694; 489 antibodies from 37 providers. DR DNASU; 2189; -. DR Ensembl; ENST00000378643.8; ENSP00000367910.4; ENSG00000221829.11. DR Ensembl; ENST00000448890.2; ENSP00000409607.2; ENSG00000221829.11. DR GeneID; 2189; -. DR KEGG; hsa:2189; -. DR MANE-Select; ENST00000378643.8; ENSP00000367910.4; NM_004629.2; NP_004620.1. DR AGR; HGNC:3588; -. DR CTD; 2189; -. DR DisGeNET; 2189; -. DR GeneCards; FANCG; -. DR GeneReviews; FANCG; -. DR HGNC; HGNC:3588; FANCG. DR HPA; ENSG00000221829; Low tissue specificity. DR MalaCards; FANCG; -. DR MIM; 602956; gene. DR MIM; 614082; phenotype. DR neXtProt; NX_O15287; -. DR OpenTargets; ENSG00000221829; -. DR Orphanet; 84; Fanconi anemia. DR PharmGKB; PA28002; -. DR VEuPathDB; HostDB:ENSG00000221829; -. DR eggNOG; ENOG502QVUI; Eukaryota. DR GeneTree; ENSGT00390000007195; -. DR HOGENOM; CLU_018870_0_0_1; -. DR InParanoid; O15287; -. DR OMA; CCLAWRA; -. DR OrthoDB; 5304064at2759; -. DR PhylomeDB; O15287; -. DR TreeFam; TF330722; -. DR PathwayCommons; O15287; -. DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway. DR Reactome; R-HSA-9833482; PKR-mediated signaling. DR SignaLink; O15287; -. DR SIGNOR; O15287; -. DR BioGRID-ORCS; 2189; 79 hits in 1172 CRISPR screens. DR ChiTaRS; FANCG; human. DR GeneWiki; FANCG; -. DR GenomeRNAi; 2189; -. DR Pharos; O15287; Tbio. DR PRO; PR:O15287; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; O15287; Protein. DR Bgee; ENSG00000221829; Expressed in ventricular zone and 160 other cell types or tissues. DR ExpressionAtlas; O15287; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:ComplexPortal. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0043240; C:Fanconi anaemia nuclear complex; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0003684; F:damaged DNA binding; TAS:ProtInc. DR GO; GO:0006974; P:DNA damage response; IBA:GO_Central. DR GO; GO:0006281; P:DNA repair; TAS:ProtInc. DR GO; GO:0036297; P:interstrand cross-link repair; NAS:ComplexPortal. DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB. DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl. DR GO; GO:0009314; P:response to radiation; IEA:Ensembl. DR GO; GO:0007286; P:spermatid development; IEA:Ensembl. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1. DR InterPro; IPR039684; FANCG. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. DR PANTHER; PTHR15254:SF2; FANCONI ANEMIA GROUP G PROTEIN; 1. DR PANTHER; PTHR15254; FANCONI ANEMIA GROUP G PROTEIN FAMILY MEMBER; 1. DR SMART; SM00028; TPR; 3. DR SUPFAM; SSF48452; TPR-like; 2. DR Genevisible; O15287; HS. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Disease variant; DNA damage; DNA repair; KW Fanconi anemia; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW TPR repeat. FT CHAIN 1..622 FT /note="Fanconi anemia group G protein" FT /id="PRO_0000106292" FT REPEAT 246..279 FT /note="TPR 1" FT REPEAT 344..377 FT /note="TPR 2" FT REPEAT 453..486 FT /note="TPR 3" FT REPEAT 514..547 FT /note="TPR 4" FT MOD_RES 7 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18212739" FT VARIANT 71 FT /note="L -> P (in FANCG; associated with a mild clinical FT phenotype; disruption of HES1-binding; no effect on FT FANCA-binding)" FT /evidence="ECO:0000269|PubMed:11093276, FT ECO:0000269|PubMed:18550849" FT /id="VAR_017495" FT VARIANT 294 FT /note="G -> E (in dbSNP:rs17880082)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_021103" FT VARIANT 297 FT /note="T -> I (in dbSNP:rs2237857)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_020311" FT VARIANT 330 FT /note="P -> S (in dbSNP:rs4986940)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_021104" FT VARIANT 378 FT /note="S -> L (in dbSNP:rs4986939)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_021105" FT VARIANT 430 FT /note="K -> E (in dbSNP:rs17881054)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_021106" FT VARIANT 513 FT /note="R -> Q (in dbSNP:rs17885240)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_021107" FT VARIANT 603 FT /note="S -> F (in dbSNP:rs17878854)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_021108" FT VARIANT 607 FT /note="A -> T (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs758407400)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035864" FT MUTAGEN 7 FT /note="S->A: Loss of BRCA2-, FANCD2- and XRCC3-binding. No FT effect on complex formation with FANCA and FANCF." FT /evidence="ECO:0000269|PubMed:18212739" FT MUTAGEN 383 FT /note="S->A: No effect on BRCA2-, FANCA-, FANCF-, nor FT XRCC3-binding." FT /evidence="ECO:0000269|PubMed:18212739" FT MUTAGEN 387 FT /note="S->A: No effect on BRCA2-, FANCA-, FANCF-, nor FT XRCC3-binding." FT /evidence="ECO:0000269|PubMed:18212739" FT MUTAGEN 546 FT /note="G->R: No effect on HES1-, nor FANCA-binding." FT /evidence="ECO:0000269|PubMed:18550849" SQ SEQUENCE 622 AA; 68554 MW; 4BC7475472AC3C84 CRC64; MSRQTTSVGS SCLDLWREKN DRLVRQAKVA QNSGLTLRRQ QLAQDALEGL RGLLHSLQGL PAAVPVLPLE LTVTCNFIIL RASLAQGFTE DQAQDIQRSL ERVLETQEQQ GPRLEQGLRE LWDSVLRASC LLPELLSALH RLVGLQAALW LSADRLGDLA LLLETLNGSQ SGASKDLLLL LKTWSPPAEE LDAPLTLQDA QGLKDVLLTA FAYRQGLQEL ITGNPDKALS SLHEAASGLC PRPVLVQVYT ALGSCHRKMG NPQRALLYLV AALKEGSAWG PPLLEASRLY QQLGDTTAEL ESLELLVEAL NVPCSSKAPQ FLIEVELLLP PPDLASPLHC GTQSQTKHIL ASRCLQTGRA GDAAEHYLDL LALLLDSSEP RFSPPPSPPG PCMPEVFLEA AVALIQAGRA QDALTLCEEL LSRTSSLLPK MSRLWEDARK GTKELPYCPL WVSATHLLQG QAWVQLGAQK VAISEFSRCL ELLFRATPEE KEQGAAFNCE QGCKSDAALQ QLRAAALISR GLEWVASGQD TKALQDFLLS VQMCPGNRDT YFHLLQTLKR LDRRDEATAL WWRLEAQTKG SHEDALWSLP LYLESYLSWI RPSDRDAFLE EFRTSLPKSC DL //