FANCI_HUMAN
ID FANCI_HUMAN Reviewed; 1328 AA.
AC Q9NVI1; A4ZVE4; A5YMH4; A6NJZ0; Q96JN1; Q96ST0; Q9BT96;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 4.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Fanconi anemia group I protein;
DE Short=Protein FACI;
GN Name=FANCI; Synonyms=KIAA1794;
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] (ISOFORM 3), FUNCTION, UBIQUITINATION AT
RP LYS-523, PHOSPHORYLATION AT SER-730; THR-952 AND SER-1121, SUBCELLULAR
RP LOCATION, INTERACTION WITH FANCD2, VARIANTS FANCI LEU-55 AND GLN-1285, AND
RP CHARACTERIZATION OF VARIANTS FANCI LEU-55 AND GLN-1285.
RX PubMed=17412408; DOI=10.1016/j.cell.2007.03.009;
RA Smogorzewska A., Matsuoka S., Vinciguerra P., McDonald E.R. III,
RA Hurov K.E., Luo J., Ballif B.A., Gygi S.P., Hofmann K., D'Andrea A.D.,
RA Elledge S.J.;
RT "Identification of the FANCI protein, a monoubiquitinated FANCD2 paralog
RT required for DNA repair.";
RL Cell 129:289-301(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, UBIQUITINATION AT
RP LYS-523, SUBCELLULAR LOCATION, INTERACTION WITH FANCD2, AND VARIANT FANCI
RP TYR-858.
RX PubMed=17460694; DOI=10.1038/nsmb1252;
RA Sims A.E., Spiteri E., Sims R.J. III, Arita A.G., Lach F.P., Landers T.,
RA Wurm M., Freund M., Neveling K., Hanenberg H., Auerbach A.D., Huang T.T.;
RT "FANCI is a second monoubiquitinated member of the Fanconi anemia
RT pathway.";
RL Nat. Struct. Mol. Biol. 14:564-567(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT
RP VAL-86.
RC TISSUE=Brain, and Skin;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 175-1324 (ISOFORM 2), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 342-1328 (ISOFORM 1), AND VARIANT SER-742.
RC TISSUE=Teratocarcinoma;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 527-1328 (ISOFORM 3), AND VARIANT
RP SER-742.
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [7]
RP PROTEIN SEQUENCE OF 438-447; 781-788; 809-819; 885-897; 965-994 AND
RP 1079-1094, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP FUNCTION, VARIANT FANCI GLN-1285, AND VARIANT LEU-55.
RX PubMed=17452773; DOI=10.1155/2007/151968;
RA Dorsman J.C., Levitus M., Rockx D., Rooimans M.A., Oostra A.B.,
RA Haitjema A., Bakker S.T., Steltenpool J., Schuler D., Mohan S.,
RA Schindler D., Arwert F., Pals G., Mathew C.G., Waisfisz Q., de Winter J.P.,
RA Joenje H.;
RT "Identification of the Fanconi anemia complementation group I gene,
RT FANCI.";
RL Cell. Oncol. 29:211-218(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=18445686; DOI=10.1242/jcs.019174;
RA Tegha-Dunghu J., Neumann B., Reber S., Krause R., Erfle H., Walter T.,
RA Held M., Rogers P., Hupfeld K., Ruppert T., Ellenberg J., Gruss O.J.;
RT "EML3 is a nuclear microtubule-binding protein required for the correct
RT alignment of chromosomes in metaphase.";
RL J. Cell Sci. 121:1718-1726(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP FUNCTION.
RX PubMed=19111657; DOI=10.1016/j.molcel.2008.12.003;
RA Alpi A.F., Pace P.E., Babu M.M., Patel K.J.;
RT "Mechanistic insight into site-restricted monoubiquitination of FANCD2 by
RT Ube2t, FANCL, and FANCI.";
RL Mol. Cell 32:767-777(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, 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 [15]
RP DNA-BINDING, UBIQUITINATION AT LYS-523, AND MUTAGENESIS OF LYS-523.
RX PubMed=19589784; DOI=10.1074/jbc.c109.038075;
RA Longerich S., San Filippo J., Liu D., Sung P.;
RT "FANCI binds branched DNA and is monoubiquitinated by UBE2T-FANCL.";
RL J. Biol. Chem. 284:23182-23186(2009).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=19465922; DOI=10.1038/ncb1882;
RA Chan K.L., Palmai-Pallag T., Ying S., Hickson I.D.;
RT "Replication stress induces sister-chromatid bridging at fragile site loci
RT in mitosis.";
RL Nat. Cell Biol. 11:753-760(2009).
RN [17]
RP INTERACTION WITH MTMR15.
RX PubMed=20603015; DOI=10.1016/j.cell.2010.06.021;
RA MacKay C., Declais A.C., Lundin C., Agostinho A., Deans A.J.,
RA MacArtney T.J., Hofmann K., Gartner A., West S.C., Helleday T.,
RA Lilley D.M., Rouse J.;
RT "Identification of KIAA1018/FAN1, a DNA repair nuclease recruited to DNA
RT damage by monoubiquitinated FANCD2.";
RL Cell 142:65-76(2010).
RN [18]
RP INTERACTION WITH POLN.
RX PubMed=19995904; DOI=10.1128/mcb.01124-09;
RA Moldovan G.L., Madhavan M.V., Mirchandani K.D., McCaffrey R.M.,
RA Vinciguerra P., D'Andrea A.D.;
RT "DNA polymerase POLN participates in cross-link repair and homologous
RT recombination.";
RL Mol. Cell. Biol. 30:1088-1096(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP INTERACTION WITH FANCL.
RX PubMed=21775430; DOI=10.1074/jbc.m111.244632;
RA Hodson C., Cole A.R., Lewis L.P., Miles J.A., Purkiss A., Walden H.;
RT "Structural analysis of human FANCL, the E3 ligase in the Fanconi anemia
RT pathway.";
RL J. Biol. Chem. 286:32628-32637(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, 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).
CC -!- FUNCTION: Plays an essential role in the repair of DNA double-strand
CC breaks by homologous recombination and in the repair of interstrand DNA
CC cross-links (ICLs) by promoting FANCD2 monoubiquitination by FANCL and
CC participating in recruitment to DNA repair sites. Required for
CC maintenance of chromosomal stability. Specifically binds branched DNA:
CC binds both single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA).
CC Participates in S phase and G2 phase checkpoint activation upon DNA
CC damage. {ECO:0000269|PubMed:17412408, ECO:0000269|PubMed:17452773,
CC ECO:0000269|PubMed:17460694, ECO:0000269|PubMed:19111657}.
CC -!- SUBUNIT: Interacts with FANCD2; the interaction is direct. Interacts
CC with FANCL. Interacts with MTMR15/FAN1 (PubMed:17412408,
CC PubMed:17460694, PubMed:20603015, PubMed:21775430). Interacts with POLN
CC (PubMed:19995904). {ECO:0000269|PubMed:17412408,
CC ECO:0000269|PubMed:17460694, ECO:0000269|PubMed:19995904,
CC ECO:0000269|PubMed:20603015, ECO:0000269|PubMed:21775430}.
CC -!- INTERACTION:
CC Q9NVI1; Q9BXW9: FANCD2; NbExp=2; IntAct=EBI-1013291, EBI-359343;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17412408,
CC ECO:0000269|PubMed:17460694, ECO:0000269|PubMed:19465922}. Cytoplasm
CC {ECO:0000269|PubMed:18445686}. Note=Observed in spots localized in
CC pairs on the sister chromatids of mitotic chromosome arms and not
CC centromeres, one on each chromatids. These foci coincide with common
CC fragile sites. They are frequently interlinked through BLM-associated
CC ultra-fine DNA bridges.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=3;
CC IsoId=Q9NVI1-3; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NVI1-2; Sequence=VSP_026069, VSP_020257;
CC Name=1;
CC IsoId=Q9NVI1-1; Sequence=VSP_026069;
CC Name=4;
CC IsoId=Q9NVI1-4; Sequence=VSP_035606;
CC -!- DOMAIN: The C-terminal 30 residues are probably required for function
CC in DNA repair.
CC -!- PTM: Monoubiquitinated by FANCL on Lys-523 during S phase and upon
CC genotoxic stress. Deubiquitinated by USP1 as cells enter G2/M, or once
CC DNA repair is completed. Monoubiquitination requires the FANCA-FANCB-
CC FANCC-FANCE-FANCF-FANCG-FANCM complex. Ubiquitination is required for
CC binding to chromatin, DNA repair, and normal cell cycle progression.
CC Monoubiquitination is stimulated by DNA-binding.
CC {ECO:0000269|PubMed:17412408, ECO:0000269|PubMed:17460694,
CC ECO:0000269|PubMed:19589784}.
CC -!- PTM: Phosphorylated in response to DNA damage by ATM and/or ATR.
CC {ECO:0000269|PubMed:17412408}.
CC -!- DISEASE: Fanconi anemia complementation group I (FANCI) [MIM:609053]: 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:17412408, ECO:0000269|PubMed:17452773,
CC ECO:0000269|PubMed:17460694}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04277.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91770.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB55200.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Fanconi Anemia Mutation Database;
CC URL="https://www2.rockefeller.edu/fanconi/genes/jumpi";
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DR EMBL; EF469766; ABP88002.1; -; mRNA.
DR EMBL; EF567077; ABQ63084.1; -; mRNA.
DR EMBL; AC124068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004277; AAH04277.1; ALT_INIT; mRNA.
DR EMBL; BC140769; AAI40770.1; -; mRNA.
DR EMBL; AK001581; BAA91770.1; ALT_INIT; mRNA.
DR EMBL; AK027564; BAB55200.1; ALT_INIT; mRNA.
DR EMBL; AB058697; BAB47423.1; -; mRNA.
DR CCDS; CCDS10349.2; -. [Q9NVI1-1]
DR CCDS; CCDS45346.1; -. [Q9NVI1-3]
DR RefSeq; NP_001106849.1; NM_001113378.1. [Q9NVI1-3]
DR RefSeq; NP_060663.2; NM_018193.2. [Q9NVI1-1]
DR RefSeq; XP_011520058.1; XM_011521756.2. [Q9NVI1-3]
DR RefSeq; XP_011520059.1; XM_011521757.2.
DR RefSeq; XP_011520066.1; XM_011521764.2. [Q9NVI1-1]
DR PDB; 6VAA; EM; 3.35 A; A=1-1328.
DR PDB; 6VAD; EM; 3.35 A; A=1-1328.
DR PDB; 6VAE; EM; 3.50 A; A=1-1328.
DR PDB; 6VAF; EM; 3.90 A; A=1-1328.
DR PDB; 7AY1; EM; 3.70 A; A=1-1328.
DR PDBsum; 6VAA; -.
DR PDBsum; 6VAD; -.
DR PDBsum; 6VAE; -.
DR PDBsum; 6VAF; -.
DR PDBsum; 7AY1; -.
DR AlphaFoldDB; Q9NVI1; -.
DR SMR; Q9NVI1; -.
DR BioGRID; 120511; 200.
DR ComplexPortal; CPX-6264; Fanconi anemia ID complex.
DR CORUM; Q9NVI1; -.
DR DIP; DIP-29381N; -.
DR IntAct; Q9NVI1; 69.
DR MINT; Q9NVI1; -.
DR STRING; 9606.ENSP00000310842; -.
DR GlyGen; Q9NVI1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NVI1; -.
DR PhosphoSitePlus; Q9NVI1; -.
DR SwissPalm; Q9NVI1; -.
DR BioMuta; FANCI; -.
DR DMDM; 212276518; -.
DR CPTAC; CPTAC-3283; -.
DR EPD; Q9NVI1; -.
DR jPOST; Q9NVI1; -.
DR MassIVE; Q9NVI1; -.
DR MaxQB; Q9NVI1; -.
DR PaxDb; Q9NVI1; -.
DR PeptideAtlas; Q9NVI1; -.
DR PRIDE; Q9NVI1; -.
DR ProteomicsDB; 82811; -. [Q9NVI1-3]
DR ProteomicsDB; 82812; -. [Q9NVI1-1]
DR ProteomicsDB; 82813; -. [Q9NVI1-2]
DR ProteomicsDB; 82814; -. [Q9NVI1-4]
DR Antibodypedia; 15714; 144 antibodies from 25 providers.
DR DNASU; 55215; -.
DR Ensembl; ENST00000300027.12; ENSP00000300027.8; ENSG00000140525.19. [Q9NVI1-1]
DR Ensembl; ENST00000310775.12; ENSP00000310842.8; ENSG00000140525.19. [Q9NVI1-3]
DR Ensembl; ENST00000567996.5; ENSP00000458024.1; ENSG00000140525.19. [Q9NVI1-4]
DR GeneID; 55215; -.
DR KEGG; hsa:55215; -.
DR MANE-Select; ENST00000310775.12; ENSP00000310842.8; NM_001113378.2; NP_001106849.1.
DR UCSC; uc002bnm.2; human. [Q9NVI1-3]
DR CTD; 55215; -.
DR DisGeNET; 55215; -.
DR GeneCards; FANCI; -.
DR GeneReviews; FANCI; -.
DR HGNC; HGNC:25568; FANCI.
DR HPA; ENSG00000140525; Tissue enhanced (bone marrow, lymphoid tissue, testis).
DR MalaCards; FANCI; -.
DR MIM; 609053; phenotype.
DR MIM; 611360; gene.
DR neXtProt; NX_Q9NVI1; -.
DR OpenTargets; ENSG00000140525; -.
DR Orphanet; 84; Fanconi anemia.
DR PharmGKB; PA162387928; -.
DR VEuPathDB; HostDB:ENSG00000140525; -.
DR eggNOG; KOG4553; Eukaryota.
DR GeneTree; ENSGT00390000005855; -.
DR HOGENOM; CLU_1102483_0_0_1; -.
DR InParanoid; Q9NVI1; -.
DR OMA; QHSISGY; -.
DR OrthoDB; 169407at2759; -.
DR PhylomeDB; Q9NVI1; -.
DR TreeFam; TF323694; -.
DR PathwayCommons; Q9NVI1; -.
DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR SignaLink; Q9NVI1; -.
DR SIGNOR; Q9NVI1; -.
DR BioGRID-ORCS; 55215; 116 hits in 1083 CRISPR screens.
DR ChiTaRS; FANCI; human.
DR GeneWiki; FANCI; -.
DR GenomeRNAi; 55215; -.
DR Pharos; Q9NVI1; Tbio.
DR PRO; PR:Q9NVI1; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9NVI1; protein.
DR Bgee; ENSG00000140525; Expressed in ventricular zone and 135 other tissues.
DR ExpressionAtlas; Q9NVI1; baseline and differential.
DR Genevisible; Q9NVI1; HS.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:1990391; C:DNA repair complex; IPI:ComplexPortal.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0070182; F:DNA polymerase binding; IPI:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0036297; P:interstrand cross-link repair; IC:ComplexPortal.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:MGI.
DR CDD; cd11720; FANCI; 1.
DR InterPro; IPR026171; FANCI.
DR InterPro; IPR029310; FANCI_HD1.
DR InterPro; IPR029312; FANCI_HD2.
DR InterPro; IPR029308; FANCI_S1.
DR InterPro; IPR029305; FANCI_S1-cap.
DR InterPro; IPR029315; FANCI_S2.
DR InterPro; IPR029313; FANCI_S3.
DR InterPro; IPR029314; FANCI_S4.
DR PANTHER; PTHR21818; PTHR21818; 1.
DR Pfam; PF14679; FANCI_HD1; 1.
DR Pfam; PF14680; FANCI_HD2; 1.
DR Pfam; PF14675; FANCI_S1; 1.
DR Pfam; PF14674; FANCI_S1-cap; 1.
DR Pfam; PF14676; FANCI_S2; 1.
DR Pfam; PF14677; FANCI_S3; 1.
DR Pfam; PF14678; FANCI_S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cytoplasm;
KW Direct protein sequencing; Disease variant; DNA damage; DNA repair;
KW DNA-binding; Fanconi anemia; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1328
FT /note="Fanconi anemia group I protein"
FT /id="PRO_0000248376"
FT REGION 1300..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K368"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17412408"
FT MOD_RES 952
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17412408"
FT MOD_RES 1121
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17412408"
FT CROSSLNK 523
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:17412408,
FT ECO:0000269|PubMed:17460694, ECO:0000269|PubMed:19589784"
FT VAR_SEQ 253..1328
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035606"
FT VAR_SEQ 819..878
FT /note="Missing (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026069"
FT VAR_SEQ 1117
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020257"
FT VARIANT 55
FT /note="P -> L (in FANCI; benign variant; no effect on
FT ubiquitination and DNA repair; dbSNP:rs62020347)"
FT /evidence="ECO:0000269|PubMed:17412408,
FT ECO:0000269|PubMed:17452773"
FT /id="VAR_032689"
FT VARIANT 86
FT /note="A -> V (in dbSNP:rs17803620)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032690"
FT VARIANT 686
FT /note="Q -> K (in dbSNP:rs28378332)"
FT /id="VAR_027278"
FT VARIANT 742
FT /note="C -> S (in dbSNP:rs2283432)"
FT /evidence="ECO:0000269|PubMed:11347906,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_027279"
FT VARIANT 858
FT /note="H -> Y (in FANCI)"
FT /evidence="ECO:0000269|PubMed:17460694"
FT /id="VAR_032691"
FT VARIANT 1285
FT /note="R -> Q (in FANCI; abolishes function in DNA repair;
FT dbSNP:rs121918163)"
FT /evidence="ECO:0000269|PubMed:17412408,
FT ECO:0000269|PubMed:17452773"
FT /id="VAR_032692"
FT MUTAGEN 523
FT /note="K->R: Abolishes monoubiquitination by FANCL and
FT UBE2T."
FT /evidence="ECO:0000269|PubMed:19589784"
FT CONFLICT 528
FT /note="N -> S (in Ref. 6; BAB47423)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="M -> T (in Ref. 5; BAA91770)"
FT /evidence="ECO:0000305"
FT CONFLICT 877
FT /note="I -> L (in Ref. 6; BAB47423)"
FT /evidence="ECO:0000305"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:6VAA"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 17..21
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 40..53
FT /evidence="ECO:0007829|PDB:6VAA"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 60..77
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 83..96
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 102..117
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 129..139
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 153..166
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:6VAA"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 211..221
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 226..248
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 262..280
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 285..293
FT /evidence="ECO:0007829|PDB:6VAA"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:6VAE"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:6VAA"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:6VAD"
FT HELIX 323..345
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 349..353
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 360..370
FT /evidence="ECO:0007829|PDB:6VAA"
FT TURN 371..374
FT /evidence="ECO:0007829|PDB:6VAD"
FT HELIX 376..393
FT /evidence="ECO:0007829|PDB:6VAA"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:6VAE"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 413..432
FT /evidence="ECO:0007829|PDB:6VAA"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 441..451
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 457..469
FT /evidence="ECO:0007829|PDB:6VAA"
FT TURN 472..476
FT /evidence="ECO:0007829|PDB:6VAA"
FT TURN 479..484
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 485..487
FT /evidence="ECO:0007829|PDB:6VAA"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 493..502
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 504..509
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 511..524
FT /evidence="ECO:0007829|PDB:6VAA"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 531..546
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 579..594
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 599..615
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 617..619
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 620..632
FT /evidence="ECO:0007829|PDB:6VAA"
FT STRAND 638..640
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 648..650
FT /evidence="ECO:0007829|PDB:6VAA"
FT STRAND 651..654
FT /evidence="ECO:0007829|PDB:6VAA"
FT STRAND 657..660
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 664..680
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 699..714
FT /evidence="ECO:0007829|PDB:6VAA"
FT TURN 719..722
FT /evidence="ECO:0007829|PDB:6VAA"
FT TURN 724..726
FT /evidence="ECO:0007829|PDB:6VAA"
FT STRAND 731..733
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 734..760
FT /evidence="ECO:0007829|PDB:6VAA"
FT STRAND 761..763
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 765..788
FT /evidence="ECO:0007829|PDB:6VAA"
FT TURN 789..791
FT /evidence="ECO:0007829|PDB:6VAA"
FT STRAND 798..801
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 807..818
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 823..833
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 836..855
FT /evidence="ECO:0007829|PDB:6VAA"
FT STRAND 856..858
FT /evidence="ECO:0007829|PDB:6VAA"
FT TURN 862..865
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 867..887
FT /evidence="ECO:0007829|PDB:6VAA"
FT STRAND 899..902
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 904..921
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 924..926
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 927..931
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 951..971
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 979..992
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 1001..1016
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 1022..1037
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 1043..1057
FT /evidence="ECO:0007829|PDB:6VAA"
FT STRAND 1059..1062
FT /evidence="ECO:0007829|PDB:6VAA"
FT TURN 1077..1083
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 1084..1109
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 1128..1149
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 1157..1183
FT /evidence="ECO:0007829|PDB:6VAA"
FT TURN 1184..1186
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 1192..1203
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 1205..1218
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 1236..1246
FT /evidence="ECO:0007829|PDB:6VAE"
FT HELIX 1249..1269
FT /evidence="ECO:0007829|PDB:6VAA"
FT TURN 1270..1272
FT /evidence="ECO:0007829|PDB:6VAA"
FT STRAND 1276..1278
FT /evidence="ECO:0007829|PDB:6VAA"
FT HELIX 1293..1296
FT /evidence="ECO:0007829|PDB:6VAE"
SQ SEQUENCE 1328 AA; 149324 MW; 07E80FD2F0BCCB32 CRC64;
MDQKILSLAA EKTADKLQEF LQTLREGDLT NLLQNQAVKG KVAGALLRAI FKGSPCSEEA
GTLRRRKIYT CCIQLVESGD LQKEIASEII GLLMLEAHHF PGPLLVELAN EFISAVREGS
LVNGKSLELL PIILTALATK KENLAYGKGV LSGEECKKQL INTLCSGRWD QQYVIQLTSM
FKDVPLTAEE VEFVVEKALS MFSKMNLQEI PPLVYQLLVL SSKGSRKSVL EGIIAFFSAL
DKQHNEEQSG DELLDVVTVP SGELRHVEGT IILHIVFAIK LDYELGRELV KHLKVGQQGD
SNNNLSPFSI ALLLSVTRIQ RFQDQVLDLL KTSVVKSFKD LQLLQGSKFL QNLVPHRSYV
STMILEVVKN SVHSWDHVTQ GLVELGFILM DSYGPKKVLD GKTIETSPSL SRMPNQHACK
LGANILLETF KIHEMIRQEI LEQVLNRVVT RASSPISHFL DLLSNIVMYA PLVLQSCSSK
VTEAFDYLSF LPLQTVQRLL KAVQPLLKVS MSMRDCLILV LRKAMFANQL DARKSAVAGF
LLLLKNFKVL GSLSSSQCSQ SLSVSQVHVD VHSHYNSVAN ETFCLEIMDS LRRCLSQQAD
VRLMLYEGFY DVLRRNSQLA NSVMQTLLSQ LKQFYEPKPD LLPPLKLEAC ILTQGDKISL
QEPLDYLLCC IQHCLAWYKN TVIPLQQGEE EEEEEEAFYE DLDDILESIT NRMIKSELED
FELDKSADFS QSTSIGIKNN ICAFLVMGVC EVLIEYNFSI SSFSKNRFED ILSLFMCYKK
LSDILNEKAG KAKTKMANKT SDSLLSMKFV SSLLTALFRD SIQSHQESLS VLRSSNEFMR
YAVNVALQKV QQLKETGHVS GPDGQNPEKI FQNLCDITRV LLWRYTSIPT SVEESGKKEK
GKSISLLCLE GLQKIFSAVQ QFYQPKIQQF LRALDVTDKE GEEREDADVS VTQRTAFQIR
QFQRSLLNLL SSQEEDFNSK EALLLVTVLT SLSKLLEPSS PQFVQMLSWT SKICKENSRE
DALFCKSLMN LLFSLHVSYK SPVILLRDLS QDIHGHLGDI DQDVEVEKTN HFAIVNLRTA
APTVCLLVLS QAEKVLEEVD WLITKLKGQV SQETLSEEAS SQATLPNQPV EKAIIMQLGT
LLTFFHELVQ TALPSGSCVD TLLKDLCKMY TTLTALVRYY LQVCQSSGGI PKNMEKLVKL
SGSHLTPLCY SFISYVQNKS KSLNYTGEKK EKPAAVATAM ARVLRETKPI PNLIFAIEQY
EKFLIHLSKK SKVNLMQHMK LSTSRDFKIK GNILDMVLRE DGEDENEEGT ASEHGGQNKE
PAKKKRKK
