[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, VARIANTS FA TRP-302 AND HIS-1236, AND VARIANT LEU-714. TISSUE=Lymphoblast; DOI=10.1016/S1097-2765(01)00172-1; PubMed=11239453 [NCBI, ExPASy, EBI, Israel, Japan] Timmers C., Taniguchi T., Hejna J., Reifsteck C., Lucas L., Bruun D., Thayer M., Cox B., Olson S., D'Andrea A.D., Moses R., Grompe M.; "Positional cloning of a novel Fanconi anemia gene, FANCD2."; Mol. Cell 7:241-248(2001).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-33; MET-61; HIS-65; MET-172; ALA-193; GLN-328; VAL-446; ARG-456; PRO-623; LEU-714; ARG-865 AND VAL-901. NIEHS SNPs program; Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). TISSUE=Lung; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-860 (ISOFORM 1). TISSUE=Teratocarcinoma; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; "Complete sequencing and characterization of 21,243 full-length human cDNAs."; Nat. Genet. 36:40-45(2004).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 502-1471 (ISOFORM 3). TISSUE=Melanoma; DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan] Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.; "The full-ORF clone resource of the German cDNA consortium."; BMC Genomics 8:399-399(2007).
[6]	FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-561, MASS SPECTROMETRY, MUTAGENESIS OF LYS-561, AND INTERACTION WITH BRCA1. DOI=10.1016/S1097-2765(01)00173-3; PubMed=11239454 [NCBI, ExPASy, EBI, Israel, Japan] Garcia-Higuera I., Taniguchi T., Ganesan S., Meyn M.S., Timmers C., Hejna J., Grompe M., D'Andrea A.D.; "Interaction of the Fanconi anemia proteins and BRCA1 in a common pathway."; Mol. Cell 7:249-262(2001).
[7]	FUNCTION, UBIQUITINATION, AND MUTAGENESIS OF LYS-561. DOI=10.1182/blood-2002-01-0278; PubMed=12239151 [NCBI, ExPASy, EBI, Israel, Japan] Taniguchi T., Garcia-Higuera I., Andreassen P.R., Gregory R.C., Grompe M., D'Andrea A.D.; "S-phase-specific interaction of the Fanconi anemia protein, FANCD2, with BRCA1 and RAD51."; Blood 100:2414-2420(2002).
[8]	FUNCTION, PHOSPHORYLATION AT SER-222 AND SER-1404, MUTAGENESIS OF SER-222; LYS-561; SER-1257; SER-1401; SER-1404 AND SER-1418, AND MASS SPECTROMETRY. DOI=10.1016/S0092-8674(02)00747-X; PubMed=12086603 [NCBI, ExPASy, EBI, Israel, Japan] Taniguchi T., Garcia-Higuera I., Xu B., Andreassen P.R., Gregory R.C., Kim S.-T., Lane W.S., Kastan M.B., D'Andrea A.D.; "Convergence of the fanconi anemia and ataxia telangiectasia signaling pathways."; Cell 109:459-472(2002).
[9]	SUBCELLULAR LOCATION, AND INTERACTION WITH FANCE. DOI=10.1093/emboj/cdf355; PubMed=12093742 [NCBI, ExPASy, EBI, Israel, Japan] Pace P., Johnson M., Tan W.M., Mosedale G., Sng C., Hoatlin M.E., de Winter J.P., Joenje H., Gergely F., Patel K.J.; "FANCE: the link between Fanconi anaemia complex assembly and activity."; EMBO J. 21:3414-3423(2002).
[10]	INTERACTION WITH FANCE. DOI=10.1182/blood-2002-11-3517; PubMed=12649160 [NCBI, ExPASy, EBI, Israel, Japan] Gordon S.M., Buchwald M.; "Fanconi anemia protein complex: mapping protein interactions in the yeast 2- and 3-hybrid systems."; Blood 102:136-141(2003).
[11]	INTERACTION WITH MEN1, AND IDENTIFICATION BY MASS SPECTROMETRY. PubMed=12874027 [NCBI, ExPASy, EBI, Israel, Japan] Jin S., Mao H., Schnepp R.W., Sykes S.M., Silva A.C., D'Andrea A.D., Hua X.; "Menin associates with FANCD2, a protein involved in repair of DNA damage."; Cancer Res. 63:4204-4210(2003).
[12]	TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND FUNCTION. DOI=10.1002/path.1450; PubMed=14517836 [NCBI, ExPASy, EBI, Israel, Japan] Hoelzel M., van Diest P.J., Bier P., Wallisch M., Hoatlin M.E., Joenje H., de Winter J.P.; "FANCD2 protein is expressed in proliferating cells of human tissues that are cancer-prone in Fanconi anaemia."; J. Pathol. 201:198-203(2003).
[13]	UBIQUITINATION BY FANCL. DOI=10.1038/ng1241; PubMed=12973351 [NCBI, ExPASy, EBI, Israel, Japan] Meetei A.R., de Winter J.P., Medhurst A.L., Wallisch M., Waisfisz Q., van de Vrugt H.J., Oostra A.B., Yan Z., Ling C., Bishop C.E., Hoatlin M.E., Joenje H., Wang W.; "A novel ubiquitin ligase is deficient in Fanconi anemia."; Nat. Genet. 35:165-170(2003).
[14]	PHOSPHORYLATION BY ATR. DOI=10.1038/sj.emboj.7600113; PubMed=14988723 [NCBI, ExPASy, EBI, Israel, Japan] Pichierri P., Rosselli F.; "The DNA crosslink-induced S-phase checkpoint depends on ATR-CHK1 and ATR-NBS1-FANCD2 pathways."; EMBO J. 23:1178-1187(2004).
[15]	INTERACTION WITH BLM. DOI=10.1038/sj.emboj.7600277; PubMed=15257300 [NCBI, ExPASy, EBI, Israel, Japan] Pichierri P., Franchitto A., Rosselli F.; "BLM and the FANC proteins collaborate in a common pathway in response to stalled replication forks."; EMBO J. 23:3154-3163(2004).
[16]	FUNCTION, PHOSPHORYLATION BY ATR, AND UBIQUITINATION. DOI=10.1101/gad.1196104; PubMed=15314022 [NCBI, ExPASy, EBI, Israel, Japan] Andreassen P.R., D'Andrea A.D., Taniguchi T.; "ATR couples FANCD2 monoubiquitination to the DNA-damage response."; Genes Dev. 18:1958-1963(2004).
[17]	FUNCTION, AND INTERACTION WITH BRCA2. DOI=10.1093/hmg/ddh135; PubMed=15115758 [NCBI, ExPASy, EBI, Israel, Japan] Hussain S., Wilson J.B., Medhurst A.L., Hejna J., Witt E., Ananth S., Davies A., Masson J.-Y., Moses R., West S.C., de Winter J.P., Ashworth A., Jones N.J., Mathew C.G.; "Direct interaction of FANCD2 with BRCA2 in DNA damage response pathways."; Hum. Mol. Genet. 13:1241-1248(2004).
[18]	FUNCTION. DOI=10.1074/jbc.M407160200; PubMed=15377654 [NCBI, ExPASy, EBI, Israel, Japan] Freie B.W., Ciccone S.L.M., Li X., Plett P.A., Orschell C.M., Srour E.F., Hanenberg H., Schindler D., Lee S.-H., Clapp D.W.; "A role for the Fanconi anemia C protein in maintaining the DNA damage-induced G2 checkpoint."; J. Biol. Chem. 279:50986-50993(2004).
[19]	UBIQUITINATION, AND INTERACTION WITH BRCA2. DOI=10.1128/MCB.24.13.5850-5862.2004; PubMed=15199141 [NCBI, ExPASy, EBI, Israel, Japan] Wang X.Z., Andreassen P.R., D'Andrea A.D.; "Functional interaction of monoubiquitinated FANCD2 and BRCA2/FANCD1 in chromatin."; Mol. Cell. Biol. 24:5850-5862(2004).
[20]	UBIQUITINATION. DOI=10.1038/ng1458; PubMed=15502827 [NCBI, ExPASy, EBI, Israel, Japan] Meetei A.R., Levitus M., Xue Y., Medhurst A.L., Zwaan M., Ling C., Rooimans M.A., Bier P., Hoatlin M., Pals G., de Winter J.P., Wang W., Joenje H.; "X-linked inheritance of Fanconi anemia complementation group B."; Nat. Genet. 36:1219-1224(2004).
[21]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592; SER-717 AND SER-1412 (ISOFORMS 1/2/3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1435 (ISOFORM 2), AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.; "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[22]	FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-561, AND CHARACTERIZATION OF ISOFORM 2. DOI=10.1182/blood-2003-11-3997; PubMed=15454491 [NCBI, ExPASy, EBI, Israel, Japan] Montes de Oca R., Andreassen P.R., Margossian S.P., Gregory R.C., Taniguchi T., Wang X.Z., Houghtaling S., Grompe M., D'Andrea A.D.; "Regulated interaction of the Fanconi anemia protein, FANCD2, with chromatin."; Blood 105:1003-1009(2005).
[23]	FUNCTION. DOI=10.1093/hmg/ddi065; PubMed=15661754 [NCBI, ExPASy, EBI, Israel, Japan] Howlett N.G., Taniguchi T., Durkin S.G., D'Andrea A.D., Glover T.W.; "The Fanconi anemia pathway is required for the DNA replication stress response and for the regulation of common fragile site stability."; Hum. Mol. Genet. 14:693-701(2005).
[24]	FUNCTION. DOI=10.1074/jbc.M414669200; PubMed=15671039 [NCBI, ExPASy, EBI, Israel, Japan] Ohashi A., Zdzienicka M.Z., Chen J., Couch F.J.; "FANCD2 functions independently of BRCA2 and RAD51 associated homologous recombination in response to DNA damage."; J. Biol. Chem. 280:14877-14883(2005).
[25]	INTERACTION WITH USP1, AND DEUBIQUITINATION. DOI=10.1016/j.molcel.2005.01.008; PubMed=15694335 [NCBI, ExPASy, EBI, Israel, Japan] Nijman S.M.B., Huang T.T., Dirac A.M.G., Brummelkamp T.R., Kerkhoven R.M., D'Andrea A.D., Bernards R.; "The deubiquitinating enzyme USP1 regulates the Fanconi Anemia pathway."; Mol. Cell 17:331-339(2005).
[26]	UBIQUITINATION. DOI=10.1038/ng1626; PubMed=16116422 [NCBI, ExPASy, EBI, Israel, Japan] Meetei A.R., Medhurst A.L., Ling C., Xue Y., Singh T.R., Bier P., Steltenpool J., Stone S., Dokal I., Mathew C.G., Hoatlin M., Joenje H., de Winter J.P., Wang W.; "A human ortholog of archaeal DNA repair protein Hef is defective in Fanconi anemia complementation group M."; Nat. Genet. 37:958-963(2005).
[27]	FUNCTION, AND MUTAGENESIS OF SER-222 AND LYS-561. DOI=10.1073/pnas.0407796102; PubMed=15650050 [NCBI, ExPASy, EBI, Israel, Japan] Nakanishi K., Yang Y.-G., Pierce A.J., Taniguchi T., Digweed M., D'Andrea A.D., Wang Z.-Q., Jasin M.; "Human Fanconi anemia monoubiquitination pathway promotes homologous DNA repair."; Proc. Natl. Acad. Sci. U.S.A. 102:1110-1115(2005).
[28]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-684, AND MASS SPECTROMETRY. DOI=10.1038/sj.emboj.7601384; PubMed=17053785 [NCBI, ExPASy, EBI, Israel, Japan] Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A., Lottspeich F., Chen Z.; "Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling."; EMBO J. 25:5058-5070(2006).
[29]	INTERACTION WITH FANCI. DOI=10.1016/j.cell.2007.03.009; PubMed=17412408 [NCBI, ExPASy, EBI, Israel, Japan] Smogorzewska A., Matsuoka S., Vinciguerra P., McDonald E.R. III, Hurov K.E., Luo J., Ballif B.A., Gygi S.P., Hofmann K., D'Andrea A.D., Elledge S.J.; "Identification of the FANCI protein, a monoubiquitinated FANCD2 paralog required for DNA repair."; Cell 129:289-301(2007).
[30]	INTERACTION WITH FANCI. DOI=10.1038/nsmb1252; PubMed=17460694 [NCBI, ExPASy, EBI, Israel, Japan] Sims A.E., Spiteri E., Sims R.J. III, Arita A.G., Lach F.P., Landers T., Wurm M., Freund M., Neveling K., Hanenberg H., Auerbach A.D., Huang T.T.; "FANCI is a second monoubiquitinated member of the Fanconi anemia pathway."; Nat. Struct. Mol. Biol. 14:564-567(2007).
[31]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-178; SER-592; THR-596; SER-717; SER-1412 AND SER-1418, AND MASS SPECTROMETRY. DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan] Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."; Science 316:1160-1166(2007).
[32]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, AND MASS SPECTROMETRY. DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan] Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.; "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."; Mol. Cell 31:438-448(2008).
[33]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1412, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.; "A quantitative atlas of mitotic phosphorylation."; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[34]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.

Comments

FUNCTION: Required for maintenance of chromosomal stability. Promotes accurate and efficient pairing of homologs during meiosis. Involved in the repair of DNA double-strand breaks, both by homologous recombination and single-strand annealing. May participate in S phase and G2 phase checkpoint activation upon DNA damage. Promotes BRCA2/FANCD1 loading onto damaged chromatin. May also be involved in B-cell immunoglobulin isotype switching.
SUBUNIT: Interacts directly with FANCE and FANCI. Interacts with USP1 and MEN1. The ubiquitinated form specifically interacts with BRCA1, BRCA2 and BLM.
INTERACTION:
P51587:BRCA2; NbExp=9; IntAct=EBI-359343, EBI-79792;
P51587:BRCA2; NbExp=2; IntAct=EBI-596878, EBI-79792;
Q9HB96:FANCE; NbExp=2; IntAct=EBI-359343, EBI-396803;
Q9NVI1:FANCI; NbExp=1; IntAct=EBI-359343, EBI-1013291;
O00255:MEN1; NbExp=4; IntAct=EBI-359343, EBI-592789;
SUBCELLULAR LOCATION: Nucleus. Note=Concentrates in nuclear foci during S phase and upon genotoxic stress.

ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q9BXW9-1
Note: Less abundant than isoform 2, may be not functional.
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q9BXW9-2
Note: Phosphorylated on Ser-1435.
Features which should be applied to build the isoform sequence: VSP_013887, VSP_013888.

Name	3
Isoform ID	Q9BXW9-3
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_013885, VSP_013886.

Name	4
Isoform ID	Q9BXW9-4
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_013883, VSP_013884.

TISSUE SPECIFICITY: Highly expressed in germinal center cells of the spleen, tonsil, and reactive lymph nodes, and in the proliferating basal layer of squamous epithelium of tonsil, esophagus, oropharynx, larynx and cervix. Expressed in cytotrophoblastic cells of the placenta and exocrine cells of the pancreas (at protein level). Highly expressed in testis, where expression is restricted to maturing spermatocytes.
DEVELOPMENTAL STAGE: Highly expressed in fetal oocytes, and in hematopoietic cells of the fetal liver and bone marrow (at protein level).
DOMAIN: The C-terminal 24 residues of isoform 2 are required for its function.
PTM: Monoubiquitinated on Lys-561 during S phase and upon genotoxic stress (isoform 1 and isoform 2). Deubiquitinated by USP1 as cells enter G2/M, or once DNA repair is completed. Monoubiquitination requires the FANCA-FANCB-FANCC-FANCE-FANCF-FANCG-FANCM complex, RPA1 and ATR, and is mediated by FANCL/PHF9. Ubiquitination is required for binding to chromatin, interaction with BRCA1 and BRCA2, DNA repair, and normal cell cycle progression, but not for phosphorylation on Ser-222 or interaction with MEN1.
PTM: Phosphorylated in response to various genotoxic stresses by ATM and/or ATR. Upon ionizing radiation, phosphorylated by ATM on Ser-222 and Ser-1404. Phosphorylation on Ser-222 is required for S-phase checkpoint activation, but not for ubiquitination, foci formation, or DNA repair. In contrast, phosphorylation by ATR on other sites may be required for ubiquitination and foci formation.
DISEASE: Defects in FANCD2 are a cause of Fanconi anemia (FA) [MIM:227650]. FA is a genetically heterogeneous, autosomal recessive disorder characterized by progressive pancytopenia, a diverse assortment of congenital malformations, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage), and defective DNA repair.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/FAD.html";.
WEB RESOURCE: Name=Fanconi Anemia Mutation Database; URL="http://www.rockefeller.edu/fanconi/mutate/jumpd2.html";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=FANCD2";.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/fancd2/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF230336; AAL05980.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273251; AAK18772.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273222; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273223; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273227; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273231; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273235; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273243; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273241; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273239; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273245; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273246; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273247; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273248; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273249; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273250; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273236; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273237; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273238; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273224; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273226; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273228; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273230; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273232; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273234; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273240; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273242; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273244; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273233; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273229; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273225; AAK18772.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273251; AAK18773.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273222; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273223; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273224; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273225; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273226; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273227; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273228; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273229; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273230; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273231; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273232; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273233; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273234; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273235; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273236; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273237; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273238; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273239; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273240; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273241; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273242; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273243; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273244; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273245; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273246; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273247; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273248; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273249; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273250; AAK18773.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF340183; AAK15369.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ341263; ABC67466.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013582; AAH13582.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK022613; BAB14132.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL832427; CAH10647.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00075081; -.
IPI00604399; -.
IPI00604576; -.
IPI00604753; -.

RefSeq

NP_001018125.1; -.
NP_149075.2; -.

UniGene

Hs.208388

3D structure databases

ModBase

Q9BXW9.

Protein-protein interaction databases

IntAct

Q9BXW9; 14.

PTM databases

PhosphoSite

Q9BXW9; -.

Enzyme and pathway databases

Pathway_Interaction_DB

bard1pathway; BARD1 signaling events.

Organism-specific databases

GC03P010043; -.

HIX0003044; -.

HGNC:3585; FANCD2.

227646; gene+phenotype. [NCBI / EBI]
227650; phenotype. [NCBI / EBI]

Orphanet

84; Fanconi anemia.

PharmGKB

PA27999; -.

Gene expression databases

Q9BXW9; -.

Q9BXW9; -.

HS_FANCD2; -.

ENSG00000144554; Homo sapiens.

Ontologies

GO:0005694;	Cellular component: chromosome (inferred from electronic annotation from UniProtKB-KW).
GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0007049;	Biological process: cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0006281;	Biological process: DNA repair (inferred from electronic annotation from UniProtKB-KW).
GO:0010332;	Biological process: response to gamma radiation (inferred from direct assay from UniProtKB).
QuickGo view.

Proteomic databases

PRIDE

Q9BXW9; -.

Genome annotation databases

Ensembl

ENSG00000144554; Homo sapiens. [Contig view]

GeneID

2177; -.

KEGG

hsa:2177; -.

Phylogenomic databases

HOGENOM

Q9BXW9; -.

HOVERGEN

Q9BXW9; -.

OMA

Q9BXW9; LTVPILD.

Other

NextBio

8791; -.

SOURCE

FANCD2; Homo sapiens.

ProtoNet

Q9BXW9.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Cell cycle; Chromosomal protein; Disease mutation; DNA damage; DNA repair; Fanconi anemia; Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism; Ubl conjugation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1471`	`1471`	`Fanconi anemia group D2 protein.`	`PRO_0000087168`
`REGION`	`1 291`	`291`	`Interaction with FANCE.`
`REGION`	`248 359`	`112`	`Interaction with BRCA2.`
`MOD_RES`	`167 167`		`Phosphoserine.`
`MOD_RES`	`178 178`		`Phosphoserine.`
`MOD_RES`	`222 222`		`Phosphoserine; by ATM.`
`MOD_RES`	`592 592`		`Phosphoserine.`
`MOD_RES`	`596 596`		`Phosphothreonine.`
`MOD_RES`	`684 684`		`Phosphotyrosine.`
`MOD_RES`	`717 717`		`Phosphoserine.`
`MOD_RES`	`1401 1401`		`Phosphoserine; by ATM (Probable).`
`MOD_RES`	`1404 1404`		`Phosphoserine; by ATM.`
`MOD_RES`	`1412 1412`		`Phosphoserine.`
`MOD_RES`	`1418 1418`		`Phosphoserine.`
`CROSSLNK`	`561 561`		`Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).`
`VAR_SEQ`	`232 241`		`SDLLIENTSL -> RWINPLSSSK (in isoform 4).`	`VSP_013883`
`VAR_SEQ`	`242 1471`		`Missing (in isoform 4).`	`VSP_013884`
`VAR_SEQ`	`1229 1249`		`HTFVVFFRVMMAELEKTVKKI -> FMKRNSSTGTWLFETSVSSST (in isoform 3).`	`VSP_013885`
`VAR_SEQ`	`1250 1471`		`Missing (in isoform 3).`	`VSP_013886`
`VAR_SEQ`	`1428 1451`		`VSLQNPPESGTDGCILLIVLSWWS -> DGEEDEVSAGEKEQDSDESYDDSD (in isoform 2).`	`VSP_013887`
`VAR_SEQ`	`1452 1471`		`Missing (in isoform 2).`	`VSP_013888`
`VARIANT`	`33 33`	`1`	`K -> R.`	`VAR_025827`
`VARIANT`	`61 61`	`1`	`T -> M.`	`VAR_025828`
`VARIANT`	`65 65`	`1`	`Q -> H.`	`VAR_025829`
`VARIANT`	`126 126`	`1`	`S -> G (in FA).`	`VAR_022559`
`VARIANT`	`172 172`	`1`	`I -> M (in dbSNP:rs35173688 [NCBI]).`	`VAR_025830`
`VARIANT`	`193 193`	`1`	`T -> A.`	`VAR_025831`
`VARIANT`	`302 302`	`1`	`R -> W (in FA).`	`VAR_022560`
`VARIANT`	`328 328`	`1`	`R -> Q.`	`VAR_025832`
`VARIANT`	`446 446`	`1`	`L -> V (in dbSNP:rs34557223 [NCBI]).`	`VAR_025833`
`VARIANT`	`456 456`	`1`	`L -> R (in dbSNP:rs35782247 [NCBI]).`	`VAR_025834`
`VARIANT`	`623 623`	`1`	`Q -> P (in dbSNP:rs36070315 [NCBI]).`	`VAR_025835`
`VARIANT`	`714 714`	`1`	`P -> L (common polymorphism; dbSNP:rs3864017 [NCBI]).`	`VAR_022561`
`VARIANT`	`865 865`	`1`	`K -> R (in dbSNP:rs35546777 [NCBI]).`	`VAR_025836`
`VARIANT`	`901 901`	`1`	`G -> V (in dbSNP:rs35495399 [NCBI]).`	`VAR_025837`
`VARIANT`	`1236 1236`	`1`	`R -> H (in FA; no effect on ubiquitination).`	`VAR_022562`
`MUTAGEN`	`222 222`		`S->A: Reduces phosphorylation by ATM. No effect on ubiquitination, foci formation or DNA repair ability, but impairs S-phase checkpoint activation.`
`MUTAGEN`	`561 561`		`K->R: Abolishes ubiquitination; impairs chromatin binding, foci formation and DNA repair. No effect on S-222 phosphorylation by ATM.`
`MUTAGEN`	`1257 1257`		`S->A: No effect on phosphorylation by ATM.`
`MUTAGEN`	`1401 1401`		`S->A: Reduces phosphorylation by ATM; when associated with A-1404 and A-1418.`
`MUTAGEN`	`1404 1404`		`S->A: Reduces phosphorylation by ATM; when associated with A-1401 and A-1418.`
`MUTAGEN`	`1418 1418`		`S->A: Reduces phosphorylation by ATM; when associated with A-1401 and A-1404.`
`CONFLICT`	`257 257`		`N -> D (in Ref. 4; BAB14132).`
`CONFLICT`	`557 557`		`L -> S (in Ref. 4; BAB14132).`
`CONFLICT`	`589 589`		`R -> G (in Ref. 4; BAB14132).`

Sequence information

Length: 1471 AA [This is the length of the unprocessed precursor]

Molecular weight: 166462 Da [This is the MW of the unprocessed precursor]

CRC64: 4F74873A1D45A9AE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVSKRRLSKS EDKESLTEDA SKTRKQPLSK KTKKSHIANE VEENDSIFVK LLKISGIILK 

        70         80         90        100        110        120 
TGESQNQLAV DQIAFQKKLF QTLRRHPSYP KIIEEFVSGL ESYIEDEDSF RNCLLSCERL 

       130        140        150        160        170        180 
QDEEASMGAS YSKSLIKLLL GIDILQPAII KTLFEKLPEY FFENKNSDEI NIPRLIVSQL 

       190        200        210        220        230        240 
KWLDRVVDGK DLTTKIMQLI SIAPENLQHD IITSLPEILG DSQHADVGKE LSDLLIENTS 

       250        260        270        280        290        300 
LTVPILDVLS SLRLDPNFLL KVRQLVMDKL SSIRLEDLPV IIKFILHSVT AMDTLEVISE 

       310        320        330        340        350        360 
LREKLDLQHC VLPSRLQASQ VKLKSKGRAS SSGNQESSGQ SCIILLFDVI KSAIRYEKTI 

       370        380        390        400        410        420 
SEAWIKAIEN TASVSEHKVF DLVMLFIIYS TNTQTKKYID RVLRNKIRSG CIQEQLLQST 

       430        440        450        460        470        480 
FSVHYLVLKD MCSSILSLAQ SLLHSLDQSI ISFGSLLYKY AFKFFDTYCQ QEVVGALVTH 

       490        500        510        520        530        540 
ICSGNEAEVD TALDVLLELV VLNPSAMMMN AVFVKGILDY LDNISPQQIR KLFYVLSTLA 

       550        560        570        580        590        600 
FSKQNEASSH IQDDMHLVIR KQLSSTVFKY KLIGIIGAVT MAGIMAADRS ESPSLTQERA 

       610        620        630        640        650        660 
NLSDEQCTQV TSLLQLVHSC SEQSPQASAL YYDEFANLIQ HEKLDPKALE WVGHTICNDF 

       670        680        690        700        710        720 
QDAFVVDSCV VPEGDFPFPV KALYGLEEYD TQDGIAINLL PLLFSQDFAK DGGPVTSQES 

       730        740        750        760        770        780 
GQKLVSPLCL APYFRLLRLC VERQHNGNLE EIDGLLDCPI FLTDLEPGEK LESMSAKERS 

       790        800        810        820        830        840 
FMCSLIFLTL NWFREIVNAF CQETSPEMKG KVLTRLKHIV ELQIILEKYL AVTPDYVPPL 

       850        860        870        880        890        900 
GNFDVETLDI TPHTVTAISA KIRKKGKIER KQKTDGSKTS SSDTLSEEKN SECDPTPSHR 

       910        920        930        940        950        960 
GQLNKEFTGK EEKTSLLLHN SHAFFRELDI EVFSILHCGL VTKFILDTEM HTEATEVVQL 

       970        980        990       1000       1010       1020 
GPPELLFLLE DLSQKLESML TPPIARRVPF LKNKGSRNIG FSHLQQRSAQ EIVHCVFQLL 

      1030       1040       1050       1060       1070       1080 
TPMCNHLENI HNYFQCLAAE NHGVVDGPGV KVQEYHIMSS CYQRLLQIFH GLFAWSGFSQ 

      1090       1100       1110       1120       1130       1140 
PENQNLLYSA LHVLSSRLKQ GEHSQPLEEL LSQSVHYLQN FHQSIPSFQC ALYLIRLLMV 

      1150       1160       1170       1180       1190       1200 
ILEKSTASAQ NKEKIASLAR QFLCRVWPSG DKEKSNISND QLHALLCIYL EHTESILKAI 

      1210       1220       1230       1240       1250       1260 
EEIAGVGVPE LINSPKDASS STFPTLTRHT FVVFFRVMMA ELEKTVKKIE PGTAADSQQI 

      1270       1280       1290       1300       1310       1320 
HEEKLLYWNM AVRDFSILIN LIKVFDSHPV LHVCLKYGRL FVEAFLKQCM PLLDFSFRKH 

      1330       1340       1350       1360       1370       1380 
REDVLSLLET FQLDTRLLHH LCGHSKIHQD TRLTQHVPLL KKTLELLVCR VKAMLTLNNC 

      1390       1400       1410       1420       1430       1440 
REAFWLGNLK NRDLQGEEIK SQNSQESTAD ESEDDMSSQA SKSKATEVSL QNPPESGTDG 

      1450       1460       1470 
CILLIVLSWW SRTLPTYVYC QMLLCPFPFP P

Q9BXW9 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools