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Fanconi anemia group D2 protein (Protein FACD2)

 FACD2_HUMAN             Reviewed;        1451 AA.
Q9BXW9; Q2LA86; Q69YP9; Q6PJN7; Q9BQ06; Q9H9T9;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
26-NOV-2014, sequence version 2.
22-NOV-2017, entry version 156.
RecName: Full=Fanconi anemia group D2 protein;
Short=Protein FACD2;
Name=FANCD2; Synonyms=FACD;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION,
TISSUE SPECIFICITY, VARIANTS FANCD2 TRP-302 AND HIS-1236, AND VARIANT
LEU-714.
TISSUE=Lymphoblast;
PubMed=11239453; DOI=10.1016/S1097-2765(01)00172-1;
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;
PubMed=15489334; DOI=10.1101/gr.2596504;
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;
PubMed=14702039; DOI=10.1038/ng1285;
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 502-1451 (ISOFORM 3).
TISSUE=Melanoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder 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, MUTAGENESIS
OF LYS-561, INTERACTION WITH BRCA1, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=11239454; DOI=10.1016/S1097-2765(01)00173-3;
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.
PubMed=12239151; DOI=10.1182/blood-2002-01-0278;
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
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12086603; DOI=10.1016/S0092-8674(02)00747-X;
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.
PubMed=12093742; DOI=10.1093/emboj/cdf355;
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.
PubMed=12649160; DOI=10.1182/blood-2002-11-3517;
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;
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.
PubMed=14517836; DOI=10.1002/path.1450;
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.
PubMed=12973351; DOI=10.1038/ng1241;
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.
PubMed=14988723; DOI=10.1038/sj.emboj.7600113;
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.
PubMed=15257300; DOI=10.1038/sj.emboj.7600277;
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.
PubMed=15314022; DOI=10.1101/gad.1196104;
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.
PubMed=15115758; DOI=10.1093/hmg/ddh135;
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.
PubMed=15377654; DOI=10.1074/jbc.M407160200;
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.
PubMed=15199141; DOI=10.1128/MCB.24.13.5850-5862.2004;
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.
PubMed=15502827; DOI=10.1038/ng1458;
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]
FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-561, AND
CHARACTERIZATION (ISOFORM 2).
PubMed=15454491; DOI=10.1182/blood-2003-11-3997;
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).
[22]
FUNCTION.
PubMed=15661754; DOI=10.1093/hmg/ddi065;
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).
[23]
FUNCTION.
PubMed=15671039; DOI=10.1074/jbc.M414669200;
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).
[24]
INTERACTION WITH USP1, AND DEUBIQUITINATION.
PubMed=15694335; DOI=10.1016/j.molcel.2005.01.008;
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).
[25]
UBIQUITINATION.
PubMed=16116422; DOI=10.1038/ng1626;
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).
[26]
FUNCTION, AND MUTAGENESIS OF SER-222 AND LYS-561.
PubMed=15650050; DOI=10.1073/pnas.0407796102;
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).
[27]
UBIQUITINATION.
PubMed=16916645; DOI=10.1016/j.molcel.2006.06.024;
Machida Y.J., Machida Y., Chen Y., Gurtan A.M., Kupfer G.M.,
D'Andrea A.D., Dutta A.;
"UBE2T is the E2 in the Fanconi anemia pathway and undergoes negative
autoregulation.";
Mol. Cell 23:589-596(2006).
[28]
INTERACTION WITH FANCI.
PubMed=17412408; DOI=10.1016/j.cell.2007.03.009;
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).
[29]
INTERACTION WITH FANCI.
PubMed=17460694; DOI=10.1038/nsmb1252;
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).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592 AND SER-1412, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
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).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
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).
[32]
UBIQUITINATION AT LYS-561, AND MUTAGENESIS OF LYS-561.
PubMed=19111657; DOI=10.1016/j.molcel.2008.12.003;
Alpi A.F., Pace P.E., Babu M.M., Patel K.J.;
"Mechanistic insight into site-restricted monoubiquitination of FANCD2
by Ube2t, FANCL, and FANCI.";
Mol. Cell 32:767-777(2008).
[33]
INTERACTION WITH BRCA2; FANCG AND XRCC3.
PubMed=18212739; DOI=10.1038/sj.onc.1211034;
Wilson J.B., Yamamoto K., Marriott A.S., Hussain S., Sung P.,
Hoatlin M.E., Mathew C.G., Takata M., Thompson L.H., Kupfer G.M.,
Jones N.J.;
"FANCG promotes formation of a newly identified protein complex
containing BRCA2, FANCD2 and XRCC3.";
Oncogene 27:3641-3652(2008).
[34]
INTERACTION WITH DCLRE1B.
PubMed=18469862; DOI=10.1038/onc.2008.139;
Bae J.B., Mukhopadhyay S.S., Liu L., Zhang N., Tan J., Akhter S.,
Liu X., Shen X., Li L., Legerski R.J.;
"Snm1B/Apollo mediates replication fork collapse and S Phase
checkpoint activation in response to DNA interstrand cross-links.";
Oncogene 27:5045-5056(2008).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1412, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
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).
[36]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[38]
SUBCELLULAR LOCATION.
PubMed=19465922; DOI=10.1038/ncb1882;
Chan K.L., Palmai-Pallag T., Ying S., Hickson I.D.;
"Replication stress induces sister-chromatid bridging at fragile site
loci in mitosis.";
Nat. Cell Biol. 11:753-760(2009).
[39]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19465921; DOI=10.1038/ncb1883;
Naim V., Rosselli F.;
"The FANC pathway and BLM collaborate during mitosis to prevent micro-
nucleation and chromosome abnormalities.";
Nat. Cell Biol. 11:761-768(2009).
[40]
UBIQUITINATION AT LYS-561, INTERACTION WITH MTMR15, AND MUTAGENESIS OF
LYS-561.
PubMed=20603015; DOI=10.1016/j.cell.2010.06.021;
MacKay C., Declais A.C., Lundin C., Agostinho A., Deans A.J.,
MacArtney T.J., Hofmann K., Gartner A., West S.C., Helleday T.,
Lilley D.M., Rouse J.;
"Identification of KIAA1018/FAN1, a DNA repair nuclease recruited to
DNA damage by monoubiquitinated FANCD2.";
Cell 142:65-76(2010).
[41]
UBIQUITINATION AT LYS-561, INTERACTION WITH MTMR15, AND MUTAGENESIS OF
LYS-561.
PubMed=20603016; DOI=10.1016/j.cell.2010.06.022;
Kratz K., Schopf B., Kaden S., Sendoel A., Eberhard R., Lademann C.,
Cannavo E., Sartori A.A., Hengartner M.O., Jiricny J.;
"Deficiency of FANCD2-associated nuclease KIAA1018/FAN1 sensitizes
cells to interstrand crosslinking agents.";
Cell 142:77-88(2010).
[42]
UBIQUITINATION AT LYS-561, INTERACTION WITH MTMR15, AND MUTAGENESIS OF
LYS-561.
PubMed=20603073; DOI=10.1016/j.molcel.2010.06.023;
Smogorzewska A., Desetty R., Saito T.T., Schlabach M., Lach F.P.,
Sowa M.E., Clark A.B., Kunkel T.A., Harper J.W., Colaiacovo M.P.,
Elledge S.J.;
"A genetic screen identifies FAN1, a Fanconi anemia-associated
nuclease necessary for DNA interstrand crosslink repair.";
Mol. Cell 39:36-47(2010).
[43]
INTERACTION WITH POLN.
PubMed=19995904; DOI=10.1128/MCB.01124-09;
Moldovan G.L., Madhavan M.V., Mirchandani K.D., McCaffrey R.M.,
Vinciguerra P., D'Andrea A.D.;
"DNA polymerase POLN participates in cross-link repair and homologous
recombination.";
Mol. Cell. Biol. 30:1088-1096(2010).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-594; SER-717;
SER-1412; SER-1423; THR-1426 AND SER-1435, VARIANT [LARGE SCALE
ANALYSIS] LEU-714, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[45]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[46]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1435, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592; SER-1257 AND
SER-1412, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- 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. Plays a role in preventing breakage and loss of
missegregating chromatin at the end of cell division, particularly
after replication stress. Required for the targeting, or
stabilization, of BLM to non-centromeric abnormal structures
induced by replicative stress. Promotes BRCA2/FANCD1 loading onto
damaged chromatin. May also be involved in B-cell immunoglobulin
isotype switching. {ECO:0000269|PubMed:11239453,
ECO:0000269|PubMed:11239454, ECO:0000269|PubMed:12086603,
ECO:0000269|PubMed:12239151, ECO:0000269|PubMed:14517836,
ECO:0000269|PubMed:15115758, ECO:0000269|PubMed:15314022,
ECO:0000269|PubMed:15377654, ECO:0000269|PubMed:15454491,
ECO:0000269|PubMed:15650050, ECO:0000269|PubMed:15661754,
ECO:0000269|PubMed:15671039, ECO:0000269|PubMed:19465921}.
-!- SUBUNIT: Interacts directly with FANCE and FANCI. Interacts with
USP1 and MEN1. The ubiquitinated form specifically interacts with
BRCA1 and BLM. Both the nonubiquitinated and the monoubiquitinated
forms interact with BRCA2; this interaction is mediated by
phosphorylated FANCG and the complex also includes XCCR3. The
ubiquitinated form specifically interacts with MTMR15/FAN1 (via
UBZ-type zinc finger), leading to recruit MTMR15/FAN1 to sites of
DNA damage. Interacts with DCLRE1B/Apollo (PubMed:11239454,
PubMed:12093742, PubMed:12649160, PubMed:12874027,
PubMed:15115758, PubMed:15199141, PubMed:15257300,
PubMed:15694335, PubMed:17412408, PubMed:17460694,
PubMed:18212739, PubMed:18469862, PubMed:20603015,
PubMed:20603016, PubMed:20603073). Interacts with POLN
(PubMed:19995904). {ECO:0000269|PubMed:11239454,
ECO:0000269|PubMed:12093742, ECO:0000269|PubMed:12649160,
ECO:0000269|PubMed:12874027, ECO:0000269|PubMed:15115758,
ECO:0000269|PubMed:15199141, ECO:0000269|PubMed:15257300,
ECO:0000269|PubMed:15694335, ECO:0000269|PubMed:17412408,
ECO:0000269|PubMed:17460694, ECO:0000269|PubMed:18212739,
ECO:0000269|PubMed:18469862, ECO:0000269|PubMed:19995904,
ECO:0000269|PubMed:20603015, ECO:0000269|PubMed:20603016,
ECO:0000269|PubMed:20603073}.
-!- INTERACTION:
P51587:BRCA2; NbExp=16; IntAct=EBI-359343, EBI-79792;
P49716:CEBPD; NbExp=8; IntAct=EBI-359343, EBI-7962058;
Q9NVI1:FANCI; NbExp=2; IntAct=EBI-359343, EBI-1013291;
Q16658:FSCN1; NbExp=6; IntAct=EBI-359343, EBI-351076;
O00255:MEN1; NbExp=4; IntAct=EBI-359343, EBI-592789;
P49959:MRE11; NbExp=6; IntAct=EBI-359343, EBI-396513;
O60934:NBN; NbExp=6; IntAct=EBI-359343, EBI-494844;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11239454,
ECO:0000269|PubMed:12093742, ECO:0000269|PubMed:19465921,
ECO:0000269|PubMed:19465922}. Note=Concentrates in nuclear foci
during S phase and upon genotoxic stress. At the onset of mitosis,
excluded from chromosomes and diffuses into the cytoplasm,
returning to the nucleus at the end of cell division. Observed in
a few spots localized in pairs on the sister chromatids of mitotic
chromosome arms and not centromeres, one on each chromatids. These
foci coincide with common fragile sites and could be sites of
replication fork stalling. The foci are frequently interlinked
through BLM-associated ultra-fine DNA bridges. Following
aphidicolin treatment, targets chromatid gaps and breaks.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=2;
IsoId=Q9BXW9-2; Sequence=Displayed;
Name=1;
IsoId=Q9BXW9-1; Sequence=VSP_057198;
Note=Less abundant than isoform 2, may be not functional.;
Name=3;
IsoId=Q9BXW9-3; Sequence=VSP_013885, VSP_013886;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9BXW9-4; Sequence=VSP_013883, VSP_013884;
Note=No experimental confirmation available.;
-!- 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.
{ECO:0000269|PubMed:11239453, ECO:0000269|PubMed:14517836,
ECO:0000269|PubMed:15454491}.
-!- DEVELOPMENTAL STAGE: Highly expressed in fetal oocytes, and in
hematopoietic cells of the fetal liver and bone marrow (at protein
level). {ECO:0000269|PubMed:14517836}.
-!- 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 by FANCL in complex with E2 ligases UBE2T or
UBE2W (isoform 1 and isoform 2). Deubiquitinated by USP1 as cells
enter G2/M, or once DNA repair is completed. Monoubiquitination
requires the joint intervention of the FANC core complex,
including FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, and FANCM, and
proteins involved in cell cycle checkpoints and DNA repair,
including RPA1, ATR, CHEK1 and BRCA1, and is mediated by
FANCL/PHF9. Ubiquitination is required for binding to chromatin,
interaction with BRCA1, BRCA2 and MTMR15/FAN1, DNA repair, and
normal cell cycle progression, but not for phosphorylation on Ser-
222 or interaction with MEN1. {ECO:0000269|PubMed:11239454,
ECO:0000269|PubMed:12086603, ECO:0000269|PubMed:15694335,
ECO:0000269|PubMed:19111657, ECO:0000269|PubMed:20603015,
ECO:0000269|PubMed:20603016, ECO:0000269|PubMed:20603073}.
-!- 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.
{ECO:0000269|PubMed:12086603, ECO:0000269|PubMed:15694335}.
-!- DISEASE: Fanconi anemia complementation group D2 (FANCD2)
[MIM:227646]: A disorder affecting all bone marrow elements and
resulting in anemia, leukopenia and thrombopenia. It is associated
with cardiac, renal and limb malformations, dermal pigmentary
changes, 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. {ECO:0000269|PubMed:11239453}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=BAB14132.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/FADID103.html";
-!- WEB RESOURCE: Name=Fanconi Anemia Mutation Database;
URL="http://www2.rockefeller.edu/fanconi/genes/jumpd2";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/fancd2/";
-----------------------------------------------------------------------
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EMBL; AF230336; AAL05980.1; -; mRNA.
EMBL; AF273251; AAK18772.1; -; Genomic_DNA.
EMBL; AF273222; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273223; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273227; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273231; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273235; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273243; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273241; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273239; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273245; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273246; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273247; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273248; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273249; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273250; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273236; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273237; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273238; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273224; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273226; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273228; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273230; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273232; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273234; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273240; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273242; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273244; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273233; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273229; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273225; AAK18772.1; JOINED; Genomic_DNA.
EMBL; AF273251; AAK18773.1; -; Genomic_DNA.
EMBL; AF273222; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273223; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273224; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273225; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273226; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273227; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273228; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273229; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273230; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273231; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273232; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273233; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273234; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273235; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273236; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273237; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273238; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273239; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273240; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273241; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273242; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273243; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273244; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273245; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273246; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273247; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273248; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273249; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF273250; AAK18773.1; JOINED; Genomic_DNA.
EMBL; AF340183; AAK15369.1; -; mRNA.
EMBL; DQ341263; ABC67466.1; -; Genomic_DNA.
EMBL; BC013582; AAH13582.1; -; mRNA.
EMBL; AK022613; BAB14132.1; ALT_INIT; mRNA.
EMBL; AL832427; CAH10647.1; -; mRNA.
CCDS; CCDS2595.1; -. [Q9BXW9-1]
CCDS; CCDS33696.1; -. [Q9BXW9-2]
RefSeq; NP_001018125.1; NM_001018115.2. [Q9BXW9-2]
RefSeq; NP_001306913.1; NM_001319984.1. [Q9BXW9-2]
RefSeq; NP_149075.2; NM_033084.4. [Q9BXW9-1]
UniGene; Hs.208388; -.
ProteinModelPortal; Q9BXW9; -.
SMR; Q9BXW9; -.
BioGrid; 108474; 89.
CORUM; Q9BXW9; -.
DIP; DIP-27606N; -.
DIP; DIP-29382N; -.
IntAct; Q9BXW9; 44.
MINT; MINT-190855; -.
STRING; 9606.ENSP00000287647; -.
ChEMBL; CHEMBL2157857; -.
iPTMnet; Q9BXW9; -.
PhosphoSitePlus; Q9BXW9; -.
BioMuta; FANCD2; -.
DMDM; 67461071; -.
EPD; Q9BXW9; -.
PaxDb; Q9BXW9; -.
PeptideAtlas; Q9BXW9; -.
PRIDE; Q9BXW9; -.
DNASU; 2177; -.
Ensembl; ENST00000287647; ENSP00000287647; ENSG00000144554. [Q9BXW9-1]
Ensembl; ENST00000383807; ENSP00000373318; ENSG00000144554. [Q9BXW9-2]
Ensembl; ENST00000419585; ENSP00000398754; ENSG00000144554. [Q9BXW9-2]
Ensembl; ENST00000431693; ENSP00000399354; ENSG00000144554. [Q9BXW9-4]
GeneID; 2177; -.
KEGG; hsa:2177; -.
UCSC; uc003buw.4; human. [Q9BXW9-2]
CTD; 2177; -.
DisGeNET; 2177; -.
EuPathDB; HostDB:ENSG00000144554.10; -.
GeneCards; FANCD2; -.
GeneReviews; FANCD2; -.
H-InvDB; HIX0003045; -.
HGNC; HGNC:3585; FANCD2.
HPA; CAB016117; -.
HPA; HPA063742; -.
MalaCards; FANCD2; -.
MIM; 227646; phenotype.
MIM; 613984; gene.
neXtProt; NX_Q9BXW9; -.
OpenTargets; ENSG00000144554; -.
Orphanet; 84; Fanconi anemia.
PharmGKB; PA27999; -.
eggNOG; KOG4712; Eukaryota.
eggNOG; ENOG410XT6B; LUCA.
GeneTree; ENSGT00390000016970; -.
HOGENOM; HOG000060189; -.
HOVERGEN; HBG060904; -.
InParanoid; Q9BXW9; -.
KO; K10891; -.
OMA; SHIQDDM; -.
OrthoDB; EOG091G07FG; -.
TreeFam; TF101106; -.
Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
SIGNOR; Q9BXW9; -.
ChiTaRS; FANCD2; human.
GeneWiki; FANCD2; -.
GenomeRNAi; 2177; -.
PRO; PR:Q9BXW9; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000144554; -.
CleanEx; HS_FANCD2; -.
ExpressionAtlas; Q9BXW9; baseline and differential.
Genevisible; Q9BXW9; HS.
GO; GO:0000793; C:condensed chromosome; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0070182; F:DNA polymerase binding; IPI:UniProtKB.
GO; GO:0048854; P:brain morphogenesis; IEA:Ensembl.
GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
GO; GO:0006281; P:DNA repair; IBA:GO_Central.
GO; GO:0007276; P:gamete generation; IEA:Ensembl.
GO; GO:0036297; P:interstrand cross-link repair; TAS:Reactome.
GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
GO; GO:2000348; P:regulation of CD40 signaling pathway; IEA:Ensembl.
GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
GO; GO:0045589; P:regulation of regulatory T cell differentiation; IEA:Ensembl.
GO; GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
GO; GO:0010332; P:response to gamma radiation; IDA:UniProtKB.
GO; GO:0007129; P:synapsis; IEA:Ensembl.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR029448; FANCD2.
Pfam; PF14631; FancD2; 1.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Complete proteome; Disease mutation;
DNA damage; DNA repair; Fanconi anemia; Isopeptide bond; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
CHAIN 1 1451 Fanconi anemia group D2 protein.
/FTId=PRO_0000087168.
REGION 1 291 Interaction with FANCE.
REGION 248 359 Interaction with BRCA2.
MOD_RES 8 8 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 222 222 Phosphoserine; by ATM.
{ECO:0000269|PubMed:12086603}.
MOD_RES 592 592 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:23186163}.
MOD_RES 594 594 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 717 717 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1257 1257 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1401 1401 Phosphoserine; by ATM. {ECO:0000305}.
MOD_RES 1404 1404 Phosphoserine; by ATM.
{ECO:0000269|PubMed:12086603}.
MOD_RES 1412 1412 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1423 1423 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1426 1426 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1435 1435 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CROSSLNK 561 561 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:11239454,
ECO:0000269|PubMed:19111657,
ECO:0000269|PubMed:20603015,
ECO:0000269|PubMed:20603016,
ECO:0000269|PubMed:20603073}.
VAR_SEQ 232 241 SDLLIENTSL -> RWINPLSSSK (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013883.
VAR_SEQ 242 1451 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013884.
VAR_SEQ 1229 1249 HTFVVFFRVMMAELEKTVKKI -> FMKRNSSTGTWLFETS
VSSST (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_013885.
VAR_SEQ 1250 1451 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_013886.
VAR_SEQ 1428 1451 DGEEDEVSAGEKEQDSDESYDDSD -> VSLQNPPESGTDG
CILLIVLSWWSRTLPTYVYCQMLLCPFPFPP (in
isoform 1).
/FTId=VSP_057198.
VARIANT 33 33 K -> R (in dbSNP:rs34691009).
{ECO:0000269|Ref.2}.
/FTId=VAR_025827.
VARIANT 61 61 T -> M (in dbSNP:rs35110529).
{ECO:0000269|Ref.2}.
/FTId=VAR_025828.
VARIANT 65 65 Q -> H (in dbSNP:rs36084488).
{ECO:0000269|Ref.2}.
/FTId=VAR_025829.
VARIANT 126 126 S -> G (in FANCD2; dbSNP:rs764507146).
/FTId=VAR_022559.
VARIANT 172 172 I -> M (in dbSNP:rs35173688).
{ECO:0000269|Ref.2}.
/FTId=VAR_025830.
VARIANT 193 193 T -> A (in dbSNP:rs34936017).
{ECO:0000269|Ref.2}.
/FTId=VAR_025831.
VARIANT 302 302 R -> W (in FANCD2; dbSNP:rs121917787).
{ECO:0000269|PubMed:11239453}.
/FTId=VAR_022560.
VARIANT 328 328 R -> Q (in dbSNP:rs35625434).
{ECO:0000269|Ref.2}.
/FTId=VAR_025832.
VARIANT 446 446 L -> V (in dbSNP:rs34557223).
{ECO:0000269|Ref.2}.
/FTId=VAR_025833.
VARIANT 456 456 L -> R (in dbSNP:rs35782247).
{ECO:0000269|Ref.2}.
/FTId=VAR_025834.
VARIANT 623 623 Q -> P (in dbSNP:rs36070315).
{ECO:0000269|Ref.2}.
/FTId=VAR_025835.
VARIANT 714 714 P -> L (common polymorphism;
dbSNP:rs3864017).
{ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:11239453,
ECO:0000269|Ref.2}.
/FTId=VAR_022561.
VARIANT 865 865 K -> R (in dbSNP:rs35546777).
{ECO:0000269|Ref.2}.
/FTId=VAR_025836.
VARIANT 901 901 G -> V (in dbSNP:rs35495399).
{ECO:0000269|Ref.2}.
/FTId=VAR_025837.
VARIANT 1236 1236 R -> H (in FANCD2; no effect on
ubiquitination; dbSNP:rs121917786).
{ECO:0000269|PubMed:11239453}.
/FTId=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.
{ECO:0000269|PubMed:12086603,
ECO:0000269|PubMed:15650050}.
MUTAGEN 561 561 K->R: Abolishes ubiquitination; impairs
chromatin binding, foci formation and DNA
repair. Abolishes interaction with
MTMR15/FAN1. No effect on S-222
phosphorylation by ATM.
{ECO:0000269|PubMed:11239454,
ECO:0000269|PubMed:12086603,
ECO:0000269|PubMed:12239151,
ECO:0000269|PubMed:15454491,
ECO:0000269|PubMed:15650050,
ECO:0000269|PubMed:19111657,
ECO:0000269|PubMed:20603015,
ECO:0000269|PubMed:20603016,
ECO:0000269|PubMed:20603073}.
MUTAGEN 1257 1257 S->A: No effect on phosphorylation by
ATM. {ECO:0000269|PubMed:12086603}.
MUTAGEN 1401 1401 S->A: Reduces phosphorylation by ATM;
when associated with A-1404 and A-1418.
{ECO:0000269|PubMed:12086603}.
MUTAGEN 1404 1404 S->A: Reduces phosphorylation by ATM;
when associated with A-1401 and A-1418.
{ECO:0000269|PubMed:12086603}.
MUTAGEN 1418 1418 S->A: Reduces phosphorylation by ATM;
when associated with A-1401 and A-1404.
{ECO:0000269|PubMed:12086603}.
CONFLICT 257 257 N -> D (in Ref. 4; BAB14132).
{ECO:0000305}.
CONFLICT 557 557 L -> S (in Ref. 4; BAB14132).
{ECO:0000305}.
CONFLICT 589 589 R -> G (in Ref. 4; BAB14132).
{ECO:0000305}.
SEQUENCE 1451 AA; 164128 MW; BF931980ADA67405 CRC64;
MVSKRRLSKS EDKESLTEDA SKTRKQPLSK KTKKSHIANE VEENDSIFVK LLKISGIILK
TGESQNQLAV DQIAFQKKLF QTLRRHPSYP KIIEEFVSGL ESYIEDEDSF RNCLLSCERL
QDEEASMGAS YSKSLIKLLL GIDILQPAII KTLFEKLPEY FFENKNSDEI NIPRLIVSQL
KWLDRVVDGK DLTTKIMQLI SIAPENLQHD IITSLPEILG DSQHADVGKE LSDLLIENTS
LTVPILDVLS SLRLDPNFLL KVRQLVMDKL SSIRLEDLPV IIKFILHSVT AMDTLEVISE
LREKLDLQHC VLPSRLQASQ VKLKSKGRAS SSGNQESSGQ SCIILLFDVI KSAIRYEKTI
SEAWIKAIEN TASVSEHKVF DLVMLFIIYS TNTQTKKYID RVLRNKIRSG CIQEQLLQST
FSVHYLVLKD MCSSILSLAQ SLLHSLDQSI ISFGSLLYKY AFKFFDTYCQ QEVVGALVTH
ICSGNEAEVD TALDVLLELV VLNPSAMMMN AVFVKGILDY LDNISPQQIR KLFYVLSTLA
FSKQNEASSH IQDDMHLVIR KQLSSTVFKY KLIGIIGAVT MAGIMAADRS ESPSLTQERA
NLSDEQCTQV TSLLQLVHSC SEQSPQASAL YYDEFANLIQ HEKLDPKALE WVGHTICNDF
QDAFVVDSCV VPEGDFPFPV KALYGLEEYD TQDGIAINLL PLLFSQDFAK DGGPVTSQES
GQKLVSPLCL APYFRLLRLC VERQHNGNLE EIDGLLDCPI FLTDLEPGEK LESMSAKERS
FMCSLIFLTL NWFREIVNAF CQETSPEMKG KVLTRLKHIV ELQIILEKYL AVTPDYVPPL
GNFDVETLDI TPHTVTAISA KIRKKGKIER KQKTDGSKTS SSDTLSEEKN SECDPTPSHR
GQLNKEFTGK EEKTSLLLHN SHAFFRELDI EVFSILHCGL VTKFILDTEM HTEATEVVQL
GPPELLFLLE DLSQKLESML TPPIARRVPF LKNKGSRNIG FSHLQQRSAQ EIVHCVFQLL
TPMCNHLENI HNYFQCLAAE NHGVVDGPGV KVQEYHIMSS CYQRLLQIFH GLFAWSGFSQ
PENQNLLYSA LHVLSSRLKQ GEHSQPLEEL LSQSVHYLQN FHQSIPSFQC ALYLIRLLMV
ILEKSTASAQ NKEKIASLAR QFLCRVWPSG DKEKSNISND QLHALLCIYL EHTESILKAI
EEIAGVGVPE LINSPKDASS STFPTLTRHT FVVFFRVMMA ELEKTVKKIE PGTAADSQQI
HEEKLLYWNM AVRDFSILIN LIKVFDSHPV LHVCLKYGRL FVEAFLKQCM PLLDFSFRKH
REDVLSLLET FQLDTRLLHH LCGHSKIHQD TRLTQHVPLL KKTLELLVCR VKAMLTLNNC
REAFWLGNLK NRDLQGEEIK SQNSQESTAD ESEDDMSSQA SKSKATEDGE EDEVSAGEKE
QDSDESYDDS D


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