Reviewed, UniProtKB/Swiss-Prot Q9BXW9 (FACD2_HUMAN)

Names and origin

Protein names

Recommended name:
    Fanconi anemia group D2 protein
      Short name=Protein FACD2

Gene names

Name:	FANCD2
Synonyms:	FACD

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1471 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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. Ref.1 Ref.6 Ref.7 Ref.8 Ref.12 Ref.16 Ref.17 Ref.18 Ref.22 Ref.23 Ref.24 Ref.27
Subunit structure	Interacts directly with FANCE and FANCI. Interacts with USP1 and MEN1. The ubiquitinated form specifically interacts with BRCA1, BRCA2 and BLM. Ref.6 Ref.17 Ref.9 Ref.10 Ref.11 Ref.15 Ref.19 Ref.25 Ref.29 Ref.30
Subcellular location	Nucleus. Note: Concentrates in nuclear foci during S phase and upon genotoxic stress. Ref.6 Ref.9
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. Ref.1 Ref.12 Ref.22
Developmental stage	Highly expressed in fetal oocytes, and in hematopoietic cells of the fetal liver and bone marrow (at protein level). Ref.12
Domain	The C-terminal 24 residues of isoform 2 are required for its function.
Post-translational modification	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. 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. Ref.8 Ref.16 Ref.14 Ref.21 Ref.28 Ref.31 Ref.32 Ref.33 Ref.34
Involvement in 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. Ref.1 Ref.9 Ref.10 Ref.29 Ref.30 Ref.13

Ontologies

Keywords
Biological process	Cell cycle DNA damage DNA repair
Cellular component	Chromosomal protein Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Fanconi anemia
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW cell cycle Inferred from electronic annotation. Source: UniProtKB-KW response to gamma radiation Ref.11 Inferred from direct assay. Source: UniProtKB
Cellular component	chromosome Inferred from electronic annotation. Source: UniProtKB-KW nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	protein binding Ref.9 Ref.11 Ref.30 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRCA2	P51587	9	EBI-359343,EBI-79792
BRCA2	P51587	2	EBI-596878,EBI-79792
FANCE	Q9HB96	2	EBI-359343,EBI-396803
FANCI	Q9NVI1	1	EBI-359343,EBI-1013291
MEN1	O00255	4	EBI-359343,EBI-592789

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BXW9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Less abundant than isoform 2, may be not functional.

Isoform 2 (identifier: Q9BXW9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1428-1451: VSLQNPPESGTDGCILLIVLSWWS → DGEEDEVSAGEKEQDSDESYDDSD
     1452-1471: Missing.

Note: Phosphorylated on Ser-1435.

Isoform 3 (identifier: Q9BXW9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1229-1249: HTFVVFFRVMMAELEKTVKKI → FMKRNSSTGTWLFETSVSSST
     1250-1471: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: Q9BXW9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     232-241: SDLLIENTSL → RWINPLSSSK
     242-1471: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1471	1471	Fanconi anemia group D2 protein		PRO_0000087168
Regions
	Region	1 – 291	291	Interaction with FANCE
	Region	248 – 359	112	Interaction with BRCA2
Amino acid modifications
	Modified residue	167	1	Phosphoserine Ref.31
	Modified residue	178	1	Phosphoserine Ref.31
	Modified residue	222	1	Phosphoserine; by ATM Ref.8
	Modified residue	592	1	Phosphoserine Ref.21 Ref.31 Ref.32 Ref.33
	Modified residue	596	1	Phosphothreonine Ref.31
	Modified residue	684	1	Phosphotyrosine Ref.28
	Modified residue	717	1	Phosphoserine Ref.21 Ref.31
	Modified residue	1401	1	Phosphoserine; by ATM Probable
	Modified residue	1404	1	Phosphoserine; by ATM Ref.8
	Modified residue	1412	1	Phosphoserine Ref.21 Ref.31 Ref.34
	Modified residue	1418	1	Phosphoserine Ref.31
	Cross-link	561		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6
Natural variations
	Alternative sequence	232 – 241	10	SDLLIENTSL → RWINPLSSSK in isoform 4.		VSP_013883
	Alternative sequence	242 – 1471	1230	Missing in isoform 4.		VSP_013884
	Alternative sequence	1229 – 1249	21	HTFVV…TVKKI → FMKRNSSTGTWLFETSVSSS T in isoform 3.		VSP_013885
	Alternative sequence	1250 – 1471	222	Missing in isoform 3.		VSP_013886
	Alternative sequence	1428 – 1451	24	VSLQN…LSWWS → DGEEDEVSAGEKEQDSDESY DDSD in isoform 2.		VSP_013887
	Alternative sequence	1452 – 1471	20	Missing in isoform 2.		VSP_013888
	Natural variant	33	1	K → R		VAR_025827
	Natural variant	61	1	T → M		VAR_025828
	Natural variant	65	1	Q → H		VAR_025829
	Natural variant	126	1	S → G in FA.		VAR_022559
	Natural variant	172	1	I → M: dbSNP rs35173688. Ref.2		VAR_025830
	Natural variant	193	1	T → A		VAR_025831
	Natural variant	302	1	R → W in FA. Ref.1		VAR_022560
	Natural variant	328	1	R → Q		VAR_025832
	Natural variant	446	1	L → V: dbSNP rs34557223. Ref.2		VAR_025833
	Natural variant	456	1	L → R: dbSNP rs35782247. Ref.2		VAR_025834
	Natural variant	623	1	Q → P: dbSNP rs36070315. Ref.2		VAR_025835
	Natural variant	714	1	P → L Common polymorphism. dbSNP rs3864017. Ref.1 Ref.2		VAR_022561
	Natural variant	865	1	K → R: dbSNP rs35546777. Ref.2		VAR_025836
	Natural variant	901	1	G → V: dbSNP rs35495399. Ref.2		VAR_025837
	Natural variant	1236	1	R → H in FA; no effect on ubiquitination. Ref.1		VAR_022562
Experimental info
	Mutagenesis	222	1	S → A: Reduces phosphorylation by ATM. No effect on ubiquitination, foci formation or DNA repair ability, but impairs S-phase checkpoint activation. Ref.8 Ref.27
	Mutagenesis	561	1	K → R: Abolishes ubiquitination; impairs chromatin binding, foci formation and DNA repair. No effect on S-222 phosphorylation by ATM. Ref.6 Ref.7 Ref.8 Ref.22 Ref.27
	Mutagenesis	1257	1	S → A: No effect on phosphorylation by ATM. Ref.8
	Mutagenesis	1401	1	S → A: Reduces phosphorylation by ATM; when associated with A-1404 and A-1418. Ref.8
	Mutagenesis	1404	1	S → A: Reduces phosphorylation by ATM; when associated with A-1401 and A-1418. Ref.8
	Mutagenesis	1418	1	S → A: Reduces phosphorylation by ATM; when associated with A-1401 and A-1404. Ref.8
	Sequence conflict	257	1	N → D in BAB14132. Ref.4
	Sequence conflict	557	1	L → S in BAB14132. Ref.4
	Sequence conflict	589	1	R → G in BAB14132. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 4F74873A1D45A9AE	FASTA	1,471	166,462
	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
	Isoform 2. Checksum: BF931980ADA67405	FASTA	1,451	164,128
	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 SKSKATEDGE EDEVSAGEKE 1450 QDSDESYDDS D
	Isoform 3. Checksum: EAA0E12DE9F079D1	FASTA	1,249	140,737
	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 EEIAGVGVPE LINSPKDASS STFPTLTRFM KRNSSTGTWL FETSVSSST
	Isoform 4. Checksum: 4078C6A54D083DDE	FASTA	241	27,501
	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 LRWINPLSSS K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Positional cloning of a novel Fanconi anemia gene, FANCD2." 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. Mol. Cell 7:241-248(2001) [PubMed: 11239453] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, VARIANTS FA TRP-302 AND HIS-1236, VARIANT LEU-714. Tissue: Lymphoblast.
[2]	NIEHS SNPs program Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], 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.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Lung.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-860 (ISOFORM 1). Tissue: Teratocarcinoma.
[5]	"The full-ORF clone resource of the German cDNA consortium." 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. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 502-1471 (ISOFORM 3). Tissue: Melanoma.
[6]	"Interaction of the Fanconi anemia proteins and BRCA1 in a common pathway." Garcia-Higuera I., Taniguchi T., Ganesan S., Meyn M.S., Timmers C., Hejna J., Grompe M., D'Andrea A.D. Mol. Cell 7:249-262(2001) [PubMed: 11239454] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-561, MASS SPECTROMETRY, MUTAGENESIS OF LYS-561, INTERACTION WITH BRCA1.
[7]	"S-phase-specific interaction of the Fanconi anemia protein, FANCD2, with BRCA1 and RAD51." Taniguchi T., Garcia-Higuera I., Andreassen P.R., Gregory R.C., Grompe M., D'Andrea A.D. Blood 100:2414-2420(2002) [PubMed: 12239151] [Abstract] Cited for: FUNCTION, UBIQUITINATION, MUTAGENESIS OF LYS-561.
[8]	"Convergence of the fanconi anemia and ataxia telangiectasia signaling pathways." 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. Cell 109:459-472(2002) [PubMed: 12086603] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-222 AND SER-1404, MUTAGENESIS OF SER-222; LYS-561; SER-1257; SER-1401; SER-1404 AND SER-1418, MASS SPECTROMETRY.
[9]	"FANCE: the link between Fanconi anaemia complex assembly and activity." 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. EMBO J. 21:3414-3423(2002) [PubMed: 12093742] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH FANCE.
[10]	"Fanconi anemia protein complex: mapping protein interactions in the yeast 2- and 3-hybrid systems." Gordon S.M., Buchwald M. Blood 102:136-141(2003) [PubMed: 12649160] [Abstract] Cited for: INTERACTION WITH FANCE.
[11]	"Menin associates with FANCD2, a protein involved in repair of DNA damage." Jin S., Mao H., Schnepp R.W., Sykes S.M., Silva A.C., D'Andrea A.D., Hua X. Cancer Res. 63:4204-4210(2003) [PubMed: 12874027] [Abstract] Cited for: INTERACTION WITH MEN1, IDENTIFICATION BY MASS SPECTROMETRY.
[12]	"FANCD2 protein is expressed in proliferating cells of human tissues that are cancer-prone in Fanconi anaemia." Hoelzel M., van Diest P.J., Bier P., Wallisch M., Hoatlin M.E., Joenje H., de Winter J.P. J. Pathol. 201:198-203(2003) [PubMed: 14517836] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, FUNCTION.
[13]	"A novel ubiquitin ligase is deficient in Fanconi anemia." 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. Nat. Genet. 35:165-170(2003) [PubMed: 12973351] [Abstract] Cited for: UBIQUITINATION BY FANCL.
[14]	"The DNA crosslink-induced S-phase checkpoint depends on ATR-CHK1 and ATR-NBS1-FANCD2 pathways." Pichierri P., Rosselli F. EMBO J. 23:1178-1187(2004) [PubMed: 14988723] [Abstract] Cited for: PHOSPHORYLATION BY ATR.
[15]	"BLM and the FANC proteins collaborate in a common pathway in response to stalled replication forks." Pichierri P., Franchitto A., Rosselli F. EMBO J. 23:3154-3163(2004) [PubMed: 15257300] [Abstract] Cited for: INTERACTION WITH BLM.
[16]	"ATR couples FANCD2 monoubiquitination to the DNA-damage response." Andreassen P.R., D'Andrea A.D., Taniguchi T. Genes Dev. 18:1958-1963(2004) [PubMed: 15314022] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION BY ATR, UBIQUITINATION.
[17]	"Direct interaction of FANCD2 with BRCA2 in DNA damage response pathways." 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. Hum. Mol. Genet. 13:1241-1248(2004) [PubMed: 15115758] [Abstract] Cited for: FUNCTION, INTERACTION WITH BRCA2.
[18]	"A role for the Fanconi anemia C protein in maintaining the DNA damage-induced G2 checkpoint." 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. J. Biol. Chem. 279:50986-50993(2004) [PubMed: 15377654] [Abstract] Cited for: FUNCTION.
[19]	"Functional interaction of monoubiquitinated FANCD2 and BRCA2/FANCD1 in chromatin." Wang X.Z., Andreassen P.R., D'Andrea A.D. Mol. Cell. Biol. 24:5850-5862(2004) [PubMed: 15199141] [Abstract] Cited for: UBIQUITINATION, INTERACTION WITH BRCA2.
[20]	"X-linked inheritance of Fanconi anemia complementation group B." 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. Nat. Genet. 36:1219-1224(2004) [PubMed: 15502827] [Abstract] Cited for: UBIQUITINATION.
[21]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: 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), MASS SPECTROMETRY. Tissue: Epithelium.
[22]	"Regulated interaction of the Fanconi anemia protein, FANCD2, with chromatin." 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. Blood 105:1003-1009(2005) [PubMed: 15454491] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-561, CHARACTERIZATION (ISOFORM 2).
[23]	"The Fanconi anemia pathway is required for the DNA replication stress response and for the regulation of common fragile site stability." Howlett N.G., Taniguchi T., Durkin S.G., D'Andrea A.D., Glover T.W. Hum. Mol. Genet. 14:693-701(2005) [PubMed: 15661754] [Abstract] Cited for: FUNCTION.
[24]	"FANCD2 functions independently of BRCA2 and RAD51 associated homologous recombination in response to DNA damage." Ohashi A., Zdzienicka M.Z., Chen J., Couch F.J. J. Biol. Chem. 280:14877-14883(2005) [PubMed: 15671039] [Abstract] Cited for: FUNCTION.
[25]	"The deubiquitinating enzyme USP1 regulates the Fanconi Anemia pathway." Nijman S.M.B., Huang T.T., Dirac A.M.G., Brummelkamp T.R., Kerkhoven R.M., D'Andrea A.D., Bernards R. Mol. Cell 17:331-339(2005) [PubMed: 15694335] [Abstract] Cited for: INTERACTION WITH USP1, DEUBIQUITINATION.
[26]	"A human ortholog of archaeal DNA repair protein Hef is defective in Fanconi anemia complementation group M." 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. Nat. Genet. 37:958-963(2005) [PubMed: 16116422] [Abstract] Cited for: UBIQUITINATION.
[27]	"Human Fanconi anemia monoubiquitination pathway promotes homologous DNA repair." Nakanishi K., Yang Y.-G., Pierce A.J., Taniguchi T., Digweed M., D'Andrea A.D., Wang Z.-Q., Jasin M. Proc. Natl. Acad. Sci. U.S.A. 102:1110-1115(2005) [PubMed: 15650050] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF SER-222 AND LYS-561.
[28]	"Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling." Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A., Lottspeich F., Chen Z. EMBO J. 25:5058-5070(2006) [PubMed: 17053785] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-684, MASS SPECTROMETRY.
[29]	"Identification of the FANCI protein, a monoubiquitinated FANCD2 paralog required for DNA repair." 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. Cell 129:289-301(2007) [PubMed: 17412408] [Abstract] Cited for: INTERACTION WITH FANCI.
[30]	"FANCI is a second monoubiquitinated member of the Fanconi anemia pathway." 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. Nat. Struct. Mol. Biol. 14:564-567(2007) [PubMed: 17460694] [Abstract] Cited for: INTERACTION WITH FANCI.
[31]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." 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. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-178; SER-592; THR-596; SER-717; SER-1412 AND SER-1418, MASS SPECTROMETRY.
[32]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, MASS SPECTROMETRY.
[33]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, MASS SPECTROMETRY.
[34]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1412, MASS SPECTROMETRY.
[35]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Fanconi Anemia Mutation Database

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF230336 mRNA. Translation: AAL05980.1. AF273251 , AF273222, AF273223, AF273227, AF273231, AF273235, AF273243, AF273241, AF273239, AF273245, AF273246, AF273247, AF273248, AF273249, AF273250, AF273236, AF273237, AF273238, AF273224, AF273226, AF273228, AF273230, AF273232, AF273234, AF273240, AF273242, AF273244, AF273233, AF273229, AF273225 Genomic DNA. Translation: AAK18772.1. AF273251 , AF273222, AF273223, AF273224, AF273225, AF273226, AF273227, AF273228, AF273229, AF273230, AF273231, AF273232, AF273233, AF273234, AF273235, AF273236, AF273237, AF273238, AF273239, AF273240, AF273241, AF273242, AF273243, AF273244, AF273245, AF273246, AF273247, AF273248, AF273249, AF273250 Genomic DNA. Translation: AAK18773.1. AF340183 mRNA. Translation: AAK15369.1. DQ341263 Genomic DNA. Translation: ABC67466.1. BC013582 mRNA. Translation: AAH13582.1. AK022613 mRNA. Translation: BAB14132.1. Different initiation. AL832427 mRNA. Translation: CAH10647.1.
IPI	IPI00075081. IPI00604399. IPI00604576. IPI00604753.
RefSeq	NP_001018125.1. NP_149075.2.
UniGene	Hs.208388
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BXW9. 14 interactions.
STRING	Q9BXW9.
PTM databases
PhosphoSite	Q9BXW9.
Proteomic databases
PRIDE	Q9BXW9.
Genome annotation databases
Ensembl	ENST00000287647; ENSP00000287647; ENSG00000144554; Homo sapiens. [Genome view] ENST00000383806; ENSP00000373317; ENSG00000144554; Homo sapiens. [Genome view] ENST00000383807; ENSP00000373318; ENSG00000144554; Homo sapiens. [Genome view] ENST00000417070; ENSP00000403176; ENSG00000144554; Homo sapiens. [Genome view] ENST00000419585; ENSP00000398754; ENSG00000144554; Homo sapiens. [Genome view] ENST00000421731; ENSP00000389936; ENSG00000144554; Homo sapiens. [Genome view] ENST00000431693; ENSP00000399354; ENSG00000144554; Homo sapiens. [Genome view] ENST00000435522; ENSP00000402166; ENSG00000144554; Homo sapiens. [Genome view] ENST00000438741; ENSP00000387392; ENSG00000144554; Homo sapiens. [Genome view]
GeneID	2177.
KEGG	hsa:2177.
UCSC	uc003buv.2. human. uc003buw.1. human. uc003bux.1. human.
Organism-specific databases
CTD	2177.
GeneCards	GC03P010043.
H-InvDB	HIX0003044.
HGNC	HGNC:3585. FANCD2.
MIM	227646. gene+phenotype. 227650. phenotype.
Orphanet	84. Fanconi anemia.
PharmGKB	PA27999.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q9BXW9.
HOVERGEN	Q9BXW9.
OMA	LTVPILD.
Enzyme and pathway databases
Pathway_Interaction_DB	bard1pathway. BARD1 signaling events.
Reactome	REACT_216. DNA Repair.
Gene expression databases
ArrayExpress	Q9BXW9.
Bgee	Q9BXW9.
CleanEx	HS_FANCD2.
Genevestigator	Q9BXW9.
GermOnline	ENSG00000144554. Homo sapiens.
Family and domain databases
ProtoNet	Search...
Other Resources
NextBio	8791.
SOURCE	Search...

Entry information

Entry name

FACD2_HUMAN

Accession

Primary (citable) accession number: Q9BXW9
Secondary accession number(s): Q2LA86 , Q69YP9, Q6PJN7, Q9BQ06, Q9H9T9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 1, 2001
Last modified:	November 3, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.