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Q9BXW9

- FACD2_HUMAN

UniProt

Q9BXW9 - FACD2_HUMAN

Protein

Fanconi anemia group D2 protein

Gene

FANCD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    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.13 Publications

    GO - Molecular functioni

    1. DNA polymerase binding Source: UniProt
    2. protein binding Source: IntAct

    GO - Biological processi

    1. DNA repair Source: Reactome
    2. gamete generation Source: Ensembl
    3. response to gamma radiation Source: UniProtKB
    4. synapsis Source: Ensembl

    Keywords - Biological processi

    Cell cycle, DNA damage, DNA repair

    Enzyme and pathway databases

    ReactomeiREACT_18265. Regulation of the Fanconi anemia pathway.
    REACT_18410. Fanconi Anemia pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fanconi anemia group D2 protein
    Short name:
    Protein FACD2
    Gene namesi
    Name:FANCD2
    Synonyms:FACD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:3585. FANCD2.

    Subcellular locationi

    Nucleus 4 Publications
    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.

    GO - Cellular componenti

    1. condensed chromosome Source: Ensembl
    2. Golgi apparatus Source: HPA
    3. intracellular membrane-bounded organelle Source: HPA
    4. nucleoplasm Source: Reactome
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti126 – 1261S → G in FANCD2.
    VAR_022559
    Natural varianti302 – 3021R → W in FANCD2. 1 Publication
    VAR_022560
    Natural varianti1236 – 12361R → H in FANCD2; no effect on ubiquitination. 1 Publication
    VAR_022562

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi222 – 2221S → A: Reduces phosphorylation by ATM. No effect on ubiquitination, foci formation or DNA repair ability, but impairs S-phase checkpoint activation. 2 Publications
    Mutagenesisi561 – 5611K → R: Abolishes ubiquitination; impairs chromatin binding, foci formation and DNA repair. Abolishes interaction with MTMR15/FAN1. No effect on S-222 phosphorylation by ATM. 9 Publications
    Mutagenesisi1257 – 12571S → A: No effect on phosphorylation by ATM. 1 Publication
    Mutagenesisi1401 – 14011S → A: Reduces phosphorylation by ATM; when associated with A-1404 and A-1418. 1 Publication
    Mutagenesisi1404 – 14041S → A: Reduces phosphorylation by ATM; when associated with A-1401 and A-1418. 1 Publication
    Mutagenesisi1418 – 14181S → A: Reduces phosphorylation by ATM; when associated with A-1401 and A-1404. 1 Publication

    Keywords - Diseasei

    Disease mutation, Fanconi anemia

    Organism-specific databases

    MIMi227646. phenotype.
    Orphaneti84. Fanconi anemia.
    PharmGKBiPA27999.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14711471Fanconi anemia group D2 proteinPRO_0000087168Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei8 – 81Phosphoserine1 Publication
    Modified residuei222 – 2221Phosphoserine; by ATM1 Publication
    Cross-linki561 – 561Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)5 Publications
    Modified residuei592 – 5921Phosphoserine1 Publication
    Modified residuei594 – 5941Phosphoserine1 Publication
    Modified residuei717 – 7171Phosphoserine1 Publication
    Modified residuei1401 – 14011Phosphoserine; by ATMCurated
    Modified residuei1404 – 14041Phosphoserine; by ATM1 Publication
    Modified residuei1412 – 14121Phosphoserine3 Publications

    Post-translational modificationi

    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 MEN1.7 Publications
    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.2 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9BXW9.
    PaxDbiQ9BXW9.
    PRIDEiQ9BXW9.

    PTM databases

    PhosphoSiteiQ9BXW9.

    Expressioni

    Tissue specificityi

    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.3 Publications

    Developmental stagei

    Highly expressed in fetal oocytes, and in hematopoietic cells of the fetal liver and bone marrow (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ9BXW9.
    BgeeiQ9BXW9.
    CleanExiHS_FANCD2.
    GenevestigatoriQ9BXW9.

    Organism-specific databases

    HPAiCAB016117.
    HPA054101.

    Interactioni

    Subunit structurei

    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.15 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRCA2P5158716EBI-359343,EBI-79792
    FANCIQ9NVI12EBI-359343,EBI-1013291
    FSCN1Q166586EBI-359343,EBI-351076
    MEN1O002554EBI-359343,EBI-592789
    MRE11AP499596EBI-359343,EBI-396513
    NBNO609346EBI-359343,EBI-494844

    Protein-protein interaction databases

    BioGridi108474. 40 interactions.
    DIPiDIP-27606N.
    DIP-29382N.
    IntActiQ9BXW9. 19 interactions.
    MINTiMINT-190855.
    STRINGi9606.ENSP00000287647.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BXW9.
    SMRiQ9BXW9. Positions 46-848.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 291291Interaction with FANCEAdd
    BLAST
    Regioni248 – 359112Interaction with BRCA2Add
    BLAST

    Domaini

    The C-terminal 24 residues of isoform 2 are required for its function.

    Phylogenomic databases

    eggNOGiNOG305332.
    HOGENOMiHOG000060189.
    HOVERGENiHBG060904.
    InParanoidiQ9BXW9.
    KOiK10891.
    OMAiSHIQDDM.
    OrthoDBiEOG7QZGB3.
    PhylomeDBiQ9BXW9.
    TreeFamiTF101106.

    Family and domain databases

    InterProiIPR029448. FANCD2.
    [Graphical view]
    PfamiPF14631. FancD2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BXW9-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MVSKRRLSKS EDKESLTEDA SKTRKQPLSK KTKKSHIANE VEENDSIFVK     50
    LLKISGIILK TGESQNQLAV DQIAFQKKLF QTLRRHPSYP KIIEEFVSGL 100
    ESYIEDEDSF RNCLLSCERL QDEEASMGAS YSKSLIKLLL GIDILQPAII 150
    KTLFEKLPEY FFENKNSDEI NIPRLIVSQL KWLDRVVDGK DLTTKIMQLI 200
    SIAPENLQHD IITSLPEILG DSQHADVGKE LSDLLIENTS LTVPILDVLS 250
    SLRLDPNFLL KVRQLVMDKL SSIRLEDLPV IIKFILHSVT AMDTLEVISE 300
    LREKLDLQHC VLPSRLQASQ VKLKSKGRAS SSGNQESSGQ SCIILLFDVI 350
    KSAIRYEKTI SEAWIKAIEN TASVSEHKVF DLVMLFIIYS TNTQTKKYID 400
    RVLRNKIRSG CIQEQLLQST FSVHYLVLKD MCSSILSLAQ SLLHSLDQSI 450
    ISFGSLLYKY AFKFFDTYCQ QEVVGALVTH ICSGNEAEVD TALDVLLELV 500
    VLNPSAMMMN AVFVKGILDY LDNISPQQIR KLFYVLSTLA FSKQNEASSH 550
    IQDDMHLVIR KQLSSTVFKY KLIGIIGAVT MAGIMAADRS ESPSLTQERA 600
    NLSDEQCTQV TSLLQLVHSC SEQSPQASAL YYDEFANLIQ HEKLDPKALE 650
    WVGHTICNDF QDAFVVDSCV VPEGDFPFPV KALYGLEEYD TQDGIAINLL 700
    PLLFSQDFAK DGGPVTSQES GQKLVSPLCL APYFRLLRLC VERQHNGNLE 750
    EIDGLLDCPI FLTDLEPGEK LESMSAKERS FMCSLIFLTL NWFREIVNAF 800
    CQETSPEMKG KVLTRLKHIV ELQIILEKYL AVTPDYVPPL GNFDVETLDI 850
    TPHTVTAISA KIRKKGKIER KQKTDGSKTS SSDTLSEEKN SECDPTPSHR 900
    GQLNKEFTGK EEKTSLLLHN SHAFFRELDI EVFSILHCGL VTKFILDTEM 950
    HTEATEVVQL GPPELLFLLE DLSQKLESML TPPIARRVPF LKNKGSRNIG 1000
    FSHLQQRSAQ EIVHCVFQLL TPMCNHLENI HNYFQCLAAE NHGVVDGPGV 1050
    KVQEYHIMSS CYQRLLQIFH GLFAWSGFSQ PENQNLLYSA LHVLSSRLKQ 1100
    GEHSQPLEEL LSQSVHYLQN FHQSIPSFQC ALYLIRLLMV ILEKSTASAQ 1150
    NKEKIASLAR QFLCRVWPSG DKEKSNISND QLHALLCIYL EHTESILKAI 1200
    EEIAGVGVPE LINSPKDASS STFPTLTRHT FVVFFRVMMA ELEKTVKKIE 1250
    PGTAADSQQI HEEKLLYWNM AVRDFSILIN LIKVFDSHPV LHVCLKYGRL 1300
    FVEAFLKQCM PLLDFSFRKH REDVLSLLET FQLDTRLLHH LCGHSKIHQD 1350
    TRLTQHVPLL KKTLELLVCR VKAMLTLNNC REAFWLGNLK NRDLQGEEIK 1400
    SQNSQESTAD ESEDDMSSQA SKSKATEVSL QNPPESGTDG CILLIVLSWW 1450
    SRTLPTYVYC QMLLCPFPFP P 1471

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

    Length:1,471
    Mass (Da):166,462
    Last modified:June 1, 2001 - v1
    Checksum:i4F74873A1D45A9AE
    GO
    Isoform 2 (identifier: Q9BXW9-2) [UniParc]FASTAAdd to Basket

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

    Note: Contains a phosphoserine at position 1423. Contains a phosphothreonine at position 1426. Contains a phosphoserine at position 1435.

    Show »
    Length:1,451
    Mass (Da):164,128
    Checksum:iBF931980ADA67405
    GO
    Isoform 3 (identifier: Q9BXW9-3) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:1,249
    Mass (Da):140,737
    Checksum:iEAA0E12DE9F079D1
    GO
    Isoform 4 (identifier: Q9BXW9-4) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:241
    Mass (Da):27,501
    Checksum:i4078C6A54D083DDE
    GO

    Sequence cautioni

    The sequence BAB14132.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti257 – 2571N → D in BAB14132. (PubMed:14702039)Curated
    Sequence conflicti557 – 5571L → S in BAB14132. (PubMed:14702039)Curated
    Sequence conflicti589 – 5891R → G in BAB14132. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti33 – 331K → R.1 Publication
    Corresponds to variant rs34691009 [ dbSNP | Ensembl ].
    VAR_025827
    Natural varianti61 – 611T → M.1 Publication
    Corresponds to variant rs35110529 [ dbSNP | Ensembl ].
    VAR_025828
    Natural varianti65 – 651Q → H.1 Publication
    Corresponds to variant rs36084488 [ dbSNP | Ensembl ].
    VAR_025829
    Natural varianti126 – 1261S → G in FANCD2.
    VAR_022559
    Natural varianti172 – 1721I → M.1 Publication
    Corresponds to variant rs35173688 [ dbSNP | Ensembl ].
    VAR_025830
    Natural varianti193 – 1931T → A.1 Publication
    Corresponds to variant rs34936017 [ dbSNP | Ensembl ].
    VAR_025831
    Natural varianti302 – 3021R → W in FANCD2. 1 Publication
    VAR_022560
    Natural varianti328 – 3281R → Q.1 Publication
    Corresponds to variant rs35625434 [ dbSNP | Ensembl ].
    VAR_025832
    Natural varianti446 – 4461L → V.1 Publication
    Corresponds to variant rs34557223 [ dbSNP | Ensembl ].
    VAR_025833
    Natural varianti456 – 4561L → R.1 Publication
    Corresponds to variant rs35782247 [ dbSNP | Ensembl ].
    VAR_025834
    Natural varianti623 – 6231Q → P.1 Publication
    Corresponds to variant rs36070315 [ dbSNP | Ensembl ].
    VAR_025835
    Natural varianti714 – 7141P → L Common polymorphism. 3 Publications
    Corresponds to variant rs3864017 [ dbSNP | Ensembl ].
    VAR_022561
    Natural varianti865 – 8651K → R.1 Publication
    Corresponds to variant rs35546777 [ dbSNP | Ensembl ].
    VAR_025836
    Natural varianti901 – 9011G → V.1 Publication
    Corresponds to variant rs35495399 [ dbSNP | Ensembl ].
    VAR_025837
    Natural varianti1236 – 12361R → H in FANCD2; no effect on ubiquitination. 1 Publication
    VAR_022562

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei232 – 24110SDLLIENTSL → RWINPLSSSK in isoform 4. 1 PublicationVSP_013883
    Alternative sequencei242 – 14711230Missing in isoform 4. 1 PublicationVSP_013884Add
    BLAST
    Alternative sequencei1229 – 124921HTFVV…TVKKI → FMKRNSSTGTWLFETSVSSS T in isoform 3. 1 PublicationVSP_013885Add
    BLAST
    Alternative sequencei1250 – 1471222Missing in isoform 3. 1 PublicationVSP_013886Add
    BLAST
    Alternative sequencei1428 – 145124VSLQN…LSWWS → DGEEDEVSAGEKEQDSDESY DDSD in isoform 2. 1 PublicationVSP_013887Add
    BLAST
    Alternative sequencei1452 – 147120Missing in isoform 2. 1 PublicationVSP_013888Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS2595.1. [Q9BXW9-1]
    CCDS33696.1. [Q9BXW9-2]
    RefSeqiNP_001018125.1. NM_001018115.1. [Q9BXW9-2]
    NP_149075.2. NM_033084.3. [Q9BXW9-1]
    XP_005265003.1. XM_005264946.1. [Q9BXW9-2]
    XP_006713084.1. XM_006713021.1. [Q9BXW9-1]
    XP_006713085.1. XM_006713022.1. [Q9BXW9-1]
    UniGeneiHs.208388.

    Genome annotation databases

    EnsembliENST00000287647; ENSP00000287647; ENSG00000144554. [Q9BXW9-1]
    ENST00000383807; ENSP00000373318; ENSG00000144554. [Q9BXW9-2]
    ENST00000419585; ENSP00000398754; ENSG00000144554. [Q9BXW9-2]
    ENST00000431693; ENSP00000399354; ENSG00000144554. [Q9BXW9-4]
    GeneIDi2177.
    KEGGihsa:2177.
    UCSCiuc003buv.3. human. [Q9BXW9-4]
    uc003buw.3. human. [Q9BXW9-1]
    uc003bux.1. human. [Q9BXW9-2]

    Polymorphism databases

    DMDMi67461071.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    Fanconi Anemia Mutation Database
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS2595.1. [Q9BXW9-1 ]
    CCDS33696.1. [Q9BXW9-2 ]
    RefSeqi NP_001018125.1. NM_001018115.1. [Q9BXW9-2 ]
    NP_149075.2. NM_033084.3. [Q9BXW9-1 ]
    XP_005265003.1. XM_005264946.1. [Q9BXW9-2 ]
    XP_006713084.1. XM_006713021.1. [Q9BXW9-1 ]
    XP_006713085.1. XM_006713022.1. [Q9BXW9-1 ]
    UniGenei Hs.208388.

    3D structure databases

    ProteinModelPortali Q9BXW9.
    SMRi Q9BXW9. Positions 46-848.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108474. 40 interactions.
    DIPi DIP-27606N.
    DIP-29382N.
    IntActi Q9BXW9. 19 interactions.
    MINTi MINT-190855.
    STRINGi 9606.ENSP00000287647.

    Chemistry

    ChEMBLi CHEMBL2157857.

    PTM databases

    PhosphoSitei Q9BXW9.

    Polymorphism databases

    DMDMi 67461071.

    Proteomic databases

    MaxQBi Q9BXW9.
    PaxDbi Q9BXW9.
    PRIDEi Q9BXW9.

    Protocols and materials databases

    DNASUi 2177.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000287647 ; ENSP00000287647 ; ENSG00000144554 . [Q9BXW9-1 ]
    ENST00000383807 ; ENSP00000373318 ; ENSG00000144554 . [Q9BXW9-2 ]
    ENST00000419585 ; ENSP00000398754 ; ENSG00000144554 . [Q9BXW9-2 ]
    ENST00000431693 ; ENSP00000399354 ; ENSG00000144554 . [Q9BXW9-4 ]
    GeneIDi 2177.
    KEGGi hsa:2177.
    UCSCi uc003buv.3. human. [Q9BXW9-4 ]
    uc003buw.3. human. [Q9BXW9-1 ]
    uc003bux.1. human. [Q9BXW9-2 ]

    Organism-specific databases

    CTDi 2177.
    GeneCardsi GC03P010068.
    GeneReviewsi FANCD2.
    H-InvDB HIX0003045.
    HGNCi HGNC:3585. FANCD2.
    HPAi CAB016117.
    HPA054101.
    MIMi 227646. phenotype.
    613984. gene.
    neXtProti NX_Q9BXW9.
    Orphaneti 84. Fanconi anemia.
    PharmGKBi PA27999.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG305332.
    HOGENOMi HOG000060189.
    HOVERGENi HBG060904.
    InParanoidi Q9BXW9.
    KOi K10891.
    OMAi SHIQDDM.
    OrthoDBi EOG7QZGB3.
    PhylomeDBi Q9BXW9.
    TreeFami TF101106.

    Enzyme and pathway databases

    Reactomei REACT_18265. Regulation of the Fanconi anemia pathway.
    REACT_18410. Fanconi Anemia pathway.

    Miscellaneous databases

    ChiTaRSi FANCD2. human.
    GeneWikii FANCD2.
    GenomeRNAii 2177.
    NextBioi 8791.
    PROi Q9BXW9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BXW9.
    Bgeei Q9BXW9.
    CleanExi HS_FANCD2.
    Genevestigatori Q9BXW9.

    Family and domain databases

    InterProi IPR029448. FANCD2.
    [Graphical view ]
    Pfami PF14631. FancD2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, VARIANTS FANCD2 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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-860 (ISOFORM 1).
      Tissue: Teratocarcinoma.
    5. 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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-561, MUTAGENESIS OF LYS-561, INTERACTION WITH BRCA1, IDENTIFICATION BY MASS SPECTROMETRY.
    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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, FUNCTION.
    13. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION BY ATR, UBIQUITINATION.
    17. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH BRCA2.
    20. Cited for: UBIQUITINATION.
    21. Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-561, CHARACTERIZATION (ISOFORM 2).
    22. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH USP1, DEUBIQUITINATION.
    25. "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] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    26. Cited for: FUNCTION, MUTAGENESIS OF SER-222 AND LYS-561.
    27. "UBE2T is the E2 in the Fanconi anemia pathway and undergoes negative autoregulation."
      Machida Y.J., Machida Y., Chen Y., Gurtan A.M., Kupfer G.M., D'Andrea A.D., Dutta A.
      Mol. Cell 23:589-596(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    28. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FANCI.
    29. Cited for: INTERACTION WITH FANCI.
    30. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592 AND SER-1412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    31. "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] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    32. "Mechanistic insight into site-restricted monoubiquitination of FANCD2 by Ube2t, FANCL, and FANCI."
      Alpi A.F., Pace P.E., Babu M.M., Patel K.J.
      Mol. Cell 32:767-777(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-561, MUTAGENESIS OF LYS-561.
    33. "FANCG promotes formation of a newly identified protein complex containing BRCA2, FANCD2 and XRCC3."
      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.
      Oncogene 27:3641-3652(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BRCA2; FANCG AND XRCC3.
    34. "Snm1B/Apollo mediates replication fork collapse and S Phase checkpoint activation in response to DNA interstrand cross-links."
      Bae J.B., Mukhopadhyay S.S., Liu L., Zhang N., Tan J., Akhter S., Liu X., Shen X., Li L., Legerski R.J.
      Oncogene 27:5045-5056(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DCLRE1B.
    35. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    36. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    37. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    38. "Replication stress induces sister-chromatid bridging at fragile site loci in mitosis."
      Chan K.L., Palmai-Pallag T., Ying S., Hickson I.D.
      Nat. Cell Biol. 11:753-760(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    39. "The FANC pathway and BLM collaborate during mitosis to prevent micro-nucleation and chromosome abnormalities."
      Naim V., Rosselli F.
      Nat. Cell Biol. 11:761-768(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    40. "Identification of KIAA1018/FAN1, a DNA repair nuclease recruited to DNA damage by monoubiquitinated FANCD2."
      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.
      Cell 142:65-76(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-561, INTERACTION WITH MTMR15, MUTAGENESIS OF LYS-561.
    41. "Deficiency of FANCD2-associated nuclease KIAA1018/FAN1 sensitizes cells to interstrand crosslinking agents."
      Kratz K., Schopf B., Kaden S., Sendoel A., Eberhard R., Lademann C., Cannavo E., Sartori A.A., Hengartner M.O., Jiricny J.
      Cell 142:77-88(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-561, INTERACTION WITH MTMR15, MUTAGENESIS OF LYS-561.
    42. "A genetic screen identifies FAN1, a Fanconi anemia-associated nuclease necessary for DNA interstrand crosslink repair."
      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.
      Mol. Cell 39:36-47(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-561, INTERACTION WITH MTMR15, MUTAGENESIS OF LYS-561.
    43. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-594; SER-717 AND SER-1412, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1423; THR-1426 AND SER-1435 (ISOFORM 2), VARIANT [LARGE SCALE ANALYSIS] LEU-714, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    44. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    45. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1435 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiFACD2_HUMAN
    AccessioniPrimary (citable) accession number: Q9BXW9
    Secondary accession number(s): Q2LA86
    , Q69YP9, Q6PJN7, Q9BQ06, Q9H9T9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 122 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3