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Q9BXW9

- FACD2_HUMAN

UniProt

Q9BXW9 - FACD2_HUMAN

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Protein
Fanconi anemia group D2 protein
Gene
FANCD2, FACD
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

GO - Biological processi

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

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
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.4 Publications

GO - Cellular componenti

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 protein
PRO_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 ATM Inferred
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.
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.3 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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 291291Interaction with FANCE
Add
BLAST
Regioni248 – 359112Interaction with BRCA2
Add
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.

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.
VSP_013883
Alternative sequencei242 – 14711230Missing in isoform 4.
VSP_013884Add
BLAST
Alternative sequencei1229 – 124921HTFVV…TVKKI → FMKRNSSTGTWLFETSVSSS T in isoform 3.
VSP_013885Add
BLAST
Alternative sequencei1250 – 1471222Missing in isoform 3.
VSP_013886Add
BLAST
Alternative sequencei1428 – 145124VSLQN…LSWWS → DGEEDEVSAGEKEQDSDESY DDSD in isoform 2.
VSP_013887Add
BLAST
Alternative sequencei1452 – 147120Missing in isoform 2.
VSP_013888Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti257 – 2571N → D in BAB14132. 1 Publication
Sequence conflicti557 – 5571L → S in BAB14132. 1 Publication
Sequence conflicti589 – 5891R → G in BAB14132. 1 Publication

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]
ENST00000383806; ENSP00000373317; ENSG00000144554. [Q9BXW9-3]
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...

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 ]
ENST00000383806 ; ENSP00000373317 ; ENSG00000144554 . [Q9BXW9-3 ]
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...

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  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: September 3, 2014
This is version 121 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

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