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Protein

Fanconi anemia group F protein

Gene

FANCF

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • activation of mitophagy in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • DNA repair Source: Reactome
  • ovarian follicle development Source: Ensembl
  • spermatogenesis Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

ReactomeiREACT_18410. Fanconi Anemia pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Fanconi anemia group F protein
Short name:
Protein FACF
Gene namesi
Name:FANCF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:3587. FANCF.

Subcellular locationi

GO - Cellular componenti

  • Fanconi anaemia nuclear complex Source: UniProtKB
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Fanconi anemia complementation group F (FANCF)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:603467

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi209 – 2091L → R: Reduced monoubiquitination of FANCD2. 1 Publication
Mutagenesisi251 – 2511F → R: Reduced monoubiquitination of FANCD2. 1 Publication
Mutagenesisi287 – 2871Y → A: Strongly reduced monoubiquitination of FANCD2; when associated with A-289; A-339; A-341 and A-344. 1 Publication
Mutagenesisi289 – 2891L → A: Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-339; A-341 and A-344. 1 Publication
Mutagenesisi339 – 3391F → A: Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-289; A-341 and A-344. 1 Publication
Mutagenesisi341 – 3411V → A: Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-289; A-339 and A-344. 1 Publication
Mutagenesisi344 – 3441L → A: Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-289; A-339 and A-341. 1 Publication

Keywords - Diseasei

Fanconi anemia

Organism-specific databases

MIMi603467. phenotype.
Orphaneti84. Fanconi anemia.
PharmGKBiPA28001.

Polymorphism and mutation databases

BioMutaiFANCF.
DMDMi23821547.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 374374Fanconi anemia group F proteinPRO_0000087188Add
BLAST

Proteomic databases

MaxQBiQ9NPI8.
PaxDbiQ9NPI8.
PRIDEiQ9NPI8.

PTM databases

PhosphoSiteiQ9NPI8.

Expressioni

Gene expression databases

BgeeiQ9NPI8.
CleanExiHS_FANCF.
ExpressionAtlasiQ9NPI8. baseline and differential.
GenevisibleiQ9NPI8. HS.

Interactioni

Subunit structurei

Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM. The complex is not found in FA patients. In complex with FANCA, FANCG and FANCL, but not with FANCC, nor FANCE, interacts with HES1; this interaction may be essential for the stability and nuclear localization of FA core complex proteins.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FANCAO153605EBI-81589,EBI-81570
FANCGO152874EBI-81589,EBI-81610

Protein-protein interaction databases

BioGridi108483. 14 interactions.
IntActiQ9NPI8. 8 interactions.
MINTiMINT-157055.
STRINGi9606.ENSP00000330875.

Structurei

Secondary structure

1
374
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi160 – 17415Combined sources
Helixi186 – 19510Combined sources
Helixi198 – 20912Combined sources
Helixi235 – 2439Combined sources
Helixi245 – 25410Combined sources
Helixi257 – 26610Combined sources
Helixi268 – 2703Combined sources
Helixi271 – 28313Combined sources
Beta strandi286 – 2883Combined sources
Turni289 – 2924Combined sources
Beta strandi293 – 2953Combined sources
Helixi304 – 31512Combined sources
Helixi319 – 33517Combined sources
Helixi346 – 3549Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IQCX-ray2.40A156-357[»]
ProteinModelPortaliQ9NPI8.
SMRiQ9NPI8. Positions 159-357.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NPI8.

Family & Domainsi

Phylogenomic databases

eggNOGiNOG41771.
GeneTreeiENSGT00390000005623.
HOVERGENiHBG051550.
InParanoidiQ9NPI8.
KOiK10893.
OMAiWARYLRH.
OrthoDBiEOG7S4X6V.
PhylomeDBiQ9NPI8.
TreeFamiTF332957.

Family and domain databases

InterProiIPR025825. FANCF.
[Graphical view]
ProDomiPD321645. PD321645. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

Q9NPI8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESLLQHLDR FSELLAVSST TYVSTWDPAT VRRALQWARY LRHIHRRFGR
60 70 80 90 100
HGPIRTALER RLHNQWRQEG GFGRGPVPGL ANFQALGHCD VLLSLRLLEN
110 120 130 140 150
RALGDAARYH LVQQLFPGPG VRDADEETLQ ESLARLARRR SAVHMLRFNG
160 170 180 190 200
YRENPNLQED SLMKTQAELL LERLQEVGKA EAERPARFLS SLWERLPQNN
210 220 230 240 250
FLKVIAVALL QPPLSRRPQE ELEPGIHKSP GEGSQVLVHW LLGNSEVFAA
260 270 280 290 300
FCRALPAGLL TLVTSRHPAL SPVYLGLLTD WGQRLHYDLQ KGIWVGTESQ
310 320 330 340 350
DVPWEELHNR FQSLCQAPPP LKDKVLTALE TCKAQDGDFE VPGLSIWTDL
360 370
LLALRSGAFR KRQVLGLSAG LSSV
Length:374
Mass (Da):42,254
Last modified:October 1, 2000 - v1
Checksum:i1F295CD1FBE6ED7D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti295 – 2951V → I.
Corresponds to variant rs7103293 [ dbSNP | Ensembl ].
VAR_050988
Natural varianti320 – 3201P → L.1 Publication
Corresponds to variant rs45451294 [ dbSNP | Ensembl ].
VAR_022270

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF181995 mRNA. Translation: AAF26298.1.
AF181994 mRNA. Translation: AAF26297.1.
AK023153 mRNA. Translation: BAB14433.1.
AY928335 Genomic DNA. Translation: AAX09677.1.
BC047028 mRNA. Translation: AAH47028.1.
BC093867 mRNA. Translation: AAH93867.1.
BC101807 mRNA. Translation: AAI01808.1.
CCDSiCCDS7857.1.
RefSeqiNP_073562.1. NM_022725.3.
UniGeneiHs.632151.

Genome annotation databases

EnsembliENST00000327470; ENSP00000330875; ENSG00000183161.
GeneIDi2188.
KEGGihsa:2188.
UCSCiuc001mql.1. human.

Keywords - Coding sequence diversityi

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:
EMBLi
GenBanki
DDBJi
Links Updated
AF181995 mRNA. Translation: AAF26298.1.
AF181994 mRNA. Translation: AAF26297.1.
AK023153 mRNA. Translation: BAB14433.1.
AY928335 Genomic DNA. Translation: AAX09677.1.
BC047028 mRNA. Translation: AAH47028.1.
BC093867 mRNA. Translation: AAH93867.1.
BC101807 mRNA. Translation: AAI01808.1.
CCDSiCCDS7857.1.
RefSeqiNP_073562.1. NM_022725.3.
UniGeneiHs.632151.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IQCX-ray2.40A156-357[»]
ProteinModelPortaliQ9NPI8.
SMRiQ9NPI8. Positions 159-357.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108483. 14 interactions.
IntActiQ9NPI8. 8 interactions.
MINTiMINT-157055.
STRINGi9606.ENSP00000330875.

Chemistry

BindingDBiQ9NPI8.
ChEMBLiCHEMBL2157856.

PTM databases

PhosphoSiteiQ9NPI8.

Polymorphism and mutation databases

BioMutaiFANCF.
DMDMi23821547.

Proteomic databases

MaxQBiQ9NPI8.
PaxDbiQ9NPI8.
PRIDEiQ9NPI8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000327470; ENSP00000330875; ENSG00000183161.
GeneIDi2188.
KEGGihsa:2188.
UCSCiuc001mql.1. human.

Organism-specific databases

CTDi2188.
GeneCardsiGC11M022600.
GeneReviewsiFANCF.
HGNCiHGNC:3587. FANCF.
MIMi603467. phenotype.
613897. gene.
neXtProtiNX_Q9NPI8.
Orphaneti84. Fanconi anemia.
PharmGKBiPA28001.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG41771.
GeneTreeiENSGT00390000005623.
HOVERGENiHBG051550.
InParanoidiQ9NPI8.
KOiK10893.
OMAiWARYLRH.
OrthoDBiEOG7S4X6V.
PhylomeDBiQ9NPI8.
TreeFamiTF332957.

Enzyme and pathway databases

ReactomeiREACT_18410. Fanconi Anemia pathway.

Miscellaneous databases

ChiTaRSiFANCF. human.
EvolutionaryTraceiQ9NPI8.
GeneWikiiFANCF.
GenomeRNAii2188.
NextBioi8843.
PROiQ9NPI8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NPI8.
CleanExiHS_FANCF.
ExpressionAtlasiQ9NPI8. baseline and differential.
GenevisibleiQ9NPI8. HS.

Family and domain databases

InterProiIPR025825. FANCF.
[Graphical view]
ProDomiPD321645. PD321645. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN FANCF.
  2. "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].
  3. NIEHS SNPs program
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-320.
  4. "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].
    Tissue: Brain and Skin.
  5. "Structural determinants of human FANCF protein that function in the assembly of a DNA damage signaling complex."
    Kowal P., Gurtan A.M., Stuckert P., D'Andrea A.D., Ellenberger T.
    J. Biol. Chem. 282:2047-2055(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 156-357, MUTAGENESIS OF LEU-209; PHE-251; TYR-287; LEU-289; PHE-339; VAL-341 AND LEU-344, SUBUNIT.
  6. "The Fanconi anemia protein FANCF forms a nuclear complex with FANCA, FANCC and FANCG."
    de Winter J.P., van der Weel L., de Groot J., Stone S., Waisfisz Q., Arwert F., Scheper R.J., Kruyt F.A.E., Hoatlin M.E., Joenje H.
    Hum. Mol. Genet. 9:2665-2674(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  7. "A multiprotein nuclear complex connects Fanconi anemia and Bloom syndrome."
    Meetei A.R., Sechi S., Wallisch M., Yang D., Young M.K., Joenje H., Hoatlin M.E., Wang W.
    Mol. Cell. Biol. 23:3417-3426(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH FANCA; FANCC; FANCE; FANCG AND FANCL.
  8. Cited for: IDENTIFICATION IN A COMPLEX WITH FANCA; FANCB; FANCC; FANCE; FANCG AND FANCL.
  9. "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: IDENTIFICATION IN A COMPLEX WITH FANCA; FANCB; FANCC; FANCE; FANCG; FANCL AND FANCM.
  10. "HES1 is a novel interactor of the Fanconi anemia core complex."
    Tremblay C.S., Huang F.F., Habi O., Huard C.C., Godin C., Levesque G., Carreau M.
    Blood 112:2062-2070(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HES1, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiFANCF_HUMAN
AccessioniPrimary (citable) accession number: Q9NPI8
Secondary accession number(s): Q52LM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 1, 2000
Last modified: June 24, 2015
This is version 123 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.