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Q9NPI8 (FANCF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fanconi anemia group F protein

Short name=Protein FACF
Gene names
Name:FANCF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Subcellular location

Nucleus Ref.6 Ref.10.

Involvement in disease

Fanconi anemia complementation group F (FANCF) [MIM:603467]: 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. Ref.1

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DiseaseFanconi anemia
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Traceable author statement. Source: Reactome

   Cellular_componentFanconi anaemia nuclear complex

Inferred from direct assay PubMed 20347428. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FANCAO153605EBI-81589,EBI-81570
FANCGO152874EBI-81589,EBI-81610

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 374374Fanconi anemia group F protein
PRO_0000087188

Natural variations

Natural variant2951V → I.
Corresponds to variant rs7103293 [ dbSNP | Ensembl ].
VAR_050988
Natural variant3201P → L. Ref.3
Corresponds to variant rs45451294 [ dbSNP | Ensembl ].
VAR_022270

Experimental info

Mutagenesis2091L → R: Reduced monoubiquitination of FANCD2. Ref.5
Mutagenesis2511F → R: Reduced monoubiquitination of FANCD2. Ref.5
Mutagenesis2871Y → A: Strongly reduced monoubiquitination of FANCD2; when associated with A-289; A-339; A-341 and A-344. Ref.5
Mutagenesis2891L → A: Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-339; A-341 and A-344. Ref.5
Mutagenesis3391F → A: Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-289; A-341 and A-344. Ref.5
Mutagenesis3411V → A: Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-289; A-339 and A-344. Ref.5
Mutagenesis3441L → A: Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-289; A-339 and A-341. Ref.5

Secondary structure

.......................... 374
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NPI8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 1F295CD1FBE6ED7D

FASTA37442,254
        10         20         30         40         50         60 
MESLLQHLDR FSELLAVSST TYVSTWDPAT VRRALQWARY LRHIHRRFGR HGPIRTALER 

        70         80         90        100        110        120 
RLHNQWRQEG GFGRGPVPGL ANFQALGHCD VLLSLRLLEN RALGDAARYH LVQQLFPGPG 

       130        140        150        160        170        180 
VRDADEETLQ ESLARLARRR SAVHMLRFNG YRENPNLQED SLMKTQAELL LERLQEVGKA 

       190        200        210        220        230        240 
EAERPARFLS SLWERLPQNN FLKVIAVALL QPPLSRRPQE ELEPGIHKSP GEGSQVLVHW 

       250        260        270        280        290        300 
LLGNSEVFAA FCRALPAGLL TLVTSRHPAL SPVYLGLLTD WGQRLHYDLQ KGIWVGTESQ 

       310        320        330        340        350        360 
DVPWEELHNR FQSLCQAPPP LKDKVLTALE TCKAQDGDFE VPGLSIWTDL LLALRSGAFR 

       370 
KRQVLGLSAG LSSV 

« Hide

References

« Hide 'large scale' references
[1]"The Fanconi anaemia gene FANCF encodes a novel protein with homology to ROM."
de Winter J.P., Rooimans M.A., van der Weel L., van Berkel C.G.M., de Groot J., Waisfisz Q., Pronk J.C., Arwert F., Mathew C.G., Scheper R.J., Hoatlin M.E., Buchwald M., Joenje H.
Nat. Genet. 24:15-16(2000) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"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] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_073562.1. NM_022725.3.
UniGeneHs.632151.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IQCX-ray2.40A156-357[»]
ProteinModelPortalQ9NPI8.
SMRQ9NPI8. Positions 159-357.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108483. 15 interactions.
IntActQ9NPI8. 6 interactions.
MINTMINT-157055.
STRING9606.ENSP00000330875.

Chemistry

ChEMBLCHEMBL2157856.

PTM databases

PhosphoSiteQ9NPI8.

Polymorphism databases

DMDM23821547.

Proteomic databases

PaxDbQ9NPI8.
PRIDEQ9NPI8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327470; ENSP00000330875; ENSG00000183161.
GeneID2188.
KEGGhsa:2188.
UCSCuc001mql.1. human.

Organism-specific databases

CTD2188.
GeneCardsGC11M022600.
HGNCHGNC:3587. FANCF.
MIM603467. phenotype.
613897. gene.
neXtProtNX_Q9NPI8.
Orphanet84. Fanconi anemia.
PharmGKBPA28001.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41771.
HOVERGENHBG051550.
InParanoidQ9NPI8.
KOK10893.
OMAWARYLRH.
OrthoDBEOG7S4X6V.
PhylomeDBQ9NPI8.
TreeFamTF332957.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressQ9NPI8.
BgeeQ9NPI8.
CleanExHS_FANCF.
GenevestigatorQ9NPI8.

Family and domain databases

ProtoNetSearch...

Other

ChiTaRSFANCF. human.
EvolutionaryTraceQ9NPI8.
GeneWikiFANCF.
GenomeRNAi2188.
NextBio8843.
PROQ9NPI8.
SOURCESearch...

Entry information

Entry nameFANCF_HUMAN
AccessionPrimary (citable) accession number: Q9NPI8
Secondary accession number(s): Q52LM0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM