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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

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

BioCyciZFISH:G66-33769-MONOMER.
ReactomeiR-HSA-6783310. Fanconi Anemia Pathway.
SIGNORiQ9NPI8.

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
Proteomesi
  • UP000005640 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)DescriptionActionsGraphical viewLength
Mutagenesisi209L → R: Reduced monoubiquitination of FANCD2. 1 Publication1
Mutagenesisi251F → R: Reduced monoubiquitination of FANCD2. 1 Publication1
Mutagenesisi287Y → A: Strongly reduced monoubiquitination of FANCD2; when associated with A-289; A-339; A-341 and A-344. 1 Publication1
Mutagenesisi289L → A: Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-339; A-341 and A-344. 1 Publication1
Mutagenesisi339F → A: Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-289; A-341 and A-344. 1 Publication1
Mutagenesisi341V → A: Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-289; A-339 and A-344. 1 Publication1
Mutagenesisi344L → A: Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-289; A-339 and A-341. 1 Publication1

Keywords - Diseasei

Fanconi anemia

Organism-specific databases

DisGeNETi2188.
MalaCardsiFANCF.
MIMi603467. phenotype.
OpenTargetsiENSG00000183161.
Orphaneti84. Fanconi anemia.
PharmGKBiPA28001.

Chemistry databases

ChEMBLiCHEMBL2157856.

Polymorphism and mutation databases

BioMutaiFANCF.
DMDMi23821547.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000871881 – 374Fanconi anemia group F proteinAdd BLAST374

Proteomic databases

EPDiQ9NPI8.
MaxQBiQ9NPI8.
PaxDbiQ9NPI8.
PeptideAtlasiQ9NPI8.
PRIDEiQ9NPI8.

PTM databases

iPTMnetiQ9NPI8.
PhosphoSitePlusiQ9NPI8.

Expressioni

Gene expression databases

BgeeiENSG00000183161.
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 interactors.
IntActiQ9NPI8. 8 interactors.
MINTiMINT-157055.
STRINGi9606.ENSP00000330875.

Chemistry databases

BindingDBiQ9NPI8.

Structurei

Secondary structure

1374
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi160 – 174Combined sources15
Helixi186 – 195Combined sources10
Helixi198 – 209Combined sources12
Helixi235 – 243Combined sources9
Helixi245 – 254Combined sources10
Helixi257 – 266Combined sources10
Helixi268 – 270Combined sources3
Helixi271 – 283Combined sources13
Beta strandi286 – 288Combined sources3
Turni289 – 292Combined sources4
Beta strandi293 – 295Combined sources3
Helixi304 – 315Combined sources12
Helixi319 – 335Combined sources17
Helixi346 – 354Combined sources9

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9NPI8.

Family & Domainsi

Phylogenomic databases

eggNOGiENOG410IKQV. Eukaryota.
ENOG4111WMC. LUCA.
GeneTreeiENSGT00390000005623.
HOVERGENiHBG051550.
InParanoidiQ9NPI8.
KOiK10893.
OMAiWARYLRH.
OrthoDBiEOG091G18J8.
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_050988295V → I.Corresponds to variant rs7103293dbSNPEnsembl.1
Natural variantiVAR_022270320P → L.1 PublicationCorresponds to variant rs45451294dbSNPEnsembl.1

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.2. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IQCX-ray2.40A156-357[»]
ProteinModelPortaliQ9NPI8.
SMRiQ9NPI8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiQ9NPI8.
ChEMBLiCHEMBL2157856.

PTM databases

iPTMnetiQ9NPI8.
PhosphoSitePlusiQ9NPI8.

Polymorphism and mutation databases

BioMutaiFANCF.
DMDMi23821547.

Proteomic databases

EPDiQ9NPI8.
MaxQBiQ9NPI8.
PaxDbiQ9NPI8.
PeptideAtlasiQ9NPI8.
PRIDEiQ9NPI8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000327470; ENSP00000330875; ENSG00000183161.
GeneIDi2188.
KEGGihsa:2188.
UCSCiuc001mql.2. human.

Organism-specific databases

CTDi2188.
DisGeNETi2188.
GeneCardsiFANCF.
GeneReviewsiFANCF.
HGNCiHGNC:3587. FANCF.
MalaCardsiFANCF.
MIMi603467. phenotype.
613897. gene.
neXtProtiNX_Q9NPI8.
OpenTargetsiENSG00000183161.
Orphaneti84. Fanconi anemia.
PharmGKBiPA28001.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IKQV. Eukaryota.
ENOG4111WMC. LUCA.
GeneTreeiENSGT00390000005623.
HOVERGENiHBG051550.
InParanoidiQ9NPI8.
KOiK10893.
OMAiWARYLRH.
OrthoDBiEOG091G18J8.
PhylomeDBiQ9NPI8.
TreeFamiTF332957.

Enzyme and pathway databases

BioCyciZFISH:G66-33769-MONOMER.
ReactomeiR-HSA-6783310. Fanconi Anemia Pathway.
SIGNORiQ9NPI8.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000183161.
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...

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: November 2, 2016
This is version 136 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

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 one 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.