Q9HB96 · FANCE_HUMAN
- ProteinFanconi anemia group E protein
- GeneFANCE
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids536 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
As part of the Fanconi anemia (FA) complex functions in DNA cross-links repair. Required for the nuclear accumulation of FANCC and provides a critical bridge between the FA complex and FANCD2.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | centrosome | |
Cellular Component | chromatin | |
Cellular Component | chromosome | |
Cellular Component | cytosol | |
Cellular Component | Fanconi anaemia nuclear complex | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Biological Process | interstrand cross-link repair |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFanconi anemia group E protein
- Short namesProtein FACE
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9HB96
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Fanconi anemia complementation group E (FANCE)
- Note
- 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 alsoMIM:600901
Natural variants in FANCE
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_038022 | 184 | P>Q | in FANCE; uncertain significance; dbSNP:rs373268808 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_023372 | 89 | in dbSNP:rs45600543 | |||
Sequence: R → L | ||||||
Natural variant | VAR_038022 | 184 | in FANCE; uncertain significance; dbSNP:rs373268808 | |||
Sequence: P → Q | ||||||
Natural variant | VAR_023373 | 204 | in dbSNP:rs7761870 | |||
Sequence: S → L | ||||||
Natural variant | VAR_023374 | 340 | in dbSNP:rs45524646 | |||
Sequence: G → R | ||||||
Natural variant | VAR_023375 | 343 | in dbSNP:rs45467798 | |||
Sequence: R → Q | ||||||
Mutagenesis | 346 | Non-phosphorylatable by CHEK1, not polyubiquitinated and unable to complement the mitomycin C hypersensitivity of cells lacking FANCE; when associated with A-374. | ||||
Sequence: T → A | ||||||
Mutagenesis | 374 | Non-phosphorylatable by CHEK1, not polyubiquitinated and unable to complement the mitomycin C hypersensitivity of cells lacking FANCE; when associated with A-346. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_023376 | 502 | in dbSNP:rs9462088 | |||
Sequence: A → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 924 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000087187 | 1-536 | UniProt | Fanconi anemia group E protein | |||
Sequence: MATPDAGLPGAEGVEPAPWAQLEAPARLLLQALQAGPEGARRGLGVLRALGSRGWEPFDWGRLLEALCREEPVVQGPDGRLELKPLLLRLPRICQRNLMSLLMAVRPSLPESGLLSVLQIAQQDLAPDPDAWLRALGELLRRDLGVGTSMEGASPLSERCQRQLQSLCRGLGLGGRRLKSPQAPDPEEEENRDSQQPGKRRKDSEEEAASPEGKRVPKRLRCWEEEEDHEKERPEHKSLESLADGGSASPIKDQPVMAVKTGEDGSNLDDAKGLAESLELPKAIQDQLPRLQQLLKTLEEGLEGLEDAPPVELQLLHECSPSQMDLLCAQLQLPQLSDLGLLRLCTWLLALSPDLSLSNATVLTRSLFLGRILSLTSSASRLLTTALTSFCAKYTYPVCSALLDPVLQAPGTGPAQTELLCCLVKMESLEPDAQVLMLGQILELPWKEETFLVLQSLLERQVEMTPEKFSVLMEKLCKKGLAATTSMAYAKLMLTVMTKYQANITETQRLGLAMALEPNTTFLRKSLKAALKHLGP | |||||||
Modified residue (large scale data) | 180 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 194 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 210 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 238 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 241 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 247 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 249 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 249 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 346 | UniProt | Phosphothreonine; by CHEK1 | ||||
Sequence: T | |||||||
Modified residue | 374 | UniProt | Phosphoserine; by CHEK1 | ||||
Sequence: S |
Post-translational modification
Phosphorylated. Phosphorylation by CHEK1 at Thr-346 and Ser-374 regulates its function in DNA cross-links repair.
Ubiquitinated. Phosphorylation by CHEK1 induces polyubiquitination and degradation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
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. Interacts with FANCC and FANCD2.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9HB96 | FANCC Q00597 | 3 | EBI-396803, EBI-81625 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 150-371 | Interaction with FANCC | ||||
Sequence: MEGASPLSERCQRQLQSLCRGLGLGGRRLKSPQAPDPEEEENRDSQQPGKRRKDSEEEAASPEGKRVPKRLRCWEEEEDHEKERPEHKSLESLADGGSASPIKDQPVMAVKTGEDGSNLDDAKGLAESLELPKAIQDQLPRLQQLLKTLEEGLEGLEDAPPVELQLLHECSPSQMDLLCAQLQLPQLSDLGLLRLCTWLLALSPDLSLSNATVLTRSLFLGR | ||||||
Region | 171-252 | Disordered | ||||
Sequence: LGLGGRRLKSPQAPDPEEEENRDSQQPGKRRKDSEEEAASPEGKRVPKRLRCWEEEEDHEKERPEHKSLESLADGGSASPIK | ||||||
Compositional bias | 181-240 | Basic and acidic residues | ||||
Sequence: PQAPDPEEEENRDSQQPGKRRKDSEEEAASPEGKRVPKRLRCWEEEEDHEKERPEHKSLE |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length536
- Mass (Da)58,711
- Last updated2001-03-01 v1
- Checksum0E94D8C469C791A5
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8Q3WMB8 | A0A8Q3WMB8_HUMAN | FANCE | 441 | ||
A0A3B3ITU7 | A0A3B3ITU7_HUMAN | FANCE | 503 | ||
A0A8Q3WL50 | A0A8Q3WL50_HUMAN | FANCE | 451 | ||
A0A8Q3SIL2 | A0A8Q3SIL2_HUMAN | FANCE | 339 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 181-240 | Basic and acidic residues | ||||
Sequence: PQAPDPEEEENRDSQQPGKRRKDSEEEAASPEGKRVPKRLRCWEEEEDHEKERPEHKSLE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF265210 EMBL· GenBank· DDBJ | AAG16743.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ020173 EMBL· GenBank· DDBJ | AAY26395.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK292522 EMBL· GenBank· DDBJ | BAF85211.1 EMBL· GenBank· DDBJ | mRNA | ||
AL022721 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471081 EMBL· GenBank· DDBJ | EAX03830.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC046359 EMBL· GenBank· DDBJ | AAH46359.1 EMBL· GenBank· DDBJ | mRNA |