CCNF
entrez
899
canonical
uniprot
P41002
canonical
ensembl
ENSG00000162063
resolver
ensp
ENSP00000380256
resolver
enst
ENST00000397066
resolver
genesymbol
CCNF
resolver
genesymbol_syn
FBX1
resolver
genesymbol_syn
FBXO1
resolver
hgnc
HGNC:1591
resolver
uniprot
B2R8H3
resolver
uniprot
Q59HD0
resolver
uniprot
Q96EG9
resolver
uniprot_entry
CCNF_HUMAN
resolver
uniprot_entry
Q59HD0_HUMAN
resolver
uniprot_sec
B2R8H3
resolver
uniprot_sec
Q96EG9
resolver
amino_acid_sequence
MGSGGVVHCRCAKCFCYPTKRRIRRRPRNLTILSLPEDVLFHILKWLSVEDILAVRAVHSQLKDLVDNHASVWACASFQELWPSPGNLKLFERAAEKGNFEAAVKLGIAYLYNEGLSVSDEARAEVNGLKASRFFSLAERLNVGAAPFIWLFIRPPWSVSGSCCKAVVHESLRAECQLQRTHKASILHCLGRVLSLFEDEEKQQQAHDLFEEAAHQGCLTSSYLLWESDRRTDVSDPGRCLHSFRKLRDYAAKGCWEAQLSLAKACANANQLGLEVRASSEIVCQLFQASQAVSKQQVFSVQKGLNDTMRYILIDWLVEVATMKDFTSLCLHLTVECVDRYLRRRLVPRYRLQLLGIACMVICTRFISKEILTIREAVWLTDNTYKYEDLVRMMGEIVSALEGKIRVPTVVDYKEVLLTLVPVELRTQHLCSFLCELSLLHTSLSAYAPARLAAAALLLARLTHGQTQPWTTQLWDLTGFSYEDLIPCVLSLHKKCFHDDAPKDYRQVSLTAVKQRFEDKRYGEISQEEVLSYSQLCAALGVTQDSPDPPTFLSTGEIHAFLSSPSGRRTKRKRENSLQEDRGSFVTTPTAELSSQEETLLGSFLDWSLDCCSGYEGDQESEGEKEGDVTAPSGILDVTVVYLNPEQHCCQESSDEEACPEDKGPQDPQALALDTQIPATPGPKPLVRTSREPGKDVTTSGYSSVSTASPTSSVDGGLGALPQPTSVLSLDSDSHTQPCHHQARKSCLQCRPPSPPESSVPQQQVKRINLCIHSEEEDMNLGLVRL
uniprot
proteins
disease_involvement
DISEASE: Frontotemporal dementia and/or amyotrophic lateral sclerosis 5 (FTDALS5) [MIM:619141]: A neurodegenerative disorder characterized by frontotemporal dementia and/or amyotrophic lateral sclerosis in affected individuals. There is high intrafamilial variation. Frontotemporal dementia is characterized by frontal and temporal lobe atrophy associated with neuronal loss, gliosis, and dementia. Patients exhibit progressive changes in social, behavioral, and/or language function. Amyotrophic lateral sclerosis is characterized by the death of motor neurons in the brain, brainstem, and spinal cord, resulting in fatal paralysis. FTDALS5 is an autosomal dominant form with age-dependent penetrance. Penetrance is estimated to be 50% by age 56 and 100% by age 61. {ECO:0000269|PubMed:27080313, ECO:0000269|PubMed:28852778}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:20596027, PubMed:22632967, PubMed:26818844, PubMed:27080313, PubMed:27653696, PubMed:28852778). The SCF(CCNF) E3 ubiquitin-protein ligase complex is an integral component of the ubiquitin proteasome system (UPS) and links proteasome degradation to the cell cycle (PubMed:20596027, PubMed:26818844, PubMed:27653696, PubMed:8706131). Mediates the substrate recognition and the proteasomal degradation of various target proteins involved in the regulation of cell cycle progression and in the maintenance of genome stability (PubMed:20596027, PubMed:22632967, PubMed:26818844, PubMed:27653696). Mediates the ubiquitination and proteasomal degradation of CP110 during G2 phase, thereby acting as an inhibitor of centrosome reduplication (PubMed:20596027). In G2, mediates the ubiquitination and subsequent degradation of ribonucleotide reductase RRM2, thereby maintaining a balanced pool of dNTPs and genome integrity (PubMed:22632967). In G2, mediates the ubiquitination and proteasomal degradation of CDC6, thereby suppressing DNA re-replication and preventing genome instability (PubMed:26818844). Involved in the ubiquitination and degradation of the substrate adapter CDH1 of the anaphase-promoting complex (APC/C), thereby acting as an antagonist of APC/C in regulating G1 progression and S phase entry (PubMed:27653696). May play a role in the G2 cell cycle checkpoint control after DNA damage, possibly by promoting the ubiquitination of MYBL2/BMYB (PubMed:25557911). {ECO:0000269|PubMed:20596027, ECO:0000269|PubMed:22632967, ECO:0000269|PubMed:25557911, ECO:0000269|PubMed:26818844, ECO:0000269|PubMed:27080313, ECO:0000269|PubMed:27653696, ECO:0000269|PubMed:28852778, ECO:0000269|PubMed:8706131}.
uniprot
proteins
mass_dalton
87640
uniprot
proteins
mutagenesis
MUTAGEN 35..36; /note="LP->AA: Impairs interaction with SKP1 and CUL1 and prevents degradation of CP110, leading to promote the formation of micronuclei. Increased interaction with RRM2 and lack of RRM2 ubiquitination."; /evidence="ECO:0000269|PubMed:20596027, ECO:0000269|PubMed:22632967"; MUTAGEN 309..310; /note="MR->AA: Reduces the interaction with MYBL2/BMYB. Disrupts the interaction with CDC6. Does not disrupt interaction with CUL1."; /evidence="ECO:0000269|PubMed:25557911, ECO:0000269|PubMed:26818844"; MUTAGEN 309; /note="M->A: Reduced degradation of RRM2 after UV-induced DNA-damage. Abolishes the interaction with CP110 and RRM2; when associated with A-352."; /evidence="ECO:0000269|PubMed:20596027, ECO:0000269|PubMed:22632967"; MUTAGEN 310..313; /note="RYIL->AYIA: Reduces the interaction with FZR1/CDH1. Reduced ubiquitination. Abolishes the interaction with FZR1/CDH1; when associated with 351-R--L-354. Loss of ubiquitination and impaired degradation; when associated with 351-R--L-354."; /evidence="ECO:0000269|PubMed:27653696"; MUTAGEN 343..346; /note="RRRL->ARRA: Reduces the interaction with FZR1/CDH1."; /evidence="ECO:0000269|PubMed:27653696"; MUTAGEN 349..352; /note="RYRL->AYRA: Reduces the interaction with FZR1/CDH1."; /evidence="ECO:0000269|PubMed:27653696"; MUTAGEN 351..354; /note="RLQL->ALQA: Reduces the interaction with FZR1/CDH1. Abolishes the interaction with FZR1/CDH1; when associated with 310-R--L-313. Loss of ubiquitination and impaired degradation; when associated with 310-R--L-313."; /evidence="ECO:0000269|PubMed:27653696"; MUTAGEN 352; /note="L->A: Abolishes the interaction with CP110 and RRM2; when associated with A-309."; /evidence="ECO:0000269|PubMed:20596027, ECO:0000269|PubMed:22632967"; MUTAGEN 767..770; /note="RINL->AINA: Reduces the interaction with FZR1/CDH1."; /evidence="ECO:0000269|PubMed:27653696
uniprot
proteins
post_translational_modification
PTM: Degraded when the spindle assembly checkpoint is activated during the G2-M transition. Degradation depends on the C-terminal PEST sequence. {ECO:0000269|PubMed:12122006}.; PTM: Phosphorylated just before cells enter into mitosis. {ECO:0000269|PubMed:7813445}.; PTM: Ubiquitinated by the anaphase-promoting complex (APC/C); leading to its degradation by the proteasome. {ECO:0000269|PubMed:27653696}.
uniprot
proteins
protein_family
Cyclin AB subfamily
uniprot
proteins
protein_family
Cyclin family
uniprot
proteins
pubmed
10716937
uniprot
proteins
pubmed
12122006
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
20596027
uniprot
proteins
pubmed
22441691
uniprot
proteins
pubmed
22632967
uniprot
proteins
pubmed
25557911
uniprot
proteins
pubmed
26818844
uniprot
proteins
pubmed
27080313
uniprot
proteins
pubmed
27653696
uniprot
proteins
pubmed
28852778
uniprot
proteins
pubmed
7813445
uniprot
proteins
pubmed
7896286
uniprot
proteins
pubmed
8706131
uniprot
proteins
sequence_length
786
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10716937, ECO:0000269|PubMed:22632967, ECO:0000269|PubMed:26818844, ECO:0000269|PubMed:7813445}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:7813445}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:20596027}. Note=Localization to the centrosome is rare in S phase cells and increases in G2 cells. Localizes to both the mother and daughter centrioles. Localization to centrosomes is not dependent on CP110. Localizes to the nucleus in G2 phase. {ECO:0000269|PubMed:20596027, ECO:0000269|PubMed:26818844}.
uniprot
proteins