FBX4_BOVIN
ID FBX4_BOVIN Reviewed; 387 AA.
AC Q3T0J1;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=F-box only protein 4;
GN Name=FBXO4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex that mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. Promotes ubiquitination of CCND1 and its subsequent
CC proteasomal degradation. Recognizes TERF1 and promotes its
CC ubiquitination together with UBE2D1 (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer. Directly interacts with SKP1 and CUL1. Part of the
CC SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXO4)
CC formed of CUL1, SKP1, RBX1 and FBXO4. Interacts with TERF1; this
CC interaction is prevented in the presence of GNL3L. Identified in a
CC complex with CRYAB and CCND1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Phosphorylation at Ser-11 varies during the cell cycle. It is low
CC in resting cells and high in the S phase and the G2/M phase of the cell
CC cycle. Phosphorylation is decreased during late G1 phase.
CC Phosphorylation at Ser-11 is important for homodimerization and for
CC optimal ubiquitin ligase activity towards CCND1 (By similarity).
CC {ECO:0000250}.
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DR EMBL; BC102371; AAI02372.1; -; mRNA.
DR RefSeq; NP_001029789.1; NM_001034617.1.
DR AlphaFoldDB; Q3T0J1; -.
DR SMR; Q3T0J1; -.
DR STRING; 9913.ENSBTAP00000022583; -.
DR PaxDb; Q3T0J1; -.
DR Ensembl; ENSBTAT00000022583; ENSBTAP00000022583; ENSBTAG00000016981.
DR GeneID; 534852; -.
DR KEGG; bta:534852; -.
DR CTD; 26272; -.
DR VEuPathDB; HostDB:ENSBTAG00000016981; -.
DR VGNC; VGNC:28910; FBXO4.
DR eggNOG; ENOG502QUXD; Eukaryota.
DR GeneTree; ENSGT00390000014416; -.
DR InParanoid; Q3T0J1; -.
DR OMA; RQIHGIG; -.
DR OrthoDB; 680454at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000016981; Expressed in oocyte and 105 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0019725; P:cellular homeostasis; IEA:Ensembl.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IEA:Ensembl.
DR GO; GO:0035726; P:common myeloid progenitor cell proliferation; IEA:Ensembl.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:1902916; P:positive regulation of protein polyubiquitination; IEA:Ensembl.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IEA:Ensembl.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IEA:Ensembl.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:2000001; P:regulation of DNA damage checkpoint; IEA:Ensembl.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR039588; FBXO4.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR16008; PTHR16008; 1.
DR Pfam; PF12937; F-box-like; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..387
FT /note="F-box only protein 4"
FT /id="PRO_0000240133"
FT DOMAIN 56..102
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHQ0"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKT5"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKT5"
SQ SEQUENCE 387 AA; 43965 MW; 505054228AC769C4 CRC64;
MAGSDPGSRG SSPQPPHSDW GRLEAAFLSG WRNFWQSVGK ERAAPRASAE EVDEEASSLT
RLPIDVQLYI LSFLSPHDLC QLGSTSRYWN ETVRDPILWR YFLLRDLPSW SSVDWKSLPD
LEILKKPISE VTNGAFFDYM AVYKMCCPHT RRSSKSSRPM YGAVTSFLHS LIIQNEPRFA
MFGPGLEELN TSLVLSLMSS EELCPTAGLP QRQIDGIGSG VSFQLNNQHK FNILILYSTT
RKERDRAREE HTSAVNKMFS VQNEGDDQQG SRYSVIPQIQ KVCEVVDGFI YVANAEAHKR
HEWQDEFSRI MAMTDPAFGS SGRPMLVLSC ISQANVKRMP CFYLAHELRL NHLNHPWMVQ
DTEAETLTGF LNGIQWILEE VESKHAR
