ID FXL14_HUMAN Reviewed; 418 AA. AC Q8N1E6; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 10-JUN-2026, entry version 175. DE RecName: Full=F-box/LRR-repeat protein 14; DE AltName: Full=F-box and leucine-rich repeat protein 14; GN Name=FBXL14; Synonyms=FBL14; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] RP FUNCTION, INTERACTION WITH SNAI1, SUBCELLULAR LOCATION, AND INDUCTION BY RP HYPOXIA. RX PubMed=19955572; DOI=10.1074/jbc.m109.065995; RA Vinas-Castells R., Beltran M., Valls G., Gomez I., Garcia J.M., RA Montserrat-Sentis B., Baulida J., Bonilla F., de Herreros A.G., Diaz V.M.; RT "The hypoxia-controlled FBXL14 ubiquitin ligase targets SNAIL1 for RT proteasome degradation."; RL J. Biol. Chem. 285:3794-3805(2010). CC -!- FUNCTION: Substrate-recognition component of some SCF (SKP1-CUL1-F-box CC protein)-type E3 ubiquitin-protein ligase complexes. The SCF(FBXL14) CC complex acts by mediating ubiquitination and subsequent degradation of CC SNAI1. {ECO:0000269|PubMed:19955572}. CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) ubiquitin-protein ligase CC complex. Interacts with SKP1 and CUL1 (By similarity). Interacts with CC SNAI1; the interaction requires the phosphorylation of the two serine CC residues in the substrate destruction motif D-S-G-X(2,3,4)-S. CC {ECO:0000250, ECO:0000269|PubMed:19955572}. CC -!- INTERACTION: CC Q8N1E6; P63208: SKP1; NbExp=7; IntAct=EBI-6425532, EBI-307486; CC Q8N1E6; O95863: SNAI1; NbExp=2; IntAct=EBI-6425532, EBI-1045459; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19955572}. CC -!- INDUCTION: Down-regulated by hypoxia. {ECO:0000269|PubMed:19955572}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC028132; AAH28132.1; -; mRNA. DR CCDS; CCDS8509.1; -. DR RefSeq; NP_689654.1; NM_152441.3. DR AlphaFoldDB; Q8N1E6; -. DR SMR; Q8N1E6; -. DR BioGRID; 126870; 40. DR ComplexPortal; CPX-2319; SCF E3 ubiquitin ligase complex, FBXL14 variant. DR FunCoup; Q8N1E6; 655. DR IntAct; Q8N1E6; 43. DR MINT; Q8N1E6; -. DR STRING; 9606.ENSP00000344855; -. DR GlyGen; Q8N1E6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8N1E6; -. DR PhosphoSitePlus; Q8N1E6; -. DR BioMuta; FBXL14; -. DR DMDM; 48428083; -. DR jPOST; Q8N1E6; -. DR MassIVE; Q8N1E6; -. DR PaxDb; 9606-ENSP00000344855; -. DR PeptideAtlas; Q8N1E6; -. DR ProteomicsDB; 71590; -. DR Pumba; Q8N1E6; -. DR Antibodypedia; 41744; 107 antibodies from 23 providers. DR DNASU; 144699; -. DR Ensembl; ENST00000339235.4; ENSP00000344855.3; ENSG00000171823.8. DR GeneID; 144699; -. DR KEGG; hsa:144699; -. DR MANE-Select; ENST00000339235.4; ENSP00000344855.3; NM_152441.3; NP_689654.1. DR UCSC; uc001qjh.3; human. DR AGR; HGNC:28624; -. DR ClinPGx; PA134979350; -. DR CTD; 144699; -. DR DisGeNET; 144699; -. DR GeneCards; FBXL14; -. DR HGNC; HGNC:28624; FBXL14. DR HPA; ENSG00000171823; Low tissue specificity. DR MIM; 609081; gene. DR OpenTargets; ENSG00000171823; -. DR VEuPathDB; HostDB:ENSG00000171823; -. DR eggNOG; KOG1947; Eukaryota. DR GeneTree; ENSGT00940000159857; -. DR HOGENOM; CLU_016072_7_0_1; -. DR InParanoid; Q8N1E6; -. DR OMA; DQALVHI; -. DR OrthoDB; 2585512at2759; -. DR PAN-GO; Q8N1E6; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q8N1E6; -. DR PathwayCommons; Q8N1E6; -. DR Reactome; R-HSA-8951664; Neddylation. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q8N1E6; -. DR SIGNOR; Q8N1E6; -. DR Agora; ENSG00000171823; -. DR BioGRID-ORCS; 144699; 15 hits in 1194 CRISPR screens. DR ChiTaRS; FBXL14; human. DR GenomeRNAi; 144699; -. DR Pharos; Q8N1E6; Tbio. DR PRO; PR:Q8N1E6; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q8N1E6; protein. DR Bgee; ENSG00000171823; Expressed in left testis and 114 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:ComplexPortal. DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB. DR CDD; cd22125; F-box_FBXL14; 1. DR FunFam; 3.80.10.10:FF:000051; F-box and leucine-rich repeat protein 14; 1. DR FunFam; 3.80.10.10:FF:000075; F-box/LRR-repeat protein 14 isoform X1; 1. DR FunFam; 1.20.1280.50:FF:000059; Partner of Paired; 1. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2. DR InterPro; IPR036047; F-box-like_dom_sf. DR InterPro; IPR001810; F-box_dom. DR InterPro; IPR047932; FBXL14_F-box. DR InterPro; IPR057207; FBXL15_LRR. DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp. DR InterPro; IPR032675; LRR_dom_sf. DR PANTHER; PTHR13318:SF190; PARTNER OF PAIRED, ISOFORM B; 1. DR PANTHER; PTHR13318; PARTNER OF PAIRED, ISOFORM B-RELATED; 1. DR Pfam; PF12937; F-box-like; 1. DR Pfam; PF25372; LRR_FBXL15; 2. DR SMART; SM00367; LRR_CC; 11. DR SUPFAM; SSF81383; F-box domain; 1. DR SUPFAM; SSF52047; RNI-like; 1. PE 1: Evidence at protein level; KW Cytoplasm; Leucine-rich repeat; Proteomics identification; KW Reference proteome; Repeat; Ubl conjugation pathway. FT CHAIN 1..418 FT /note="F-box/LRR-repeat protein 14" FT /id="PRO_0000119861" FT DOMAIN 2..48 FT /note="F-box" FT REPEAT 144..163 FT /note="LRR 1" FT REPEAT 170..191 FT /note="LRR 2" FT REPEAT 203..225 FT /note="LRR 3" FT REPEAT 229..250 FT /note="LRR 4" FT REPEAT 254..275 FT /note="LRR 5" FT REGION 2..48 FT /note="Required for down-regulation of SNAI1" FT VARIANT 220 FT /note="L -> V (in dbSNP:rs35571553)" FT /id="VAR_049033" SQ SEQUENCE 418 AA; 45886 MW; 5779961C8177779F CRC64; METHISCLFP ELLAMIFGYL DVRDKGRAAQ VCTAWRDAAY HKSVWRGVEA KLHLRRANPS LFPSLQARGI RRVQILSLRR SLSYVIQGMA NIESLNLSGC YNLTDNGLGH AFVQEIGSLR ALNLSLCKQI TDSSLGRIAQ YLKGLEVLEL GGCSNITNTG LLLIAWGLQR LKSLNLRSCR HLSDVGIGHL AGMTRSAAEG CLGLEQLTLQ DCQKLTDLSL KHISRGLTGL RLLNLSFCGG ISDAGLLHLS HMGSLRSLNL RSCDNISDTG IMHLAMGSLR LSGLDVSFCD KVGDQSLAYI AQGLDGLKSL SLCSCHISDD GINRMVRQMH GLRTLNIGQC VRITDKGLEL IAEHLSQLTG IDLYGCTRIT KRGLERITQL PCLKVLNLGL WQMTDSEKEA RGDFSPLFTV RTRGSSRR //