ID FXL20_HUMAN Reviewed; 436 AA. AC Q96IG2; A8K729; Q38J52; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 2. DT 10-JUN-2026, entry version 184. DE RecName: Full=F-box/LRR-repeat protein 20; DE AltName: Full=F-box and leucine-rich repeat protein 20; DE AltName: Full=F-box/LRR-repeat protein 2-like; GN Name=FBXL20; Synonyms=FBL2; 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 [MRNA] (ISOFORM 2). RA Stavropoulou A.V., Alao J.P., Lam E.W.F., Coombes R.C., Vigushin D.M.; RT "Identification of a novel FBXL20 splice variant."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon; 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 [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417 AND SER-421, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box CC protein)-type E3 ubiquitin ligase complex. Role in neural transmission CC (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with SKP1 and CUL1. {ECO:0000250}. CC -!- INTERACTION: CC Q96IG2; P63151: PPP2R2A; NbExp=4; IntAct=EBI-8835647, EBI-1048931; CC Q96IG2; P63208: SKP1; NbExp=8; IntAct=EBI-8835647, EBI-307486; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96IG2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96IG2-2; Sequence=VSP_030769; 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; DQ223959; ABB03906.1; -; mRNA. DR EMBL; AK291844; BAF84533.1; -; mRNA. DR EMBL; BC007557; AAH07557.2; -; mRNA. DR CCDS; CCDS32640.1; -. [Q96IG2-1] DR CCDS; CCDS54116.1; -. [Q96IG2-2] DR RefSeq; NP_001171835.1; NM_001184906.2. [Q96IG2-2] DR RefSeq; NP_116264.2; NM_032875.2. [Q96IG2-1] DR AlphaFoldDB; Q96IG2; -. DR SMR; Q96IG2; -. DR BioGRID; 124392; 20. DR ComplexPortal; CPX-2873; SCF E3 ubiquitin ligase complex, FBXL20 variant. DR CORUM; Q96IG2; -. DR FunCoup; Q96IG2; 591. DR IntAct; Q96IG2; 9. DR NDEx; IQUERY-CP-FBXL20; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000264658; -. DR TCDB; 8.A.92.1.17; the g-protein AlphaBetaGama complex (gpc) family. DR GlyGen; Q96IG2; 1 site. DR iPTMnet; Q96IG2; -. DR PhosphoSitePlus; Q96IG2; -. DR SwissPalm; Q96IG2; -. DR BioMuta; FBXL20; -. DR DMDM; 38503141; -. DR jPOST; Q96IG2; -. DR MassIVE; Q96IG2; -. DR PaxDb; 9606-ENSP00000264658; -. DR PeptideAtlas; Q96IG2; -. DR ProteomicsDB; 76826; -. [Q96IG2-1] DR ProteomicsDB; 76827; -. [Q96IG2-2] DR Pumba; Q96IG2; -. DR Antibodypedia; 28248; 151 antibodies from 25 providers. DR DNASU; 84961; -. DR Ensembl; ENST00000264658.11; ENSP00000264658.6; ENSG00000108306.14. [Q96IG2-1] DR Ensembl; ENST00000394294.7; ENSP00000377832.3; ENSG00000108306.14. [Q96IG2-2] DR Ensembl; ENST00000583610.5; ENSP00000462271.1; ENSG00000108306.14. [Q96IG2-1] DR GeneID; 84961; -. DR KEGG; hsa:84961; -. DR MANE-Select; ENST00000264658.11; ENSP00000264658.6; NM_032875.3; NP_116264.2. DR UCSC; uc002hrt.4; human. [Q96IG2-1] DR AGR; HGNC:24679; -. DR ClinPGx; PA134976410; -. DR CTD; 84961; -. DR DisGeNET; 84961; -. DR GeneCards; FBXL20; -. DR HGNC; HGNC:24679; FBXL20. DR HPA; ENSG00000108306; Low tissue specificity. DR MIM; 609086; gene. DR OpenTargets; ENSG00000108306; -. DR VEuPathDB; HostDB:ENSG00000108306; -. DR eggNOG; KOG4341; Eukaryota. DR GeneTree; ENSGT00940000153845; -. DR HOGENOM; CLU_016072_7_1_1; -. DR InParanoid; Q96IG2; -. DR OMA; LCNRIRY; -. DR OrthoDB; 550575at2759; -. DR PAN-GO; Q96IG2; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q96IG2; -. DR PathwayCommons; Q96IG2; -. DR Reactome; R-HSA-8951664; Neddylation. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q96IG2; -. DR Agora; ENSG00000108306; -. DR BioGRID-ORCS; 84961; 15 hits in 1195 CRISPR screens. DR ChiTaRS; FBXL20; human. DR GenomeRNAi; 84961; -. DR Pharos; Q96IG2; Tbio. DR PRO; PR:Q96IG2; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q96IG2; protein. DR Bgee; ENSG00000108306; Expressed in secondary oocyte and 191 other cell types or tissues. DR ExpressionAtlas; Q96IG2; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0098793; C:presynapse; IEA:GOC. DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl. DR GO; GO:0099575; P:regulation of protein catabolic process at presynapse, modulating synaptic transmission; IEA:Ensembl. DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl. DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR CDD; cd22115; F-box_FBXL2-like; 1. DR FunFam; 3.80.10.10:FF:000339; F-box/LRR-repeat protein 2 isoform X1; 1. DR FunFam; 3.80.10.10:FF:000578; F-box/LRR-repeat protein 2 isoform X1; 1. DR FunFam; 3.80.10.10:FF:000042; F-box/LRR-repeat protein 20 isoform 2; 1. DR FunFam; 1.20.1280.50:FF:000013; F-box/LRR-repeat protein 20 isoform X1; 1. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2. DR InterPro; IPR001810; F-box_dom. DR InterPro; IPR057207; FBXL15_LRR. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp. DR InterPro; IPR032675; LRR_dom_sf. DR PANTHER; PTHR13318:SF47; F-BOX_LRR-REPEAT PROTEIN 20; 1. DR PANTHER; PTHR13318; PARTNER OF PAIRED, ISOFORM B-RELATED; 1. DR Pfam; PF12937; F-box-like; 1. DR Pfam; PF13516; LRR_6; 2. DR Pfam; PF25372; LRR_FBXL15; 1. DR SMART; SM00256; FBOX; 1. DR SMART; SM00367; LRR_CC; 12. DR SUPFAM; SSF52047; RNI-like; 1. DR PROSITE; PS50181; FBOX; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Leucine-rich repeat; Phosphoprotein; KW Proteomics identification; Reference proteome; Repeat; KW Ubl conjugation pathway. FT CHAIN 1..436 FT /note="F-box/LRR-repeat protein 20" FT /id="PRO_0000119870" FT DOMAIN 22..68 FT /note="F-box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080" FT REPEAT 74..100 FT /note="LRR 1" FT REPEAT 101..126 FT /note="LRR 2" FT REPEAT 127..152 FT /note="LRR 3" FT REPEAT 153..178 FT /note="LRR 4" FT REPEAT 179..204 FT /note="LRR 5" FT REPEAT 205..230 FT /note="LRR 6" FT REPEAT 231..256 FT /note="LRR 7" FT REPEAT 257..282 FT /note="LRR 8" FT REPEAT 283..308 FT /note="LRR 9" FT REPEAT 309..334 FT /note="LRR 10" FT REPEAT 335..363 FT /note="LRR 11" FT REPEAT 364..388 FT /note="LRR 12" FT REPEAT 389..414 FT /note="LRR 13" FT MOD_RES 417 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 421 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 134..165 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_030769" FT CONFLICT 17 FT /note="S -> P (in Ref. 1; BAF84533)" FT /evidence="ECO:0000305" FT CONFLICT 375 FT /note="L -> F (in Ref. 1; BAF84533)" FT /evidence="ECO:0000305" SQ SEQUENCE 436 AA; 48423 MW; 39CD04A505C8CE3E CRC64; MRRDVNGVTK SRFEMFSNSD EAVINKKLPK ELLLRIFSFL DVVTLCRCAQ VSRAWNVLAL DGSNWQRIDL FDFQRDIEGR VVENISKRCG GFLRKLSLRG CLGVGDNALR TFAQNCRNIE VLNLNGCTKT TDATCTSLSK FCSKLRHLDL ASCTSITNMS LKALSEGCPL LEQLNISWCD QVTKDGIQAL VRGCGGLKAL FLKGCTQLED EALKYIGAHC PELVTLNLQT CLQITDEGLI TICRGCHKLQ SLCASGCSNI TDAILNALGQ NCPRLRILEV ARCSQLTDVG FTTLARNCHE LEKMDLEECV QITDSTLIQL SIHCPRLQVL SLSHCELITD DGIRHLGNGA CAHDQLEVIE LDNCPLITDA SLEHLKSCHS LERIELYDCQ QITRAGIKRL RTHLPNIKVH AYFAPVTPPP SVGGSRQRFC RCCIIL //