FXL20_HUMAN
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 03-AUG-2022, entry version 166.
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; P63208: SKP1; NbExp=4; 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;
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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_001184906.1. [Q96IG2-2]
DR RefSeq; NP_116264.2; NM_032875.2. [Q96IG2-1]
DR AlphaFoldDB; Q96IG2; -.
DR SMR; Q96IG2; -.
DR BioGRID; 124392; 12.
DR IntAct; Q96IG2; 5.
DR STRING; 9606.ENSP00000264658; -.
DR iPTMnet; Q96IG2; -.
DR PhosphoSitePlus; Q96IG2; -.
DR SwissPalm; Q96IG2; -.
DR BioMuta; FBXL20; -.
DR DMDM; 38503141; -.
DR EPD; Q96IG2; -.
DR jPOST; Q96IG2; -.
DR MassIVE; Q96IG2; -.
DR MaxQB; Q96IG2; -.
DR PaxDb; Q96IG2; -.
DR PeptideAtlas; Q96IG2; -.
DR PRIDE; Q96IG2; -.
DR ProteomicsDB; 76826; -. [Q96IG2-1]
DR ProteomicsDB; 76827; -. [Q96IG2-2]
DR Antibodypedia; 28248; 164 antibodies from 26 providers.
DR DNASU; 84961; -.
DR Ensembl; ENST00000264658.11; ENSP00000264658.6; ENSG00000108306.13. [Q96IG2-1]
DR Ensembl; ENST00000394294.7; ENSP00000377832.3; ENSG00000108306.13. [Q96IG2-2]
DR Ensembl; ENST00000583610.5; ENSP00000462271.1; ENSG00000108306.13. [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 CTD; 84961; -.
DR DisGeNET; 84961; -.
DR GeneCards; FBXL20; -.
DR HGNC; HGNC:24679; FBXL20.
DR HPA; ENSG00000108306; Low tissue specificity.
DR MIM; 609086; gene.
DR neXtProt; NX_Q96IG2; -.
DR OpenTargets; ENSG00000108306; -.
DR PharmGKB; PA134976410; -.
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 PhylomeDB; Q96IG2; -.
DR TreeFam; TF313434; -.
DR PathwayCommons; Q96IG2; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q96IG2; -.
DR BioGRID-ORCS; 84961; 14 hits in 1117 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 190 other tissues.
DR ExpressionAtlas; Q96IG2; baseline and differential.
DR Genevisible; Q96IG2; HS.
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:0001662; P:behavioral fear response; 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 Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF13516; LRR_6; 4.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00367; LRR_CC; 12.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Leucine-rich repeat; Phosphoprotein;
KW Reference proteome; Repeat; 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
