ID FBXL7_HUMAN Reviewed; 491 AA. AC Q9UJT9; B9EGF1; D6RDY7; O94926; DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 09-APR-2025, entry version 182. DE RecName: Full=F-box/LRR-repeat protein 7; DE AltName: Full=F-box and leucine-rich repeat protein 7; DE AltName: Full=F-box protein FBL6/FBL7; GN Name=FBXL7; Synonyms=FBL6, FBL7, KIAA0840; 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 1). RX PubMed=10945468; DOI=10.1006/geno.2000.6211; RA Ilyin G.P., Rialland M., Pigeon C., Guguen-Guillouzo C.; RT "cDNA cloning and expression analysis of new members of the mammalian F-box RT protein family."; RL Genomics 67:40-47(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10048485; DOI=10.1093/dnares/5.6.355; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [3] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Testis; 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 41-483 (ISOFORM 1). RX PubMed=10531035; DOI=10.1016/s0960-9822(00)80020-2; RA Cenciarelli C., Chiaur D.S., Guardavaccaro D., Parks W., Vidal M., RA Pagano M.; RT "Identification of a family of human F-box proteins."; RL Curr. Biol. 9:1177-1179(1999). RN [8] RP FUNCTION. RX PubMed=25778398; DOI=10.1074/jbc.m114.629931; RA Liu Y., Lear T., Iannone O., Shiva S., Corey C., Rajbhandari S., Jerome J., RA Chen B.B., Mallampalli R.K.; RT "The Proapoptotic F-box Protein Fbxl7 Regulates Mitochondrial Function by RT Mediating the Ubiquitylation and Proteasomal Degradation of Survivin."; RL J. Biol. Chem. 290:11843-11852(2015). RN [9] RP FUNCTION, AND INTERACTION WITH BIRC5. RX PubMed=28218735; DOI=10.1038/oncsis.2016.80; RA Kamran M., Long Z.J., Xu D., Lv S.S., Liu B., Wang C.L., Xu J., Lam E.W., RA Liu Q.; RT "Aurora kinase A regulates Survivin stability through targeting FBXL7 in RT gastric cancer drug resistance and prognosis."; RL Oncogenesis 6:E298-E298(2017). CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box CC protein) E3 ubiquitin-protein ligase complex (PubMed:25778398). During CC mitosis, it mediates the ubiquitination and subsequent proteasomal CC degradation of AURKA, causing mitotic arrest (By similarity). It also CC regulates mitochondrial function by mediating the ubiquitination and CC proteasomal degradation of the apoptosis inhibitor BIRC5 CC (PubMed:25778398, PubMed:28218735). {ECO:0000250|UniProtKB:Q5BJ29, CC ECO:0000269|PubMed:25778398, ECO:0000269|PubMed:28218735}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:25778398, ECO:0000269|PubMed:28218735}. CC -!- SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase CC complex SCF(FBXL7) composed of CUL1, SKP1, RBX1 and FBXL7 (By CC similarity). Interacts with AURKA; interaction takes place during CC mitosis but not in interphase (By similarity). Interacts with BIRC5; CC this interaction allows BIRC5 to be polyubiquitinated by the SCF(FBXL7) CC E3 ubiquitin-protein ligase complex (PubMed:28218735). CC {ECO:0000250|UniProtKB:Q5BJ29, ECO:0000269|PubMed:28218735}. CC -!- INTERACTION: CC Q9UJT9; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-914660, EBI-11977403; CC Q9UJT9; Q92609: TBC1D5; NbExp=3; IntAct=EBI-914660, EBI-742381; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000250|UniProtKB:Q5BJ29}. Note=Localizes to CC the centrosome during spindle formation. CC {ECO:0000250|UniProtKB:Q5BJ29}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UJT9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UJT9-2; Sequence=VSP_054751; CC -!- SIMILARITY: Belongs to the FBXL7 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA74863.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; AF199356; AAF09248.1; -; mRNA. DR EMBL; AB020647; BAA74863.2; ALT_INIT; mRNA. DR EMBL; AC091970; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC091872; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC027332; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC010638; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC010477; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471102; EAX08029.1; -; Genomic_DNA. DR EMBL; BC075061; AAH75061.1; -; mRNA. DR EMBL; BC136424; AAI36425.1; -; mRNA. DR EMBL; AF174593; AAF04514.1; -; mRNA. DR CCDS; CCDS54833.1; -. [Q9UJT9-1] DR CCDS; CCDS64129.1; -. [Q9UJT9-2] DR RefSeq; NP_001265246.1; NM_001278317.2. [Q9UJT9-2] DR RefSeq; NP_036436.1; NM_012304.5. [Q9UJT9-1] DR RefSeq; XP_011512300.1; XM_011513998.2. [Q9UJT9-2] DR RefSeq; XP_047272956.1; XM_047417000.1. [Q9UJT9-2] DR RefSeq; XP_054208147.1; XM_054352172.1. [Q9UJT9-2] DR RefSeq; XP_054208148.1; XM_054352173.1. [Q9UJT9-2] DR AlphaFoldDB; Q9UJT9; -. DR SMR; Q9UJT9; -. DR BioGRID; 116803; 25. DR ComplexPortal; CPX-2683; SCF E3 ubiquitin ligase complex, FBXL7 variant. DR IntAct; Q9UJT9; 7. DR STRING; 9606.ENSP00000423630; -. DR GlyGen; Q9UJT9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UJT9; -. DR PhosphoSitePlus; Q9UJT9; -. DR BioMuta; FBXL7; -. DR DMDM; 37537858; -. DR MassIVE; Q9UJT9; -. DR PaxDb; 9606-ENSP00000423630; -. DR PeptideAtlas; Q9UJT9; -. DR ProteomicsDB; 14203; -. DR ProteomicsDB; 84649; -. [Q9UJT9-1] DR Antibodypedia; 5190; 90 antibodies from 20 providers. DR DNASU; 23194; -. DR Ensembl; ENST00000504595.2; ENSP00000423630.1; ENSG00000183580.10. [Q9UJT9-1] DR Ensembl; ENST00000510662.1; ENSP00000425184.1; ENSG00000183580.10. [Q9UJT9-2] DR GeneID; 23194; -. DR KEGG; hsa:23194; -. DR MANE-Select; ENST00000504595.2; ENSP00000423630.1; NM_012304.5; NP_036436.1. DR UCSC; uc003jfn.3; human. [Q9UJT9-1] DR AGR; HGNC:13604; -. DR CTD; 23194; -. DR DisGeNET; 23194; -. DR GeneCards; FBXL7; -. DR HGNC; HGNC:13604; FBXL7. DR HPA; ENSG00000183580; Low tissue specificity. DR MIM; 605656; gene. DR neXtProt; NX_Q9UJT9; -. DR OpenTargets; ENSG00000183580; -. DR PharmGKB; PA28027; -. DR VEuPathDB; HostDB:ENSG00000183580; -. DR eggNOG; KOG1947; Eukaryota. DR GeneTree; ENSGT00940000158009; -. DR HOGENOM; CLU_016072_5_0_1; -. DR InParanoid; Q9UJT9; -. DR OMA; ETVHVDR; -. DR OrthoDB; 423607at2759; -. DR PhylomeDB; Q9UJT9; -. DR TreeFam; TF313434; -. DR PathwayCommons; Q9UJT9; -. DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis. DR Reactome; R-HSA-8951664; Neddylation. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q9UJT9; -. DR SIGNOR; Q9UJT9; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 23194; 11 hits in 1194 CRISPR screens. DR ChiTaRS; FBXL7; human. DR GeneWiki; FBXL7; -. DR GenomeRNAi; 23194; -. DR Pharos; Q9UJT9; Tbio. DR PRO; PR:Q9UJT9; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q9UJT9; protein. DR Bgee; ENSG00000183580; Expressed in secondary oocyte and 198 other cell types or tissues. DR ExpressionAtlas; Q9UJT9; baseline and differential. DR GO; GO:0005813; C:centrosome; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB. DR GO; GO:0000151; C:ubiquitin ligase complex; NAS:UniProtKB. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB. DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB. DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB. DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; NAS:UniProtKB. DR CDD; cd22120; F-box_FBXL7; 1. DR FunFam; 3.80.10.10:FF:000122; F-box/LRR-repeat protein 7 isoform X1; 1. DR FunFam; 3.80.10.10:FF:000126; F-box/LRR-repeat protein 7 isoform X1; 1. DR FunFam; 1.20.1280.50:FF:000018; F-box/LRR-repeat protein 7 isoform X2; 1. DR Gene3D; 1.20.1280.50; -; 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; IPR001611; Leu-rich_rpt. DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp. DR InterPro; IPR032675; LRR_dom_sf. DR PANTHER; PTHR13318:SF50; F-BOX_LRR-REPEAT PROTEIN 7; 1. DR PANTHER; PTHR13318; PARTNER OF PAIRED, ISOFORM B-RELATED; 1. DR Pfam; PF12937; F-box-like; 1. DR Pfam; PF13516; LRR_6; 4. DR SMART; SM00256; FBOX; 1. DR SMART; SM00367; LRR_CC; 11. DR SUPFAM; SSF81383; F-box domain; 1. DR SUPFAM; SSF52047; RNI-like; 1. DR PROSITE; PS50181; FBOX; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; KW Leucine-rich repeat; Mitosis; Proteomics identification; KW Reference proteome; Repeat; Ubl conjugation pathway. FT CHAIN 1..491 FT /note="F-box/LRR-repeat protein 7" FT /id="PRO_0000119849" FT DOMAIN 111..157 FT /note="F-box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080" FT REPEAT 170..195 FT /note="LRR 1" FT REPEAT 196..221 FT /note="LRR 2" FT REPEAT 222..247 FT /note="LRR 3" FT REPEAT 253..281 FT /note="LRR 4" FT REPEAT 282..307 FT /note="LRR 5" FT REPEAT 308..333 FT /note="LRR 6" FT REPEAT 334..359 FT /note="LRR 7" FT REPEAT 360..385 FT /note="LRR 8" FT REPEAT 386..411 FT /note="LRR 9" FT REPEAT 412..437 FT /note="LRR 10" FT REPEAT 438..463 FT /note="LRR 11" FT REGION 1..79 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 10..26 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 27..55 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1..47 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_054751" SQ SEQUENCE 491 AA; 54575 MW; A70C092A4E748C69 CRC64; MGANNGKQYG SEGKGSSSIS SDVSSSTDHT PTKAQKNVAT SEDSDLSMRT LSTPSPALIC PPNLPGFQNG RGSSTSSSSI TGETVAMVHS PPPTRLTHPL IRLASRPQKE QASIDRLPDH SMVQIFSFLP TNQLCRCARV CRRWYNLAWD PRLWRTIRLT GETINVDRAL KVLTRRLCQD TPNVCLMLET VTVSGCRRLT DRGLYTIAQC CPELRRLEVS GCYNISNEAV FDVVSLCPNL EHLDVSGCSK VTCISLTREA SIKLSPLHGK QISIRYLDMT DCFVLEDEGL HTIAAHCTQL THLYLRRCVR LTDEGLRYLV IYCASIKELS VSDCRFVSDF GLREIAKLES RLRYLSIAHC GRVTDVGIRY VAKYCSKLRY LNARGCEGIT DHGVEYLAKN CTKLKSLDIG KCPLVSDTGL ECLALNCFNL KRLSLKSCES ITGQGLQIVA ANCFDLQTLN VQDCEVSVEA LRFVKRHCKR CVIEHTNPAF F //