ID FBX10_HUMAN Reviewed; 956 AA. AC Q9UK96; Q08AL3; Q08AL4; Q5JRT8; Q9UKC3; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 3. DT 10-JUN-2026, entry version 187. DE RecName: Full=F-box only protein 10; GN Name=FBXO10; Synonyms=FBX10, PRMT11; 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 GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). 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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-521 (ISOFORM 1). RX PubMed=10531037; DOI=10.1016/s0960-9822(00)80021-4; RA Winston J.T., Koepp D.M., Zhu C., Elledge S.J., Harper J.W.; RT "A family of mammalian F-box proteins."; RL Curr. Biol. 9:1180-1182(1999). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-162 (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 [6] RP FUNCTION IN UBIQUITINATION OF BCL2, INTERACTION WITH BCL2, SUBCELLULAR RP LOCATION, IDENTIFICATION IN THE SCF(FBXO10) COMPLEX, VARIANTS HIS-44; RP ASN-212; CYS-762 AND TRP-825, AND CHARACTERIZATION OF VARIANTS HIS-44; RP CYS-762 AND TRP-825. RX PubMed=23431138; DOI=10.1073/pnas.1217271110; RA Chiorazzi M., Rui L., Yang Y., Ceribelli M., Tishbi N., Maurer C.W., RA Ranuncolo S.M., Zhao H., Xu W., Chan W.C., Jaffe E.S., Gascoyne R.D., RA Campo E., Rosenwald A., Ott G., Delabie J., Rimsza L.M., Shaham S., RA Staudt L.M.; RT "Related F-box proteins control cell death in Caenorhabditis elegans and RT human lymphoma."; RL Proc. Natl. Acad. Sci. U.S.A. 110:3943-3948(2013). RN [7] RP INTERACTION WITH PRDM1. RX PubMed=24613396; DOI=10.1016/j.devcel.2014.01.028; RA Horn M., Geisen C., Cermak L., Becker B., Nakamura S., Klein C., Pagano M., RA Antebi A.; RT "DRE-1/FBXO11-dependent degradation of BLMP-1/BLIMP-1 governs C. elegans RT developmental timing and maturation."; RL Dev. Cell 28:697-710(2014). RN [8] RP FUNCTION. RX PubMed=28515150; DOI=10.1096/fj.201700031r; RA Evankovich J., Lear T., Mckelvey A., Dunn S., Londino J., Liu Y., RA Chen B.B., Mallampalli R.K.; RT "Receptor for advanced glycation end products is targeted by FBXO10 for RT ubiquitination and degradation."; RL FASEB J. 31:3894-3903(2017). RN [9] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=31570756; DOI=10.1038/s41375-019-0579-5; RA Guo F., Luo Y., Jiang X., Lu X., Roberti D., Lossos C., Kunkalla K., RA Magistri M., Rui L., Verdun R., Vega F., Moy V.T., Lossos I.S.; RT "Recent BCR stimulation induces a negative autoregulatory loop via FBXO10 RT mediated degradation of HGAL."; RL Leukemia 34:553-566(2020). CC -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box CC protein)-type E3 ubiquitin ligase complex. Mediates the ubiquitination CC and degradation of BCL2, an antiapoptotic protein, thereby playing a CC role in apoptosis by controlling the stability of BCL2. Targets also CC the receptor for advanced glycation end products RAGE for CC ubiquitination and subsequent lysosomal degradation (PubMed:28515150). CC Directly controls HGAL/GCSAM ubiquitination and degradation and thereby CC decreases BCR signaling (PubMed:31570756). CC {ECO:0000269|PubMed:23431138, ECO:0000269|PubMed:28515150, CC ECO:0000269|PubMed:31570756}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Component of the SCF(FBXO10) complex consisting of CUL1, SKP1 CC and FBXO10 (PubMed:23431138). Interacts with BCL2 (PubMed:23431138). CC Interacts with PRDM1 (PubMed:24613396). {ECO:0000269|PubMed:23431138, CC ECO:0000269|PubMed:24613396}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23431138, CC ECO:0000269|PubMed:31570756}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UK96-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UK96-2; Sequence=VSP_056318; CC -!- DISEASE: Note=Defects in FBXO10 may be a cause of diffuse large B-cell CC lymphoma by allowing the accumulation of BCL2, an oncoprotein that has CC a critical role in lymphomas. {ECO:0000269|PubMed:23431138}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF03705.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF03705.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305}; CC Sequence=AAF04519.1; 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; AL513165; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471071; EAW58274.1; -; Genomic_DNA. DR EMBL; CH471071; EAW58275.1; -; Genomic_DNA. DR EMBL; BC125124; AAI25125.1; -; mRNA. DR EMBL; BC125125; AAI25126.1; -; mRNA. DR EMBL; BC140785; AAI40786.1; -; mRNA. DR EMBL; BC171785; AAI71785.1; -; mRNA. DR EMBL; AF176705; AAF03705.1; ALT_SEQ; mRNA. DR EMBL; AF174598; AAF04519.1; ALT_INIT; mRNA. DR CCDS; CCDS47966.1; -. [Q9UK96-1] DR RefSeq; NP_036298.2; NM_012166.3. [Q9UK96-1] DR RefSeq; XP_016870108.1; XM_017014619.2. [Q9UK96-1] DR RefSeq; XP_047279176.1; XM_047423220.1. [Q9UK96-1] DR RefSeq; XP_047279177.1; XM_047423221.1. [Q9UK96-1] DR RefSeq; XP_054218697.1; XM_054362722.1. [Q9UK96-1] DR RefSeq; XP_054218698.1; XM_054362723.1. [Q9UK96-1] DR RefSeq; XP_054218699.1; XM_054362724.1. [Q9UK96-1] DR AlphaFoldDB; Q9UK96; -. DR SMR; Q9UK96; -. DR BioGRID; 117651; 45. DR ComplexPortal; CPX-7923; SCF E3 ubiquitin ligase complex, FBXO10 variant. DR CORUM; Q9UK96; -. DR FunCoup; Q9UK96; 315. DR IntAct; Q9UK96; 45. DR NDEx; MUSIC2-C5190-FBXO10; Osteosarcoma (U2OS) cell map - DNA replication and repair system (48 proteins). DR STRING; 9606.ENSP00000403802; -. DR iPTMnet; Q9UK96; -. DR PhosphoSitePlus; Q9UK96; -. DR SwissPalm; Q9UK96; -. DR BioMuta; FBXO10; -. DR DMDM; 296439345; -. DR jPOST; Q9UK96; -. DR MassIVE; Q9UK96; -. DR PaxDb; 9606-ENSP00000403802; -. DR PeptideAtlas; Q9UK96; -. DR ProteomicsDB; 58678; -. DR ProteomicsDB; 84741; -. [Q9UK96-1] DR Pumba; Q9UK96; -. DR Antibodypedia; 26292; 56 antibodies from 16 providers. DR DNASU; 26267; -. DR Ensembl; ENST00000432825.7; ENSP00000403802.2; ENSG00000147912.14. [Q9UK96-1] DR Ensembl; ENST00000967086.1; ENSP00000637145.1; ENSG00000147912.14. [Q9UK96-1] DR GeneID; 26267; -. DR KEGG; hsa:26267; -. DR MANE-Select; ENST00000432825.7; ENSP00000403802.2; NM_012166.3; NP_036298.2. DR UCSC; uc004aab.3; human. [Q9UK96-1] DR AGR; HGNC:13589; -. DR ClinPGx; PA28030; -. DR CTD; 26267; -. DR DisGeNET; 26267; -. DR GeneCards; FBXO10; -. DR HGNC; HGNC:13589; FBXO10. DR HPA; ENSG00000147912; Tissue enhanced (skeletal). DR MIM; 609092; gene. DR OpenTargets; ENSG00000147912; -. DR VEuPathDB; HostDB:ENSG00000147912; -. DR eggNOG; KOG1777; Eukaryota. DR GeneTree; ENSGT00530000063425; -. DR HOGENOM; CLU_013632_0_0_1; -. DR InParanoid; Q9UK96; -. DR OMA; CNLIFMP; -. DR OrthoDB; 427974at2759; -. DR PAN-GO; Q9UK96; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q9UK96; -. DR PathwayCommons; Q9UK96; -. DR Reactome; R-HSA-8951664; Neddylation. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q9UK96; -. DR UniPathway; UPA00143; -. DR Agora; ENSG00000147912; -. DR BioGRID-ORCS; 26267; 10 hits in 1196 CRISPR screens. DR ChiTaRS; FBXO10; human. DR GenomeRNAi; 26267; -. DR Pharos; Q9UK96; Tbio. DR PRO; PR:Q9UK96; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9UK96; protein. DR Bgee; ENSG00000147912; Expressed in adrenal tissue and 126 other cell types or tissues. DR ExpressionAtlas; Q9UK96; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0000151; C:ubiquitin ligase complex; NAS:UniProtKB. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; NAS:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0016567; P:protein ubiquitination; NAS:UniProtKB. DR GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; NAS:ComplexPortal. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB. DR CDD; cd22090; F-box_FBXO10; 1. DR FunFam; 1.20.1280.50:FF:000009; F-box only protein 10; 1. DR FunFam; 2.160.20.10:FF:000015; F-box only protein 10; 1. DR FunFam; 2.160.20.10:FF:000017; F-box only protein 10; 1. DR FunFam; 2.160.20.10:FF:000022; F-box only protein 10; 1. DR Gene3D; 1.20.1280.50; -; 1. DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 3. DR InterPro; IPR039448; Beta_helix. DR InterPro; IPR006633; Carb-bd_sugar_hydrolysis-dom. DR InterPro; IPR036047; F-box-like_dom_sf. DR InterPro; IPR001810; F-box_dom. DR InterPro; IPR007742; NosD_dom. DR InterPro; IPR022441; Para_beta_helix_rpt-2. DR InterPro; IPR006626; PbH1. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR InterPro; IPR051550; SCF-Subunits/Alg-Epimerases. DR NCBIfam; TIGR03804; para_beta_helix; 1. DR PANTHER; PTHR22990; F-BOX ONLY PROTEIN; 1. DR PANTHER; PTHR22990:SF15; F-BOX ONLY PROTEIN 10; 1. DR Pfam; PF13229; Beta_helix; 1. DR Pfam; PF12937; F-box-like; 1. DR Pfam; PF05048; NosD; 1. DR SMART; SM00722; CASH; 3. DR SMART; SM00256; FBOX; 1. DR SMART; SM00710; PbH1; 18. DR SUPFAM; SSF81383; F-box domain; 1. DR SUPFAM; SSF51126; Pectin lyase-like; 4. DR PROSITE; PS50181; FBOX; 1. PE 1: Evidence at protein level; KW Alternative splicing; Apoptosis; Cytoplasm; Phosphoprotein; KW Proteomics identification; Reference proteome; Repeat; KW Ubl conjugation pathway. FT CHAIN 1..956 FT /note="F-box only protein 10" FT /id="PRO_0000119889" FT DOMAIN 1..48 FT /note="F-box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080" FT REPEAT 198..217 FT /note="PbH1 1" FT REPEAT 238..260 FT /note="PbH1 2" FT REPEAT 427..448 FT /note="PbH1 3" FT REPEAT 449..470 FT /note="PbH1 4" FT REPEAT 471..493 FT /note="PbH1 5" FT REPEAT 494..516 FT /note="PbH1 6" FT REPEAT 538..560 FT /note="PbH1 7" FT REPEAT 561..583 FT /note="PbH1 8" FT REPEAT 584..606 FT /note="PbH1 9" FT REPEAT 607..629 FT /note="PbH1 10" FT REPEAT 630..652 FT /note="PbH1 11" FT REPEAT 653..675 FT /note="PbH1 12" FT REPEAT 717..739 FT /note="PbH1 13" FT REPEAT 740..762 FT /note="PbH1 14" FT REPEAT 764..786 FT /note="PbH1 15" FT REPEAT 787..809 FT /note="PbH1 16" FT REPEAT 832..854 FT /note="PbH1 17" FT REGION 314..367 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 316..336 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 351..361 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 321 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7TQF2" FT MOD_RES 326 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7TQF2" FT VAR_SEQ 1..475 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_056318" FT VARIANT 44 FT /note="R -> H (found in a patient with lymphoma; inhibits FT interaction with SKP1; dbSNP:rs780121584)" FT /evidence="ECO:0000269|PubMed:23431138" FT /id="VAR_070692" FT VARIANT 212 FT /note="H -> N (found in a patient with lymphoma; FT dbSNP:rs7044561)" FT /evidence="ECO:0000269|PubMed:23431138" FT /id="VAR_055801" FT VARIANT 762 FT /note="V -> C (found in a patient with lymphoma; partial FT loss of function in controlling the stability of BCL2; FT requires 2 nucleotide substitutions)" FT /evidence="ECO:0000269|PubMed:23431138" FT /id="VAR_070693" FT VARIANT 825 FT /note="R -> W (found in a patient with lymphoma; partial FT loss of function in controlling the stability of BCL2; FT dbSNP:rs573535073)" FT /evidence="ECO:0000269|PubMed:23431138" FT /id="VAR_070694" SQ SEQUENCE 956 AA; 105195 MW; 3F9BDEBE0139B16F CRC64; MEAGGLPLEL WRMILAYLHL PDLGRCSLVC RAWYELILSL DSTRWRQLCL GCTECRHPNW PNQPDVEPES WREAFKQHYL ASKTWTKNAL DLESSICFSL FRRRRERRTL SVGPGREFDS LGSALAMASL YDRIVLFPGV YEEQGEIILK VPVEIVGQGK LGEVALLASI DQHCSTTRLC NLVFTPAWFS PIMYKTTSGH VQFDNCNFEN GHIQVHGPGT CQVKFCTFKN THIFLHNVPL CVLENCEFVG SENNSVTVEG HPSADKNWAY KYLLGLIKSS PTFLPTEDSD FLMSLDLESR DQAWSPKTCD IVIEGSQSPT SPASSSPKPG SKAGSQEAEV GSDGERVAQT PDSSDGGLSP SGEDEDEDQL MYRLSYQVQG PRPVLGGSFL GPPLPGASIQ LPSCLVLNSL QQELQKDKEA MALANSVQGC LIRKCLFRDG KGGVFVCSHG RAKMEGNIFR NLTYAVRCIH NSKIIMLRND IYRCRASGIF LRLEGGGLIA GNNIYHNAEA GVDIRKKSNP LILCNQIHHG LRSGIVVLGN GKGIIRNNQI FSNKEAGIYI LYHGNPVVSG NHIFKGRAAG IAVNENGKGL ITENVIRENQ WGGVDIRRGG IPVLRSNLIC FGYSDGVVVG DEGKGLIEGN TIYANKGCGV WMMSSSLPHV TSNHVSYNGL YGVAVFSQKD GSSELPRGHR AQENFSEDGD AILWETELEK EDDPLRRPIT IALVESNSIN HNGASGLYVQ SSEALHVITN VIHANGDRGI TVAQSSQPTR VANNSISCNR QSGVKVEAQC KVELRGNGIY DNRGHGIITK GDSTIVIEND IIGNRGSGLQ LLPRSDTKVI KNRIHSFRAY GIAVRGRAKA LVQENIIFQG KTSKTIFQQI SNNRECIMQN NKFLVFKKKS DTWRLVNPPA RPHLENSLRR PSAAHNGQKV TAMATRITAR VEGGYHSNRS VFCTIL //