FBX10_HUMAN
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 03-AUG-2022, entry version 169.
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).
CC -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box
CC protein)-type E3 ubiquitin ligase complex. The SCF(FBXO10) complex
CC mediates ubiquitination and degradation of BCL2, an antiapoptotic
CC protein, thereby playing a role in apoptosis by controlling the
CC stability of BCL2. {ECO:0000269|PubMed:23431138}.
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 -!- 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};
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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_012166.2. [Q9UK96-1]
DR RefSeq; XP_006716817.1; XM_006716754.3. [Q9UK96-2]
DR RefSeq; XP_016870108.1; XM_017014619.1. [Q9UK96-1]
DR AlphaFoldDB; Q9UK96; -.
DR SMR; Q9UK96; -.
DR BioGRID; 117651; 44.
DR CORUM; Q9UK96; -.
DR IntAct; Q9UK96; 9.
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; Q9UK96; -.
DR PeptideAtlas; Q9UK96; -.
DR PRIDE; Q9UK96; -.
DR ProteomicsDB; 58678; -.
DR ProteomicsDB; 84741; -. [Q9UK96-1]
DR Antibodypedia; 26292; 66 antibodies from 17 providers.
DR DNASU; 26267; -.
DR Ensembl; ENST00000432825.7; ENSP00000403802.2; ENSG00000147912.13. [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 CTD; 26267; -.
DR DisGeNET; 26267; -.
DR GeneCards; FBXO10; -.
DR HGNC; HGNC:13589; FBXO10.
DR HPA; ENSG00000147912; Tissue enhanced (skeletal).
DR MIM; 609092; gene.
DR neXtProt; NX_Q9UK96; -.
DR OpenTargets; ENSG00000147912; -.
DR PharmGKB; PA28030; -.
DR VEuPathDB; HostDB:ENSG00000147912; -.
DR eggNOG; KOG1777; Eukaryota.
DR GeneTree; ENSGT00530000063425; -.
DR HOGENOM; CLU_013632_0_0_1; -.
DR InParanoid; Q9UK96; -.
DR OMA; IFMPAWF; -.
DR OrthoDB; 281542at2759; -.
DR PhylomeDB; Q9UK96; -.
DR TreeFam; TF313602; -.
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 BioGRID-ORCS; 26267; 10 hits in 1118 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 124 other tissues.
DR ExpressionAtlas; Q9UK96; baseline and differential.
DR Genevisible; Q9UK96; HS.
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; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR Gene3D; 2.160.20.10; -; 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 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; SSF51126; SSF51126; 4.
DR SUPFAM; SSF81383; SSF81383; 1.
DR TIGRFAMs; TIGR03804; para_beta_helix; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat; 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 314..332
FT /note="Polar residues"
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 (requires 2 nucleotide substitutions; found
FT in a patient with lymphoma; partial loss of function in
FT controlling the stability of BCL2)"
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
