FBX11_MOUSE
ID FBX11_MOUSE Reviewed; 930 AA.
AC Q7TPD1; A1A595; E9QP06; Q08EB9; Q08EC0; Q80UP0;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=F-box only protein 11;
GN Name=Fbxo11;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Fetal brain, and Mammary tumor;
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 [3]
RP CHARACTERIZATION OF JEFF MUTANT.
RX PubMed=12943368; DOI=10.1007/s10162-002-3015-9;
RA Hardisty R.E., Erven A., Logan K., Morse S., Guionaud S., Sancho-Oliver S.,
RA Hunter A.J., Brown S.D., Steel K.P.;
RT "The deaf mouse mutant Jeff (Jf) is a single gene model of otitis media.";
RL J. Assoc. Res. Otolaryngol. 4:130-138(2003).
RN [4]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, CHARACTERIZATION OF JEFF AND MUTT
RP MUTANTS, AND MUTAGENESIS OF SER-331 AND GLN-578.
RX PubMed=17035249; DOI=10.1093/hmg/ddl403;
RA Hardisty-Hughes R.E., Tateossian H., Morse S.A., Romero M.R., Middleton A.,
RA Tymowska-Lalanne Z., Hunter A.J., Cheeseman M., Brown S.D.;
RT "A mutation in the F-box gene, Fbxo11, causes otitis media in the Jeff
RT mouse.";
RL Hum. Mol. Genet. 15:3273-3279(2006).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. The SCF(FBXO11)
CC complex mediates ubiquitination and degradation of BCL6, thereby
CC playing a role in the germinal center B-cells terminal differentiation
CC toward memory B-cells and plasma cells. The SCF(FBXO11) complex also
CC mediates ubiquitination and degradation of DTL, an important step for
CC the regulation of TGF-beta signaling, cell migration and the timing of
CC the cell-cycle progression and exit. Binds to and neddylates
CC phosphorylated p53/TP53, inhibiting its transcriptional activity.
CC SCF(FBXO11) does not seem to direct ubiquitination of p53/TP53.
CC {ECO:0000250|UniProtKB:Q86XK2}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the SCF(FBXO11) complex consisting of CUL1, RBX1,
CC SKP1 and FBXO11. Interacts with p53/TP53, BCL6 and DTL (when not
CC phosphorylated). Interacts with PRMD1. {ECO:0000250|UniProtKB:Q86XK2}.
CC -!- INTERACTION:
CC Q7TPD1; P41183: Bcl6; NbExp=2; IntAct=EBI-15955324, EBI-6253762;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7TPD1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TPD1-2; Sequence=VSP_053353;
CC Name=3;
CC IsoId=Q7TPD1-3; Sequence=VSP_053353, VSP_053354;
CC -!- TISSUE SPECIFICITY: At 9.5 dpc and 10.5 dpc, expression is restricted
CC to developing heart tissue. By 11.5 dpc and 12.5 dpc, detected in liver
CC and subsequently in muscle by 13.5 dpc. At 14.5 dpc, still detected in
CC heart, liver and muscle and also in the developing secondary palate
CC including the nasal, medial and oral epithelia of the palatal shelves.
CC At 15.5 dpc and 16.5 dpc, expressed in lung, kidney, heart, liver,
CC muscle and adrenal gland. At this time, fusion of the palate shelves
CC has occurred, with expression confined to the nasal and oral epithelia.
CC At 17.5 dpc, expression in the lung is confined to bronchial epithelial
CC cells and is evident in bone marrow, skin, tissue macrophages,
CC osteoblasts, kidney, liver and spleen. At 18.5 dpc, expressed in bone
CC marrow, liver, kidney and muscle but decreases in heart and lung. At
CC this time, first detected in the middle ear epithelium. At the newborn
CC stage, expression is strong in the middle ear where it is confined to
CC mucin-secreting cells, as well as persisting in bone marrow, kidney and
CC liver. Middle ear expression persists in postnatal head tissue at 4 and
CC 13 days after birth and has declined by 21 days after birth. In the
CC adult, expression is seen in alveolar macrophages of the lung,
CC glomeruli and collecting tubules of the kidney, midbrain, heart and
CC muscle. {ECO:0000269|PubMed:17035249}.
CC -!- DEVELOPMENTAL STAGE: Not detected at 8.5 dpc. Expressed from 9.5 dpc
CC throughout development and into adulthood (at protein level).
CC {ECO:0000269|PubMed:17035249}.
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; AC087233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049946; AAH49946.1; -; mRNA.
DR EMBL; BC055343; AAH55343.1; -; mRNA.
DR EMBL; BC117884; AAI17885.1; -; mRNA.
DR EMBL; BC117885; AAI17886.1; -; mRNA.
DR EMBL; BC128479; AAI28480.1; -; mRNA.
DR CCDS; CCDS37717.1; -. [Q7TPD1-1]
DR RefSeq; NP_001074503.1; NM_001081034.2. [Q7TPD1-1]
DR RefSeq; NP_001335177.1; NM_001348248.1. [Q7TPD1-2]
DR RefSeq; XP_006524267.1; XM_006524204.3.
DR AlphaFoldDB; Q7TPD1; -.
DR SMR; Q7TPD1; -.
DR BioGRID; 230356; 6.
DR DIP; DIP-59433N; -.
DR IntAct; Q7TPD1; 1.
DR STRING; 10090.ENSMUSP00000005504; -.
DR iPTMnet; Q7TPD1; -.
DR PhosphoSitePlus; Q7TPD1; -.
DR EPD; Q7TPD1; -.
DR MaxQB; Q7TPD1; -.
DR PaxDb; Q7TPD1; -.
DR PeptideAtlas; Q7TPD1; -.
DR PRIDE; Q7TPD1; -.
DR ProteomicsDB; 272960; -. [Q7TPD1-1]
DR ProteomicsDB; 272961; -. [Q7TPD1-2]
DR ProteomicsDB; 272962; -. [Q7TPD1-3]
DR Antibodypedia; 15211; 358 antibodies from 29 providers.
DR Ensembl; ENSMUST00000005504; ENSMUSP00000005504; ENSMUSG00000005371. [Q7TPD1-1]
DR Ensembl; ENSMUST00000130379; ENSMUSP00000121206; ENSMUSG00000005371. [Q7TPD1-3]
DR Ensembl; ENSMUST00000235112; ENSMUSP00000157024; ENSMUSG00000005371. [Q7TPD1-3]
DR GeneID; 225055; -.
DR KEGG; mmu:225055; -.
DR UCSC; uc008dvf.1; mouse. [Q7TPD1-1]
DR UCSC; uc008dvg.1; mouse. [Q7TPD1-3]
DR CTD; 80204; -.
DR MGI; MGI:2147134; Fbxo11.
DR VEuPathDB; HostDB:ENSMUSG00000005371; -.
DR eggNOG; KOG1777; Eukaryota.
DR GeneTree; ENSGT00530000063425; -.
DR InParanoid; Q7TPD1; -.
DR OMA; LGYFEAN; -.
DR OrthoDB; 355502at2759; -.
DR PhylomeDB; Q7TPD1; -.
DR TreeFam; TF313602; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 225055; 7 hits in 76 CRISPR screens.
DR ChiTaRS; Fbxo11; mouse.
DR PRO; PR:Q7TPD1; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q7TPD1; protein.
DR Bgee; ENSMUSG00000005371; Expressed in animal zygote and 256 other tissues.
DR ExpressionAtlas; Q7TPD1; baseline and differential.
DR Genevisible; Q7TPD1; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IMP:CACAO.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; IPR029799; FBX11/DRE-1.
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; IPR003126; Znf_UBR.
DR PANTHER; PTHR22990:SF20; PTHR22990:SF20; 1.
DR Pfam; PF13229; Beta_helix; 2.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00722; CASH; 3.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00710; PbH1; 19.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF51126; SSF51126; 3.
DR SUPFAM; SSF81383; SSF81383; 1.
DR TIGRFAMs; TIGR03804; para_beta_helix; 4.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..930
FT /note="F-box only protein 11"
FT /id="PRO_0000119891"
FT DOMAIN 156..202
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 398..420
FT /note="PbH1 1"
FT REPEAT 421..443
FT /note="PbH1 2"
FT REPEAT 444..466
FT /note="PbH1 3"
FT REPEAT 467..489
FT /note="PbH1 4"
FT REPEAT 490..512
FT /note="PbH1 5"
FT REPEAT 513..535
FT /note="PbH1 6"
FT REPEAT 536..558
FT /note="PbH1 7"
FT REPEAT 559..581
FT /note="PbH1 8"
FT REPEAT 582..604
FT /note="PbH1 9"
FT REPEAT 605..627
FT /note="PbH1 10"
FT REPEAT 628..650
FT /note="PbH1 11"
FT REPEAT 651..673
FT /note="PbH1 12"
FT REPEAT 674..696
FT /note="PbH1 13"
FT REPEAT 697..719
FT /note="PbH1 14"
FT REPEAT 720..742
FT /note="PbH1 15"
FT REPEAT 743..765
FT /note="PbH1 16"
FT REPEAT 766..788
FT /note="PbH1 17"
FT REPEAT 789..811
FT /note="PbH1 18"
FT REPEAT 812..833
FT /note="PbH1 19"
FT ZN_FING 836..907
FT /note="UBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT REGION 1..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..75
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..87
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053353"
FT VAR_SEQ 152
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053354"
FT MUTAGEN 331
FT /note="S->L: In Mutt mutant; 13% of heterozygotes show a
FT reduced startle response to a toneburst of 24 kHz and a
FT mild craniofacial abnormality. 17% of homozygotes show
FT perinatal lethality. Surviving homozygotes demonstrate a
FT marked craniofacial abnormality and reduced hearing."
FT /evidence="ECO:0000269|PubMed:17035249"
FT MUTAGEN 578
FT /note="Q->L: In Jeff mutant; heterozygotes are deaf with
FT chronic proliferative otitis media, have a shortened snout
FT and occipital region, and are smaller than wild-type
FT littermates. Homozygotes demonstrate perinatal lethality
FT due to respiratory problems, are born with upper eyelids
FT open and show clefting of the hard or soft palate as well
FT as facial clefting."
FT /evidence="ECO:0000269|PubMed:12943368,
FT ECO:0000269|PubMed:17035249"
FT CONFLICT 251
FT /note="G -> R (in Ref. 2; AAI17886)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="V -> F (in Ref. 2; AAH49946)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 930 AA; 103728 MW; 0F644A34F1936393 CRC64;
MNSVRAANRR PRRVSRPRPV QQQQQQPPQQ PPPQPPQQQP PPQPPQQPPQ QQPPPPPQQQ
PPPPPPPPPP PPQDRNNAGE RDDVPADMVA EESGPGAQNS PYQLRRKTLL PKRTACPTKS
SMEGASTSTT ENFGHRAKRA RVSGKSQDLS AAPAEQYLQE KLPDEVVLKI FSYLLEQDLC
RAACVCKRFS ELANDPILWK RLYMEVFEYT RPMMHPEPGK FYQINPEEYE HPNPWKESFQ
QLYKGAHVKP GFAEHFYSNP ARYKGRENML YYDTIEDALG GVQEAHFDGL IFVHSGIYTD
EWIYIESPIT MIGAAPGKVA DKVIIENTRD STFVFMEGSE DAYVGYMTIR FNPDDKSAQH
HNAHHCLEIT VNCSPIIDHC IIRSTCTVGS AVCVSGQGAC PTIKHCNISD CENVGLYITD
HAQGIYEDNE ISNNALAGIW VKNHGNPIIR RNHIHHGRDV GVFTFDHGMG YFESCNIHRN
RIAGFEVKAY ANPTVVRCEI HHGQTGGIYV HEKGRGQFIE NKIYANNFAG VWITSNSDPT
IRGNSIFNGN QGGVYIFGDG RGLIEGNDIY GNALAGIQIR TNSCPIVRHN KIHDGQHGGI
YVHEKGQGVI EENEVYSNTL AGVWVTTGST PVLRRNRIHS GKQVGVYFYD NGHGVLEDND
IYNHMYSGVQ IRTGSNPKIR RNKIWGGQNG GILVYNSGLG CIEDNEIFDN AMAGVWIKTD
SNPTLRRNKI HDGRDGGICI FNGGRGLLEE NDIFRNAQAG VLISTNSHPV LRKNRIFDGF
AAGIEITNHA TATLEGNQIF NNRFGGLFLA SGVNVTMKDN KIMNNQDAIE KAVSRGQCLY
KISSYTSYPM HDFYRCHTCN TTDRNAICVN CIKKCHQGHD VEFIRHDRFF CDCGAGTLSN
PCTLAGEPTH DTDTLYDSAP PIESNTLQHN
