FBX3_MOUSE
ID FBX3_MOUSE Reviewed; 480 AA.
AC Q9DC63; A2BHN5; A2BHN7; Q3TKB0; Q3U9C1; Q8C7I0; Q8CEJ0; Q91VI9; Q9D2J5;
AC Q9JIE4;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=F-box only protein 3;
GN Name=Fbxo3; Synonyms=Fba, Fbx3;
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 [MRNA] (ISOFORM 2).
RC TISSUE=Liver;
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 STRAIN=C57BL/6J; TISSUE=Bone marrow, Hippocampus, Liver, Lung, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Substrate recognition component of the SCF (SKP1-CUL1-F-box
CC protein)-type E3 ubiquitin ligase complex. Mediates the ubiquitination
CC of HIPK2 and probably that of EP300, leading to rapid degradation by
CC the proteasome. In the presence of PML, HIPK2 ubiquitination still
CC occurs, but degradation is prevented. PML, HIPK2 and FBXO3 may act
CC synergically to activate p53/TP53-dependent transactivation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex
CC consisting of FBXO3, SKP1, CUL1 and RBX1. Interacts with PML,
CC interaction is direct and takes place either alone or within the SCF
CC complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with PML
CC at the peripheries of nuclear bodies. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9DC63-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DC63-2; Sequence=VSP_039616, VSP_039617;
CC Name=3;
CC IsoId=Q9DC63-3; Sequence=VSP_039615, VSP_039616, VSP_039617;
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DR EMBL; AF233226; AAF67156.1; -; mRNA.
DR EMBL; AK004544; BAB23360.1; -; mRNA.
DR EMBL; AK019550; BAB31793.1; -; mRNA.
DR EMBL; AK028048; BAC25719.1; -; mRNA.
DR EMBL; AK031428; BAC27398.1; -; mRNA.
DR EMBL; AK049870; BAC33965.1; -; mRNA.
DR EMBL; AK050195; BAC34118.1; -; mRNA.
DR EMBL; AK151130; BAE30138.1; -; mRNA.
DR EMBL; AK151857; BAE30746.1; -; mRNA.
DR EMBL; AK152780; BAE31491.1; -; mRNA.
DR EMBL; AK167075; BAE39235.1; -; mRNA.
DR EMBL; BX640578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL27711.1; -; Genomic_DNA.
DR EMBL; CH466519; EDL27712.1; -; Genomic_DNA.
DR EMBL; BC010212; AAH10212.2; -; mRNA.
DR EMBL; BC058253; AAH58253.1; -; mRNA.
DR CCDS; CCDS16484.1; -. [Q9DC63-1]
DR CCDS; CCDS16485.1; -. [Q9DC63-2]
DR RefSeq; NP_065618.1; NM_020593.2. [Q9DC63-2]
DR RefSeq; NP_997598.1; NM_212433.1. [Q9DC63-1]
DR AlphaFoldDB; Q9DC63; -.
DR SMR; Q9DC63; -.
DR BioGRID; 208300; 18.
DR STRING; 10090.ENSMUSP00000028603; -.
DR iPTMnet; Q9DC63; -.
DR PhosphoSitePlus; Q9DC63; -.
DR EPD; Q9DC63; -.
DR MaxQB; Q9DC63; -.
DR PaxDb; Q9DC63; -.
DR PeptideAtlas; Q9DC63; -.
DR PRIDE; Q9DC63; -.
DR ProteomicsDB; 267351; -. [Q9DC63-1]
DR ProteomicsDB; 267352; -. [Q9DC63-2]
DR ProteomicsDB; 267353; -. [Q9DC63-3]
DR Antibodypedia; 25751; 140 antibodies from 23 providers.
DR DNASU; 57443; -.
DR Ensembl; ENSMUST00000028603; ENSMUSP00000028603; ENSMUSG00000027180. [Q9DC63-1]
DR Ensembl; ENSMUST00000102565; ENSMUSP00000099625; ENSMUSG00000027180. [Q9DC63-2]
DR Ensembl; ENSMUST00000111135; ENSMUSP00000106765; ENSMUSG00000027180. [Q9DC63-3]
DR GeneID; 57443; -.
DR KEGG; mmu:57443; -.
DR UCSC; uc008lji.1; mouse. [Q9DC63-2]
DR UCSC; uc008ljk.1; mouse. [Q9DC63-1]
DR CTD; 26273; -.
DR MGI; MGI:1929084; Fbxo3.
DR VEuPathDB; HostDB:ENSMUSG00000027180; -.
DR eggNOG; KOG4408; Eukaryota.
DR GeneTree; ENSGT00940000153571; -.
DR InParanoid; Q9DC63; -.
DR OMA; YRDLVSC; -.
DR PhylomeDB; Q9DC63; -.
DR TreeFam; TF329795; -.
DR BioGRID-ORCS; 57443; 8 hits in 73 CRISPR screens.
DR ChiTaRS; Fbxo3; mouse.
DR PRO; PR:Q9DC63; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9DC63; protein.
DR Bgee; ENSMUSG00000027180; Expressed in sternocleidomastoid and 257 other tissues.
DR ExpressionAtlas; Q9DC63; baseline and differential.
DR Genevisible; Q9DC63; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR Gene3D; 2.60.40.1470; -; 1.
DR Gene3D; 3.40.1580.10; -; 1.
DR InterPro; IPR007474; ApaG_domain.
DR InterPro; IPR036767; ApaG_sf.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR028388; FBXO3.
DR InterPro; IPR018958; Knr4/Smi1-like_dom.
DR InterPro; IPR037883; Knr4/Smi1-like_sf.
DR PANTHER; PTHR46550:SF3; PTHR46550:SF3; 1.
DR Pfam; PF04379; DUF525; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF09346; SMI1_KNR4; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00860; SMI1_KNR4; 1.
DR SUPFAM; SSF110069; SSF110069; 1.
DR SUPFAM; SSF160631; SSF160631; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS51087; APAG; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..480
FT /note="F-box only protein 3"
FT /id="PRO_0000119878"
FT DOMAIN 10..56
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT DOMAIN 278..408
FT /note="ApaG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00412"
FT REGION 419..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..455
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 36..40
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_039615"
FT VAR_SEQ 414..415
FT /note="EM -> VS (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10945468"
FT /id="VSP_039616"
FT VAR_SEQ 416..480
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10945468"
FT /id="VSP_039617"
FT CONFLICT 63
FT /note="I -> M (in Ref. 2; BAB31793)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="V -> M (in Ref. 2; BAC34118)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="E -> V (in Ref. 2; BAC25719)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="Q -> K (in Ref. 2; BAB31793)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="P -> H (in Ref. 2; BAE30746/BAE30138)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="E -> A (in Ref. 2; BAE30746/BAE30138)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 480 AA; 55227 MW; 9AD9565076A67787 CRC64;
MAAVEAETGL LTLESLPTDP LLLILSFVDY RDLINCCYVS RRLSQLSTHD PLWRRHCKKY
WLISEEEKAG KSQCWRSLFI ETYSDVGRYI DHYAAIKKAW RDLKKYLEPR CPRMVLSLKE
GAREEDLDAV EAQIGCKLPD DYRCSYRIHN GQKLVVPGLL GSMALSNHYR SEDLLDVDTA
AGGFQQRQGL KYCLPLTFCI HTGLSQYIAV EAAEGRNKNE VFYQCPDQMA RNPAAIDMFI
IGATFTDWFT SYVNNVVSGG FPIIRDQIFR YIHDPECVAT TGDITVSVST SFLPELSSVH
PPHYFFTYRI RIEMSRDALP EKACQLDSRY WRITNAKGDV EEVQGPGVVG EFPIISPGRI
YEYTSCTTFS TTSGYMEGYY TFHFLYFKDK VFNVAIPRFH MACPTFRVSI ARLEMGPDEY
EEMEEEAEEE EEEENDDSAD MDESDESDAD ENESDEGEGE ARRRRVFDVP IRRRRCSRLF
