FBX9_MOUSE
ID FBX9_MOUSE Reviewed; 437 AA.
AC Q8BK06; Q8VDY6; Q9D349; Q9JJC5;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=F-box only protein 9;
GN Name=Fbxo9; ORFNames=MNCb-2471;
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 MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Colon, and Embryo;
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 MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORMS 2 AND 3),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-10 (ISOFORMS 2 AND 3), CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 3), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, 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 a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2
CC in a CK2-dependent manner, thereby directly regulating mTOR signaling.
CC SCF(FBXO9) recognizes and binds mTORC1-bound TTI1 and TELO2 when they
CC are phosphorylated by CK2 following growth factor deprivation, leading
CC to their degradation. In contrast, the SCF(FBXO9) does not mediate
CC ubiquitination of TTI1 and TELO2 when they are part of the mTORC2
CC complex. As a consequence, mTORC1 is inactivated to restrain cell
CC growth and protein translation, while mTORC2 is activated due to the
CC relief of feedback inhibition by mTORC1 (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase
CC complex SCF(FBXO9) composed of CUL1, SKP1, RBX1 and FBXO9. Interacts
CC with TTI1 and TELO2; when TTI1 and TELO2 are phosphorylated by CK2 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BK06-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BK06-2; Sequence=VSP_012929;
CC Name=3;
CC IsoId=Q8BK06-3; Sequence=VSP_012929, VSP_012930, VSP_012931;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95068.1; Type=Frameshift; 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; AB041585; BAA95068.1; ALT_FRAME; mRNA.
DR EMBL; AK077607; BAC36897.1; -; mRNA.
DR EMBL; AK018482; BAB31231.1; -; mRNA.
DR EMBL; BC020074; AAH20074.1; -; mRNA.
DR CCDS; CCDS52863.1; -. [Q8BK06-2]
DR CCDS; CCDS52864.1; -. [Q8BK06-1]
DR RefSeq; NP_001074959.1; NM_001081490.2. [Q8BK06-1]
DR RefSeq; NP_076094.2; NM_023605.2. [Q8BK06-2]
DR AlphaFoldDB; Q8BK06; -.
DR BioGRID; 214770; 6.
DR STRING; 10090.ENSMUSP00000001402; -.
DR iPTMnet; Q8BK06; -.
DR PhosphoSitePlus; Q8BK06; -.
DR EPD; Q8BK06; -.
DR MaxQB; Q8BK06; -.
DR PaxDb; Q8BK06; -.
DR PRIDE; Q8BK06; -.
DR ProteomicsDB; 270969; -. [Q8BK06-1]
DR ProteomicsDB; 270970; -. [Q8BK06-2]
DR ProteomicsDB; 270971; -. [Q8BK06-3]
DR Antibodypedia; 30968; 178 antibodies from 26 providers.
DR DNASU; 71538; -.
DR Ensembl; ENSMUST00000001402; ENSMUSP00000001402; ENSMUSG00000001366. [Q8BK06-1]
DR Ensembl; ENSMUST00000085311; ENSMUSP00000082419; ENSMUSG00000001366. [Q8BK06-2]
DR Ensembl; ENSMUST00000159099; ENSMUSP00000125381; ENSMUSG00000001366. [Q8BK06-3]
DR GeneID; 71538; -.
DR KEGG; mmu:71538; -.
DR UCSC; uc033jlp.1; mouse. [Q8BK06-2]
DR UCSC; uc033jlr.1; mouse. [Q8BK06-1]
DR CTD; 26268; -.
DR MGI; MGI:1918788; Fbxo9.
DR VEuPathDB; HostDB:ENSMUSG00000001366; -.
DR eggNOG; KOG2997; Eukaryota.
DR GeneTree; ENSGT00390000014256; -.
DR HOGENOM; CLU_041758_0_0_1; -.
DR InParanoid; Q8BK06; -.
DR OMA; DEFRENW; -.
DR OrthoDB; 1407789at2759; -.
DR PhylomeDB; Q8BK06; -.
DR TreeFam; TF324797; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 71538; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Fbxo9; mouse.
DR PRO; PR:Q8BK06; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BK06; protein.
DR Bgee; ENSMUSG00000001366; Expressed in medial vestibular nucleus and 257 other tissues.
DR ExpressionAtlas; Q8BK06; baseline and differential.
DR Genevisible; Q8BK06; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; IMP:MGI.
DR GO; GO:0045087; P:innate immune response; IMP:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0032006; P:regulation of TOR signaling; ISS:UniProtKB.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR045118; FBXO9/FBXO48.
DR InterPro; IPR045464; Hrt3/FBXO9_C.
DR InterPro; IPR036181; MIT_dom_sf.
DR PANTHER; PTHR12874; PTHR12874; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF19270; FBO_C; 1.
DR SUPFAM; SSF116846; SSF116846; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Phosphoprotein;
KW Reference proteome; TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..437
FT /note="F-box only protein 9"
FT /id="PRO_0000119887"
FT REPEAT 84..117
FT /note="TPR"
FT DOMAIN 175..226
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..2
FT /note="MS -> M (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_012929"
FT VAR_SEQ 180..195
FT /note="VLPMEVLMYIFRWVVS -> GVAPWLLSLRNPWTSG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012930"
FT VAR_SEQ 196..437
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012931"
FT CONFLICT 42
FT /note="F -> C (in Ref. 2; BAB31231)"
FT /evidence="ECO:0000305"
FT INIT_MET Q8BK06-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES Q8BK06-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES Q8BK06-2:10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT INIT_MET Q8BK06-3:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES Q8BK06-3:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES Q8BK06-3:10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
SQ SEQUENCE 437 AA; 50760 MW; 8950C6F658F61FCB CRC64;
MSAEAEEDCH SDADRVGDEG NESPAERDLQ AQLQMFRAQW MFELTPGVGS SHGETRPCRA
GRSSMLKAAA DTKGRQELAK EEKARELFLQ AVEEEQNGAL YEAIKFYRRA MQLVPDIEFK
ITYTRSPDGD GVGSGYIEEN EDASKMADLL SYFQQQLTLQ ESVLKLCQPE LETSQTHISV
LPMEVLMYIF RWVVSSDLDL RSLEQLSLVC RGFYICARDP EIWRLACLKV WGRSCMKLVP
YASWREMFLE RPRVRFDGVY ISKTTYIRQG EQSLDGFYRA WHQVEYYRYM RFFPDGHVMM
LTTPEEPPSI VPRLRTRNTR TDAILLGHYR LSQDADNQTK VFAVITKKKE EKPLDHKYRY
FRRVPVQEAD HSFHVGLQLC SSGHQRFNKL IWIHHSCHIT YKATGETAVS AFEIDKMYTP
LLFARVRSYT AFSERPL
