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F-box/WD repeat-containing protein 5 (F-box and WD-40 domain-containing protein 5)

 FBXW5_MOUSE             Reviewed;         573 AA.
Q9QXW2; A2AJ36; A2AJ37; E9QMP0; Q3U368;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
28-MAR-2018, entry version 132.
RecName: Full=F-box/WD repeat-containing protein 5;
AltName: Full=F-box and WD-40 domain-containing protein 5;
Name=Fbxw5; Synonyms=Fbw5;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
INTERACTION WITH SKP1.
PubMed=10531037; DOI=10.1016/S0960-9822(00)80021-4;
Winston J.T., Koepp D.M., Zhu C., Elledge S.J., Harper J.W.;
"A family of mammalian F-box proteins.";
Curr. Biol. 9:1180-1182(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, and NOD; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
FUNCTION, AND INTERACTION WITH EPS8.
PubMed=23314863; DOI=10.1038/ncb2661;
Werner A., Disanza A., Reifenberger N., Habeck G., Becker J.,
Calabrese M., Urlaub H., Lorenz H., Schulman B., Scita G.,
Melchior F.;
"SCF(Fbxw5) mediates transient degradation of actin remodeller Eps8 to
allow proper mitotic progression.";
Nat. Cell Biol. 15:179-188(2013).
[8]
INTERACTION WITH TNFAIP8L1.
PubMed=24444419; DOI=10.1111/jnc.12643;
Ha J.Y., Kim J.S., Kang Y.H., Bok E., Kim Y.S., Son J.H.;
"Tnfaip8 l1/Oxi-beta binds to FBXW5, increasing autophagy through
activation of TSC2 in a Parkinson's disease model.";
J. Neurochem. 129:527-538(2014).
-!- FUNCTION: Substrate recognition component of both SCF (SKP1-CUL1-
F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein
ligase complexes. Substrate-specific adapter of the DCX(FBXW5) E3
ubiquitin-protein ligase complex which mediates the
polyubiquitination and subsequent degradation of TSC2. May also
act as a negative regulator of MAP3K7/TAK1 signaling in the
interleukin-1B (IL1B) signaling pathway. Substrate recognition
component of the SCF(FBXW5) E3 ubiquitin-protein ligase complex
which mediates the ubiquitination and subsequent proteasomal
degradation of SASS6 during S phase, leading to prevent centriole
reduplication (By similarity). The SCF(FBXW5) complex also
mediates ubiquitination and degradation of actin-regulator EPS8
during G2 phase, leading to the transient degradation of EPS8 and
subsequent cell shape changes required to allow mitotic
progression. {ECO:0000250, ECO:0000269|PubMed:23314863}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein
ligase complex SCF(FBXW5) composed of CUL1, SKP1, RBX1 and FBXW5.
Component of the DCX(FBXW5) E3 ubiquitin ligase complex, at least
composed of (CUL4A or CUL4B), DDB1, FBXW5 and RBX1. Interacts with
CDC20, TSC1, TSC2 and SASS6 (By similarity). Interacts with EPS8.
Interacts with TNFAIP8L1; TNFAIP8L1 competes with TSC2 to bind
FBXW5 increasing TSC2 stability by preventing its ubiquitination.
{ECO:0000250, ECO:0000269|PubMed:10531037,
ECO:0000269|PubMed:23314863, ECO:0000269|PubMed:24444419}.
-!- INTERACTION:
Q9WTX5:Skp1; NbExp=2; IntAct=EBI-16031930, EBI-1202363;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q969U6}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9QXW2-1; Sequence=Displayed;
Name=2;
IsoId=Q9QXW2-2; Sequence=VSP_042293, VSP_042294;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed in adult and embryonal
tissues. {ECO:0000269|PubMed:10531037}.
-!- DOMAIN: The F-box domain mediates interaction with components of
SCF (SKP1-CUL1-F-box protein) complexes, while WD repeats mediate
interaction with components of DCX (DDB1-CUL4-X-box) complexes.
{ECO:0000250}.
-!- DOMAIN: The D-box (destruction box) mediate the interaction with
APC proteins, and acts as a recognition signal for degradation via
the ubiquitin-proteasome pathway. {ECO:0000250}.
-!- PTM: Phosphorylated at Ser-151 by PLK4 during the G1/S transition,
leading to inhibit its ability to ubiquitinate SASS6.
{ECO:0000250}.
-!- PTM: Ubiquitinated and degraded by the APC/C complex during
mitosis and G1 phase. {ECO:0000250}.
-!- SIMILARITY: Belongs to the FBXW5 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAM25630.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF176520; AAF09130.1; -; mRNA.
EMBL; AK019715; BAB31841.1; -; mRNA.
EMBL; AK154911; BAE32921.1; -; mRNA.
EMBL; AL732557; CAM25629.1; -; Genomic_DNA.
EMBL; AL732557; CAM25630.1; ALT_SEQ; Genomic_DNA.
EMBL; CH466542; EDL08255.1; -; Genomic_DNA.
EMBL; BC010776; AAH10776.1; -; mRNA.
CCDS; CCDS15778.1; -. [Q9QXW2-1]
RefSeq; NP_038936.1; NM_013908.4. [Q9QXW2-1]
UniGene; Mm.29170; -.
ProteinModelPortal; Q9QXW2; -.
BioGrid; 205976; 4.
DIP; DIP-60700N; -.
IntAct; Q9QXW2; 1.
STRING; 10090.ENSMUSP00000015239; -.
iPTMnet; Q9QXW2; -.
PhosphoSitePlus; Q9QXW2; -.
PaxDb; Q9QXW2; -.
PRIDE; Q9QXW2; -.
Ensembl; ENSMUST00000015239; ENSMUSP00000015239; ENSMUSG00000015095. [Q9QXW2-1]
GeneID; 30839; -.
KEGG; mmu:30839; -.
UCSC; uc008isj.1; mouse. [Q9QXW2-1]
UCSC; uc008isk.1; mouse. [Q9QXW2-2]
CTD; 54461; -.
MGI; MGI:1354731; Fbxw5.
eggNOG; ENOG410IEAX; Eukaryota.
eggNOG; ENOG410XTK0; LUCA.
GeneTree; ENSGT00730000111276; -.
HOGENOM; HOG000231549; -.
HOVERGEN; HBG051595; -.
InParanoid; Q9QXW2; -.
KO; K10263; -.
OMA; PHQIGFK; -.
OrthoDB; EOG091G04E0; -.
TreeFam; TF324320; -.
Reactome; R-MMU-8951664; Neddylation.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
ChiTaRS; Fbxw5; mouse.
PRO; PR:Q9QXW2; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000015095; -.
CleanEx; MM_FBXW5; -.
ExpressionAtlas; Q9QXW2; baseline and differential.
Genevisible; Q9QXW2; MM.
GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0010824; P:regulation of centrosome duplication; ISS:UniProtKB.
GO; GO:0007088; P:regulation of mitotic nuclear division; IDA:UniProtKB.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR036047; F-box-like_dom_sf.
InterPro; IPR001810; F-box_dom.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF12937; F-box-like; 1.
Pfam; PF00400; WD40; 2.
SMART; SM00256; FBOX; 1.
SMART; SM00320; WD40; 3.
SUPFAM; SSF50978; SSF50978; 2.
SUPFAM; SSF81383; SSF81383; 2.
PROSITE; PS50181; FBOX; 1.
PROSITE; PS50082; WD_REPEATS_2; 2.
PROSITE; PS50294; WD_REPEATS_REGION; 2.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Phosphoprotein;
Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway;
WD repeat.
CHAIN 1 573 F-box/WD repeat-containing protein 5.
/FTId=PRO_0000050993.
DOMAIN 3 49 F-box. {ECO:0000255|PROSITE-
ProRule:PRU00080}.
REPEAT 90 129 WD 1.
REPEAT 470 509 WD 2.
REPEAT 511 551 WD 3.
MOTIF 308 316 D-box.
MOD_RES 151 151 Phosphoserine; by PLK4.
{ECO:0000250|UniProtKB:Q969U6}.
VAR_SEQ 1 1 M -> MLSAVEFSGGQLVGLARTAMSGTPDYQSLPGVGDEE
AWVQSRHWWVSGPSGQNVTM (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_042293.
VAR_SEQ 530 573 LTASDDATIKAWRSPRIVRVLQAPRPRPRPRPRPFFSWFAS
HRR -> PDSQRRCHYQSLAFTTHCSCSAGSTPSPPPSPPP
LLLLVCQP (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_042294.
SEQUENCE 573 AA; 64646 MW; B71B3B207D3091B1 CRC64;
MDEGGLPLLP DSLVYQIFLS LGPADVLAAG LVCRQWQAVS RDEFLWKEQF YRYYQVARDV
PRHPAATSWY EEFRRLYDMV PCVEVQTLKE HTDQVLHLSF SHSGYQFASC SKDCTVKIWN
NDLTISLLHS ADMRPYNWSY TQFSQFNQDD SLLLASGVFL GPHNSSSGEI AVISLDSFAL
LSRVRNKPYD VFGCWLTETS LISGNLHRIG DITSCSVLWL NNAFQDVESE NVNVVKRLFK
IQNLNASTIR TVMVADCSRF DSPDLLLDAS DQAGLPCRVF DLGGDTEEEA TDPGLHTSGS
DHVKKGLRRV FDSVLDGHGQ LSDCALETKV AELLAQGHTK PPECNDADTR NKYLIFTTGC
LTYSPHQIGI KQILPHQMTT AGPVLGEGRG SDAFFDALDH VIDVHGHIIG MGLSPDNRYL
YVNSRAWPPG SVVADPMQPP PIAEEIDLLV FDLKTMREVK RALRAHRAYT PNDECFFIFL
DVSRDFVASG AEDRHGYIWD RHYNICLAKL RHEDVVNSVA FSPQEQELLL TASDDATIKA
WRSPRIVRVL QAPRPRPRPR PRPFFSWFAS HRR


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