Full text data of FBXL20
FBXL20
(FBL2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
F-box/LRR-repeat protein 20 (F-box and leucine-rich repeat protein 20; F-box/LRR-repeat protein 2-like)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
F-box/LRR-repeat protein 20 (F-box and leucine-rich repeat protein 20; F-box/LRR-repeat protein 2-like)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Comments
Isoform Q96IG2-2 was detected.
Isoform Q96IG2-2 was detected.
UniProt
Q96IG2
ID FXL20_HUMAN Reviewed; 436 AA.
AC Q96IG2; A8K729; Q38J52;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2003, sequence version 2.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=F-box/LRR-repeat protein 20;
DE AltName: Full=F-box and leucine-rich repeat protein 20;
DE AltName: Full=F-box/LRR-repeat protein 2-like;
GN Name=FBXL20; Synonyms=FBL2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Stavropoulou A.V., Alao J.P., Lam E.W.F., Coombes R.C., Vigushin D.M.;
RT "Identification of a novel FBXL20 splice variant.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-
CC box protein)-type E3 ubiquitin ligase complex. Role in neural
CC transmission (By similarity).
CC -!- SUBUNIT: Interacts with SKP1 and CUL1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96IG2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96IG2-2; Sequence=VSP_030769;
CC -!- SIMILARITY: Contains 1 F-box domain.
CC -!- SIMILARITY: Contains 13 LRR (leucine-rich) repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; DQ223959; ABB03906.1; -; mRNA.
DR EMBL; AK291844; BAF84533.1; -; mRNA.
DR EMBL; BC007557; AAH07557.2; -; mRNA.
DR RefSeq; NP_001171835.1; NM_001184906.1.
DR RefSeq; NP_116264.2; NM_032875.2.
DR UniGene; Hs.462946; -.
DR ProteinModelPortal; Q96IG2; -.
DR SMR; Q96IG2; 28-389.
DR STRING; 9606.ENSP00000264658; -.
DR PhosphoSite; Q96IG2; -.
DR DMDM; 38503141; -.
DR PaxDb; Q96IG2; -.
DR PRIDE; Q96IG2; -.
DR DNASU; 84961; -.
DR Ensembl; ENST00000264658; ENSP00000264658; ENSG00000108306.
DR Ensembl; ENST00000394294; ENSP00000377832; ENSG00000108306.
DR Ensembl; ENST00000583610; ENSP00000462271; ENSG00000108306.
DR GeneID; 84961; -.
DR KEGG; hsa:84961; -.
DR UCSC; uc002hrt.3; human.
DR CTD; 84961; -.
DR GeneCards; GC17M037409; -.
DR HGNC; HGNC:24679; FBXL20.
DR HPA; HPA044748; -.
DR HPA; HPA050397; -.
DR MIM; 609086; gene.
DR neXtProt; NX_Q96IG2; -.
DR PharmGKB; PA134976410; -.
DR eggNOG; NOG300245; -.
DR HOGENOM; HOG000230659; -.
DR HOVERGEN; HBG051586; -.
DR InParanoid; Q96IG2; -.
DR KO; K10268; -.
DR OrthoDB; EOG7CVPXM; -.
DR PhylomeDB; Q96IG2; -.
DR GenomeRNAi; 84961; -.
DR NextBio; 75475; -.
DR PRO; PR:Q96IG2; -.
DR ArrayExpress; Q96IG2; -.
DR Bgee; Q96IG2; -.
DR CleanEx; HS_FBXL20; -.
DR Genevestigator; Q96IG2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00367; LRR_CC; 2.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Leucine-rich repeat; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1 436 F-box/LRR-repeat protein 20.
FT /FTId=PRO_0000119870.
FT DOMAIN 22 68 F-box.
FT REPEAT 74 100 LRR 1.
FT REPEAT 101 126 LRR 2.
FT REPEAT 127 152 LRR 3.
FT REPEAT 153 178 LRR 4.
FT REPEAT 179 204 LRR 5.
FT REPEAT 205 230 LRR 6.
FT REPEAT 231 256 LRR 7.
FT REPEAT 257 282 LRR 8.
FT REPEAT 283 308 LRR 9.
FT REPEAT 309 334 LRR 10.
FT REPEAT 335 363 LRR 11.
FT REPEAT 364 388 LRR 12.
FT REPEAT 389 414 LRR 13.
FT MOD_RES 417 417 Phosphothreonine.
FT MOD_RES 421 421 Phosphoserine (By similarity).
FT VAR_SEQ 134 165 Missing (in isoform 2).
FT /FTId=VSP_030769.
FT CONFLICT 17 17 S -> P (in Ref. 1; BAF84533).
FT CONFLICT 375 375 L -> F (in Ref. 1; BAF84533).
SQ SEQUENCE 436 AA; 48423 MW; 39CD04A505C8CE3E CRC64;
MRRDVNGVTK SRFEMFSNSD EAVINKKLPK ELLLRIFSFL DVVTLCRCAQ VSRAWNVLAL
DGSNWQRIDL FDFQRDIEGR VVENISKRCG GFLRKLSLRG CLGVGDNALR TFAQNCRNIE
VLNLNGCTKT TDATCTSLSK FCSKLRHLDL ASCTSITNMS LKALSEGCPL LEQLNISWCD
QVTKDGIQAL VRGCGGLKAL FLKGCTQLED EALKYIGAHC PELVTLNLQT CLQITDEGLI
TICRGCHKLQ SLCASGCSNI TDAILNALGQ NCPRLRILEV ARCSQLTDVG FTTLARNCHE
LEKMDLEECV QITDSTLIQL SIHCPRLQVL SLSHCELITD DGIRHLGNGA CAHDQLEVIE
LDNCPLITDA SLEHLKSCHS LERIELYDCQ QITRAGIKRL RTHLPNIKVH AYFAPVTPPP
SVGGSRQRFC RCCIIL
//
ID FXL20_HUMAN Reviewed; 436 AA.
AC Q96IG2; A8K729; Q38J52;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2003, sequence version 2.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=F-box/LRR-repeat protein 20;
DE AltName: Full=F-box and leucine-rich repeat protein 20;
DE AltName: Full=F-box/LRR-repeat protein 2-like;
GN Name=FBXL20; Synonyms=FBL2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Stavropoulou A.V., Alao J.P., Lam E.W.F., Coombes R.C., Vigushin D.M.;
RT "Identification of a novel FBXL20 splice variant.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-
CC box protein)-type E3 ubiquitin ligase complex. Role in neural
CC transmission (By similarity).
CC -!- SUBUNIT: Interacts with SKP1 and CUL1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96IG2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96IG2-2; Sequence=VSP_030769;
CC -!- SIMILARITY: Contains 1 F-box domain.
CC -!- SIMILARITY: Contains 13 LRR (leucine-rich) repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; DQ223959; ABB03906.1; -; mRNA.
DR EMBL; AK291844; BAF84533.1; -; mRNA.
DR EMBL; BC007557; AAH07557.2; -; mRNA.
DR RefSeq; NP_001171835.1; NM_001184906.1.
DR RefSeq; NP_116264.2; NM_032875.2.
DR UniGene; Hs.462946; -.
DR ProteinModelPortal; Q96IG2; -.
DR SMR; Q96IG2; 28-389.
DR STRING; 9606.ENSP00000264658; -.
DR PhosphoSite; Q96IG2; -.
DR DMDM; 38503141; -.
DR PaxDb; Q96IG2; -.
DR PRIDE; Q96IG2; -.
DR DNASU; 84961; -.
DR Ensembl; ENST00000264658; ENSP00000264658; ENSG00000108306.
DR Ensembl; ENST00000394294; ENSP00000377832; ENSG00000108306.
DR Ensembl; ENST00000583610; ENSP00000462271; ENSG00000108306.
DR GeneID; 84961; -.
DR KEGG; hsa:84961; -.
DR UCSC; uc002hrt.3; human.
DR CTD; 84961; -.
DR GeneCards; GC17M037409; -.
DR HGNC; HGNC:24679; FBXL20.
DR HPA; HPA044748; -.
DR HPA; HPA050397; -.
DR MIM; 609086; gene.
DR neXtProt; NX_Q96IG2; -.
DR PharmGKB; PA134976410; -.
DR eggNOG; NOG300245; -.
DR HOGENOM; HOG000230659; -.
DR HOVERGEN; HBG051586; -.
DR InParanoid; Q96IG2; -.
DR KO; K10268; -.
DR OrthoDB; EOG7CVPXM; -.
DR PhylomeDB; Q96IG2; -.
DR GenomeRNAi; 84961; -.
DR NextBio; 75475; -.
DR PRO; PR:Q96IG2; -.
DR ArrayExpress; Q96IG2; -.
DR Bgee; Q96IG2; -.
DR CleanEx; HS_FBXL20; -.
DR Genevestigator; Q96IG2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00367; LRR_CC; 2.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Leucine-rich repeat; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1 436 F-box/LRR-repeat protein 20.
FT /FTId=PRO_0000119870.
FT DOMAIN 22 68 F-box.
FT REPEAT 74 100 LRR 1.
FT REPEAT 101 126 LRR 2.
FT REPEAT 127 152 LRR 3.
FT REPEAT 153 178 LRR 4.
FT REPEAT 179 204 LRR 5.
FT REPEAT 205 230 LRR 6.
FT REPEAT 231 256 LRR 7.
FT REPEAT 257 282 LRR 8.
FT REPEAT 283 308 LRR 9.
FT REPEAT 309 334 LRR 10.
FT REPEAT 335 363 LRR 11.
FT REPEAT 364 388 LRR 12.
FT REPEAT 389 414 LRR 13.
FT MOD_RES 417 417 Phosphothreonine.
FT MOD_RES 421 421 Phosphoserine (By similarity).
FT VAR_SEQ 134 165 Missing (in isoform 2).
FT /FTId=VSP_030769.
FT CONFLICT 17 17 S -> P (in Ref. 1; BAF84533).
FT CONFLICT 375 375 L -> F (in Ref. 1; BAF84533).
SQ SEQUENCE 436 AA; 48423 MW; 39CD04A505C8CE3E CRC64;
MRRDVNGVTK SRFEMFSNSD EAVINKKLPK ELLLRIFSFL DVVTLCRCAQ VSRAWNVLAL
DGSNWQRIDL FDFQRDIEGR VVENISKRCG GFLRKLSLRG CLGVGDNALR TFAQNCRNIE
VLNLNGCTKT TDATCTSLSK FCSKLRHLDL ASCTSITNMS LKALSEGCPL LEQLNISWCD
QVTKDGIQAL VRGCGGLKAL FLKGCTQLED EALKYIGAHC PELVTLNLQT CLQITDEGLI
TICRGCHKLQ SLCASGCSNI TDAILNALGQ NCPRLRILEV ARCSQLTDVG FTTLARNCHE
LEKMDLEECV QITDSTLIQL SIHCPRLQVL SLSHCELITD DGIRHLGNGA CAHDQLEVIE
LDNCPLITDA SLEHLKSCHS LERIELYDCQ QITRAGIKRL RTHLPNIKVH AYFAPVTPPP
SVGGSRQRFC RCCIIL
//
MIM
609086
*RECORD*
*FIELD* NO
609086
*FIELD* TI
*609086 F-BOX AND LEUCINE-RICH REPEAT PROTEIN 20; FBXL20
;;FBL20;;
FBL2;;
SCRAPPER; SCR
read more*FIELD* TX
DESCRIPTION
Members of the F-box protein family, such as FBXL20, are characterized
by an approximately 40-amino acid F-box motif. SCF complexes, formed by
SKP1 (601434), cullin (see CUL1; 603134), and F-box proteins, act as
protein-ubiquitin ligases. F-box proteins interact with SKP1 through the
F box, and they interact with ubiquitination targets through other
protein interaction domains (Jin et al., 2004).
CLONING
Jin et al. (2004) reported that the FBXL20 protein contains an
N-terminal F box and 12 tandem leucine-rich repeats.
By searching databases for sequences with characteristics of neuronal
membrane-bound E3 ligases, Yao et al. (2007) identified human FBXL20,
which they called SCRAPPER. They cloned mouse Scrapper by RT-PCR of
newborn mouse brain. The deduced 438-amino acid mouse protein contains
an F box, leucine-rich repeats, and a C-terminal CAAX domain for
prenylation and membrane targeting. Western blot analysis of mouse
tissues showed highest protein levels in brain, and expression increased
with development from midgestation to adult. In situ hybridization of
mouse brain detected Scrapper enriched in CA1, CA3, and dentate gyrus
regions of hippocampus, as well as in cerebellum and olfactory bulb.
Immunofluorescence analysis detected colocalization of Scrapper with a
presynapse marker in neurons.
GENE FUNCTION
Yao et al. (2007) found that Scrapper mRNA was induced by forskolin, a
cAMP signaling activator, in mouse primary hippocampal neurons. Scrapper
directly bound and ubiquitinated Rim1 (RIMS1; 606629), a modulator of
presynaptic plasticity, in vitro.
MAPPING
Jin et al. (2004) stated that the FBXL20 gene maps to chromosome 17q21.2
and that the mouse Fbxl20 gene maps to chromosome 11D.
ANIMAL MODEL
Yao et al. (2007) found that Scr-knockout mice died stochastically after
birth and had reduced life span and smaller body size compared with
wildtype littermates. Necropsy of Scr-knockout mice was unremarkable,
except for a smaller pancreas. In neurons from Scr-knockout mice, Rim1
had a longer half-life, with significant reduction in ubiquitination and
defective Rim1 degradation, resulting in altered electrophysiologic
synaptic activity, i.e., increased frequency of miniature excitatory
postsynaptic currents. The phenotype of Scr-knockout mice was
phenocopied by Rim1 overexpression and could be rescued by reexpression
of Scrapper or knockdown of Rim1. Proteasome inhibition resulted in
upregulation of Rim1 and synaptic vesicle release probability, and these
effects were blocked by impairment of Scrapper. Yao et al. (2007)
concluded that SCRAPPER has an essential function in regulating the
proteasome-mediated degradation of RIM1 required for synaptic tuning.
*FIELD* RF
1. Jin, J.; Cardozo, T.; Lovering, R. C.; Elledge, S. J.; Pagano,
M.; Harper, J. W.: Systematic analysis and nomenclature of mammalian
F-box proteins. Genes Dev. 18: 2573-2580, 2004.
2. Yao, I.; Takagi, H.; Ageta, H.; Kahyo, T.; Sato, S.; Hatanaka,
K.; Fukuda, Y.; Chiba, T.; Morone, N.; Yuasa, S.; Inokuchi, K.; Ohtsuka,
T.; MacGregor, G. R.; Tanaka, K.; Setou, M.: SCRAPPER-dependent ubiquitination
of active zone protein RIM1 regulates synaptic vesicle release. Cell 130:
943-957, 2007. Note: Erratum: Cell 131: 190 only, 2007.
*FIELD* CN
Patricia A. Hartz - updated: 2/7/2008
*FIELD* CD
Patricia A. Hartz: 12/14/2004
*FIELD* ED
terry: 07/05/2012
wwang: 2/27/2008
mgross: 2/8/2008
terry: 2/7/2008
mgross: 12/14/2004
*RECORD*
*FIELD* NO
609086
*FIELD* TI
*609086 F-BOX AND LEUCINE-RICH REPEAT PROTEIN 20; FBXL20
;;FBL20;;
FBL2;;
SCRAPPER; SCR
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DESCRIPTION
Members of the F-box protein family, such as FBXL20, are characterized
by an approximately 40-amino acid F-box motif. SCF complexes, formed by
SKP1 (601434), cullin (see CUL1; 603134), and F-box proteins, act as
protein-ubiquitin ligases. F-box proteins interact with SKP1 through the
F box, and they interact with ubiquitination targets through other
protein interaction domains (Jin et al., 2004).
CLONING
Jin et al. (2004) reported that the FBXL20 protein contains an
N-terminal F box and 12 tandem leucine-rich repeats.
By searching databases for sequences with characteristics of neuronal
membrane-bound E3 ligases, Yao et al. (2007) identified human FBXL20,
which they called SCRAPPER. They cloned mouse Scrapper by RT-PCR of
newborn mouse brain. The deduced 438-amino acid mouse protein contains
an F box, leucine-rich repeats, and a C-terminal CAAX domain for
prenylation and membrane targeting. Western blot analysis of mouse
tissues showed highest protein levels in brain, and expression increased
with development from midgestation to adult. In situ hybridization of
mouse brain detected Scrapper enriched in CA1, CA3, and dentate gyrus
regions of hippocampus, as well as in cerebellum and olfactory bulb.
Immunofluorescence analysis detected colocalization of Scrapper with a
presynapse marker in neurons.
GENE FUNCTION
Yao et al. (2007) found that Scrapper mRNA was induced by forskolin, a
cAMP signaling activator, in mouse primary hippocampal neurons. Scrapper
directly bound and ubiquitinated Rim1 (RIMS1; 606629), a modulator of
presynaptic plasticity, in vitro.
MAPPING
Jin et al. (2004) stated that the FBXL20 gene maps to chromosome 17q21.2
and that the mouse Fbxl20 gene maps to chromosome 11D.
ANIMAL MODEL
Yao et al. (2007) found that Scr-knockout mice died stochastically after
birth and had reduced life span and smaller body size compared with
wildtype littermates. Necropsy of Scr-knockout mice was unremarkable,
except for a smaller pancreas. In neurons from Scr-knockout mice, Rim1
had a longer half-life, with significant reduction in ubiquitination and
defective Rim1 degradation, resulting in altered electrophysiologic
synaptic activity, i.e., increased frequency of miniature excitatory
postsynaptic currents. The phenotype of Scr-knockout mice was
phenocopied by Rim1 overexpression and could be rescued by reexpression
of Scrapper or knockdown of Rim1. Proteasome inhibition resulted in
upregulation of Rim1 and synaptic vesicle release probability, and these
effects were blocked by impairment of Scrapper. Yao et al. (2007)
concluded that SCRAPPER has an essential function in regulating the
proteasome-mediated degradation of RIM1 required for synaptic tuning.
*FIELD* RF
1. Jin, J.; Cardozo, T.; Lovering, R. C.; Elledge, S. J.; Pagano,
M.; Harper, J. W.: Systematic analysis and nomenclature of mammalian
F-box proteins. Genes Dev. 18: 2573-2580, 2004.
2. Yao, I.; Takagi, H.; Ageta, H.; Kahyo, T.; Sato, S.; Hatanaka,
K.; Fukuda, Y.; Chiba, T.; Morone, N.; Yuasa, S.; Inokuchi, K.; Ohtsuka,
T.; MacGregor, G. R.; Tanaka, K.; Setou, M.: SCRAPPER-dependent ubiquitination
of active zone protein RIM1 regulates synaptic vesicle release. Cell 130:
943-957, 2007. Note: Erratum: Cell 131: 190 only, 2007.
*FIELD* CN
Patricia A. Hartz - updated: 2/7/2008
*FIELD* CD
Patricia A. Hartz: 12/14/2004
*FIELD* ED
terry: 07/05/2012
wwang: 2/27/2008
mgross: 2/8/2008
terry: 2/7/2008
mgross: 12/14/2004