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Reviewed, UniProtKB/Swiss-Prot Q9CZV8 (FXL20_MOUSE)

Last modified October 13, 2009. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    F-box/LRR-repeat protein 20
Alternative name(s):
    F-box and leucine-rich repeat protein 20
    F-box/LRR-repeat protein 2-like
Gene names
Name: Fbxl20
Synonyms: Fbl2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length436 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Isoform 3 regulates neural transmission by binding and ubiquitinating RIMS1, a modulator of presynaptic plasticity. Ref.1

Subunit structure

Interacts with SKP1A and CUL1. Ref.1

Subcellular location

Cytoplasm. Note: Isoform 3 is present at the presynaptic membrane. Ref.1

Tissue specificity

Highly expressed in brain. Ref.1

Disruption phenotype

Altered electrophysiological synaptic activity, with increased frequency of miniature excitatory postsynaptic currents. Ref.1

Sequence similarities

Contains 1 F-box domain.

Contains 12 LRR (leucine-rich) repeats.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainLeucine-rich repeat
Repeat
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processmodification-dependent protein catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding Ref.1

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Rims1Q99NE52EBI-1551033,EBI-775541
RPS27AP629881EBI-1551033,EBI-413034From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9CZV8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9CZV8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     277-436: Missing.
Isoform 3 (identifier: Q9CZV8-3)

Also known as: Scrapper;

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MRRDVNGVTKSRFE → MAPSRDRLLHFGFKAT

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 436436F-box/LRR-repeat protein 20
PRO_0000119871

Regions

Domain22 – 6847F-box
Repeat90 – 11526LRR 1
Repeat116 – 14126LRR 2
Repeat142 – 16726LRR 3
Repeat168 – 19326LRR 4
Repeat194 – 21926LRR 5
Repeat220 – 24526LRR 6
Repeat246 – 27126LRR 7
Repeat272 – 29726LRR 8
Repeat298 – 32326LRR 9
Repeat324 – 34926LRR 10
Repeat353 – 37725LRR 11
Repeat378 – 40326LRR 12

Amino acid modifications

Modified residue4171Phosphothreonine Ref.6 Ref.7
Modified residue4211Phosphoserine Ref.6

Natural variations

Alternative sequence1 – 1414MRRDV…KSRFE → MAPSRDRLLHFGFKAT in isoform 3.
VSP_030770
Alternative sequence277 – 436160Missing in isoform 2.
VSP_008968

Experimental info

Sequence conflict401L → P in BAB28039. Ref.2
Sequence conflict379 – 3813HSL → PSF in ABU95014. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 5, 2008. Version 3.
Checksum: 3218F38C02EA1BCE

FASTA43648,396
        10         20         30         40         50         60 
MRRDVNGVTK SRFEMFSNSD EAVINKKLPK ELLLRIFSFL DVVTLCRCAQ VSRAWNVLAL 

        70         80         90        100        110        120 
DGSNWQRIDL FDFQRDIEGR VVENISKRCG GFLRKLSLRG CLGVGDNALR TFAQNCRNIE 

       130        140        150        160        170        180 
VLSLNGCTKT TDATCTSLSK FCSKLRHLDL ASCTSITNMS LKALSEGCPL LEQLNISWCD 

       190        200        210        220        230        240 
QVTKDGIQAL VRGCGGLKAL FLKGCTQLED EALKYIGAHC PELVTLNLQT CLQITDEGLI 

       250        260        270        280        290        300 
TICRGCHKLQ SLCASGCSNI TDAILNALGQ NCPRLRILEV ARCSQLTDVG FTTLARNCHE 

       310        320        330        340        350        360 
LEKMDLEECV QITDSTLIQL SIHCPRLQVL SLSHCELITD DGIRHLGNGA CAHDQLEVIE 

       370        380        390        400        410        420 
LDNCPLITDA SLEHLKSCHS LERIELYDCQ QITRAGIKRL RTHLPNIKVH AYFAPVTPPP 

       430 
SVGGSRQRFC RCCIIL 

« Hide

Isoform 2.

Checksum: 982994F91A265E1E
Show »

FASTA27630,460
Isoform 3 (Scrapper).

Checksum: 305466A743427E36
Show »

FASTA43848,548

References

« Hide 'large scale' references
[1]"SCRAPPER-dependent ubiquitination of active zone protein RIM1 regulates synaptic vesicle release."
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.
Cell 130:943-957(2007) [PubMed: 17803915] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH RIMS1, SKP1 AND CUL1, DISRUPTION PHENOTYPE.
Strain: C57BL/6J.
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Cerebellum, Embryo and Lung.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Natural killer cell.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417 AND SER-421, MASS SPECTROMETRY.
Tissue: Liver.
[7]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417, MASS SPECTROMETRY.
Tissue: Macrophage.
+Additional computationally mapped references.

Cross-references

Sequence databases

EF649694 mRNA. Translation: ABU95014.1.
AK012109 mRNA. Translation: BAB28039.1. Different initiation.
AK036217 mRNA. Translation: BAC29349.1.
AK144786 mRNA. Translation: BAE26066.1. Different initiation.
AK220232 mRNA. Translation: BAD90157.1. Different initiation.
AL591205, AL591209 Genomic DNA. Translation: CAM21260.1.
AL591209, AL591205 Genomic DNA. Translation: CAM20406.1.
BC116713 mRNA. Translation: AAI16714.1.
IPIIPI00406404.
IPI00605645.
IPI00874641.
RefSeqNP_082425.1.
UniGeneMm.218350

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9CZV8. 5 interactions.
STRINGQ9CZV8.

PTM databases

PhosphoSiteQ9CZV8.

Proteomic databases

PRIDEQ9CZV8.

Genome annotation databases

EnsemblENSMUST00000075071; ENSMUSP00000074580; ENSMUSG00000020883; Mus musculus. [Genome view]
ENSMUST00000103143; ENSMUSP00000099432; ENSMUSG00000020883; Mus musculus. [Genome view]
GeneID72194.
KEGGmmu:72194.
UCSCuc007lfm.1. mouse.

Organism-specific databases

CTD72194.
MGIMGI:1919444. Fbxl20.

Phylogenomic databases

HOVERGENQ9CZV8.

Gene expression databases

ArrayExpressQ9CZV8.
BgeeQ9CZV8.
CleanExMM_FBXL20.
GenevestigatorQ9CZV8.
GermOnlineENSMUSG00000020883. Mus musculus.

Family and domain databases

InterProIPR001810. F-box.
IPR006553. Leu-rich_rpt_Cys-con_subtyp.
[Graphical view]
PfamPF00646. F-box. 1 hit.
[Graphical view]
SMARTSM00256. FBOX. 1 hit.
SM00367. LRR_CC. 2 hits.
[Graphical view]
PROSITEPS50181. FBOX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio335667.
SOURCESearch...

Entry information

Entry nameFXL20_MOUSE
AccessionPrimary (citable) accession number: Q9CZV8
Secondary accession number(s): A7YE80 expand/collapse secondary AC list , Q3UMN2, Q571F7, Q8BZ95
Entry history
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: February 5, 2008
Last modified: October 13, 2009
This is version 70 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents