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D4ABB4 (FXL15_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
F-box/LRR-repeat protein 15
Gene names
Name:Fbxl15
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length300 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of SMURF1, thereby acting as a positive regulator of the BMP signaling pathway. Required for dorsal/ventral pattern formation. Also mediates ubiquitination of SMURF2 and WWP2 By similarity. Required for bone mass maintenance. Ref.3

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXL15) composed of CUL1, SKP1, RBX1 and FBXL15 By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the FBXL15 family.

Contains 1 F-box domain.

Contains 5 LRR (leucine-rich) repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 300300F-box/LRR-repeat protein 15
PRO_0000410905

Regions

Domain19 – 6648F-box
Repeat141 – 16222LRR 1
Repeat167 – 18822LRR 2
Repeat194 – 21522LRR 3
Repeat220 – 24122LRR 4
Repeat246 – 26722LRR 5
Region113 – 269157Interaction with SMURF1 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Sequences

Sequence LengthMass (Da)Tools
D4ABB4 [UniParc].

Last modified April 20, 2010. Version 1.
Checksum: 43FE513A84A5E1F0

FASTA30033,180
        10         20         30         40         50         60 
MEPPMEQSGG EQEPGAVRLL DLPWEDVLLP HVLNWVPLRQ LLRLQRVSRA FRALVQLHLA 

        70         80         90        100        110        120 
RLRRFDAAQV GPQIPRAALV RLLRDAEGLQ ELALAPCHEW LLDEDLVPVL ARNPQLRSVA 

       130        140        150        160        170        180 
LAGCGQLSRR ALGALAEGCP RLQRISLAHC DWVDGLALRG LADRCPALEE LDLTACRQLK 

       190        200        210        220        230        240 
DEAIVYLAQR RGAGLRSLSL AVNANVGDTA VQELARNCPQ LEHLDLTGCL RVGSDGVRTL 

       250        260        270        280        290        300 
AEYCPALRSL RVRHCHHVAE PSLSRLRKRG VDIDVEPPLH QALVLLQDMA GFAPFVNLQV 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"SCF(FBXL15) regulates BMP signalling by directing the degradation of HECT-type ubiquitin ligase Smurf1."
Cui Y., He S., Xing C., Lu K., Wang J., Xing G., Meng A., Jia S., He F., Zhang L.
EMBO J. 30:2675-2689(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC096363 Genomic DNA. No translation available.
CH473986 Genomic DNA. Translation: EDL94345.1.
RefSeqNP_001101073.1. NM_001107603.1.
UniGeneRn.49395.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDED4ABB4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000026471; ENSRNOP00000026471; ENSRNOG00000019509.
GeneID309453.
KEGGrno:309453.

Organism-specific databases

CTD79176.
RGD1306444. Fbxl15.

Phylogenomic databases

GeneTreeENSGT00750000117578.
KOK10281.
OMACHHVAES.
OrthoDBEOG78PVBD.
PhylomeDBD4ABB4.
TreeFamTF326769.

Enzyme and pathway databases

UniPathwayUPA00143.

Family and domain databases

InterProIPR001810. F-box_dom.
[Graphical view]
PfamPF00646. F-box. 1 hit.
[Graphical view]
SUPFAMSSF81383. SSF81383. 1 hit.
ProtoNetSearch...

Other

NextBio660814.
PROD4ABB4.

Entry information

Entry nameFXL15_RAT
AccessionPrimary (citable) accession number: D4ABB4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: April 20, 2010
Last modified: May 14, 2014
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways