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D4ABB4

- FXL15_RAT

UniProt

D4ABB4 - FXL15_RAT

Protein

F-box/LRR-repeat protein 15

Gene

Fbxl15

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 31 (01 Oct 2014)
      Sequence version 1 (20 Apr 2010)
      Previous versions | rss
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    Functioni

    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.By similarity1 Publication

    Pathwayi

    GO - Molecular functioni

    1. ubiquitin-protein transferase activity Source: Ensembl

    GO - Biological processi

    1. bone mineralization Source: UniProtKB
    2. dorsal/ventral pattern formation Source: UniProtKB
    3. G2/M transition of mitotic cell cycle Source: UniProtKB
    4. positive regulation of BMP signaling pathway Source: UniProtKB
    5. protein ubiquitination Source: UniProtKB
    6. SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    F-box/LRR-repeat protein 15
    Gene namesi
    Name:Fbxl15
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi1306444. Fbxl15.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. SCF ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 300300F-box/LRR-repeat protein 15PRO_0000410905Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiD4ABB4.

    Interactioni

    Subunit structurei

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

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 6648F-boxAdd
    BLAST
    Repeati141 – 16222LRR 1Add
    BLAST
    Repeati167 – 18822LRR 2Add
    BLAST
    Repeati194 – 21522LRR 3Add
    BLAST
    Repeati220 – 24122LRR 4Add
    BLAST
    Repeati246 – 26722LRR 5Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni113 – 269157Interaction with SMURF1By similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the FBXL15 family.Curated
    Contains 1 F-box domain.Curated
    Contains 5 LRR (leucine-rich) repeats.Curated

    Keywords - Domaini

    Leucine-rich repeat, Repeat

    Phylogenomic databases

    GeneTreeiENSGT00750000117578.
    KOiK10281.
    OMAiCHHVAES.
    OrthoDBiEOG78PVBD.
    PhylomeDBiD4ABB4.
    TreeFamiTF326769.

    Family and domain databases

    InterProiIPR001810. F-box_dom.
    [Graphical view]
    PfamiPF00646. F-box. 1 hit.
    [Graphical view]
    SUPFAMiSSF81383. SSF81383. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    D4ABB4-1 [UniParc]FASTAAdd to Basket

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    MEPPMEQSGG EQEPGAVRLL DLPWEDVLLP HVLNWVPLRQ LLRLQRVSRA    50
    FRALVQLHLA RLRRFDAAQV GPQIPRAALV RLLRDAEGLQ ELALAPCHEW 100
    LLDEDLVPVL ARNPQLRSVA LAGCGQLSRR ALGALAEGCP RLQRISLAHC 150
    DWVDGLALRG LADRCPALEE LDLTACRQLK DEAIVYLAQR RGAGLRSLSL 200
    AVNANVGDTA VQELARNCPQ LEHLDLTGCL RVGSDGVRTL AEYCPALRSL 250
    RVRHCHHVAE PSLSRLRKRG VDIDVEPPLH QALVLLQDMA GFAPFVNLQV 300
    Length:300
    Mass (Da):33,180
    Last modified:April 20, 2010 - v1
    Checksum:i43FE513A84A5E1F0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC096363 Genomic DNA. No translation available.
    CH473986 Genomic DNA. Translation: EDL94345.1.
    RefSeqiNP_001101073.1. NM_001107603.1.
    UniGeneiRn.49395.

    Genome annotation databases

    EnsembliENSRNOT00000026471; ENSRNOP00000026471; ENSRNOG00000019509.
    GeneIDi309453.
    KEGGirno:309453.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC096363 Genomic DNA. No translation available.
    CH473986 Genomic DNA. Translation: EDL94345.1 .
    RefSeqi NP_001101073.1. NM_001107603.1.
    UniGenei Rn.49395.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi D4ABB4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000026471 ; ENSRNOP00000026471 ; ENSRNOG00000019509 .
    GeneIDi 309453.
    KEGGi rno:309453.

    Organism-specific databases

    CTDi 79176.
    RGDi 1306444. Fbxl15.

    Phylogenomic databases

    GeneTreei ENSGT00750000117578.
    KOi K10281.
    OMAi CHHVAES.
    OrthoDBi EOG78PVBD.
    PhylomeDBi D4ABB4.
    TreeFami TF326769.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    NextBioi 660814.
    PROi D4ABB4.

    Family and domain databases

    InterProi IPR001810. F-box_dom.
    [Graphical view ]
    Pfami PF00646. F-box. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81383. SSF81383. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiFXL15_RAT
    AccessioniPrimary (citable) accession number: D4ABB4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 28, 2011
    Last sequence update: April 20, 2010
    Last modified: October 1, 2014
    This is version 31 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3