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D4ABB4

- FXL15_RAT

UniProt

D4ABB4 - FXL15_RAT

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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

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.1 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
Complete GO annotation...

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
Complete GO annotation...

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-acetylmethionine By 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 SMURF1 By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the FBXL15 family.
Contains 1 F-box domain.

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

« Hide

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 30 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

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