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Protein

F-box/LRR-repeat protein 15

Gene

Fbxl15

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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 and bone mass maintenance. Also mediates ubiquitination of SMURF2 and WWP2 (By similarity).By similarity

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

GO - Biological processi

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
Alternative name(s):
F-box only protein 37
Gene namesi
Name:Fbxl15
Synonyms:Fbxo37
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1915681. Fbxl15.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 300300F-box/LRR-repeat protein 15PRO_0000119932Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ91W61.
MaxQBiQ91W61.
PaxDbiQ91W61.
PeptideAtlasiQ91W61.
PRIDEiQ91W61.

PTM databases

iPTMnetiQ91W61.
PhosphoSiteiQ91W61.

Expressioni

Tissue specificityi

Expressed in heart, liver, spleen, bone, muscle, brain and kidney (at protein level).1 Publication

Gene expression databases

BgeeiQ91W61.
CleanExiMM_FBXL15.
GenevisibleiQ91W61. MM.

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026256.

Structurei

3D structure databases

ProteinModelPortaliQ91W61.
SMRiQ91W61. Positions 74-252.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiENOG410IT1W. Eukaryota.
ENOG4111ZPI. LUCA.
GeneTreeiENSGT00760000119059.
HOVERGENiHBG051578.
InParanoidiQ91W61.
KOiK10281.
OMAiLKVNHCH.
OrthoDBiEOG78PVBD.
PhylomeDBiQ91W61.
TreeFamiTF326769.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR001810. F-box_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR006553. Leu-rich_rpt_Cys-con_subtyp.
[Graphical view]
PfamiPF00646. F-box. 1 hit.
PF13516. LRR_6. 1 hit.
[Graphical view]
SMARTiSM00367. LRR_CC. 6 hits.
[Graphical view]
SUPFAMiSSF81383. SSF81383. 1 hit.

Sequencei

Sequence statusi: Complete.

Q91W61-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPPMEQSGG EQEPGAVRLL DLPWEDVLLP HVLNWVPLRQ LLRLQRVSRA
60 70 80 90 100
FRALVQLHLA RLRRFDAAQV GPQIPRAALA RLLRDAEGLQ ELALAPCHEW
110 120 130 140 150
LSDEDLVPVL ARNPQLRSVA LAGCGQLSRR ALGALAEGCP RLQRLSLAHC
160 170 180 190 200
DWVDGLALRG LADRCPALEE LDLTACRQLK DEAIVYLAQR RGAGLRSLSL
210 220 230 240 250
AVNANVGDTA VQELARNCPQ LEHLDLTGCL RVGSDGVRTL AEYCPALRSL
260 270 280 290 300
RVRHCHHVAE PSLSRLRKRG VDIDVEPPLH QALVLLQDMA GFAPFVNLQV
Length:300
Mass (Da):33,125
Last modified:June 16, 2009 - v2
Checksum:iD5DD5B9428F4887C
GO

Sequence cautioni

The sequence AK003032 differs from that shown. Reason: Frameshift at position 36. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131E → D in AK003032 (PubMed:16141072).Curated
Sequence conflicti245 – 2451P → S in AK003032 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003032 mRNA. No translation available.
AK172339 mRNA. Translation: BAE42956.1.
CH466534 Genomic DNA. Translation: EDL41989.1.
BC016499 mRNA. Translation: AAH16499.1.
CCDSiCCDS38007.1.
RefSeqiNP_598455.2. NM_133694.2.
UniGeneiMm.19973.

Genome annotation databases

EnsembliENSMUST00000026256; ENSMUSP00000026256; ENSMUSG00000025226.
ENSMUST00000177667; ENSMUSP00000137489; ENSMUSG00000025226.
GeneIDi68431.
KEGGimmu:68431.
UCSCiuc008hte.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003032 mRNA. No translation available.
AK172339 mRNA. Translation: BAE42956.1.
CH466534 Genomic DNA. Translation: EDL41989.1.
BC016499 mRNA. Translation: AAH16499.1.
CCDSiCCDS38007.1.
RefSeqiNP_598455.2. NM_133694.2.
UniGeneiMm.19973.

3D structure databases

ProteinModelPortaliQ91W61.
SMRiQ91W61. Positions 74-252.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026256.

PTM databases

iPTMnetiQ91W61.
PhosphoSiteiQ91W61.

Proteomic databases

EPDiQ91W61.
MaxQBiQ91W61.
PaxDbiQ91W61.
PeptideAtlasiQ91W61.
PRIDEiQ91W61.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026256; ENSMUSP00000026256; ENSMUSG00000025226.
ENSMUST00000177667; ENSMUSP00000137489; ENSMUSG00000025226.
GeneIDi68431.
KEGGimmu:68431.
UCSCiuc008hte.1. mouse.

Organism-specific databases

CTDi79176.
MGIiMGI:1915681. Fbxl15.

Phylogenomic databases

eggNOGiENOG410IT1W. Eukaryota.
ENOG4111ZPI. LUCA.
GeneTreeiENSGT00760000119059.
HOVERGENiHBG051578.
InParanoidiQ91W61.
KOiK10281.
OMAiLKVNHCH.
OrthoDBiEOG78PVBD.
PhylomeDBiQ91W61.
TreeFamiTF326769.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiQ91W61.
SOURCEiSearch...

Gene expression databases

BgeeiQ91W61.
CleanExiMM_FBXL15.
GenevisibleiQ91W61. MM.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR001810. F-box_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR006553. Leu-rich_rpt_Cys-con_subtyp.
[Graphical view]
PfamiPF00646. F-box. 1 hit.
PF13516. LRR_6. 1 hit.
[Graphical view]
SMARTiSM00367. LRR_CC. 6 hits.
[Graphical view]
SUPFAMiSSF81383. SSF81383. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
  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. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. "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: TISSUE SPECIFICITY.

Entry informationi

Entry nameiFXL15_MOUSE
AccessioniPrimary (citable) accession number: Q91W61
Secondary accession number(s): Q3T9R4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: June 16, 2009
Last modified: July 6, 2016
This is version 111 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.