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Protein

F-box/LRR-repeat protein 15

Gene

FBXL15

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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 WWP2.1 Publication

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 - Biological processi

  • bone mineralization Source: UniProtKB
  • dorsal/ventral pattern formation Source: UniProtKB
  • G2/M transition of mitotic cell cycle Source: UniProtKB
  • positive regulation of BMP signaling pathway Source: UniProtKB
  • protein ubiquitination Source: UniProtKB
  • 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
Alternative name(s):
F-box only protein 37
Gene namesi
Name:FBXL15
Synonyms:FBXO37
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:28155. FBXL15.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • SCF ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134928704.

Polymorphism and mutation databases

BioMutaiFBXL15.
DMDMi239938631.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 300300F-box/LRR-repeat protein 15PRO_0000119931Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9H469.
MaxQBiQ9H469.
PaxDbiQ9H469.
PRIDEiQ9H469.

PTM databases

PhosphoSiteiQ9H469.

Expressioni

Gene expression databases

BgeeiQ9H469.
CleanExiHS_FBXL15.
ExpressionAtlasiQ9H469. baseline and differential.
GenevisibleiQ9H469. HS.

Interactioni

Subunit structurei

Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXL15) composed of CUL1, SKP1, RBX1 and FBXL15.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SMURF1Q9HCE76EBI-6144096,EBI-976466
SMURF2Q9HAU43EBI-6144096,EBI-396727

Protein-protein interaction databases

BioGridi122593. 20 interactions.
IntActiQ9H469. 17 interactions.
MINTiMINT-8199055.
STRINGi9606.ENSP00000224862.

Structurei

3D structure databases

ProteinModelPortaliQ9H469.
SMRiQ9H469. 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 SMURF1Add
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.
InParanoidiQ9H469.
KOiK10281.
OMAiLKVNHCH.
OrthoDBiEOG78PVBD.
PhylomeDBiQ9H469.
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.

Q9H469-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPPMEPSGG EQEPGAVRFL DLPWEDVLLP HVLNRVPLRQ LLRLQRVSRA
60 70 80 90 100
FRSLVQLHLA GLRRFDAAQV GPQIPRAALA RLLRDAEGLQ ELALAPCHEW
110 120 130 140 150
LSDEDLVPVL ARNPQLRSVA LGGCGQLSRR ALGALAEGCP RLQRLSLAHC
160 170 180 190 200
DWVDGLALRG LADRCPALEE LDLTACRQLK DEAIVYLAQR RGAGLRSLSL
210 220 230 240 250
AVNANVGDAA VQELARNCPE LHHLDLTGCL RVGSDGVRTL AEYCPVLRSL
260 270 280 290 300
RVRHCHHVAE SSLSRLRKRG VDIDVEPPLH QALVLLQDMA GFAPFVNLQV
Length:300
Mass (Da):32,998
Last modified:June 16, 2009 - v2
Checksum:i3AF8CAFDDF75D720
GO

Sequence cautioni

The sequence AAH02912.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH36120.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAI12517.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI12518.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI12519.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI12520.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI12522.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti164 – 1641R → H in AAH36120 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL121928 Genomic DNA. Translation: CAI12517.1. Sequence problems.
AL121928 Genomic DNA. Translation: CAI12518.1. Sequence problems.
AL121928 Genomic DNA. Translation: CAI12519.1. Sequence problems.
AL121928 Genomic DNA. Translation: CAI12520.1. Sequence problems.
AL121928 Genomic DNA. Translation: CAI12522.2. Different initiation.
BC002912 mRNA. Translation: AAH02912.1. Different initiation.
BC036120 mRNA. Translation: AAH36120.1. Different initiation.
BC130566 mRNA. Translation: AAI30567.1.
CCDSiCCDS31273.1.
RefSeqiNP_077302.3. NM_024326.3.
XP_005270207.1. XM_005270150.3.
XP_005270208.1. XM_005270151.2.
UniGeneiHs.380081.

Genome annotation databases

EnsembliENST00000224862; ENSP00000224862; ENSG00000107872.
GeneIDi79176.
KEGGihsa:79176.
UCSCiuc001kvk.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL121928 Genomic DNA. Translation: CAI12517.1. Sequence problems.
AL121928 Genomic DNA. Translation: CAI12518.1. Sequence problems.
AL121928 Genomic DNA. Translation: CAI12519.1. Sequence problems.
AL121928 Genomic DNA. Translation: CAI12520.1. Sequence problems.
AL121928 Genomic DNA. Translation: CAI12522.2. Different initiation.
BC002912 mRNA. Translation: AAH02912.1. Different initiation.
BC036120 mRNA. Translation: AAH36120.1. Different initiation.
BC130566 mRNA. Translation: AAI30567.1.
CCDSiCCDS31273.1.
RefSeqiNP_077302.3. NM_024326.3.
XP_005270207.1. XM_005270150.3.
XP_005270208.1. XM_005270151.2.
UniGeneiHs.380081.

3D structure databases

ProteinModelPortaliQ9H469.
SMRiQ9H469. Positions 74-252.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122593. 20 interactions.
IntActiQ9H469. 17 interactions.
MINTiMINT-8199055.
STRINGi9606.ENSP00000224862.

PTM databases

PhosphoSiteiQ9H469.

Polymorphism and mutation databases

BioMutaiFBXL15.
DMDMi239938631.

Proteomic databases

EPDiQ9H469.
MaxQBiQ9H469.
PaxDbiQ9H469.
PRIDEiQ9H469.

Protocols and materials databases

DNASUi79176.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000224862; ENSP00000224862; ENSG00000107872.
GeneIDi79176.
KEGGihsa:79176.
UCSCiuc001kvk.2. human.

Organism-specific databases

CTDi79176.
GeneCardsiFBXL15.
H-InvDBHIX0025922.
HGNCiHGNC:28155. FBXL15.
MIMi610287. gene.
neXtProtiNX_Q9H469.
PharmGKBiPA134928704.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IT1W. Eukaryota.
ENOG4111ZPI. LUCA.
GeneTreeiENSGT00760000119059.
HOVERGENiHBG051578.
InParanoidiQ9H469.
KOiK10281.
OMAiLKVNHCH.
OrthoDBiEOG78PVBD.
PhylomeDBiQ9H469.
TreeFamiTF326769.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiFBXL15. human.
GenomeRNAii79176.
NextBioi68153.
PROiQ9H469.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H469.
CleanExiHS_FBXL15.
ExpressionAtlasiQ9H469. baseline and differential.
GenevisibleiQ9H469. HS.

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 DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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].
    Tissue: Hypothalamus and Lung carcinoma.
  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, SUBCELLULAR LOCATION, IDENTIFICATION IN A SCF PROTEIN LIGASE COMPLEX, INTERACTION WITH SMURF1; SMURF2 AND WWP2.
  4. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFXL15_HUMAN
AccessioniPrimary (citable) accession number: Q9H469
Secondary accession number(s): A1L4J8
, B1AKX8, B1AKX9, B1AKY0, B1AKY1, C9JWA4, Q0D2Q3, Q49AL7, Q5JWA5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: June 16, 2009
Last modified: May 11, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. 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.