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Protein

F-box/LRR-repeat protein 2

Gene

Fbxl2

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

Functioni

Calcium-activated substrate recognition component of the SCF (SKP1-cullin-F-box protein) E3 ubiquitin-protein ligase complex, SCF(FBXL2), which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Unlike many F-box proteins, FBXL2 does not seem to target phosphodegron within its substrates but rather calmodulin-binding motifs and is thereby antagonized by calmodulin. This is the case for the cyclins CCND2 and CCND3 which polyubiquitination and subsequent degradation are inhibited by calmodulin. Through CCND2 and CCND3 degradation induces cell-cycle arrest in G0. SCF(FBXL2) also mediates PIK3R2 ubiquitination and proteasomal degradation thereby regulating phosphatidylinositol 3-kinase signaling and autophagy (By similarity). PCYT1A monoubiquitination by SCF(FBXL2) and subsequent degradation regulates synthesis of phosphatidylcholine, which is utilized for formation of membranes and of pulmonary surfactant (PubMed:21343341).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Calcium, Calmodulin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
F-box/LRR-repeat protein 2Curated
Alternative name(s):
F-box and leucine-rich repeat protein 2Imported
Gene namesi
Name:Fbxl2Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1919429. Fbxl2.

Subcellular locationi

  • Membrane By similarity; Lipid-anchor By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 423423F-box/LRR-repeat protein 2PRO_0000119841Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi420 – 4201S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Prenylation

Proteomic databases

EPDiQ8BH16.
MaxQBiQ8BH16.
PaxDbiQ8BH16.
PRIDEiQ8BH16.

Expressioni

Gene expression databases

BgeeiQ8BH16.
CleanExiMM_FBXL2.
ExpressionAtlasiQ8BH16. baseline and differential.
GenevisibleiQ8BH16. MM.

Interactioni

Subunit structurei

Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXL2) composed of CUL1, SKP1, RBX1 and FBXL2 (By similarity). Interacts with PCYT1A (PubMed:21343341). Interacts with calmodulin; may antagonize substrate ubiquitination by SCF(FBXL2) (PubMed:21343341). Interacts with CCND2 and CCND3. Interacts with PIK3R2; PIK3R2 is a substrate ubiquitinated by the SCF(FBXL2) complex. May interact with PIK3R1. Interacts with PTPN13 (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi215202. 3 interactions.
STRINGi10090.ENSMUSP00000035090.

Structurei

3D structure databases

ProteinModelPortaliQ8BH16.
SMRiQ8BH16. Positions 15-345.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 5547F-boxPROSITE-ProRule annotationAdd
BLAST
Repeati61 – 8727LRR 1Add
BLAST
Repeati88 – 11326LRR 2Add
BLAST
Repeati114 – 13926LRR 3Add
BLAST
Repeati140 – 16526LRR 4Add
BLAST
Repeati166 – 19126LRR 5Add
BLAST
Repeati192 – 21726LRR 6Add
BLAST
Repeati218 – 24326LRR 7Add
BLAST
Repeati244 – 26926LRR 8Add
BLAST
Repeati270 – 29526LRR 9Add
BLAST
Repeati296 – 32126LRR 10Add
BLAST
Repeati322 – 35029LRR 11Add
BLAST
Repeati351 – 37525LRR 12Add
BLAST
Repeati376 – 40126LRR 13Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni80 – 9011Interaction with Calmodulin1 PublicationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi420 – 4234CAAX motif

Domaini

The CAAX motif is a signal for the geranylgeranylation of FBXL2 and is required for its association with cell membranes and the recruitment of substrates to the active SCF(FBXL2) complex.By similarity

Sequence similaritiesi

Contains 1 F-box domain.PROSITE-ProRule annotation
Contains 13 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG4341. Eukaryota.
ENOG410XQ54. LUCA.
GeneTreeiENSGT00760000119059.
HOGENOMiHOG000230659.
HOVERGENiHBG051586.
InParanoidiQ8BH16.
KOiK10268.
OMAiSKCVELT.
OrthoDBiEOG7CVPXM.
PhylomeDBiQ8BH16.
TreeFamiTF313434.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR001810. F-box_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR006553. Leu-rich_rpt_Cys-con_subtyp.
[Graphical view]
PfamiPF12937. F-box-like. 1 hit.
PF13516. LRR_6. 4 hits.
[Graphical view]
SMARTiSM00256. FBOX. 1 hit.
SM00367. LRR_CC. 11 hits.
[Graphical view]
PROSITEiPS50181. FBOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BH16-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVFSNSDDGL INKKLPKELL LRIFSFLDIV TLCRCAQISK AWNILALDGS
60 70 80 90 100
NWQRVDLFNF QTDVEGRVVE NISKRCGGFL RKLSLRGCIG VGDSSLKTFA
110 120 130 140 150
QNCRNIEHLN LNGCTKITDS TCYSLSRFCS KLKHLDLTSC VSVTNSSLKG
160 170 180 190 200
ISEGCRNLEY LNLSWCDQIT KEGIEALVRG CRGLKALLLR GCTQLEDEAL
210 220 230 240 250
KHIQNHCHEL VSLNLQSCSR ITDDGVVQIC RGCHRLQALC LSGCSNLTDA
260 270 280 290 300
SLTALGLNCP RLQVLEAARC SHLTDAGFTL LARNCHELEK MDLEECVLIT
310 320 330 340 350
DSTLVQLSIH CPKLQALSLS HCELITDEGI LHLSSSTCGH ERLRVLELDN
360 370 380 390 400
CLLVTDASLE HLENCRGLER LELYDCQQVT RAGIKRMRAQ LPHVKVHAYF
410 420
APVTPPPAVA GSGHRLCRCC VIL
Length:423
Mass (Da):46,890
Last modified:March 1, 2003 - v1
Checksum:i597713D0407195CC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti277 – 2771G → S in BAC32036 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK039010 mRNA. Translation: BAC30203.1.
AK044693 mRNA. Translation: BAC32036.1.
AK045742 mRNA. Translation: BAC32477.1.
AK089994 mRNA. Translation: BAC41033.1.
CCDSiCCDS40790.1.
RefSeqiNP_848739.1. NM_178624.6.
UniGeneiMm.386808.

Genome annotation databases

EnsembliENSMUST00000035090; ENSMUSP00000035090; ENSMUSG00000032507.
ENSMUST00000117537; ENSMUSP00000114075; ENSMUSG00000032507.
GeneIDi72179.
KEGGimmu:72179.
UCSCiuc009rxa.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK039010 mRNA. Translation: BAC30203.1.
AK044693 mRNA. Translation: BAC32036.1.
AK045742 mRNA. Translation: BAC32477.1.
AK089994 mRNA. Translation: BAC41033.1.
CCDSiCCDS40790.1.
RefSeqiNP_848739.1. NM_178624.6.
UniGeneiMm.386808.

3D structure databases

ProteinModelPortaliQ8BH16.
SMRiQ8BH16. Positions 15-345.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215202. 3 interactions.
STRINGi10090.ENSMUSP00000035090.

Proteomic databases

EPDiQ8BH16.
MaxQBiQ8BH16.
PaxDbiQ8BH16.
PRIDEiQ8BH16.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035090; ENSMUSP00000035090; ENSMUSG00000032507.
ENSMUST00000117537; ENSMUSP00000114075; ENSMUSG00000032507.
GeneIDi72179.
KEGGimmu:72179.
UCSCiuc009rxa.1. mouse.

Organism-specific databases

CTDi25827.
MGIiMGI:1919429. Fbxl2.

Phylogenomic databases

eggNOGiKOG4341. Eukaryota.
ENOG410XQ54. LUCA.
GeneTreeiENSGT00760000119059.
HOGENOMiHOG000230659.
HOVERGENiHBG051586.
InParanoidiQ8BH16.
KOiK10268.
OMAiSKCVELT.
OrthoDBiEOG7CVPXM.
PhylomeDBiQ8BH16.
TreeFamiTF313434.

Miscellaneous databases

ChiTaRSiFbxl2. mouse.
PROiQ8BH16.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BH16.
CleanExiMM_FBXL2.
ExpressionAtlasiQ8BH16. baseline and differential.
GenevisibleiQ8BH16. MM.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR001810. F-box_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR006553. Leu-rich_rpt_Cys-con_subtyp.
[Graphical view]
PfamiPF12937. F-box-like. 1 hit.
PF13516. LRR_6. 4 hits.
[Graphical view]
SMARTiSM00256. FBOX. 1 hit.
SM00367. LRR_CC. 11 hits.
[Graphical view]
PROSITEiPS50181. FBOX. 1 hit.
[Graphical view]
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: C57BL/6J.
    Tissue: Brain, Hypothalamus and Retina.
  2. "Calmodulin antagonizes a calcium-activated SCF ubiquitin E3 ligase subunit, FBXL2, to regulate surfactant homeostasis."
    Chen B.B., Coon T.A., Glasser J.R., Mallampalli R.K.
    Mol. Cell. Biol. 31:1905-1920(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PCYT1A AND CALMODULIN, MISCELLANEOUS.

Entry informationi

Entry nameiFBXL2_MOUSE
AccessioniPrimary (citable) accession number: Q8BH16
Secondary accession number(s): Q8BXM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

May play a role in P. Aeruginosa-induced surfactant deficiency by inhibiting PCYT1A in a calcium-dependent manner.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.