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Protein

F-box/LRR-repeat protein 2

Gene

FBXL2

Organism
Homo sapiens (Human)
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 may induce cell-cycle arrest in G0. SCF(FBXL2) may also mediate PIK3R2 ubiquitination and proteasomal degradation thereby regulating phosphatidylinositol 3-kinase signaling and indirectly autophagy (PubMed:22323446, PubMed:22020328, PubMed:23604317). PCYT1A monoubiquitination by SCF(FBXL2) and subsequent degradation may regulate synthesis of phosphatidylcholine, which is utilized for formation of membranes and of pulmonary surfactant (By similarity).By similarity3 Publications

GO - Molecular functioni

  1. phosphatidylinositol 3-kinase regulatory subunit binding Source: UniProtKB
  2. protein phosphatase binding Source: UniProtKB
  3. ubiquitin-protein transferase activity Source: Ensembl

GO - Biological processi

  1. cellular protein modification process Source: ProtInc
  2. protein monoubiquitination Source: Ensembl
  3. protein ubiquitination Source: UniProtKB
  4. proteolysis Source: ProtInc
  5. regulation of autophagy Source: UniProtKB
  6. regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  7. SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  8. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, 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
F-box protein FBL2/FBL31 PublicationImported
Gene namesi
Name:FBXL2Imported
Synonyms:FBL2Imported, FBL31 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:13598. FBXL2.

Subcellular locationi

  1. Membrane 1 Publication; Lipid-anchor 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. membrane Source: UniProtKB
  3. SCF ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi420 – 4201C → S: Loss of geranylgeranylation and association to membranes. Loss of interaction with NS5A, PIK3R1 and PIK3R2. No effect on interaction with PTPN13. 2 Publications

Organism-specific databases

PharmGKBiPA28021.

Polymorphism and mutation databases

BioMutaiFBXL2.
DMDMi145559475.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 423423F-box/LRR-repeat protein 2PRO_0000119840Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi420 – 4201S-geranylgeranyl cysteine1 Publication

Keywords - PTMi

Lipoprotein, Prenylation

Proteomic databases

MaxQBiQ9UKC9.
PaxDbiQ9UKC9.
PRIDEiQ9UKC9.

Expressioni

Tissue specificityi

Expressed in brain, heart, kidney, liver, lung, pancreas and placenta.1 Publication

Gene expression databases

BgeeiQ9UKC9.
CleanExiHS_FBXL2.
ExpressionAtlasiQ9UKC9. baseline and differential.
GenevestigatoriQ9UKC9.

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 (PubMed:10531037). Interacts with PCYT1A. Interacts with calmodulin; may antagonize substrate ubiquitination by SCF(FBXL2) (By similarity). Interacts with CCND2 and CCND3 (PubMed:22323446, PubMed:22020328). Interacts with PIK3R2; PIK3R2 is a substrate ubiquitinated by the SCF(FBXL2) complex (PubMed:23604317). May interact with PIK3R1 (PubMed:23604317). Interacts with PTPN13. Interacts with hepatitis C virus non-structural protein 5A (NS5A) and less efficiently, with hepatitis C virus non-structural protein 5B (NS5B); a reaction crucial for hepatitis C virus RNA replication (PubMed:15893726).1 PublicationBy similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP90AB1P082382EBI-724253,EBI-352572

Protein-protein interaction databases

BioGridi117355. 15 interactions.
IntActiQ9UKC9. 7 interactions.
MINTiMINT-1390736.
STRINGi9606.ENSP00000417601.

Structurei

3D structure databases

ProteinModelPortaliQ9UKC9.
SMRiQ9UKC9. Positions 15-394.
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 CalmodulinBy similarityAdd
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.1 Publication1 Publication

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

eggNOGiNOG300245.
GeneTreeiENSGT00760000119059.
HOGENOMiHOG000230659.
HOVERGENiHBG051586.
InParanoidiQ9UKC9.
KOiK10268.
OMAiHSCETIS.
OrthoDBiEOG7CVPXM.
PhylomeDBiQ9UKC9.
TreeFamiTF313434.

Family and domain databases

InterProiIPR001810. F-box_dom.
IPR006553. Leu-rich_rpt_Cys-con_subtyp.
[Graphical view]
PfamiPF00646. F-box. 1 hit.
[Graphical view]
SMARTiSM00256. FBOX. 1 hit.
SM00367. LRR_CC. 2 hits.
[Graphical view]
PROSITEiPS50181. FBOX. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UKC9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVFSNNDEGL INKKLPKELL LRIFSFLDIV TLCRCAQISK AWNILALDGS
60 70 80 90 100
NWQRIDLFNF QTDVEGRVVE NISKRCGGFL RKLSLRGCIG VGDSSLKTFA
110 120 130 140 150
QNCRNIEHLN LNGCTKITDS TCYSLSRFCS KLKHLDLTSC VSITNSSLKG
160 170 180 190 200
ISEGCRNLEY LNLSWCDQIT KDGIEALVRG CRGLKALLLR GCTQLEDEAL
210 220 230 240 250
KHIQNYCHEL VSLNLQSCSR ITDEGVVQIC RGCHRLQALC LSGCSNLTDA
260 270 280 290 300
SLTALGLNCP RLQILEAARC SHLTDAGFTL LARNCHELEK MDLEECILIT
310 320 330 340 350
DSTLIQLSIH CPKLQALSLS HCELITDDGI LHLSNSTCGH ERLRVLELDN
360 370 380 390 400
CLLITDVALE HLENCRGLER LELYDCQQVT RAGIKRMRAQ LPHVKVHAYF
410 420
APVTPPTAVA GSGQRLCRCC VIL
Length:423
Mass (Da):47,062
Last modified:April 17, 2007 - v3
Checksum:i61938E434618BA3D
GO
Isoform 2 (identifier: Q9UKC9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     132-199: Missing.

Note: No experimental confirmation available.

Show »
Length:355
Mass (Da):39,613
Checksum:iF1C3CDED0C7F0131
GO

Sequence cautioni

The sequence AAF03128.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621T → I in AAF04510 (PubMed:10531035).Curated
Sequence conflicti62 – 621T → I in AAF03128 (PubMed:10531037).Curated
Sequence conflicti62 – 621T → I in CAG33402 (Ref. 5) Curated
Sequence conflicti77 – 771G → V in AAF04510 (PubMed:10531035).Curated
Sequence conflicti81 – 811R → K in BAA91691 (PubMed:14702039).Curated
Sequence conflicti108 – 1081H → Q in BAG61062 (PubMed:14702039).Curated
Sequence conflicti174 – 1741I → W in CAB43222 (PubMed:17974005).Curated
Sequence conflicti320 – 3201S → P in CAB43222 (PubMed:17974005).Curated
Sequence conflicti342 – 3421R → G in CAG33402 (Ref. 5) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti226 – 2261V → M in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036071

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei132 – 19968Missing in isoform 2. 1 PublicationVSP_044600Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF174589 mRNA. Translation: AAF04510.1.
AF176518 mRNA. Translation: AAF03128.1. Different initiation.
AF186273 mRNA. Translation: AAD56248.1.
AK001438 mRNA. Translation: BAA91691.1.
AK298967 mRNA. Translation: BAG61062.1.
CR457121 mRNA. Translation: CAG33402.1.
AC122176 Genomic DNA. No translation available.
AC123900 Genomic DNA. No translation available.
BC031556 mRNA. Translation: AAH31556.1.
AL049953 mRNA. Translation: CAB43222.1.
CCDSiCCDS2658.1. [Q9UKC9-1]
CCDS54560.1. [Q9UKC9-2]
PIRiT08680.
RefSeqiNP_001165184.1. NM_001171713.1. [Q9UKC9-2]
NP_036289.3. NM_012157.3. [Q9UKC9-1]
UniGeneiHs.475872.

Genome annotation databases

EnsembliENST00000484457; ENSP00000417601; ENSG00000153558. [Q9UKC9-1]
ENST00000507198; ENSP00000426163; ENSG00000153558. [Q9UKC9-2]
ENST00000538892; ENSP00000441228; ENSG00000153558. [Q9UKC9-2]
GeneIDi25827.
KEGGihsa:25827.
UCSCiuc003cfp.3. human. [Q9UKC9-1]
uc021wuy.1. human.

Polymorphism and mutation databases

BioMutaiFBXL2.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF174589 mRNA. Translation: AAF04510.1.
AF176518 mRNA. Translation: AAF03128.1. Different initiation.
AF186273 mRNA. Translation: AAD56248.1.
AK001438 mRNA. Translation: BAA91691.1.
AK298967 mRNA. Translation: BAG61062.1.
CR457121 mRNA. Translation: CAG33402.1.
AC122176 Genomic DNA. No translation available.
AC123900 Genomic DNA. No translation available.
BC031556 mRNA. Translation: AAH31556.1.
AL049953 mRNA. Translation: CAB43222.1.
CCDSiCCDS2658.1. [Q9UKC9-1]
CCDS54560.1. [Q9UKC9-2]
PIRiT08680.
RefSeqiNP_001165184.1. NM_001171713.1. [Q9UKC9-2]
NP_036289.3. NM_012157.3. [Q9UKC9-1]
UniGeneiHs.475872.

3D structure databases

ProteinModelPortaliQ9UKC9.
SMRiQ9UKC9. Positions 15-394.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117355. 15 interactions.
IntActiQ9UKC9. 7 interactions.
MINTiMINT-1390736.
STRINGi9606.ENSP00000417601.

Polymorphism and mutation databases

BioMutaiFBXL2.
DMDMi145559475.

Proteomic databases

MaxQBiQ9UKC9.
PaxDbiQ9UKC9.
PRIDEiQ9UKC9.

Protocols and materials databases

DNASUi25827.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000484457; ENSP00000417601; ENSG00000153558. [Q9UKC9-1]
ENST00000507198; ENSP00000426163; ENSG00000153558. [Q9UKC9-2]
ENST00000538892; ENSP00000441228; ENSG00000153558. [Q9UKC9-2]
GeneIDi25827.
KEGGihsa:25827.
UCSCiuc003cfp.3. human. [Q9UKC9-1]
uc021wuy.1. human.

Organism-specific databases

CTDi25827.
GeneCardsiGC03P033293.
HGNCiHGNC:13598. FBXL2.
MIMi605652. gene.
neXtProtiNX_Q9UKC9.
PharmGKBiPA28021.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG300245.
GeneTreeiENSGT00760000119059.
HOGENOMiHOG000230659.
HOVERGENiHBG051586.
InParanoidiQ9UKC9.
KOiK10268.
OMAiHSCETIS.
OrthoDBiEOG7CVPXM.
PhylomeDBiQ9UKC9.
TreeFamiTF313434.

Miscellaneous databases

ChiTaRSiFBXL2. human.
GeneWikiiFBXL2.
GenomeRNAii25827.
NextBioi47109.
PROiQ9UKC9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UKC9.
CleanExiHS_FBXL2.
ExpressionAtlasiQ9UKC9. baseline and differential.
GenevestigatoriQ9UKC9.

Family and domain databases

InterProiIPR001810. F-box_dom.
IPR006553. Leu-rich_rpt_Cys-con_subtyp.
[Graphical view]
PfamiPF00646. F-box. 1 hit.
[Graphical view]
SMARTiSM00256. FBOX. 1 hit.
SM00367. LRR_CC. 2 hits.
[Graphical view]
PROSITEiPS50181. FBOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SKP1, TISSUE SPECIFICITY.
  3. "cDNA cloning and expression analysis of new members of the mammalian F-box protein family."
    Ilyin G.P., Rialland M., Pigeon C., Guguen-Guillouzo C.
    Genomics 67:40-47(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
    Tissue: Brain.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 174-423 (ISOFORM 1).
    Tissue: Brain.
  9. "Identification of FBL2 as a geranylgeranylated cellular protein required for hepatitis C virus RNA replication."
    Wang C., Gale M. Jr., Keller B.C., Huang H., Brown M.S., Goldstein J.L., Ye J.
    Mol. Cell 18:425-434(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HEPATITIS C VIRUS NS5A AND NS5B, ISOPRENYLATION AT CYS-420, MUTAGENESIS OF CYS-420, SUBCELLULAR LOCATION, DOMAIN.
  10. "F-box protein FBXL2 targets cyclin D2 for ubiquitination and degradation to inhibit leukemic cell proliferation."
    Chen B.B., Glasser J.R., Coon T.A., Zou C., Miller H.L., Fenton M., McDyer J.F., Boyiadzis M., Mallampalli R.K.
    Blood 119:3132-3141(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CCND2.
  11. "F-box protein FBXL2 exerts human lung tumor suppressor-like activity by ubiquitin-mediated degradation of cyclin D3 resulting in cell cycle arrest."
    Chen B.B., Glasser J.R., Coon T.A., Mallampalli R.K.
    Oncogene 31:2566-2579(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CCND3.
  12. "FBXL2- and PTPL1-mediated degradation of p110-free p85beta regulatory subunit controls the PI(3)K signalling cascade."
    Kuchay S., Duan S., Schenkein E., Peschiaroli A., Saraf A., Florens L., Washburn M.P., Pagano M.
    Nat. Cell Biol. 15:472-480(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION AS PART OF AN SCF COMPLEX, INTERACTION WITH PIK3R1; PIK3R2 AND PTPN13, MUTAGENESIS OF CYS-420, DOMAIN.
  13. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-226.

Entry informationi

Entry nameiFBXL2_HUMAN
AccessioniPrimary (citable) accession number: Q9UKC9
Secondary accession number(s): B4DQV0
, E9PD06, Q6IAN3, Q9NVQ8, Q9UK27, Q9UKA5, Q9Y3Y9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: April 17, 2007
Last modified: April 29, 2015
This is version 125 of the entry and version 3 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

Miscellaneous

Deletion of the F-box domain creates a dominant-negative protein that inhibits replication of hepatitis C virus RNA when overexpressed in a hepatoma cell line; this inhibition could be overcome by NS5A coexpression.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.