Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01283
Entry Name
UniProt Accession
Theoretical PI
7.4
Molecular Weight
47061.62
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
F-box/LRR-repeat protein 2
Protein Synonyms/Alias
F-box and leucine-rich repeat protein 2; F-box protein FBL2/FBL3;
Gene Name
FBXL2
Gene Synonyms/Alias
FBL2; FBL3;
Created Date
21-NOV-2003
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
420
Canonical
GQRLCRCCVIL****
[1]
S-Geranylgeranylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Wang C, Gale M Jr, Keller BC, Huang H, Brown MS, Goldstein JL, Ye J.Identification of FBL2 as a geranylgeranylated cellular protein required forhepatitis C virus RNA replication. Mol Cell. 2005 May 13;18(4):425-34. PubMedPMID: 15893726.[PMID:15893726]
Functional Description
Calcium-activated substrate recognition component of a SCF (SKP1-cullin-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Unlike many F-box proteins, FBXL2 doesn't seem to target phosphodegron within its substrates but rather calmodulin-binding motifs. Targets PCYT1A for its monoubiquitination and degradation, this is antagonized by calmodulin (By similarity). Targets the cyclins CCND2 and CCND3 for polyubiquitination and degradation, leading to cell-cycle arrest in G(0), also antagonized by calmodulin. Binds to hepatitis C virus non-structural protein 5A (NS5A) in a reaction crucial for hepatitis C virus RNA replication.
Sequence Annotation
Domain: 9 55 F-box.
Region: 80 90 Interaction with Calmodulin.
Motif: 420 423 CAAX motif.
Protein Length
423 AA.
Protein Sequence
(Canonical)
MVFSNNDEGL INKKLPKELL LRIFSFLDIV TLCRCAQISK AWNILALDGS NWQRIDLFNF  60
QTDVEGRVVE NISKRCGGFL RKLSLRGCIG VGDSSLKTFA QNCRNIEHLN LNGCTKITDS  120
TCYSLSRFCS KLKHLDLTSC VSITNSSLKG ISEGCRNLEY LNLSWCDQIT KDGIEALVRG  180
CRGLKALLLR GCTQLEDEAL KHIQNYCHEL VSLNLQSCSR ITDEGVVQIC RGCHRLQALC  240
LSGCSNLTDA SLTALGLNCP RLQILEAARC SHLTDAGFTL LARNCHELEK MDLEECILIT  300
DSTLIQLSIH CPKLQALSLS HCELITDDGI LHLSNSTCGH ERLRVLELDN CLLITDVALE  360
HLENCRGLER LELYDCQQVT RAGIKRMRAQ LPHVKVHAYF APVTPPTAVA GSGQRLCRCC  420
VIL                                                                423
FASTA
(Canonical)
>LipidDB-9606-01283|Q9UKC9
MVFSNNDEGLINKKLPKELLLRIFSFLDIVTLCRCAQISKAWNILALDGSNWQRIDLFNF
QTDVEGRVVENISKRCGGFLRKLSLRGCIGVGDSSLKTFAQNCRNIEHLNLNGCTKITDS
TCYSLSRFCSKLKHLDLTSCVSITNSSLKGISEGCRNLEYLNLSWCDQITKDGIEALVRG
CRGLKALLLRGCTQLEDEALKHIQNYCHELVSLNLQSCSRITDEGVVQICRGCHRLQALC
LSGCSNLTDASLTALGLNCPRLQILEAARCSHLTDAGFTLLARNCHELEKMDLEECILIT
DSTLIQLSIHCPKLQALSLSHCELITDDGILHLSNSTCGHERLRVLELDNCLLITDVALE
HLENCRGLERLELYDCQQVTRAGIKRMRAQLPHVKVHAYFAPVTPPTAVAGSGQRLCRCC
VIL
Gene Ontology
GO:0005737; C:cytoplasm; TAS:ProtInc
GO:0016020; C:membrane; IDA:UniProtKB
GO:0004842; F:ubiquitin-protein transferase activity; TAS:ProtInc
GO:0006464; P:cellular protein modification process; TAS:ProtInc
GO:0006513; P:protein monoubiquitination; IEA:Ensembl
GO:0006508; P:proteolysis; TAS:ProtInc
GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl
GO:0016032; P:viral process; IEA:UniProtKB-KW
Interpro
InterPro; IPR001810; F-box_dom
InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp
Pfam
Pfam; PF00646; F-box;
SMART
SMART; SM00256; FBOX;
SMART; SM00367; LRR_CC;
PROSITE
PROSITE; PS50181; FBOX;
PRINTS