CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023113
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 F-box/LRR-repeat protein 3 
Protein Synonyms/Alias
 F-box and leucine-rich repeat protein 3A; F-box/LRR-repeat protein 3A 
Gene Name
 FBXL3 
Gene Synonyms/Alias
 FBL3A; FBXL3A 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
178SKSLSSLKIDDTPVDubiquitination[1, 2, 3, 4]
190PVDDPSLKVLVANNSubiquitination[1, 2, 4]
201ANNSDTLKLLKMSSCubiquitination[2, 3, 5, 6]
204SDTLKLLKMSSCPHVubiquitination[3]
321YFGRSVSKDVLGRVGubiquitination[1, 3, 7, 8]
381SAFVEFVKMCGGRLSubiquitination[9]
414QIHWEVSKHLGRVWFubiquitination[3]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [9] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094
Functional Description
 Substrate-recognition component of the SCF(FBXL3) E3 ubiquitin ligase complex involved in circadian rhythm function. Plays a key role in the maintenance of both the speed and the robustness of the circadian clock oscillation. The SCF(FBXL3) complex mainly acts in the nucleus and mediates ubiquitination and subsequent degradation of CRY1 and CRY2. Activity of the SCF(FBXL3) complex is counteracted by the SCF(FBXL21) complex. FBXL3 probably recognizes and binds phosphorylated CRY1 and CRY2. 
Sequence Annotation
 DOMAIN 34 81 F-box.
 REPEAT 119 146 LRR 1.
 REPEAT 181 207 LRR 2.
 REPEAT 208 233 LRR 3.
 REPEAT 234 259 LRR 4.
 REPEAT 316 341 LRR 5.
 REPEAT 343 368 LRR 6.
 REPEAT 369 394 LRR 7.  
Keyword
 3D-structure; Biological rhythms; Complete proteome; Cytoplasm; Leucine-rich repeat; Nucleus; Reference proteome; Repeat; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 428 AA 
Protein Sequence
MKRGGRDSDR NSSEEGTAEK SKKLRTTNEH SQTCDWGNLL QDIILQVFKY LPLLDRAHAS 60
QVCRNWNQVF HMPDLWRCFE FELNQPATSY LKATHPELIK QIIKRHSNHL QYVSFKVDSS 120
KESAEAACDI LSQLVNCSLK TLGLISTARP SFMDLPKSHF ISALTVVFVN SKSLSSLKID 180
DTPVDDPSLK VLVANNSDTL KLLKMSSCPH VSPAGILCVA DQCHGLRELA LNYHLLSDEL 240
LLALSSEKHV RLEHLRIDVV SENPGQTHFH TIQKSSWDAF IRHSPKVNLV MYFFLYEEEF 300
DPFFRYEIPA THLYFGRSVS KDVLGRVGMT CPRLVELVVC ANGLRPLDEE LIRIAERCKN 360
LSAIGLGECE VSCSAFVEFV KMCGGRLSQL SIMEEVLIPD QKYSLEQIHW EVSKHLGRVW 420
FPDMMPTW 428 
Gene Ontology
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; NAS:UniProtKB.
 GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
 GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
 GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB. 
Interpro
 IPR001810; F-box_dom_cyclin-like. 
Pfam
  
SMART
 SM00256; FBOX 
PROSITE
 PS50181; FBOX
 PS51450; LRR 
PRINTS