CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015254
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 F-box/LRR-repeat protein 19 
Protein Synonyms/Alias
 F-box and leucine-rich repeat protein 19 
Gene Name
 FBXL19 
Gene Synonyms/Alias
 FBL19 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
470RMDLSRRKSLTPPMLubiquitination[1]
498SWTGVSKKQLMWLLNubiquitination[2]
546LRWIEDVKDSQLRELubiquitination[1, 2]
561LLPPPDTKPGQTESRubiquitination[1]
688PFRCPEEKLLLKDS*ubiquitination[1]
692PEEKLLLKDS*****ubiquitination[1]
Reference
 [1] 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]
 [2] 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] 
Functional Description
 Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex (By similarity). 
Sequence Annotation
 DOMAIN 418 464 F-box.
 REPEAT 492 517 LRR 1.
 REPEAT 518 541 LRR 2.
 REPEAT 581 606 LRR 3.
 REPEAT 607 636 LRR 4.
 REPEAT 637 661 LRR 5.
 REPEAT 662 694 LRR 6.
 ZN_FING 32 78 CXXC-type.
 ZN_FING 85 151 PHD-type.  
Keyword
 Alternative splicing; Complete proteome; Leucine-rich repeat; Metal-binding; Reference proteome; Repeat; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 694 AA 
Protein Sequence
MGMKVPGKGE SGPSALLTPP MSSSSRGPGA GARRRRTRCR RCRACVRTEC GDCHFCRDMK 60
KFGGPGRMKQ SCLLRQCTAP VLPHTAVCLL CGEAGKEDTV EGEEEKFGLS LMECTICNEI 120
VHPGCLKMGK AEGVINAEIP NCWECPRCTQ EGRTSKDSGE GPGRRRADNG EEGASLGSGW 180
KLTEEPPLPP PPPRRKGPLP AGPPPEDVPG PPKRKEREAG NEPPTPRKKV KGGRERHLKK 240
VGGDACLLRG SDPGGPGLLP PRVLNPSQAF SSCHPGLPPE NWEKPKPPLA SAEGPAVPSP 300
SPQREKLERF KRMCQLLERV PDTSSSSSDS DSDSDSSGTS LSEDEAPGEA RNGRRPARGS 360
SGEKENRGGR RAVRPGSGGP LLSWPLGPAP PPRPPQLERH VVRPPPRSPE PDTLPLAAGS 420
DHPLPRAAWL RVFQHLGPRE LCICMRVCRT WSRWCYDKRL WPRMDLSRRK SLTPPMLSGV 480
VRRQPRALDL SWTGVSKKQL MWLLNRLQGL QELVLSGCSW LSVSALGSAP LPALRLLDLR 540
WIEDVKDSQL RELLLPPPDT KPGQTESRGR LQGVAELRLA GLELTDASLR LLLRHAPQLS 600
ALDLSHCAHV GDPSVHLLTA PTSPLRETLV HLNLAGCHRL TDHCLPLFRR CPRLRRLDLR 660
SCRQLSPEAC ARLAAAGPPG PFRCPEEKLL LKDS 694 
Gene Ontology
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR001810; F-box_dom_cyclin-like.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR002857; Znf_CXXC.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00646; F-box
 PF02008; zf-CXXC 
SMART
 SM00256; FBOX
 SM00249; PHD 
PROSITE
 PS50181; FBOX
 PS51058; ZF_CXXC
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS