CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022529
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Vacuolar protein sorting-associated protein 18 homolog 
Protein Synonyms/Alias
 hVPS18 
Gene Name
 VPS18 
Gene Synonyms/Alias
 KIAA1475 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
39YVNAQLEKEVPIFTKubiquitination[1]
46KEVPIFTKQRIDFTPubiquitination[1]
276ELAFYTPKLRSAPRAubiquitination[1]
362LRDHFLEKFGPLKHMacetylation[2, 3]
412MNRFDLAKEYCRERPubiquitination[1, 4]
476LAEFLQRKLASLKPAubiquitination[1]
481QRKLASLKPAERTQAubiquitination[1]
597RDPQLFYKFSPILIRubiquitination[1, 4]
758LRKKLWLKIARHVVQubiquitination[1]
810EAICSSLKAYNHHIQubiquitination[1, 4, 5]
910GAAPPPAKGSARAKEubiquitination[1]
916AKGSARAKEAEGGAAubiquitination[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] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [4] 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]
 [5] 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] 
Functional Description
 May play a role in vesicle-mediated protein trafficking to lysosomal compartments and in membrane docking/fusion reactions of late endosomes/lysosomes. 
Sequence Annotation
 REPEAT 618 772 CHCR.
 ZN_FING 853 947 RING-type.
 MOD_RES 362 362 N6-acetyllysine.
 MOD_RES 689 689 Phosphoserine.  
Keyword
 Acetylation; Coiled coil; Complete proteome; Endosome; Lysosome; Membrane; Metal-binding; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Transport; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 973 AA 
Protein Sequence
MASILDEYEN SLSRSAVLQP GCPSVGIPHS GYVNAQLEKE VPIFTKQRID FTPSERITSL 60
VVSSNQLCMS LGKDTLLRID LGKANEPNHV ELGRKDDAKV HKMFLDHTGS HLLIALSSTE 120
VLYVNRNGQK VRPLARWKGQ LVESVGWNKA LGTESSTGPI LVGTAQGHIF EAELSASEGG 180
LFGPAPDLYF RPLYVLNEEG GPAPVCSLEA ERGPDGRSFV IATTRQRLFQ FIGRAAEGAE 240
AQGFSGLFAA YTDHPPPFRE FPSNLGYSEL AFYTPKLRSA PRAFAWMMGD GVLYGALDCG 300
RPDSLLSEER VWEYPEGVGP GASPPLAIVL TQFHFLLLLA DRVEAVCTLT GQVVLRDHFL 360
EKFGPLKHMV KDSSTGQLWA YTERAVFRYH VQREARDVWR TYLDMNRFDL AKEYCRERPD 420
CLDTVLAREA DFCFRQRRYL ESARCYALTQ SYFEEIALKF LEARQEEALA EFLQRKLASL 480
KPAERTQATL LTTWLTELYL SRLGALQGDP EALTLYRETK ECFRTFLSSP RHKEWLFASR 540
ASIHELLASH GDTEHMVYFA VIMQDYERVV AYHCQHEAYE EALAVLARHR DPQLFYKFSP 600
ILIRHIPRQL VDAWIEMGSR LDARQLIPAL VNYSQGGEVQ QVSQAIRYME FCVNVLGETE 660
QAIHNYLLSL YARGRPDSLL AYLEQAGASP HRVHYDLKYA LRLCAEHGHH RACVHVYKVL 720
ELYEEAVDLA LQVDVDLAKQ CADLPEEDEE LRKKLWLKIA RHVVQEEEDV QTAMACLASC 780
PLLKIEDVLP FFPDFVTIDH FKEAICSSLK AYNHHIQELQ REMEEATASA QRIRRDLQEL 840
RGRYGTVEPQ DKCATCDFPL LNRPFYLFLC GHMFHADCLL QAVRPGLPAY KQARLEELQR 900
KLGAAPPPAK GSARAKEAEG GAATAGPSRE QLKADLDELV AAECVYCGEL MIRSIDRPFI 960
DPQRYEEEQL SWL 973 
Gene Ontology
 GO:0005884; C:actin filament; IEA:Compara.
 GO:0005769; C:early endosome; IEA:Compara.
 GO:0030897; C:HOPS complex; IDA:UniProtKB.
 GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
 GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0007032; P:endosome organization; IDA:UniProtKB.
 GO:0006886; P:intracellular protein transport; IEA:InterPro.
 GO:0007040; P:lysosome organization; IDA:UniProtKB.
 GO:0016192; P:vesicle-mediated transport; IEA:InterPro. 
Interpro
 IPR000547; Clathrin_H-chain/VPS_repeat.
 IPR007810; Pep3_Vps18. 
Pfam
 PF00637; Clathrin
 PF05131; Pep3_Vps18 
SMART
  
PROSITE
 PS50236; CHCR
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS