CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019295
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Vacuolar-sorting protein SNF8 
Protein Synonyms/Alias
 ELL-associated protein of 30 kDa; ESCRT-II complex subunit VPS22; hVps22 
Gene Name
 SNF8 
Gene Synonyms/Alias
 EAP30 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
14GAGAIAKKKLAEAKYubiquitination[1]
38DQLAQMSKQLDMFKTubiquitination[2, 3, 4, 5]
44SKQLDMFKTNLEEFAubiquitination[1, 3]
53NLEEFASKHKQEIRKubiquitination[1, 3]
130ELHQQVLKGRGKFAQubiquitination[1, 3]
134QVLKGRGKFAQDVSQubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9]
203SEIKASLKWETERARubiquitination[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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [9] 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
 Component of the endosomal sorting complex required for transport II (ESCRT-II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. The ESCRT-II complex may also play a role in transcription regulation by participating in derepression of transcription by RNA polymerase II, possibly via its interaction with ELL. Required for degradation of both endocytosed EGF and EGFR, but not for the EGFR ligand-mediated internalization. It is also required for the degradation of CXCR4. 
Sequence Annotation
  
Keyword
 3D-structure; Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Endosome; Membrane; Nucleus; Protein transport; Reference proteome; Transcription; Transcription regulation; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 258 AA 
Protein Sequence
MHRRGVGAGA IAKKKLAEAK YKERGTVLAE DQLAQMSKQL DMFKTNLEEF ASKHKQEIRK 60
NPEFRVQFQD MCATIGVDPL ASGKGFWSEM LGVGDFYYEL GVQIIEVCLA LKHRNGGLIT 120
LEELHQQVLK GRGKFAQDVS QDDLIRAIKK LKALGTGFGI IPVGGTYLIQ SVPAELNMDH 180
TVVLQLAEKN GYVTVSEIKA SLKWETERAR QVLEHLLKEG LAWLDLQAPG EAHYWLPALF 240
TDLYSQEITA EEAREALP 258 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
 GO:0005667; C:transcription factor complex; IDA:MGI.
 GO:0008134; F:transcription factor binding; IDA:MGI.
 GO:0016044; P:cellular membrane organization; TAS:Reactome.
 GO:0016197; P:endosomal transport; TAS:Reactome.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR007286; EAP30.
 IPR016689; ESCRT-2_cplx_Snf8.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF04157; EAP30 
SMART
  
PROSITE
  
PRINTS