CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000946
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Sorting nexin-3 
Protein Synonyms/Alias
 Protein SDP3 
Gene Name
 SNX3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
14DTRRLITKPQNLNDAubiquitination[1]
54TTYEIRVKTNLPIFKubiquitination[1]
61KTNLPIFKLKESTVRubiquitination[1, 2, 3, 4, 5, 6]
95VVPPLPGKAFLRQLPubiquitination[1, 2, 4, 5, 6, 7, 8]
119DNFIEERKQGLEQFIubiquitination[1, 2, 6, 7]
128GLEQFINKVAGHPLAubiquitination[1]
158DKSYTPSKIRHA***ubiquitination[1, 7]
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] 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] 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]
 [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
Functional Description
 Phosphoinositide-binding protein required for multivesicular body formation. Specifically binds phosphatidylinositol 3-phosphate (PtdIns(P3)). Plays a role in protein transport between cellular compartments. Promotes stability and cell surface expression of epithelial sodium channel (ENAC) subunits SCNN1A and SCNN1G (By similarity). Not involved in EGFR degradation. 
Sequence Annotation
 DOMAIN 27 151 PX.
 BINDING 70 70 Phosphatidylinositol 3-phosphate (By
 BINDING 72 72 Phosphatidylinositol 3-phosphate; via
 BINDING 95 95 Phosphatidylinositol 3-phosphate (By
 BINDING 118 118 Phosphatidylinositol 3-phosphate (By
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 72 72 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Chromosomal rearrangement; Complete proteome; Direct protein sequencing; Endosome; Lipid-binding; Microphthalmia; Phosphoprotein; Protein transport; Reference proteome; Transport; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 162 AA 
Protein Sequence
MAETVADTRR LITKPQNLND AYGPPSNFLE IDVSNPQTVG VGRGRFTTYE IRVKTNLPIF 60
KLKESTVRRR YSDFEWLRSE LERESKVVVP PLPGKAFLRQ LPFRGDDGIF DDNFIEERKQ 120
GLEQFINKVA GHPLAQNERC LHMFLQDEII DKSYTPSKIR HA 162 
Gene Ontology
 GO:0005769; C:early endosome; IDA:UniProtKB.
 GO:0010008; C:endosome membrane; IDA:UniProtKB.
 GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
 GO:0007154; P:cell communication; IEA:InterPro.
 GO:0006897; P:endocytosis; TAS:ProtInc.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW. 
Interpro
 IPR001683; Phox. 
Pfam
 PF00787; PX 
SMART
 SM00312; PX 
PROSITE
 PS50195; PX 
PRINTS