CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012468
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Sorting nexin-17 
Protein Synonyms/Alias
  
Gene Name
 SNX17 
Gene Synonyms/Alias
 KIAA0064 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
63LPAFPPKKLFSLTPAubiquitination[1, 2, 3]
81QRREQLEKYMQAVRQubiquitination[2]
168SLFLVREKEDGAFSFubiquitination[2]
178GAFSFVRKLQEFELPubiquitination[2, 4]
203EYKIVLRKSYWDSAYubiquitination[2]
241RGWILVTKEQHRQLKubiquitination[2]
248KEQHRQLKSLQEKVSubiquitination[2]
356AFEYLMSKDRLQWVTubiquitination[2, 5]
414SDSQQAVKSPPLLESubiquitination[2]
431ATRESMVKLSSKLSAubiquitination[2]
435SMVKLSSKLSAVSLRubiquitination[2, 6]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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] 
Functional Description
 Critical regulator of endosomal recycling of numerous receptors, channels, and other transmembrane proteins. Binds to NPxY sequences in the cytoplasmic tails of target cargos. Plays a role in the sorting of endocytosed LRP1 and APP, and prevents their degradation. Required for maintenance of normal cell surface levels of APP and LRP1. Recycles internalized integrins ITGB1, ITGB5 and their associated alpha subunits, preventing them from lysosomal degradation. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)). 
Sequence Annotation
 DOMAIN 1 109 PX.
 DOMAIN 115 206 Ras-associating.
 REGION 115 432 FERM-like.
 REGION 270 432 PTB-like F3 module.
 BINDING 36 36 Phosphatidylinositol 3-phosphate (By
 BINDING 38 38 Phosphatidylinositol 3-phosphate; via
 BINDING 62 62 Phosphatidylinositol 3-phosphate (By
 BINDING 75 75 Phosphatidylinositol 3-phosphate (By
 MOD_RES 334 334 Phosphothreonine (By similarity).
 MOD_RES 407 407 Phosphoserine.
 MOD_RES 409 409 Phosphoserine (By similarity).
 MOD_RES 415 415 Phosphoserine.
 MOD_RES 421 421 Phosphoserine.
 MOD_RES 437 437 Phosphoserine.
 MOD_RES 440 440 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Endosome; Lipid-binding; Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 470 AA 
Protein Sequence
MHFSIPETES RSGDSGGSAY VAYNIHVNGV LHCRVRYSQL LGLHEQLRKE YGANVLPAFP 60
PKKLFSLTPA EVEQRREQLE KYMQAVRQDP LLGSSETFNS FLRRAQQETQ QVPTEEVSLE 120
VLLSNGQKVL VNVLTSDQTE DVLEAVAAKL DLPDDLIGYF SLFLVREKED GAFSFVRKLQ 180
EFELPYVSVT SLRSQEYKIV LRKSYWDSAY DDDVMENRVG LNLLYAQTVS DIERGWILVT 240
KEQHRQLKSL QEKVSKKEFL RLAQTLRHYG YLRFDACVAD FPEKDCPVVV SAGNSELSLQ 300
LRLPGQQLRE GSFRVTRMRC WRVTSSVPLP SGSTSSPGRG RGEVRLELAF EYLMSKDRLQ 360
WVTITSPQAI MMSICLQSMV DELMVKKSGG SIRKMLRRRV GGTLRRSDSQ QAVKSPPLLE 420
SPDATRESMV KLSSKLSAVS LRGIGSPSTD ASASDVHGNF AFEGIGDEDL 470 
Gene Ontology
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:UniProtKB.
 GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005769; C:early endosome; IDA:UniProtKB.
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0016020; C:membrane; NAS:UniProtKB.
 GO:0050750; F:low-density lipoprotein particle receptor binding; IDA:UniProtKB.
 GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
 GO:0006707; P:cholesterol catabolic process; IC:UniProtKB.
 GO:0016197; P:endosomal transport; NAS:UniProtKB.
 GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
 GO:0006898; P:receptor-mediated endocytosis; IEA:Compara.
 GO:0030100; P:regulation of endocytosis; NAS:UniProtKB.
 GO:0007165; P:signal transduction; IEA:InterPro. 
Interpro
 IPR001683; Phox.
 IPR000159; Ras-assoc. 
Pfam
 PF00787; PX 
SMART
 SM00312; PX 
PROSITE
 PS50195; PX
 PS50200; RA 
PRINTS