CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000308
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Secretory carrier-associated membrane protein 3 
Protein Synonyms/Alias
 Secretory carrier membrane protein 3 
Gene Name
 SCAMP3 
Gene Synonyms/Alias
 C1orf3; PROPIN1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
74PSLQPSRKLSPTEPKubiquitination[1, 2, 3, 4, 5, 6, 7]
81KLSPTEPKNYGSYSTubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9]
101AATAELLKKQEELNRubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12]
102ATAELLKKQEELNRKubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 12]
109KQEELNRKAEELDRRubiquitination[2, 3]
313RTGASFQKAQQEFAAubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 13]
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] 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]
 [3] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [4] 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]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [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] 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]
 [8] 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]
 [9] 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]
 [10] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [11] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [12] 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]
 [13] 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
Functional Description
 Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface. 
Sequence Annotation
 MOD_RES 32 32 Phosphoserine.
 MOD_RES 41 41 Phosphotyrosine.
 MOD_RES 53 53 Phosphotyrosine.
 MOD_RES 76 76 Phosphoserine.
 MOD_RES 85 85 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Membrane; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Transmembrane; Transmembrane helix; Transport; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 347 AA 
Protein Sequence
MAQSRDGGNP FAEPSELDNP FQDPAVIQHR PSRQYATLDV YNPFETREPP PAYEPPAPAP 60
LPPPSAPSLQ PSRKLSPTEP KNYGSYSTQA SAAAATAELL KKQEELNRKA EELDRREREL 120
QHAALGGTAT RQNNWPPLPS FCPVQPCFFQ DISMEIPQEF QKTVSTMYYL WMCSTLALLL 180
NFLACLASFC VETNNGAGFG LSILWVLLFT PCSFVCWYRP MYKAFRSDSS FNFFVFFFIF 240
FVQDVLFVLQ AIGIPGWGFS GWISALVVPK GNTAVSVLML LVALLFTGIA VLGIVMLKRI 300
HSLYRRTGAS FQKAQQEFAA GVFSNPAVRT AAANAAAGAA ENAFRAP 347 
Gene Ontology
 GO:0000139; C:Golgi membrane; IEA:Compara.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:ProtInc.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0032526; P:response to retinoic acid; IEA:Compara. 
Interpro
 IPR007273; SCAMP. 
Pfam
 PF04144; SCAMP 
SMART
  
PROSITE
  
PRINTS