CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022491
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Vesicle-associated membrane protein-associated protein A 
Protein Synonyms/Alias
 VAMP-A; VAMP-associated protein A; VAP-A; 33 kDa VAMP-associated protein; VAP-33 
Gene Name
 VAPA 
Gene Synonyms/Alias
 VAP33 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
26PPTDLKFKGPFTDVVubiquitination[1, 2]
38DVVTTNLKLRNPSDRubiquitination[1]
90FDYDPNEKSKHKFMVubiquitination[3]
125PDELMDSKLRCVFEMacetylation[4, 5, 6]
138EMPNENDKLNDMEPSubiquitination[7]
146LNDMEPSKAVPLNASubiquitination[1, 7, 8, 9, 10]
161KQDGPMPKPHSVSLNubiquitination[9]
188RLQGEMMKLSEENRHubiquitination[2, 7, 9, 11]
205DEGLRLRKVAHSDKPubiquitination[1]
211RKVAHSDKPGSTSTAacetylation[6]
211RKVAHSDKPGSTSTAubiquitination[1, 9]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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 trafficking. 
Sequence Annotation
 DOMAIN 14 131 MSP.
 MOD_RES 125 125 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Coiled coil; Complete proteome; Endoplasmic reticulum; Membrane; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 249 AA 
Protein Sequence
MASASGAMAK HEQILVLDPP TDLKFKGPFT DVVTTNLKLR NPSDRKVCFK VKTTAPRRYC 60
VRPNSGIIDP GSTVTVSVML QPFDYDPNEK SKHKFMVQTI FAPPNTSDME AVWKEAKPDE 120
LMDSKLRCVF EMPNENDKLN DMEPSKAVPL NASKQDGPMP KPHSVSLNDT ETRKLMEECK 180
RLQGEMMKLS EENRHLRDEG LRLRKVAHSD KPGSTSTASF RDNVTSPLPS LLVVIAAIFI 240
GFFLGKFIL 249 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005874; C:microtubule; IEA:Compara.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0031982; C:vesicle; IDA:UniProtKB.
 GO:0004871; F:signal transducer activity; IMP:UniProtKB.
 GO:0005198; F:structural molecule activity; IEA:InterPro.
 GO:0008219; P:cell death; IMP:UniProtKB.
 GO:0006944; P:cellular membrane fusion; TAS:ProtInc.
 GO:0031175; P:neuron projection development; IMP:UniProtKB.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
 GO:0070972; P:protein localization to endoplasmic reticulum; IMP:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome. 
Interpro
 IPR000535; Major_sperm.
 IPR008962; PapD-like.
 IPR016763; Vesicle-associated_membrane. 
Pfam
 PF00635; Motile_Sperm 
SMART
  
PROSITE
 PS50202; MSP 
PRINTS