CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001569
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Vesicle-associated membrane protein-associated protein B/C 
Protein Synonyms/Alias
 VAMP-B/VAMP-C; VAMP-associated protein B/C; VAP-B/VAP-C 
Gene Name
 VAPB 
Gene Synonyms/Alias
 UNQ484/PRO983 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
3*****MAKVEQVLSLacetylation[1]
3*****MAKVEQVLSLubiquitination[2]
118PEDLMDSKLRCVFELacetylation[3, 4]
118PEDLMDSKLRCVFELubiquitination[4]
147IISTTASKTETPIVSacetylation[3]
147IISTTASKTETPIVSubiquitination[2, 4, 5, 6]
155TETPIVSKSLSSSLDubiquitination[5, 6, 7, 8]
Reference
 [1] 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]
 [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] 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]
 [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] 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]
 [7] 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]
 [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
Functional Description
 Participates in the endoplasmic reticulum unfolded protein response (UPR) by inducing ERN1/IRE1 activity. Involved in cellular calcium homeostasis regulation. 
Sequence Annotation
 DOMAIN 7 124 MSP.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 150 150 Phosphothreonine.
 MOD_RES 156 156 Phosphoserine.
 MOD_RES 160 160 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Amyotrophic lateral sclerosis; Coiled coil; Complete proteome; Direct protein sequencing; Disease mutation; Endoplasmic reticulum; Host-virus interaction; Membrane; Neurodegeneration; Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix; Unfolded protein response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 243 AA 
Protein Sequence
MAKVEQVLSL EPQHELKFRG PFTDVVTTNL KLGNPTDRNV CFKVKTTAPR RYCVRPNSGI 60
IDAGASINVS VMLQPFDYDP NEKSKHKFMV QSMFAPTDTS DMEAVWKEAK PEDLMDSKLR 120
CVFELPAEND KPHDVEINKI ISTTASKTET PIVSKSLSSS LDDTEVKKVM EECKRLQGEV 180
QRLREENKQF KEEDGLRMRK TVQSNSPISA LAPTGKEEGL STRLLALVVL FFIVGVIIGK 240
IAL 243 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
 GO:0005198; F:structural molecule activity; IEA:InterPro.
 GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; IDA:UniProtKB.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0006874; P:cellular calcium ion homeostasis; IMP:UniProtKB.
 GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
 GO:0019048; P:virus-host interaction; IDA:UniProtKB. 
Interpro
 IPR000535; Major_sperm.
 IPR008962; PapD-like.
 IPR016763; Vesicle-associated_membrane. 
Pfam
 PF00635; Motile_Sperm 
SMART
  
PROSITE
 PS50202; MSP 
PRINTS