CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019724
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Synaptic vesicle membrane protein VAT-1 homolog 
Protein Synonyms/Alias
  
Gene Name
 VAT1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
61TGFGGYDKVKLQSRPubiquitination[1]
63FGGYDKVKLQSRPAAubiquitination[2, 3]
230ASKHEALKENGVTHPubiquitination[2]
250TDYVDEIKKISPKGVubiquitination[2, 3, 4]
251DYVDEIKKISPKGVDubiquitination[2]
255EIKKISPKGVDIVMDubiquitination[2, 3, 4, 5, 6, 7, 8, 9]
271LGGSDTAKGYNLLKPubiquitination[2]
277AKGYNLLKPMGKVVTubiquitination[2]
295ANLLTGPKRNLMALAubiquitination[1, 2, 3, 4, 6, 7, 8, 9]
355LYNQGHIKPHIDSVWubiquitination[2, 6, 8, 9]
372EKVADAMKQMQEKKNubiquitination[2, 3, 4, 6, 7, 8, 9]
382QEKKNVGKVLLVPGPubiquitination[2, 8]
391LLVPGPEKEN*****ubiquitination[2]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [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]
 [9] 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] 
Functional Description
 Possesses ATPase activity (By similarity). Plays a part in calcium-regulated keratinocyte activation in epidermal repair mechanisms. Has no effect on cell proliferation. Negatively regulates mitochondrial fusion in cooperation with mitofusin proteins (MFN1-2). 
Sequence Annotation
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 18 18 Phosphoserine.  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Membrane; Mitochondrion; Mitochondrion outer membrane; Oxidoreductase; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 393 AA 
Protein Sequence
MSDEREVAEA ATGEDASSPP PKTEAASDPQ HPAASEGAAA AAASPPLLRC LVLTGFGGYD 60
KVKLQSRPAA PPAPGPGQLT LRLRACGLNF ADLMARQGLY DRLPPLPVTP GMEGAGVVIA 120
VGEGVSDRKA GDRVMVLNRS GMWQEEVTVP SVQTFLIPEA MTFEEAAALL VNYITAYMVL 180
FDFGNLQPGH SVLVHMAAGG VGMAAVQLCR TVENVTVFGT ASASKHEALK ENGVTHPIDY 240
HTTDYVDEIK KISPKGVDIV MDPLGGSDTA KGYNLLKPMG KVVTYGMANL LTGPKRNLMA 300
LARTWWNQFS VTALQLLQAN RAVCGFHLGY LDGEVELVSG VVARLLALYN QGHIKPHIDS 360
VWPFEKVADA MKQMQEKKNV GKVLLVPGPE KEN 393 
Gene Ontology
 GO:0016021; C:integral to membrane; TAS:ProtInc.
 GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
 GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0010637; P:negative regulation of mitochondrial fusion; IMP:UniProtKB. 
Interpro
 IPR013149; ADH_C.
 IPR013154; ADH_GroES-like.
 IPR002085; ADH_SF_Zn-type.
 IPR011032; GroES-like.
 IPR016040; NAD(P)-bd_dom.
 IPR002364; Quin_OxRdtase/zeta-crystal_CS. 
Pfam
 PF08240; ADH_N
 PF00107; ADH_zinc_N 
SMART
  
PROSITE
 PS01162; QOR_ZETA_CRYSTAL 
PRINTS