CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001177
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Vesicle-trafficking protein SEC22b 
Protein Synonyms/Alias
 ER-Golgi SNARE of 24 kDa; ERS-24; ERS24; SEC22 vesicle-trafficking protein homolog B; SEC22 vesicle-trafficking protein-like 1 
Gene Name
 SEC22B 
Gene Synonyms/Alias
 SEC22L1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
38QQYQSQAKQLFRKLNacetylation[1, 2, 3, 4]
38QQYQSQAKQLFRKLNubiquitination[4, 5, 6, 7, 8, 9, 10, 11]
81LCEAAFPKTLAFAYLsumoylation[12]
81LCEAAFPKTLAFAYLubiquitination[13]
121EFDTFIQKTKKLYIDubiquitination[5]
169ALSALDSKANNLSSLubiquitination[4, 5, 6, 7, 9, 10, 11]
178NNLSSLSKKYRQDAKubiquitination[5, 6, 11]
185KKYRQDAKYLNMHSTubiquitination[5]
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] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [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] 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]
 [11] 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]
 [12] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [13] 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
Functional Description
 SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER. 
Sequence Annotation
 DOMAIN 6 119 Longin.
 DOMAIN 134 194 v-SNARE coiled-coil homology.
 MOD_RES 38 38 N6-acetyllysine.
 MOD_RES 137 137 Phosphoserine.
 MOD_RES 140 140 Phosphothreonine.
 MOD_RES 168 168 Phosphoserine (By similarity).
 MOD_RES 177 177 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Coiled coil; Complete proteome; Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 215 AA 
Protein Sequence
MVLLTMIARV ADGLPLAASM QEDEQSGRDL QQYQSQAKQL FRKLNEQSPT RCTLEAGAMT 60
FHYIIEQGVC DLVLCEAAFP KTLAFAYLED LHSEFDEQHG KKVPTVSRPY SFIEFDTFIQ 120
KTKKLYIDSC ARRNLGSINT ELQDVQRIMV ANIEEVLQRG EALSALDSKA NNLSSLSKKY 180
RQDAKYLNMH STYAKLAAVA VFFIMLIVYV RFWWL 215 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
 GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:ProtInc.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW. 
Interpro
 IPR011012; Longin-like_dom.
 IPR010908; Longin_dom.
 IPR001388; Synaptobrevin. 
Pfam
 PF13774; Longin
 PF00957; Synaptobrevin 
SMART
  
PROSITE
 PS50859; LONGIN
 PS50892; V_SNARE 
PRINTS
 PR00219; SYNAPTOBREVN.