CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000019
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Syntaxin-binding protein 3 
Protein Synonyms/Alias
 Platelet Sec1 protein; PSP; Protein unc-18 homolog 3; Unc18-3; Protein unc-18 homolog C; Unc-18C 
Gene Name
 STXBP3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11PVAERGLKSVVWQKIubiquitination[1]
17LKSVVWQKIKATVFDubiquitination[1]
19SVVWQKIKATVFDDCubiquitination[1]
86YFITPTSKSVDCFLHubiquitination[2]
98FLHDFASKSENKYKAubiquitination[1]
214LAQLVEKKLEDYYKIubiquitination[1]
220KKLEDYYKIDEKSLIubiquitination[3]
224DYYKIDEKSLIKGKTubiquitination[1, 3, 4]
230EKSLIKGKTHSQLLIubiquitination[1]
321TKKATEGKTSLSALTubiquitination[4, 5]
332SALTQLMKKMPHFRKubiquitination[6]
333ALTQLMKKMPHFRKQubiquitination[1]
357LAEDCMNKFKLNIEKubiquitination[1, 3]
359EDCMNKFKLNIEKLCubiquitination[1, 4]
364KFKLNIEKLCKTEQDubiquitination[1, 4, 5]
367LNIEKLCKTEQDLALubiquitination[1, 2, 4]
382GTDAEGQKVKDSMRVubiquitination[1, 2, 3, 4]
384DAEGQKVKDSMRVLLubiquitination[1]
397LLPVLLNKNHDNCDKubiquitination[1]
404KNHDNCDKIRAILLYubiquitination[1]
431DRLIQNVKIENESDMubiquitination[1, 2, 3, 4, 7]
457VPQSQQGKPLRKDRSubiquitination[6]
479SRWTPFIKDIMEDAIubiquitination[1, 2]
493IDNRLDSKEWPYCSQubiquitination[1, 2]
571THVLTPKKLLDDIKMubiquitination[1]
577KKLLDDIKMLNKPKDacetylation[8]
581DDIKMLNKPKDKVSLacetylation[8]
583IKMLNKPKDKVSLIKacetylation[8]
585MLNKPKDKVSLIKDEubiquitination[1]
590KDKVSLIKDE*****ubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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]
 [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] 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]
 [8] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 Together with STX4 and VAMP2, may play a role in insulin-dependent movement of GLUT4 and in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes (By similarity). 
Sequence Annotation
 REGION 1 255 Mediates interaction with DOC2B (By
 MOD_RES 198 198 Phosphoserine (By similarity).  
Keyword
 Cell membrane; Complete proteome; Cytoplasm; Membrane; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 592 AA 
Protein Sequence
MAPPVAERGL KSVVWQKIKA TVFDDCKKEG EWKIMLLDEF TTKLLASCCK MTDLLEEGIT 60
VVENIYKNRE PVRQMKALYF ITPTSKSVDC FLHDFASKSE NKYKAAYIYF TDFCPDNLFN 120
KIKASCSKSI RRCKEINISF IPHESQVYTL DVPDAFYYCY SPDPGNAKGK DAIMETMADQ 180
IVTVCATLDE NPGVRYKSKP LDNASKLAQL VEKKLEDYYK IDEKSLIKGK THSQLLIIDR 240
GFDPVSTVLH ELTFQAMAYD LLPIENDTYK YKTDGKEKEA ILEEEDDLWV RIRHRHIAVV 300
LEEIPKLMKE ISSTKKATEG KTSLSALTQL MKKMPHFRKQ ITKQVVHLNL AEDCMNKFKL 360
NIEKLCKTEQ DLALGTDAEG QKVKDSMRVL LPVLLNKNHD NCDKIRAILL YIFSINGTTE 420
ENLDRLIQNV KIENESDMIR NWSYLGVPIV PQSQQGKPLR KDRSAEETFQ LSRWTPFIKD 480
IMEDAIDNRL DSKEWPYCSQ CPAVWNGSGA VSARQKPRAN YLEDRKNGSK LIVFVIGGIT 540
YSEVRCAYEV SQAHKSCEVI IGSTHVLTPK KLLDDIKMLN KPKDKVSLIK DE 592 
Gene Ontology
 GO:0016324; C:apical plasma membrane; IEA:Compara.
 GO:0016323; C:basolateral plasma membrane; IEA:Compara.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0031091; C:platelet alpha granule; IDA:UniProtKB.
 GO:0042581; C:specific granule; IDA:UniProtKB.
 GO:0070820; C:tertiary granule; IDA:UniProtKB.
 GO:0016044; P:cellular membrane organization; TAS:Reactome.
 GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IMP:UniProtKB.
 GO:0043312; P:neutrophil degranulation; IEP:UniProtKB.
 GO:0070527; P:platelet aggregation; IMP:UniProtKB.
 GO:0051291; P:protein heterooligomerization; IEA:Compara.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0006904; P:vesicle docking involved in exocytosis; IEA:InterPro. 
Interpro
 IPR027482; Sec-1-like_dom2.
 IPR001619; Sec1-like. 
Pfam
 PF00995; Sec1 
SMART
  
PROSITE
  
PRINTS