CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020124
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Extended synaptotagmin-1 
Protein Synonyms/Alias
 E-Syt1; Membrane-bound C2 domain-containing protein 
Gene Name
 ESYT1 
Gene Synonyms/Alias
 FAM62A; KIAA0747; MBC2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
118DEEQLTAKTLYMSHRubiquitination[1, 2, 3, 4, 5, 6, 7]
138VSFPDVEKAEWLNKIubiquitination[1, 2]
189TRVELGEKPLRIIGVubiquitination[1, 2, 5]
197PLRIIGVKVHPGQRKubiquitination[1, 5]
231EVKKYFCKAGVKGMQubiquitination[7]
344AARGLSSKDKYVKGLubiquitination[5]
349SSKDKYVKGLIEGKSubiquitination[4, 5, 7]
355VKGLIEGKSDPYALVubiquitination[1, 2, 5, 6, 7, 8]
417DDFLGRMKLDVGKVLubiquitination[5, 7]
422RMKLDVGKVLQASVLubiquitination[6]
493RAQDLPLKKGNKEPNubiquitination[5, 7]
497LPLKKGNKEPNPMVQubiquitination[2]
546QELDVQVKDDSRALTubiquitination[2, 5, 6, 7, 9]
662EAQDLIAKDRFLGGLubiquitination[5, 7]
671RFLGGLVKGKSDPYVubiquitination[4, 5, 7]
673LGGLVKGKSDPYVKLubiquitination[5]
681SDPYVKLKLAGRSFRubiquitination[5]
817LPLRKGTKHLSPYATacetylation[10, 11]
817LPLRKGTKHLSPYATubiquitination[1, 5, 7]
835GDSSHKTKTISQTSAubiquitination[2, 5, 6, 7]
855SASFLIRKPHTESLEubiquitination[2, 4, 5, 7]
1054LDEAQRRKLDVSVKSubiquitination[5]
1060RKLDVSVKSNSSFMSubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] 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]
 [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] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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
Functional Description
 May play a role as calcium-regulated intrinsic membrane protein (By similarity). 
Sequence Annotation
 DOMAIN 316 417 C2 1.
 DOMAIN 465 558 C2 2.
 DOMAIN 634 735 C2 3.
 DOMAIN 785 877 C2 4.
 DOMAIN 972 1077 C2 5.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 817 817 N6-acetyllysine.
 MOD_RES 820 820 Phosphoserine.
 MOD_RES 963 963 Phosphoserine.
 MOD_RES 1034 1034 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Coiled coil; Complete proteome; Direct protein sequencing; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1104 AA 
Protein Sequence
MERSPGEGPS PSPMDQPSAP SDPTDQPPAA HAKPDPGSGG QPAGPGAAGE ALAVLTSFGR 60
RLLVLIPVYL AGAVGLSVGF VLFGLALYLG WRRVRDEKER SLRAARQLLD DEEQLTAKTL 120
YMSHRELPAW VSFPDVEKAE WLNKIVAQVW PFLGQYMEKL LAETVAPAVR GSNPHLQTFT 180
FTRVELGEKP LRIIGVKVHP GQRKEQILLD LNISYVGDVQ IDVEVKKYFC KAGVKGMQLH 240
GVLRVILEPL IGDLPFVGAV SMFFIRRPTL DINWTGMTNL LDIPGLSSLS DTMIMDSIAA 300
FLVLPNRLLV PLVPDLQDVA QLRSPLPRGI IRIHLLAARG LSSKDKYVKG LIEGKSDPYA 360
LVRLGTQTFC SRVIDEELNP QWGETYEVMV HEVPGQEIEV EVFDKDPDKD DFLGRMKLDV 420
GKVLQASVLD DWFPLQGGQG QVHLRLEWLS LLSDAEKLEQ VLQWNWGVSS RPDPPSAAIL 480
VVYLDRAQDL PLKKGNKEPN PMVQLSIQDV TQESKAVYST NCPVWEEAFR FFLQDPQSQE 540
LDVQVKDDSR ALTLGALTLP LARLLTAPEL ILDQWFQLSS SGPNSRLYMK LVMRILYLDS 600
SEICFPTVPG CPGAWDVDSE NPQRGSSVDA PPRPCHTTPD SQFGTEHVLR IHVLEAQDLI 660
AKDRFLGGLV KGKSDPYVKL KLAGRSFRSH VVREDLNPRW NEVFEVIVTS VPGQELEVEV 720
FDKDLDKDDF LGRCKVRLTT VLNSGFLDEW LTLEDVPSGR LHLRLERLTP RPTAAELEEV 780
LQVNSLIQTQ KSAELAAALL SIYMERAEDL PLRKGTKHLS PYATLTVGDS SHKTKTISQT 840
SAPVWDESAS FLIRKPHTES LELQVRGEGT GVLGSLSLPL SELLVADQLC LDRWFTLSSG 900
QGQVLLRAQL GILVSQHSGV EAHSHSYSHS SSSLSEEPEL SGGPPHITSS APELRQRLTH 960
VDSPLEAPAG PLGQVKLTLW YYSEERKLVS IVHGCRSLRQ NGRDPPDPYV SLLLLPDKNR 1020
GTKRRTSQKK RTLSPEFNER FEWELPLDEA QRRKLDVSVK SNSSFMSRER ELLGKVQLDL 1080
AETDLSQGVA RWYDLMDNKD KGSS 1104 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. 
Interpro
 IPR000008; C2_Ca-dep.
 IPR008973; C2_Ca/lipid-bd_dom_CaLB.
 IPR020477; C2_dom.
 IPR018029; C2_membr_targeting. 
Pfam
 PF00168; C2 
SMART
 SM00239; C2 
PROSITE
 PS50004; C2 
PRINTS
 PR00360; C2DOMAIN.