CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020125
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]
138VSFPDVEKAEWLNKIubiquitination[4]
189TRVELGEKPLRIIGVubiquitination[2, 4]
197PLRIIGVKVHPGQRKubiquitination[4]
349SSKDKYVKGLIEGKSubiquitination[1, 2]
355VKGLIEGKSDPYALVubiquitination[2, 3, 4]
422RMKLDVGKVLQASVLubiquitination[3]
556QELDVQVKDDSRALTubiquitination[3]
681RFLGGLVKGKSDPYVubiquitination[1]
827LPLRKGTKHLSPYATubiquitination[4]
845GDSSHKTKTISQTSAubiquitination[3]
865SASFLIRKPHTESLEubiquitination[1]
997WYYSEERKLVSIVHGubiquitination[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] 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]
 [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] 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
 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 PMVTSELYPP QLKKGNKEPN PMVQLSIQDV TQESKAVYST NCPVWEEAFR 540
FFLQDPQSQE LDVQVKDDSR ALTLGALTLP LARLLTAPEL ILDQWFQLSS SGPNSRLYMK 600
LVMRILYLDS SEICFPTVPG CPGAWDVDSE NPQRGSSVDA PPRPCHTTPD SQFGTEHVLR 660
IHVLEAQDLI AKDRFLGGLV KGKSDPYVKL KLAGRSFRSH VVREDLNPRW NEVFEVIVTS 720
VPGQELEVEV FDKDLDKDDF LGRCKVRLTT VLNSGFLDEW LTLEDVPSGR LHLRLERLTP 780
RPTAAELEEV LQVNSLIQTQ KSAELAAALL SIYMERAEDL PLRKGTKHLS PYATLTVGDS 840
SHKTKTISQT SAPVWDESAS FLIRKPHTES LELQVRGEGT GVLGSLSLPL SELLVADQLC 900
LDRWFTLSSG QGQVLLRAQL GILVSQHSGV EAHSHSYSHS SSSLSEEPEL SGGPPHITSS 960
APELRQRLTH VDSPLEAPAG PLGQVKLTLW YYSEERKLVS IVHGCRSLRQ NGRDPPDPYV 1020
SLLLLPDKNR GTKRRTSQKK RTLSPEFNER FEWELPLDEA QRRKLDVSVK SNSSFMSRER 1080
ELLGKVQLDL AETDLSQGVA RWYDLMDNKD KGSS 1114 
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.