CPNE8_HUMAN - dbPTM
CPNE8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPNE8_HUMAN
UniProt AC Q86YQ8
Protein Name Copine-8 {ECO:0000305}
Gene Name CPNE8 {ECO:0000312|HGNC:HGNC:23498}
Organism Homo sapiens (Human).
Sequence Length 564
Subcellular Localization
Protein Description Probable calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes..
Protein Sequence MDSRYNSTAGIGDLNQLSAAIPATRVEVSVSCRNLLDRDTFSKSDPICVLYVQGVGNKEWREFGRTEVIDNTLNPDFVRKFILDYFFEERENLRFDLYDVDSKSPNLSKHDFLGQVFCTLGEIVGSQGSRLEKPIVGIPGKKCGTIILTAEELNCCRDAVLMQFCANKLDKKDFFGKSDPFLVFYRSNEDGSFTICHKTEVVKNTLNPVWQAFKISVRALCNGDYDRTIKVEVYDWDRDGSHDFIGEFTTSYRELSRGQSQFNVYEVVNPKKKGKKKKYTNSGTVTLLSFLVETEVSFLDYIKGGTQINFTVAIDFTASNGNPAQPTSLHYMNPYQLNAYGMALKAVGEIVQDYDSDKMFPALGFGAKLPPDGRISHEFALNGNPQNPYCDGIEGVMEAYYRSLKSVQLYGPTNFAPVINHVARYASSVKDGSQYFVLLIVTDGVISDMAQTKESIVNASKLPMSIIIVGVGPAEFDAMVELDGDDVRVSSRGKYAERDIVQFVPFRDYIDRSGNHILSMARLAKDVLAEIPEQFLSYMRARGIKPSPAPPPYTPPTHVLQTQI
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
5Phosphorylation---MDSRYNSTAGIG
---CCCCCCCCCCCC		19.88-
7Phosphorylation-MDSRYNSTAGIGDL
-CCCCCCCCCCCCCH		15.6528857561
8PhosphorylationMDSRYNSTAGIGDLN
CCCCCCCCCCCCCHH		25.8428857561
10UbiquitinationSRYNSTAGIGDLNQL
CCCCCCCCCCCHHHH		25.2123000965
11UbiquitinationRYNSTAGIGDLNQLS
CCCCCCCCCCHHHHH		3.4423000965
16UbiquitinationAGIGDLNQLSAAIPA
CCCCCHHHHHHHCCC		44.0523000965
58UbiquitinationYVQGVGNKEWREFGR
EEECCCCHHHHHCCC		53.3721963094
72PhosphorylationRTEVIDNTLNPDFVR
CEEEECCCCCHHHHH		24.9421815630
74UbiquitinationEVIDNTLNPDFVRKF
EEECCCCCHHHHHHH		31.8621890473
103UbiquitinationDLYDVDSKSPNLSKH
EEEECCCCCCCCCHH		66.5221906983
104PhosphorylationLYDVDSKSPNLSKHD
EEECCCCCCCCCHHH		23.9926657352
141UbiquitinationPIVGIPGKKCGTIIL
CCCCCCCCCCEEEEE		39.2633845483
142UbiquitinationIVGIPGKKCGTIILT
CCCCCCCCCEEEEEE		43.7629967540
171UbiquitinationFCANKLDKKDFFGKS
HHHHCCCCCHHCCCC		65.7623000965
172UbiquitinationCANKLDKKDFFGKSD
HHHCCCCCHHCCCCC		60.4823000965
177UbiquitinationDKKDFFGKSDPFLVF
CCCHHCCCCCCEEEE		46.6723000965
198UbiquitinationGSFTICHKTEVVKNT
CCEEEEEEECEECCC		41.8029967540
198AcetylationGSFTICHKTEVVKNT
CCEEEEEEECEECCC		41.8026051181
203UbiquitinationCHKTEVVKNTLNPVW
EEEECEECCCCCHHH		49.7629967540
241PhosphorylationYDWDRDGSHDFIGEF
EECCCCCCCCEEEEE		24.9526074081
244UbiquitinationDRDGSHDFIGEFTTS
CCCCCCCEEEEEECC		6.9121890473
260PhosphorylationRELSRGQSQFNVYEV
HHHCCCCCCCCEEEE		39.2917525332
356PhosphorylationEIVQDYDSDKMFPAL
HHHHCCCCCCCCCCC		32.66-
358AcetylationVQDYDSDKMFPALGF
HHCCCCCCCCCCCCC		46.5226051181
358UbiquitinationVQDYDSDKMFPALGF
HHCCCCCCCCCCCCC		46.5229967540
405UbiquitinationEAYYRSLKSVQLYGP
HHHHHHCCCCEEECC		50.2323000965
405AcetylationEAYYRSLKSVQLYGP
HHHHHHCCCCEEECC		50.2326051181
406PhosphorylationAYYRSLKSVQLYGPT
HHHHHCCCCEEECCC		22.0128442448
410PhosphorylationSLKSVQLYGPTNFAP
HCCCCEEECCCCHHH		12.1728152594
413PhosphorylationSVQLYGPTNFAPVIN
CCEEECCCCHHHHHH		38.3128442448
537PhosphorylationEIPEQFLSYMRARGI
HCHHHHHHHHHHCCC		20.4020068231
538PhosphorylationIPEQFLSYMRARGIK
CHHHHHHHHHHCCCC		7.8620068231
545UbiquitinationYMRARGIKPSPAPPP
HHHHCCCCCCCCCCC		42.1229967540
547PhosphorylationRARGIKPSPAPPPYT
HHCCCCCCCCCCCCC		28.7928450419
553PhosphorylationPSPAPPPYTPPTHVL
CCCCCCCCCCCCCEE		37.3428450419
554PhosphorylationSPAPPPYTPPTHVLQ
CCCCCCCCCCCCEEE		28.6825159151
557PhosphorylationPPPYTPPTHVLQTQI
CCCCCCCCCEEECCC		26.3128450419
562PhosphorylationPPTHVLQTQI-----
CCCCEEECCC-----		24.8728450419
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CPNE8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPNE8_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CPNE8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LTOR2_HUMANLAMTOR2physical
22939629
EIF3I_HUMANEIF3Iphysical
26344197
NDUS1_HUMANNDUFS1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CPNE8_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260, AND MASSSPECTROMETRY.

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