CPNE9_HUMAN - dbPTM
CPNE9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPNE9_HUMAN
UniProt AC Q8IYJ1
Protein Name Copine-9 {ECO:0000305}
Gene Name CPNE9 {ECO:0000312|HGNC:HGNC:24336}
Organism Homo sapiens (Human).
Sequence Length 553
Subcellular Localization
Protein Description Probable calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes (By similarity). Plays a role in dendrite formation by melanocytes. [PubMed: 23999003]
Protein Sequence MSLGGASERSVPATKIEITVSCRNLLDLDTFSKSDPMVVLYTQSRASQEWREFGRTEVIDNTLNPDFVRKFVLDYFFEEKQNLRFDVYNVDSKTNISKPKDFLGQAFLALGEVIGGQGSRVERTLTGVPGKKCGTILLTAEELSNCRDIATMQLCANKLDKKDFFGKSDPFLVFYRSNEDGTFTICHKTEVVKNTLNPVWQPFSIPVRALCNGDYDRTVKIDVYDWDRDGSHDFIGEFTTSYRELSKAQNQFTVYEVLNPRKKCKKKKYVNSGTVTLLSFSVDSEFTFVDYIKGGTQLNFTVAIDFTASNGNPLQPTSLHYMSPYQLSAYAMALKAVGEIIQDYDSDKLFPAYGFGAKLPPEGRISHQFPLNNNDEDPNCAGIEGVLESYFQSLRTVQLYGPTYFAPVINQVARAAAKISDGSQYYVLLIITDGVISDMTQTKEAIVSASSLPMSIIIVGVGPAMFEAMEELDGDDVRVSSRGRYAERDIVQFVPFRDYVDRSGNQVLSMARLAKDVLAEIPEQLLSYMRTRDIQPRPPPPANPSPIPAPEQP
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
2Phosphorylation------MSLGGASER
------CCCCCCCCC		35.4023403867
7Phosphorylation-MSLGGASERSVPAT
-CCCCCCCCCCCCCC		36.5023403867
10PhosphorylationLGGASERSVPATKIE
CCCCCCCCCCCCEEE		28.5323403867
14PhosphorylationSERSVPATKIEITVS
CCCCCCCCEEEEEEE		26.8723403867
30PhosphorylationRNLLDLDTFSKSDPM
CCCCCCCCCCCCCCE		36.7923663014
32PhosphorylationLLDLDTFSKSDPMVV
CCCCCCCCCCCCEEE		33.0823663014
34PhosphorylationDLDTFSKSDPMVVLY
CCCCCCCCCCEEEEE		45.8323663014
41PhosphorylationSDPMVVLYTQSRASQ
CCCEEEEEECCCCCH		7.3623663014
42PhosphorylationDPMVVLYTQSRASQE
CCEEEEEECCCCCHH		18.8623663014
44PhosphorylationMVVLYTQSRASQEWR
EEEEEECCCCCHHHH		23.2423663014
62PhosphorylationRTEVIDNTLNPDFVR
CCEEECCCCCHHHHH		24.9421815630
95N-linked_GlycosylationYNVDSKTNISKPKDF
EECCCCCCCCCCHHH		40.0316335952
132AcetylationLTGVPGKKCGTILLT
ECCCCCCCCCEEEEE		43.7620167786
135PhosphorylationVPGKKCGTILLTAEE
CCCCCCCEEEEEHHH		20.2320860994
158AcetylationTMQLCANKLDKKDFF
HHHHHHHCCCCCHHC		39.2720167786
161AcetylationLCANKLDKKDFFGKS
HHHHCCCCCHHCCCC		65.7620167786
161UbiquitinationLCANKLDKKDFFGKS
HHHHCCCCCHHCCCC		65.7623000965
162UbiquitinationCANKLDKKDFFGKSD
HHHCCCCCHHCCCCC		60.4823000965
167UbiquitinationDKKDFFGKSDPFLVF
CCCHHCCCCCCEEEE		46.6723000965
204PhosphorylationNPVWQPFSIPVRALC
CCCCCCCCCCHHHHC		32.4426356563
218PhosphorylationCNGDYDRTVKIDVYD
CCCCCCCEEEEEEEE		24.2126074081
224PhosphorylationRTVKIDVYDWDRDGS
CEEEEEEEECCCCCC		13.9426074081
231PhosphorylationYDWDRDGSHDFIGEF
EECCCCCCCCCCEEE		24.9526074081
239PhosphorylationHDFIGEFTTSYRELS
CCCCEEEECCHHHHH		15.5526074081
240PhosphorylationDFIGEFTTSYRELSK
CCCEEEECCHHHHHH		29.1426074081
241PhosphorylationFIGEFTTSYRELSKA
CCEEEECCHHHHHHH		21.0926074081
242PhosphorylationIGEFTTSYRELSKAQ
CEEEECCHHHHHHHH		13.1526074081
253O-linked_GlycosylationSKAQNQFTVYEVLNP
HHHHHCEEHHHCCCC		16.6529237092
269PhosphorylationKKCKKKKYVNSGTVT
HHCCCCCEECCCEEE		17.4725262027
270UbiquitinationKCKKKKYVNSGTVTL
HCCCCCEECCCEEEE		6.7123000965
271UbiquitinationCKKKKYVNSGTVTLL
CCCCCEECCCEEEEE		31.4723000965
272PhosphorylationKKKKYVNSGTVTLLS
CCCCEECCCEEEEEE		26.2925262027
274PhosphorylationKKYVNSGTVTLLSFS
CCEECCCEEEEEEEE		15.3325262027
276UbiquitinationYVNSGTVTLLSFSVD
EECCCEEEEEEEEEC		23.0923000965
276PhosphorylationYVNSGTVTLLSFSVD
EECCCEEEEEEEEEC		23.0925262027
279PhosphorylationSGTVTLLSFSVDSEF
CCEEEEEEEEECCCE		20.7025262027
281PhosphorylationTVTLLSFSVDSEFTF
EEEEEEEEECCCEEE		22.9525262027
284PhosphorylationLLSFSVDSEFTFVDY
EEEEEECCCEEEEEE		32.2425262027
287PhosphorylationFSVDSEFTFVDYIKG
EEECCCEEEEEEECC		20.7825262027
291PhosphorylationSEFTFVDYIKGGTQL
CCEEEEEEECCCCEE		10.1425262027
393PhosphorylationVLESYFQSLRTVQLY
HHHHHHHHHCCEEEC		15.2124719451
499PhosphorylationQFVPFRDYVDRSGNQ
EEEEHHHHCCCCCCH		10.4522210691
503PhosphorylationFRDYVDRSGNQVLSM
HHHHCCCCCCHHHHH		37.3222210691
509PhosphorylationRSGNQVLSMARLAKD
CCCCHHHHHHHHHHH		16.1322210691
527PhosphorylationEIPEQLLSYMRTRDI
HCHHHHHHHHHCCCC		26.0220068231
528PhosphorylationIPEQLLSYMRTRDIQ
CHHHHHHHHHCCCCC		7.2120068231
545PhosphorylationPPPPANPSPIPAPEQ
CCCCCCCCCCCCCCC		34.9632142685
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 CPNE9_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPNE9_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 CPNE9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CPNE9_HUMAN !!
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 CPNE9_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-95, AND MASS SPECTROMETRY.

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