CPNE3_HUMAN - dbPTM
CPNE3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPNE3_HUMAN
UniProt AC O75131
Protein Name Copine-3 {ECO:0000305}
Gene Name CPNE3 {ECO:0000312|HGNC:HGNC:2316}
Organism Homo sapiens (Human).
Sequence Length 537
Subcellular Localization Nucleus . Cytoplasm . Cell membrane . Cell junction . Cell junction, focal adhesion . Associates to the membrane in a calcium-dependent manner (PubMed:20010870). Translocates to the cell membrane and the nucleus in a calcium- or growth factor heregul
Protein Description Calcium-dependent phospholipid-binding protein that plays a role in ERBB2-mediated tumor cell migration in response to growth factor heregulin stimulation. [PubMed: 20010870]
Protein Sequence MAAQCVTKVALNVSCANLLDKDIGSKSDPLCVLFLNTSGQQWYEVERTERIKNCLNPQFSKTFIIDYYFEVVQKLKFGVYDIDNKTIELSDDDFLGECECTLGQIVSSKKLTRPLVMKTGRPAGKGSITISAEEIKDNRVVLFEMEARKLDNKDLFGKSDPYLEFHKQTSDGNWLMVHRTEVVKNNLNPVWRPFKISLNSLCYGDMDKTIKVECYDYDNDGSHDLIGTFQTTMTKLKEASRSSPVEFECINEKKRQKKKSYKNSGVISVKQCEITVECTFLDYIMGGCQLNFTVGVDFTGSNGDPRSPDSLHYISPNGVNEYLTALWSVGLVIQDYDADKMFPAFGFGAQIPPQWQVSHEFPMNFNPSNPYCNGIQGIVEAYRSCLPQIKLYGPTNFSPIINHVARFAAAATQQQTASQYFVLLIITDGVITDLDETRQAIVNASRLPMSIIIVGVGGADFSAMEFLDGDGGSLRSPLGEVAIRDIVQFVPFRQFQNAPKEALAQCVLAEIPQQVVGYFNTYKLLPPKNPATKQQKQ
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
2Acetylation------MAAQCVTKV
------CCCHHHHHH		13.26-
14PhosphorylationTKVALNVSCANLLDK
HHHHHCHHHHHHHCC		13.3630266825
21UbiquitinationSCANLLDKDIGSKSD
HHHHHHCCCCCCCCC		51.74-
21AcetylationSCANLLDKDIGSKSD
HHHHHHCCCCCCCCC		51.7426051181
25PhosphorylationLLDKDIGSKSDPLCV
HHCCCCCCCCCCEEE		29.3524275569
37PhosphorylationLCVLFLNTSGQQWYE
EEEEEEECCCCCEEE		36.0628348404
38PhosphorylationCVLFLNTSGQQWYEV
EEEEEECCCCCEEEE		33.2728348404
52MalonylationVERTERIKNCLNPQF
EECHHHHHHHCCCCC		48.0726320211
52UbiquitinationVERTERIKNCLNPQF
EECHHHHHHHCCCCC		48.07-
54S-nitrosylationRTERIKNCLNPQFSK
CHHHHHHHCCCCCCC		3.1022178444
60PhosphorylationNCLNPQFSKTFIIDY
HHCCCCCCCEEEHHH		26.0725849741
61UbiquitinationCLNPQFSKTFIIDYY
HCCCCCCCEEEHHHH		49.0621890473
76AcetylationFEVVQKLKFGVYDID
HHHHHHCCCEEEECC		47.2926051181
762-HydroxyisobutyrylationFEVVQKLKFGVYDID
HHHHHHCCCEEEECC		47.29-
76UbiquitinationFEVVQKLKFGVYDID
HHHHHHCCCEEEECC		47.29-
86PhosphorylationVYDIDNKTIELSDDD
EEECCCCEEEECCCC		26.4128102081
90PhosphorylationDNKTIELSDDDFLGE
CCCEEEECCCCCCCE		26.6328102081
109AcetylationLGQIVSSKKLTRPLV
HHHHHCCCCCCCCEE		44.2726051181
109UbiquitinationLGQIVSSKKLTRPLV
HHHHHCCCCCCCCEE		44.27-
119O-linked_GlycosylationTRPLVMKTGRPAGKG
CCCEEECCCCCCCCC		21.9623301498
125UbiquitinationKTGRPAGKGSITISA
CCCCCCCCCEEEEEH		52.1421890473
136UbiquitinationTISAEEIKDNRVVLF
EEEHHHHHCCEEEEE		52.8321890473
136AcetylationTISAEEIKDNRVVLF
EEEHHHHHCCEEEEE		52.8325953088
149UbiquitinationLFEMEARKLDNKDLF
EEEEEECCCCCCCCC		68.21-
153UbiquitinationEARKLDNKDLFGKSD
EECCCCCCCCCCCCC		56.31-
158UbiquitinationDNKDLFGKSDPYLEF
CCCCCCCCCCCCCEE		44.3321890473
158MalonylationDNKDLFGKSDPYLEF
CCCCCCCCCCCCCEE		44.3326320211
158AcetylationDNKDLFGKSDPYLEF
CCCCCCCCCCCCCEE		44.3323236377
159PhosphorylationNKDLFGKSDPYLEFH
CCCCCCCCCCCCEEE		44.1720873877
167UbiquitinationDPYLEFHKQTSDGNW
CCCCEEEEECCCCCE		61.6721890473
167AcetylationDPYLEFHKQTSDGNW
CCCCEEEEECCCCCE		61.6723954790
169PhosphorylationYLEFHKQTSDGNWLM
CCEEEEECCCCCEEE		33.3221406692
170PhosphorylationLEFHKQTSDGNWLMV
CEEEEECCCCCEEEE		40.8121406692
176SulfoxidationTSDGNWLMVHRTEVV
CCCCCEEEEEEEEEH		1.4830846556
184AcetylationVHRTEVVKNNLNPVW
EEEEEEHHCCCCCCC		45.3423236377
184UbiquitinationVHRTEVVKNNLNPVW
EEEEEEHHCCCCCCC		45.3421890473
197PhosphorylationVWRPFKISLNSLCYG
CCCCEEEECCCEECC		23.3022617229
200PhosphorylationPFKISLNSLCYGDMD
CEEEECCCEECCCCC		25.7225850435
203PhosphorylationISLNSLCYGDMDKTI
EECCCEECCCCCCCE		22.8122817900
208UbiquitinationLCYGDMDKTIKVECY
EECCCCCCCEEEEEE		45.58-
2082-HydroxyisobutyrylationLCYGDMDKTIKVECY
EECCCCCCCEEEEEE		45.58-
209PhosphorylationCYGDMDKTIKVECYD
ECCCCCCCEEEEEEE		23.0523312004
233SulfoxidationIGTFQTTMTKLKEAS
EEEEHHHHHHHHHHH		3.3628465586
235UbiquitinationTFQTTMTKLKEASRS
EEHHHHHHHHHHHHC		46.90-
240PhosphorylationMTKLKEASRSSPVEF
HHHHHHHHHCCCCCH		33.5123401153
242PhosphorylationKLKEASRSSPVEFEC
HHHHHHHCCCCCHHH		36.1823927012
243PhosphorylationLKEASRSSPVEFECI
HHHHHHCCCCCHHHC		31.6725159151
253AcetylationEFECINEKKRQKKKS
CHHHCCHHHHHCCHH		49.0925953088
253UbiquitinationEFECINEKKRQKKKS
CHHHCCHHHHHCCHH		49.09-
262UbiquitinationRQKKKSYKNSGVISV
HHCCHHCCCCCCEEE		52.2921890473
262MalonylationRQKKKSYKNSGVISV
HHCCHHCCCCCCEEE		52.2932601280
262AcetylationRQKKKSYKNSGVISV
HHCCHHCCCCCCEEE		52.2925953088
268PhosphorylationYKNSGVISVKQCEIT
CCCCCCEEEEEEEEE		22.3624667141
390UbiquitinationRSCLPQIKLYGPTNF
HHHCCCCEECCCCCC		30.34-
390AcetylationRSCLPQIKLYGPTNF
HHHCCCCEECCCCCC		30.3425953088
392PhosphorylationCLPQIKLYGPTNFSP
HCCCCEECCCCCCHH		18.9627273156
395PhosphorylationQIKLYGPTNFSPIIN
CCEECCCCCCHHHHH		44.5328152594
450PhosphorylationNASRLPMSIIIVGVG
HHHHCCCEEEEEEEC		14.5422817900
476PhosphorylationGDGGSLRSPLGEVAI
CCCCCCCCCCHHHHH		29.7521815630
528UbiquitinationTYKLLPPKNPATKQQ
CCCCCCCCCCCCHHH		73.88-
533UbiquitinationPPKNPATKQQKQ---
CCCCCCCHHHCC---		53.49-
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 CPNE3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPNE3_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 CPNE3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYQ_HUMANQARSphysical
16169070
VASP_HUMANVASPphysical
22939629
HNRH1_HUMANHNRNPH1physical
26344197
GRP75_HUMANHSPA9physical
26344197
TRAP1_HUMANTRAP1physical
27173435
SND1_HUMANSND1physical
27173435
IF2P_HUMANEIF5Bphysical
27173435
G6PI_HUMANGPIphysical
27173435
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 CPNE3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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