CNPY3_HUMAN - dbPTM
CNPY3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNPY3_HUMAN
UniProt AC Q9BT09
Protein Name Protein canopy homolog 3
Gene Name CNPY3
Organism Homo sapiens (Human).
Sequence Length 278
Subcellular Localization Endoplasmic reticulum.
Protein Description Toll-like receptor (TLR)-specific co-chaperone for HSP90B1. Required for proper TLR folding, except that of TLR3, and hence controls TLR exit from the endoplasmic reticulum. Consequently, required for both innate and adaptive immune responses (By similarity)..
Protein Sequence MDSMPEPASRCLLLLPLLLLLLLLLPAPELGPSQAGAEENDWVRLPSKCEVCKYVAVELKSAFEETGKTKEVIGTGYGILDQKASGVKYTKSDLRLIEVTETICKRLLDYSLHKERTGSNRFAKGMSETFETLHNLVHKGVKVVMDIPYELWNETSAEVADLKKQCDVLVEEFEEVIEDWYRNHQEEDLTEFLCANHVLKGKDTSCLAEQWSGKKGDTAALGGKKSKKKSSRAKAAGGRSSSSKQRKELGGLEGDPSPEEDEGIQKASPLTHSPPDEL
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
3Phosphorylation-----MDSMPEPASR
-----CCCCCCHHHH
34.6323322592
47PhosphorylationNDWVRLPSKCEVCKY
CCCEECCCCCCCCCH
55.3024719451
48 (in isoform 2)Ubiquitination-32.26-
85PhosphorylationGILDQKASGVKYTKS
CHHHHCCCCCCCCHH
51.67-
90PhosphorylationKASGVKYTKSDLRLI
CCCCCCCCHHHHHHH
20.53-
91UbiquitinationASGVKYTKSDLRLIE
CCCCCCCHHHHHHHH
38.5929967540
92PhosphorylationSGVKYTKSDLRLIEV
CCCCCCHHHHHHHHH
33.79-
100PhosphorylationDLRLIEVTETICKRL
HHHHHHHHHHHHHHH
18.02-
102PhosphorylationRLIEVTETICKRLLD
HHHHHHHHHHHHHHH
23.47-
110PhosphorylationICKRLLDYSLHKERT
HHHHHHHHHHHHHCC
17.07-
114UbiquitinationLLDYSLHKERTGSNR
HHHHHHHHHCCCCCC
54.93-
117PhosphorylationYSLHKERTGSNRFAK
HHHHHHCCCCCCCCH
46.16-
127PhosphorylationNRFAKGMSETFETLH
CCCCHHHHHHHHHHH
42.00-
153N-linked_GlycosylationDIPYELWNETSAEVA
ECCHHHHCCCHHHHH
56.1212754519
153N-linked_GlycosylationDIPYELWNETSAEVA
ECCHHHHCCCHHHHH
56.1212754519
202UbiquitinationANHVLKGKDTSCLAE
HHHHHCCCCCCHHHH
57.1329967540
212PhosphorylationSCLAEQWSGKKGDTA
CHHHHHHCCCCCCCH
40.1925159151
214AcetylationLAEQWSGKKGDTAAL
HHHHHCCCCCCCHHC
48.3325953088
225MethylationTAALGGKKSKKKSSR
CHHCCCCCCCCHHHH
71.44-
225"N6,N6-dimethyllysine"TAALGGKKSKKKSSR
CHHCCCCCCCCHHHH
71.44-
226PhosphorylationAALGGKKSKKKSSRA
HHCCCCCCCCHHHHH
53.87-
240PhosphorylationAKAAGGRSSSSKQRK
HHHCCCCCCHHHHHH
37.5427251275
241PhosphorylationKAAGGRSSSSKQRKE
HHCCCCCCHHHHHHH
36.9527251275
242PhosphorylationAAGGRSSSSKQRKEL
HCCCCCCHHHHHHHH
42.6827251275
243PhosphorylationAGGRSSSSKQRKELG
CCCCCCHHHHHHHHC
34.4518510355
257PhosphorylationGGLEGDPSPEEDEGI
CCCCCCCCHHHCCCC
50.0828450419
268PhosphorylationDEGIQKASPLTHSPP
CCCCCCCCCCCCCCC
27.7228985074
268O-linked_GlycosylationDEGIQKASPLTHSPP
CCCCCCCCCCCCCCC
27.72OGP
271O-linked_GlycosylationIQKASPLTHSPPDEL
CCCCCCCCCCCCCCC
24.5655829845
271PhosphorylationIQKASPLTHSPPDEL
CCCCCCCCCCCCCCC
24.5628450419
273PhosphorylationKASPLTHSPPDEL--
CCCCCCCCCCCCC--
32.6628450419

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 CNPY3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNPY3_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 CNPY3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PXDN_HUMANPXDNphysical
26186194
LRRC1_HUMANLRRC1physical
26186194
SCRIB_HUMANSCRIBphysical
26186194
GT252_HUMANCOLGALT2physical
26186194
SELN_HUMANSEPN1physical
26186194
LRC40_HUMANLRRC40physical
26186194
COEA1_HUMANCOL14A1physical
26186194
SELT_HUMANSELTphysical
26186194
LRC40_HUMANLRRC40physical
28514442
PXDN_HUMANPXDNphysical
28514442
LRIG1_HUMANLRIG1physical
28514442
SELT_HUMANSELTphysical
28514442
SCRIB_HUMANSCRIBphysical
28514442
COEA1_HUMANCOL14A1physical
28514442
GT252_HUMANCOLGALT2physical
28514442
LRRC1_HUMANLRRC1physical
28514442

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 CNPY3_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-153, AND MASSSPECTROMETRY.

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