CNPY2_HUMAN - dbPTM
CNPY2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNPY2_HUMAN
UniProt AC Q9Y2B0
Protein Name Protein canopy homolog 2
Gene Name CNPY2
Organism Homo sapiens (Human).
Sequence Length 182
Subcellular Localization Endoplasmic reticulum .
Protein Description Positive regulator of neurite outgrowth by stabilizing myosin regulatory light chain (MRLC). It prevents MIR-mediated MRLC ubiquitination and its subsequent proteasomal degradation..
Protein Sequence MKGWGWLALLLGALLGTAWARRSQDLHCGACRALVDELEWEIAQVDPKKTIQMGSFRINPDGSQSVVEVPYARSEAHLTELLEEICDRMKEYGEQIDPSTHRKNYVRVVGRNGESSELDLQGIRIDSDISGTLKFACESIVEEYEDELIEFFSREADNVKDKLCSKRTDLCDHALHISHDEL
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
23PhosphorylationGTAWARRSQDLHCGA
HHHHHHHCCCCCCHH
23.61-
48UbiquitinationEIAQVDPKKTIQMGS
EEEECCCCCCEEEEE
59.0722817900
48 (in isoform 2)Ubiquitination-59.0721906983
48 (in isoform 1)Ubiquitination-59.0721906983
48AcetylationEIAQVDPKKTIQMGS
EEEECCCCCCEEEEE
59.077493417
49UbiquitinationIAQVDPKKTIQMGSF
EEECCCCCCEEEEEE
57.1422817900
49AcetylationIAQVDPKKTIQMGSF
EEECCCCCCEEEEEE
57.14130663
50PhosphorylationAQVDPKKTIQMGSFR
EECCCCCCEEEEEEE
23.6721406692
55PhosphorylationKKTIQMGSFRINPDG
CCCEEEEEEEECCCC
13.1523663014
63PhosphorylationFRINPDGSQSVVEVP
EEECCCCCCEEEECC
27.0223663014
65PhosphorylationINPDGSQSVVEVPYA
ECCCCCCEEEECCCC
29.8123663014
71PhosphorylationQSVVEVPYARSEAHL
CEEEECCCCCCHHHH
21.5923663014
86GlutathionylationTELLEEICDRMKEYG
HHHHHHHHHHHHHHH
2.8422555962
902-HydroxyisobutyrylationEEICDRMKEYGEQID
HHHHHHHHHHHHHCC
48.99-
90UbiquitinationEEICDRMKEYGEQID
HHHHHHHHHHHHHCC
48.9924816145
92PhosphorylationICDRMKEYGEQIDPS
HHHHHHHHHHHCCCC
22.0520068231
99PhosphorylationYGEQIDPSTHRKNYV
HHHHCCCCCCCCCEE
32.8525159151
100PhosphorylationGEQIDPSTHRKNYVR
HHHCCCCCCCCCEEE
30.9620068231
105PhosphorylationPSTHRKNYVRVVGRN
CCCCCCCEEEEECCC
7.8324719451
115PhosphorylationVVGRNGESSELDLQG
EECCCCCCCCEECCC
30.4319664994
116PhosphorylationVGRNGESSELDLQGI
ECCCCCCCCEECCCE
37.5729255136
127PhosphorylationLQGIRIDSDISGTLK
CCCEEECCCCCHHHH
34.1821815630
130PhosphorylationIRIDSDISGTLKFAC
EEECCCCCHHHHHHH
30.6221712546
137GlutathionylationSGTLKFACESIVEEY
CHHHHHHHHHHHHHH
4.7922555962
160SuccinylationSREADNVKDKLCSKR
HHCCCCHHHHHHCCC
56.2323954790
162UbiquitinationEADNVKDKLCSKRTD
CCCCHHHHHHCCCHH
45.7524816145
171GlutathionylationCSKRTDLCDHALHIS
HCCCHHHCCHHHHCC
3.9222555962
178PhosphorylationCDHALHISHDEL---
CCHHHHCCCCCC---
17.7127050516

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 CNPY2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNPY2_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 CNPY2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
MAP1S_HUMANMAP1Sphysical
26344197
KIF22_HUMANKIF22physical
28514442
DLG3_HUMANDLG3physical
28514442
VWA1_HUMANVWA1physical
28514442
CTC1_HUMANCTC1physical
28514442
PDIA5_HUMANPDIA5physical
28514442
FBXL4_HUMANFBXL4physical
28514442
CO2A1_HUMANCOL2A1physical
28514442
STN1_HUMANOBFC1physical
28514442
GNB1L_HUMANGNB1Lphysical
28514442
WIPI3_HUMANWDR45Bphysical
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 CNPY2_HUMAN

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Related Literatures of Post-Translational Modification

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