CNN3_RAT - dbPTM
CNN3_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNN3_RAT
UniProt AC P37397
Protein Name Calponin-3
Gene Name Cnn3
Organism Rattus norvegicus (Rat).
Sequence Length 330
Subcellular Localization
Protein Description Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity..
Protein Sequence MTHFNKGPSYGLSAEVKNKIASKYDQQAEEDLRNWIEEVTGMGIGTNFQLGLKDGIILCELINKLQPGSVKKVNESSLNWPQLENIGNFIKAIQAYGMKPHDIFEANDLFENGNMTQVQTTLVALAGLAKTKGFHTTIDIGVKYAEKQTRRFDEGKLKAGQSVIGLQMGTNKCASQAGMTAYGTRRHLYDPKMQTDKPFDQTTISLQMGTNKGASQAGMSAPGTRRDIYDQKLTLQPVDNSTISLQMGTNKVASQKGMSVYGLGRQVYDPKYCAAPTEPVIHNGSQGTGTNGSEISDSDYQAEYPDEYHGEYPDEYPREYQYGDDQGIDY
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
6Acetylation--MTHFNKGPSYGLS
--CCCCCCCCCCCCC
71.8522902405
23AcetylationVKNKIASKYDQQAEE
HHHHHHHHHHHHHHH
43.77-
156AcetylationTRRFDEGKLKAGQSV
CCCCCCCCCCCCCEE
44.7822902405
158MethylationRFDEGKLKAGQSVIG
CCCCCCCCCCCEEEE
54.69-
162PhosphorylationGKLKAGQSVIGLQMG
CCCCCCCEEEEEECC
18.1323984901
175PhosphorylationMGTNKCASQAGMTAY
CCCCHHHHHHCCCCC
29.9922817900
180PhosphorylationCASQAGMTAYGTRRH
HHHHHCCCCCCCCCC
18.7927097102
182PhosphorylationSQAGMTAYGTRRHLY
HHHCCCCCCCCCCCC
15.1827097102
184PhosphorylationAGMTAYGTRRHLYDP
HCCCCCCCCCCCCCC
16.3227097102
197AcetylationDPKMQTDKPFDQTTI
CCCCCCCCCCCCCEE
51.4722902405
254PhosphorylationMGTNKVASQKGMSVY
ECCCHHHCCCCCCEE
35.1025575281
259PhosphorylationVASQKGMSVYGLGRQ
HHCCCCCCEECCCCC
22.3623984901
261PhosphorylationSQKGMSVYGLGRQVY
CCCCCCEECCCCCCC
10.1827097102
272PhosphorylationRQVYDPKYCAAPTEP
CCCCCCCCCCCCCCC
7.8422673903
277PhosphorylationPKYCAAPTEPVIHNG
CCCCCCCCCCEEECC
48.4722668510
285PhosphorylationEPVIHNGSQGTGTNG
CCEEECCCCCCCCCC
30.6522668510
288PhosphorylationIHNGSQGTGTNGSEI
EECCCCCCCCCCCCC
32.9422668510
290PhosphorylationNGSQGTGTNGSEISD
CCCCCCCCCCCCCCC
35.9222668510
293PhosphorylationQGTGTNGSEISDSDY
CCCCCCCCCCCCCCC
33.5521630457
296PhosphorylationGTNGSEISDSDYQAE
CCCCCCCCCCCCCCC
27.3221630457
298PhosphorylationNGSEISDSDYQAEYP
CCCCCCCCCCCCCCC
31.2822668510
300PhosphorylationSEISDSDYQAEYPDE
CCCCCCCCCCCCCCC
17.3622673903
304PhosphorylationDSDYQAEYPDEYHGE
CCCCCCCCCCCCCCC
20.9922673903
308PhosphorylationQAEYPDEYHGEYPDE
CCCCCCCCCCCCCCC
23.6222673903
312PhosphorylationPDEYHGEYPDEYPRE
CCCCCCCCCCCCCCH
22.1522673903
316PhosphorylationHGEYPDEYPREYQYG
CCCCCCCCCCHHCCC
18.2522673903

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
261YPhosphorylationKinaseFYNP06241
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNN3_RAT !!

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 CNN3_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MK03_RATMapk3physical
20181831
MK01_RATMapk1physical
20181831

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CNN3_RAT

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Related Literatures of Post-Translational Modification

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