CAN3_HUMAN - dbPTM
CAN3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAN3_HUMAN
UniProt AC P20807
Protein Name Calpain-3
Gene Name CAPN3
Organism Homo sapiens (Human).
Sequence Length 821
Subcellular Localization Cytoplasm.
Protein Description Calcium-regulated non-lysosomal thiol-protease..
Protein Sequence MPTVISASVAPRTAAEPRSPGPVPHPAQSKATEAGGGNPSGIYSAIISRNFPIIGVKEKTFEQLHKKCLEKKVLYVDPEFPPDETSLFYSQKFPIQFVWKRPPEICENPRFIIDGANRTDICQGELGDCWFLAAIACLTLNQHLLFRVIPHDQSFIENYAGIFHFQFWRYGEWVDVVIDDCLPTYNNQLVFTKSNHRNEFWSALLEKAYAKLHGSYEALKGGNTTEAMEDFTGGVAEFFEIRDAPSDMYKIMKKAIERGSLMGCSIDDGTNMTYGTSPSGLNMGELIARMVRNMDNSLLQDSDLDPRGSDERPTRTIIPVQYETRMACGLVRGHAYSVTGLDEVPFKGEKVKLVRLRNPWGQVEWNGSWSDRWKDWSFVDKDEKARLQHQVTEDGEFWMSYEDFIYHFTKLEICNLTADALQSDKLQTWTVSVNEGRWVRGCSAGGCRNFPDTFWTNPQYRLKLLEEDDDPDDSEVICSFLVALMQKNRRKDRKLGASLFTIGFAIYEVPKEMHGNKQHLQKDFFLYNASKARSKTYINMREVSQRFRLPPSEYVIVPSTYEPHQEGEFILRVFSEKRNLSEEVENTISVDRPVKKKKTKPIIFVSDRANSNKELGVDQESEEGKGKTSPDKQKQSPQPQPGSSDQESEEQQQFRNIFKQIAGDDMEICADELKKVLNTVVNKHKDLKTHGFTLESCRSMIALMDTDGSGKLNLQEFHHLWNKIKAWQKIFKHYDTDQSGTINSYEMRNAVNDAGFHLNNQLYDIITMRYADKHMNIDFDSFICCFVRLEGMFRAFHAFDKDGDGIIKLNVLEWLQLTMYA
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-----MPTVISASVA
-----CCCEEEEECC
29.2221712546
6Phosphorylation--MPTVISASVAPRT
--CCCEEEEECCCCC
15.3424043423
8PhosphorylationMPTVISASVAPRTAA
CCCEEEEECCCCCCC
16.4221712546
13PhosphorylationSASVAPRTAAEPRSP
EEECCCCCCCCCCCC
29.2126437602
19PhosphorylationRTAAEPRSPGPVPHP
CCCCCCCCCCCCCCC
44.9419764811
202O-linked_GlycosylationNHRNEFWSALLEKAY
CCCHHHHHHHHHHHH
17.8529351928
279PhosphorylationMTYGTSPSGLNMGEL
CCCCCCCCCCCHHHH
56.53-
417PhosphorylationKLEICNLTADALQSD
HHHEECCCHHHHHCC
14.4320068231
423PhosphorylationLTADALQSDKLQTWT
CCHHHHHCCCCCEEE
37.2520068231
428PhosphorylationLQSDKLQTWTVSVNE
HHCCCCCEEEEEEEC
33.2720068231
430PhosphorylationSDKLQTWTVSVNEGR
CCCCCEEEEEEECCC
13.2920068231
432PhosphorylationKLQTWTVSVNEGRWV
CCCEEEEEEECCCEE
16.3220068231
559PhosphorylationSEYVIVPSTYEPHQE
HHEEEECCCCCCCCC
32.50-
581PhosphorylationFSEKRNLSEEVENTI
HHCCCCCCHHHHHHC
34.9530206219
587PhosphorylationLSEEVENTISVDRPV
CCHHHHHHCCCCCCC
10.9230206219
589PhosphorylationEEVENTISVDRPVKK
HHHHHHCCCCCCCCC
18.8730206219
599PhosphorylationRPVKKKKTKPIIFVS
CCCCCCCCCCEEEEE
51.43-
621PhosphorylationELGVDQESEEGKGKT
CCCCCCCCCCCCCCC
35.0026437602
629PhosphorylationEEGKGKTSPDKQKQS
CCCCCCCCCCCCCCC
34.2926437602
636PhosphorylationSPDKQKQSPQPQPGS
CCCCCCCCCCCCCCC
32.32-
699PhosphorylationFTLESCRSMIALMDT
CCHHHHHHHEEEECC
20.90-
709PhosphorylationALMDTDGSGKLNLQE
EEECCCCCCCCCHHH
35.25-
729UbiquitinationNKIKAWQKIFKHYDT
HHHHHHHHHHHHCCC
39.13-
734PhosphorylationWQKIFKHYDTDQSGT
HHHHHHHCCCCCCCC
22.5624043423
736PhosphorylationKIFKHYDTDQSGTIN
HHHHHCCCCCCCCCC
28.8624043423
739PhosphorylationKHYDTDQSGTINSYE
HHCCCCCCCCCCHHH
40.4924043423
741PhosphorylationYDTDQSGTINSYEMR
CCCCCCCCCCHHHHH
23.4124043423
744PhosphorylationDQSGTINSYEMRNAV
CCCCCCCHHHHHHHH
20.7224043423
745PhosphorylationQSGTINSYEMRNAVN
CCCCCCHHHHHHHHH
14.8424043423

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 CAN3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAN3_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 CAN3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TITIN_HUMANTTNphysical
9642272
NECA2_HUMANNECAB2physical
16189514
FLNC_HUMANFLNCphysical
14506720
TITIN_HUMANTTNphysical
8537379
OSGI1_HUMANOSGIN1physical
25416956
NTAQ1_HUMANWDYHV1physical
25416956
SYYM_HUMANYARS2physical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
253600Limb-girdle muscular dystrophy 2A (LGMD2A)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAN3_HUMAN

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Related Literatures of Post-Translational Modification

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