CAN11_HUMAN - dbPTM
CAN11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAN11_HUMAN
UniProt AC Q9UMQ6
Protein Name Calpain-11
Gene Name CAPN11
Organism Homo sapiens (Human).
Sequence Length 739
Subcellular Localization Cytoplasmic vesicle, secretory vesicle, acrosome.
Protein Description Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction..
Protein Sequence MLYSPGPSLPESAESLDGSQEDKPRGSCAEPTFTDTGMVAHINNSRLKAKGVGQHDNAQNFGNQSFEELRAACLRKGELFEDPLFPAEPSSLGFKDLGPNSKNVQNISWQRPKDIINNPLFIMDGISPTDICQGILGDCWLLAAIGSLTTCPKLLYRVVPRGQSFKKNYAGIFHFQIWQFGQWVNVVVDDRLPTKNDKLVFVHSTERSEFWSALLEKAYAKLSGSYEALSGGSTMEGLEDFTGGVAQSFQLQRPPQNLLRLLRKAVERSSLMGCSIEVTSDSELESMTDKMLVRGHAYSVTGLQDVHYRGKMETLIRVRNPWGRIEWNGAWSDSAREWEEVASDIQMQLLHKTEDGEFWMSYQDFLNNFTLLEICNLTPDTLSGDYKSYWHTTFYEGSWRRGSSAGGCRNHPGTFWTNPQFKISLPEGDDPEDDAEGNVVVCTCLVALMQKNWRHARQQGAQLQTIGFVLYAVPKEFQNIQDVHLKKEFFTKYQDHGFSEIFTNSREVSSQLRLPPGEYIIIPSTFEPHRDADFLLRVFTEKHSESWELDEVNYAEQLQEEKVSEDDMDQDFLHLFKIVAGEGKEIGVYELQRLLNRMAIKFKSFKTKGFGLDACRCMINLMDKDGSGKLGLLEFKILWKKLKKWMDIFRECDQDHSGTLNSYEMRLVIEKAGIKLNNKVMQVLVARYADDDLIIDFDSFISCFLRLKTMFTFFLTMDPKNTGHICLSLEQWLQMTMWG
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
65PhosphorylationAQNFGNQSFEELRAA
CHHHCCCCHHHHHHH
38.3323186163
314PhosphorylationHYRGKMETLIRVRNP
EECCEEEEEEEEECC
24.8020071362
361PhosphorylationEDGEFWMSYQDFLNN
CCCCEEECHHHHHHC
15.3925954137
362PhosphorylationDGEFWMSYQDFLNNF
CCCEEECHHHHHHCC
8.9425954137
378PhosphorylationLLEICNLTPDTLSGD
CHHHHCCCCCCCCCC
12.7225954137
381PhosphorylationICNLTPDTLSGDYKS
HHCCCCCCCCCCCCC
24.8325954137
404PhosphorylationGSWRRGSSAGGCRNH
CCCCCCCCCCCCCCC
33.48-
493PhosphorylationKKEFFTKYQDHGFSE
CHHHHHHHCCCCCCH
19.00-
499PhosphorylationKYQDHGFSEIFTNSR
HHCCCCCCHHCCCCC
34.08-
509PhosphorylationFTNSREVSSQLRLPP
CCCCCHHHHCCCCCC
13.96-
510PhosphorylationTNSREVSSQLRLPPG
CCCCHHHHCCCCCCC
38.11-
679AcetylationAGIKLNNKVMQVLVA
HCCCCCHHHHHHHHH
37.707378787
709PhosphorylationSCFLRLKTMFTFFLT
HHHHHHHHHHHEEEE
23.3127135362
712PhosphorylationLRLKTMFTFFLTMDP
HHHHHHHHEEEECCC
11.5827135362
716PhosphorylationTMFTFFLTMDPKNTG
HHHHEEEECCCCCCC
17.8627135362

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 CAN11_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAN11_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 CAN11_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRCC6_HUMANXRCC6physical
21988832
KAP0_HUMANPRKAR1Aphysical
21988832
UNG_HUMANUNGphysical
21988832
SK2L2_HUMANSKIV2L2physical
26344197

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAN11_HUMAN

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Related Literatures of Post-Translational Modification

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