CAN2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CAN2_MOUSE
• UniProt AC: O08529
• Protein Name: Calpain-2 catalytic subunit
• Gene Name: Capn2
• Organism: Mus musculus (Mouse).
• Sequence Length: 700
• Subcellular Localization: Cytoplasm. Cell membrane. Translocates to the plasma membrane upon Ca(2+) binding..
• Protein Description: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226' (By similarity). Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs. [PubMed: 22711986]
• Protein Sequence: MAGIAIKLAKDREAAEGLGSHERAIKYLNQDYETLRNECLEAGALFQDPSFPALPSSLGYKELGPYSSKTRGIEWKRPTEICADPQFIIGGATRTDICQGALGDCWLLAAIASLTLNEEILARVVPPDQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAEGSEFWSALLEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELRKPPPNLFKIIQKALEKGSLLGCSIDITSAADSEAVTYQKLVKGHAYSVTGAEEVESSGSLQKLIRIRNPWGQVEWTGKWNDNCPSWNTVDPEVRANLTERQEDGEFWMSFSDFLRHYSRLEICNLTPDTLTCDSYKKWKLTKMDGNWRRGSTAGGCRNYPNTFWMNPQYLIKLEEEDEDEEDGERGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELTGQTNIHLGKNFFLTTRARERSDTFINLREVLNRFKLPPGEYVLVPSTFEPHKDGDFCIRVFSEKKADYQAVDDEIEANIEEIDANEEDIDDGFRRLFVQLAGEDAEISAFELQTILRRVLAKRQDIKSDGFSIETCKIMVDMLDEDGSGKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKLPCQLHQVIVARFADDELIIDFDNFVRCLVRLETLFKIFKQLDPENTGTIQLNLASWLSFSVL

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
2	Acetylation	------MAGIAIKLA ------CCCCEEEEH	20.35	-
7	Acetylation	-MAGIAIKLAKDREA -CCCCEEEEHHCHHH	33.11	23236377
26	Acetylation	GSHERAIKYLNQDYE CCHHHHHHHHCCCHH	42.58	22826441
50	Phosphorylation	GALFQDPSFPALPSS HCCCCCCCCCCCCHH	52.75	16809781
67	Phosphorylation	YKELGPYSSKTRGIE CCCCCCCCCCCCCCC	28.61	25338131
68	Phosphorylation	KELGPYSSKTRGIEW CCCCCCCCCCCCCCC	32.00	28464351
76	Acetylation	KTRGIEWKRPTEICA CCCCCCCCCCCCCCC	35.39	22826441
82	Glutathionylation	WKRPTEICADPQFII CCCCCCCCCCCCEEE	2.60	24333276
226	Acetylation	KPPPNLFKIIQKALE CCCCCHHHHHHHHHH	41.91	22826441
230	Acetylation	NLFKIIQKALEKGSL CHHHHHHHHHHCCCC	44.52	22826441
260	Ubiquitination	VTYQKLVKGHAYSVT EEHHHHHCCCCEECC	56.25	-
260	Malonylation	VTYQKLVKGHAYSVT EEHHHHHCCCCEECC	56.25	26320211
260	Acetylation	VTYQKLVKGHAYSVT EEHHHHHCCCCEECC	56.25	23236377
280	Ubiquitination	ESSGSLQKLIRIRNP CCCCCCEEEEEEECC	51.69	22790023
301	Glutathionylation	TGKWNDNCPSWNTVD CCCCCCCCCCCCCCC	2.93	24333276
341	Glutathionylation	HYSRLEICNLTPDTL HHCCCEECCCCCCCC	2.20	24333276
350	Glutathionylation	LTPDTLTCDSYKKWK CCCCCCCCCHHHCEE	3.53	24333276
354	Acetylation	TLTCDSYKKWKLTKM CCCCCHHHCEEEEEC	56.99	7609099
355	Acetylation	LTCDSYKKWKLTKMD CCCCHHHCEEEEECC	41.13	15609661
360	Acetylation	YKKWKLTKMDGNWRR HHCEEEEECCCCCCC	45.49	22826441
369	Phosphorylation	DGNWRRGSTAGGCRN CCCCCCCCCCCCCCC	17.17	-
370	Phosphorylation	GNWRRGSTAGGCRNY CCCCCCCCCCCCCCC	31.95	22817900
377	Phosphorylation	TAGGCRNYPNTFWMN CCCCCCCCCCCCEEC	4.40	-
405	S-nitrosylation	EEDGERGCTFLVGLI CCCCCCCHHHHHHHH	2.81	20925432
405	S-nitrosocysteine	EEDGERGCTFLVGLI CCCCCCCHHHHHHHH	2.81	-
414	Acetylation	FLVGLIQKHRRRQRK HHHHHHHHHHHHHHH	31.89	22826441
462	Phosphorylation	TTRARERSDTFINLR EECHHHCCCCEECHH	35.93	25338131
464	Phosphorylation	RARERSDTFINLREV CHHHCCCCEECHHHH	27.88	27180971
549	Phosphorylation	AGEDAEISAFELQTI HCCCCEECHHHHHHH	20.57	25777480
555	Phosphorylation	ISAFELQTILRRVLA ECHHHHHHHHHHHHH	34.30	26239621
619	Phosphorylation	REIDVDRSGTMNSYE HHCCCCCCCCCCHHH	33.87	20469934
621	Phosphorylation	IDVDRSGTMNSYEMR CCCCCCCCCCHHHHH	17.90	20469934
624	Phosphorylation	DRSGTMNSYEMRKAL CCCCCCCHHHHHHHH	16.20	20469934
625	Phosphorylation	RSGTMNSYEMRKALE CCCCCCHHHHHHHHH	14.56	20469934
637	Acetylation	ALEEAGFKLPCQLHQ HHHHCCCCCCCEEEE	51.07	22826441
640	S-nitrosocysteine	EAGFKLPCQLHQVIV HCCCCCCCEEEEEHH	11.02	-
640	Glutathionylation	EAGFKLPCQLHQVIV HCCCCCCCEEEEEHH	11.02	24333276
640	S-nitrosylation	EAGFKLPCQLHQVIV HCCCCCCCEEEEEHH	11.02	20925432
640	S-palmitoylation	EAGFKLPCQLHQVIV HCCCCCCCEEEEEHH	11.02	26165157
674	Ubiquitination	VRLETLFKIFKQLDP HHHHHHHHHHHHCCC	50.80	22790023

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
50	S	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CAN2_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CAN2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MK01_MOUSE	Mapk1	physical	14993287
TLN1_MOUSE	Tln1	physical	14993287

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.