CAN2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CAN2_HUMAN
• UniProt AC: P17655
• Protein Name: Calpain-2 catalytic subunit
• Gene Name: CAPN2
• Organism: Homo sapiens (Human).
• 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'. [PubMed: 17650508 Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs (By similarity]
• Protein Sequence: MAGIAAKLAKDREAAEGLGSHDRAIKYLNQDYEALRNECLEAGTLFQDPSFPAIPSALGFKELGPYSSKTRGIEWKRPTEICADPQFIIGGATRTDICQGALGDCWLLAAIASLTLNEEILARVVPLNQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAEGSEFWSALLEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELKKPPPNLFKIIQKALQKGSLLGCSIDITSAADSEAITFQKLVKGHAYSVTGAEEVESNGSLQKLIRIRNPWGEVEWTGRWNDNCPSWNTIDPEERERLTRRHEDGEFWMSFSDFLRHYSRLEICNLTPDTLTSDTYKKWKLTKMDGNWRRGSTAGGCRNYPNTFWMNPQYLIKLEEEDEDEEDGESGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELSGQTNIHLSKNFFLTNRARERSDTFINLREVLNRFKLPPGEYILVPSTFEPNKDGDFCIRVFSEKKADYQAVDDEIEANLEEFDISEDDIDDGFRRLFAQLAGEDAEISAFELQTILRRVLAKRQDIKSDGFSIETCKIMVDMLDSDGSGKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKMPCQLHQVIVARFADDQLIIDFDNFVRCLVRLETLFKIFKQLDPENTGTIELDLISWLCFSVL

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	------MAGIAAKLA ------CCCHHHHHH	20.35	22814378
7	Acetylation	-MAGIAAKLAKDREA -CCCHHHHHHHHHHH	39.70	23236377
23	Methylation	EGLGSHDRAIKYLNQ HCCCCHHHHHHHHHH	32.56	-
26	Ubiquitination	GSHDRAIKYLNQDYE CCHHHHHHHHHHHHH	42.58	21890473
32	Phosphorylation	IKYLNQDYEALRNEC HHHHHHHHHHHHHHH	8.04	27642862
50	Phosphorylation	GTLFQDPSFPAIPSA CCCCCCCCCCCCCHH	52.75	14993287
61	Acetylation	IPSALGFKELGPYSS CCHHCCCHHHCCCCC	50.67	156195
61	Ubiquitination	IPSALGFKELGPYSS CCHHCCCHHHCCCCC	50.67	-
67	Phosphorylation	FKELGPYSSKTRGIE CHHHCCCCCCCCCCC	28.61	29514088
68	Phosphorylation	KELGPYSSKTRGIEW HHHCCCCCCCCCCCC	32.00	25159151
69	Ubiquitination	ELGPYSSKTRGIEWK HHCCCCCCCCCCCCC	35.98	21890473
76	Acetylation	KTRGIEWKRPTEICA CCCCCCCCCCCCCCC	35.39	26051181
82	Glutathionylation	WKRPTEICADPQFII CCCCCCCCCCCCEEE	2.60	22555962
82	S-nitrosylation	WKRPTEICADPQFII CCCCCCCCCCCCEEE	2.60	2212679
182 (in isoform 2)	Ubiquitination	-	36.17	-
219	Ubiquitination	AEWYELKKPPPNLFK HHHHHCCCCCCCHHH	75.32	-
230	Ubiquitination	NLFKIIQKALQKGSL CHHHHHHHHHHCCCC	40.43	-
230	Malonylation	NLFKIIQKALQKGSL CHHHHHHHHHHCCCC	40.43	26320211
234	Ubiquitination	IIQKALQKGSLLGCS HHHHHHHCCCCCCCE	51.85	-
257	Ubiquitination	SEAITFQKLVKGHAY CCCEEHHHHHCCCCE	51.56	-
260	Acetylation	ITFQKLVKGHAYSVT EEHHHHHCCCCEECC	56.25	26051181
260	Malonylation	ITFQKLVKGHAYSVT EEHHHHHCCCCEECC	56.25	26320211
260	Ubiquitination	ITFQKLVKGHAYSVT EEHHHHHCCCCEECC	56.25	21890473
264	Phosphorylation	KLVKGHAYSVTGAEE HHHCCCCEECCCCEE	9.67	28152594
265	Phosphorylation	LVKGHAYSVTGAEEV HHCCCCEECCCCEEE	17.62	28152594
267	Phosphorylation	KGHAYSVTGAEEVES CCCCEECCCCEEECC	25.41	28152594
274	Phosphorylation	TGAEEVESNGSLQKL CCCEEECCCCCEEEE	52.22	27251275
277	Phosphorylation	EEVESNGSLQKLIRI EEECCCCCEEEEEEE	31.70	27251275
280	Acetylation	ESNGSLQKLIRIRNP CCCCCEEEEEEEECC	51.69	26051181
280	Malonylation	ESNGSLQKLIRIRNP CCCCCEEEEEEEECC	51.69	26320211
280	Ubiquitination	ESNGSLQKLIRIRNP CCCCCEEEEEEEECC	51.69	21906983
326	Sulfoxidation	HEDGEFWMSFSDFLR CCCCCEEECHHHHHH	3.35	30846556
344	Phosphorylation	RLEICNLTPDTLTSD CCCCCCCCCCCCCCC	12.72	21406692
347	Phosphorylation	ICNLTPDTLTSDTYK CCCCCCCCCCCCHHH	32.89	21406692
349	Phosphorylation	NLTPDTLTSDTYKKW CCCCCCCCCCHHHCE	27.01	21406692
350	Phosphorylation	LTPDTLTSDTYKKWK CCCCCCCCCHHHCEE	30.94	21406692
352	Phosphorylation	PDTLTSDTYKKWKLT CCCCCCCHHHCEEEE	36.69	21406692
353	Phosphorylation	DTLTSDTYKKWKLTK CCCCCCHHHCEEEEE	18.63	28152594
354	Ubiquitination	TLTSDTYKKWKLTKM CCCCCHHHCEEEEEC	55.01	-
354	Acetylation	TLTSDTYKKWKLTKM CCCCCHHHCEEEEEC	55.01	7609103
355	Acetylation	LTSDTYKKWKLTKMD CCCCHHHCEEEEECC	38.86	15609665
359	Phosphorylation	TYKKWKLTKMDGNWR HHHCEEEEECCCCCC	22.16	21601212
360	Ubiquitination	YKKWKLTKMDGNWRR HHCEEEEECCCCCCC	45.49	21906983
369	Phosphorylation	DGNWRRGSTAGGCRN CCCCCCCCCCCCCCC	17.17	27273156
370	Phosphorylation	GNWRRGSTAGGCRNY CCCCCCCCCCCCCCC	31.95	27251275
377	Phosphorylation	TAGGCRNYPNTFWMN CCCCCCCCCCCCEEC	4.40	27251275
380	Phosphorylation	GCRNYPNTFWMNPQY CCCCCCCCCEECHHH	17.73	27251275
383	Sulfoxidation	NYPNTFWMNPQYLIK CCCCCCEECHHHEEE	4.59	30846556
390	Sumoylation	MNPQYLIKLEEEDED ECHHHEEECCCCCCC	47.45	-
390	Sumoylation	MNPQYLIKLEEEDED ECHHHEEECCCCCCC	47.45	-
398 (in isoform 2)	Ubiquitination	-	56.81	-
403	Phosphorylation	EDEEDGESGCTFLVG CCCCCCCCCHHHHHH	44.70	21712546
405	Glutathionylation	EEDGESGCTFLVGLI CCCCCCCHHHHHHHH	3.19	22555962
406	Phosphorylation	EDGESGCTFLVGLIQ CCCCCCHHHHHHHHH	24.43	27251275
414	Acetylation	FLVGLIQKHRRRQRK HHHHHHHHHHHHHHH	31.89	26051181
414	Ubiquitination	FLVGLIQKHRRRQRK HHHHHHHHHHHHHHH	31.89	-
434	Phosphorylation	HTIGFGIYEVPEELS CCCCCEEEECCHHHC	15.97	27642862
450	Ubiquitination	QTNIHLSKNFFLTNR CCCEEEECCEEECCC	65.22	-
462	Phosphorylation	TNRARERSDTFINLR CCCHHHHCCCEECHH	35.93	29255136
464	Phosphorylation	RARERSDTFINLREV CHHHHCCCEECHHHH	27.88	29255136
476	Ubiquitination	REVLNRFKLPPGEYI HHHHHHCCCCCCCEE	57.77	21890473
568	Ubiquitination	LAKRQDIKSDGFSIE HHHCCCCCCCCCEEE	51.27	-
569	Phosphorylation	AKRQDIKSDGFSIET HHCCCCCCCCCEEEE	43.21	21712546
577	S-nitrosylation	DGFSIETCKIMVDML CCCEEEEEEEEEEEE	1.50	2212679
580	Sulfoxidation	SIETCKIMVDMLDSD EEEEEEEEEEEECCC	0.97	30846556
583	Sulfoxidation	TCKIMVDMLDSDGSG EEEEEEEEECCCCCC	2.81	30846556
586	Phosphorylation	IMVDMLDSDGSGKLG EEEEEECCCCCCCCC	39.65	-
589	Phosphorylation	DMLDSDGSGKLGLKE EEECCCCCCCCCCEE	37.43	21712546
591	Ubiquitination	LDSDGSGKLGLKEFY ECCCCCCCCCCEEEH	40.87	-
595	Ubiquitination	GSGKLGLKEFYILWT CCCCCCCEEEHHHHH	43.93	-
596 (in isoform 2)	Ubiquitination	-	49.04	-
607	Phosphorylation	LWTKIQKYQKIYREI HHHHHHHHHHHHHHC	9.92	26074081
611	Phosphorylation	IQKYQKIYREIDVDR HHHHHHHHHHCCCCC	14.83	26074081
619	Phosphorylation	REIDVDRSGTMNSYE HHCCCCCCCCCCHHH	33.87	26074081
621	Phosphorylation	IDVDRSGTMNSYEMR CCCCCCCCCCHHHHH	17.90	26074081
624	Phosphorylation	DRSGTMNSYEMRKAL CCCCCCCHHHHHHHH	16.20	26074081
625	Phosphorylation	RSGTMNSYEMRKALE CCCCCCHHHHHHHHH	14.56	26074081
629	Ubiquitination	MNSYEMRKALEEAGF CCHHHHHHHHHHCCC	56.89	-
637	Acetylation	ALEEAGFKMPCQLHQ HHHHCCCCCCCEEEH	40.80	26051181
637	Ubiquitination	ALEEAGFKMPCQLHQ HHHHCCCCCCCEEEH	40.80	-
638	Sulfoxidation	LEEAGFKMPCQLHQV HHHCCCCCCCEEEHH	3.61	30846556
674	Ubiquitination	VRLETLFKIFKQLDP HHHHHHHHHHHHCCC	50.80	21890473

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	MAPK1	P28482	GPS
50	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
369	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
369	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
369	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
370	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
370	T	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
370	T	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CAN2_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CPNS1_HUMAN	CAPNS1	physical	11517928
BCL2_HUMAN	BCL2	physical	12000759
BID_HUMAN	BID	physical	12000759
PTPRN_HUMAN	PTPRN	physical	11483505
TAU_HUMAN	MAPT	physical	14993287
ASNS_HUMAN	ASNS	physical	22863883
PUR9_HUMAN	ATIC	physical	22863883
LIS1_HUMAN	PAFAH1B1	physical	22863883
PAPS1_HUMAN	PAPSS1	physical	22863883
PLPHP_HUMAN	PROSC	physical	22863883
PTMA_HUMAN	PTMA	physical	22863883
RUXE_HUMAN	SNRPE	physical	22863883
TBB2A_HUMAN	TUBB2A	physical	22863883
EFTU_HUMAN	TUFM	physical	22863883
UBXN1_HUMAN	UBXN1	physical	22863883
XPO1_HUMAN	XPO1	physical	22863883
1433E_HUMAN	YWHAE	physical	22863883
UBC9_HUMAN	UBE2I	physical	23395904
ATG5_HUMAN	ATG5	physical	16998475
ATX3_HUMAN	ATXN3	physical	27731380

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.