dbPTM

CAN1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CAN1_HUMAN
UniProt AC	P07384
Protein Name	Calpain-1 catalytic subunit {ECO:0000305}
Gene Name	CAPN1 {ECO:0000312\|HGNC:HGNC:1476}
Organism	Homo sapiens (Human).
Sequence Length	714
Subcellular Localization	Cytoplasm . Cell membrane . Translocates to the plasma membrane upon Ca(2+) binding. In granular keratinocytes and in lower corneocytes, colocalizes with FLG and FLG2 (PubMed:21531719).
Protein Description	Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction..
Protein Sequence	MSEEIITPVYCTGVSAQVQKQRARELGLGRHENAIKYLGQDYEQLRVRCLQSGTLFRDEAFPPVPQSLGYKDLGPNSSKTYGIKWKRPTELLSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNDTLLHRVVPHGQSFQNGYAGIFHFQLWQFGEWVDVVVDDLLPIKDGKLVFVHSAEGNEFWSALLEKAYAKVNGSYEALSGGSTSEGFEDFTGGVTEWYELRKAPSDLYQIILKALERGSLLGCSIDISSVLDMEAITFKKLVKGHAYSVTGAKQVNYRGQVVSLIRMRNPWGEVEWTGAWSDSSSEWNNVDPYERDQLRVKMEDGEFWMSFRDFMREFTRLEICNLTPDALKSRTIRKWNTTLYEGTWRRGSTAGGCRNYPATFWVNPQFKIRLDETDDPDDYGDRESGCSFVLALMQKHRRRERRFGRDMETIGFAVYEVPPELVGQPAVHLKRDFFLANASRARSEQFINLREVSTRFRLPPGEYVVVPSTFEPNKEGDFVLRFFSEKSAGTVELDDQIQANLPDEQVLSEEEIDENFKALFRQLAGEDMEISVKELRTILNRIISKHKDLRTKGFSLESCRSMVNLMDRDGNGKLGLVEFNILWNRIRNYLSIFRKFDLDKSGSMSAYEMRMAIESAGFKLNKKLYELIITRYSEPDLAVDFDNFVCCLVRLETMFRFFKTLDTDLDGVVTFDLFKWLQLTMFA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSEEIITPV ------CCCCCCCCE	43.89	30108239
2	Acetylation	------MSEEIITPV ------CCCCCCCCE	43.89	19413330
20	Ubiquitination	GVSAQVQKQRARELG CHHHHHHHHHHHHCC	42.78	-
36	Ubiquitination	GRHENAIKYLGQDYE CCHHHHHHHHCCCHH	31.82	21906983
37	Phosphorylation	RHENAIKYLGQDYEQ CHHHHHHHHCCCHHH	15.22	29496907
42	Phosphorylation	IKYLGQDYEQLRVRC HHHHCCCHHHHHHHH	9.55	28796482
52	Phosphorylation	LRVRCLQSGTLFRDE HHHHHHHCCCCCCCC	22.31	24505115
54	Phosphorylation	VRCLQSGTLFRDEAF HHHHHCCCCCCCCCC	28.15	24505115
71	Ubiquitination	VPQSLGYKDLGPNSS CCCCCCCCCCCCCCC	44.68	21906983
77	Phosphorylation	YKDLGPNSSKTYGIK CCCCCCCCCCCCCCC	36.02	12843408
78	Phosphorylation	KDLGPNSSKTYGIKW CCCCCCCCCCCCCCC	35.34	12843408
79	Ubiquitination	DLGPNSSKTYGIKWK CCCCCCCCCCCCCCC	45.66	21906983
80	Phosphorylation	LGPNSSKTYGIKWKR CCCCCCCCCCCCCCC	29.00	12843408
81	Phosphorylation	GPNSSKTYGIKWKRP CCCCCCCCCCCCCCC	22.16	12843408
84	Ubiquitination	SSKTYGIKWKRPTEL CCCCCCCCCCCCHHH	42.15	21906983
84	Acetylation	SSKTYGIKWKRPTEL CCCCCCCCCCCCHHH	42.15	19608861
86	Ubiquitination	KTYGIKWKRPTELLS CCCCCCCCCCHHHHC	43.42	-
89	Phosphorylation	GIKWKRPTELLSNPQ CCCCCCCHHHHCCCE	43.21	28450419
93	Phosphorylation	KRPTELLSNPQFIVD CCCHHHHCCCEEEEC	60.12	26657352
193	Ubiquitination	FWSALLEKAYAKVNG HHHHHHHHHHHHHCC	46.82	21906983
229	Ubiquitination	TEWYELRKAPSDLYQ CCHHHHHCCCCHHHH	76.81	21906983
229	Trimethylation	TEWYELRKAPSDLYQ CCHHHHHCCCCHHHH	76.81	-
229	Methylation	TEWYELRKAPSDLYQ CCHHHHHCCCCHHHH	76.81	-
232	Phosphorylation	YELRKAPSDLYQIIL HHHHCCCCHHHHHHH	45.14	26657352
235	Phosphorylation	RKAPSDLYQIILKAL HCCCCHHHHHHHHHH	11.58	28152594
240	Ubiquitination	DLYQIILKALERGSL HHHHHHHHHHHHCCC	40.28	-
251	Phosphorylation	RGSLLGCSIDISSVL HCCCCCCCCCHHHHC	22.84	24719451
255	Phosphorylation	LGCSIDISSVLDMEA CCCCCCHHHHCCCCE	15.62	-
256	Phosphorylation	GCSIDISSVLDMEAI CCCCCHHHHCCCCEE	27.34	24719451
270	Acetylation	ITFKKLVKGHAYSVT EEHHHHHCCCCEEEE	56.25	25953088
270	Ubiquitination	ITFKKLVKGHAYSVT EEHHHHHCCCCEEEE	56.25	-
280	Ubiquitination	AYSVTGAKQVNYRGQ CEEEECCEEECCCCE	57.00	21906983
290	Phosphorylation	NYRGQVVSLIRMRNP CCCCEEEEEEEEECC	21.15	26437602
328	Ubiquitination	ERDQLRVKMEDGEFW HHHHEEEEECCCCCE	30.09	21906983
337	Phosphorylation	EDGEFWMSFRDFMRE CCCCCEEHHHHHHHH	14.02	24719451
354	Phosphorylation	RLEICNLTPDALKSR CHHHHCCCHHHHHHC	12.72	27153400
359	Malonylation	NLTPDALKSRTIRKW CCCHHHHHHCCCCCC	39.34	26320211
359	Acetylation	NLTPDALKSRTIRKW CCCHHHHHHCCCCCC	39.34	25953088
359	Ubiquitination	NLTPDALKSRTIRKW CCCHHHHHHCCCCCC	39.34	-
360	Phosphorylation	LTPDALKSRTIRKWN CCHHHHHHCCCCCCC	35.19	12843408
362	Phosphorylation	PDALKSRTIRKWNTT HHHHHHCCCCCCCCE	32.02	12843408
365	Ubiquitination	LKSRTIRKWNTTLYE HHHCCCCCCCCEEEE	40.73	21890473
368	Phosphorylation	RTIRKWNTTLYEGTW CCCCCCCCEEEEEEC	19.64	23882029
369	Phosphorylation	TIRKWNTTLYEGTWR CCCCCCCEEEEEECC	24.91	28152594
371	Phosphorylation	RKWNTTLYEGTWRRG CCCCCEEEEEECCCC	15.38	20090780
374	Phosphorylation	NTTLYEGTWRRGSTA CCEEEEEECCCCCCC	12.12	28152594
379	Phosphorylation	EGTWRRGSTAGGCRN EEECCCCCCCCCCCC	17.17	27273156
380	Phosphorylation	GTWRRGSTAGGCRNY EECCCCCCCCCCCCC	31.95	12843408
387	Phosphorylation	TAGGCRNYPATFWVN CCCCCCCCCEEEEEC	3.79	20090780
390	Phosphorylation	GCRNYPATFWVNPQF CCCCCCEEEEECCCE	17.33	23882029
398	Ubiquitination	FWVNPQFKIRLDETD EEECCCEEEECCCCC	22.97	21890473
404	Phosphorylation	FKIRLDETDDPDDYG EEEECCCCCCCCCCC	45.42	-
410	Phosphorylation	ETDDPDDYGDRESGC CCCCCCCCCCCHHHH	28.45	23532336
415	Phosphorylation	DDYGDRESGCSFVLA CCCCCCHHHHHHHHH	46.09	-
418	Phosphorylation	GDRESGCSFVLALMQ CCCHHHHHHHHHHHH	23.16	-
438	Sulfoxidation	ERRFGRDMETIGFAV HHHHCCCHHHHEEEE	4.76	30846556
446	Phosphorylation	ETIGFAVYEVPPELV HHHEEEEEECCHHHC	14.05	12843408
461	Ubiquitination	GQPAVHLKRDFFLAN CCCEEECCCCCHHHC	34.74	21906983
470	Phosphorylation	DFFLANASRARSEQF CCHHHCCHHHHCHHH	26.70	28060719
474	Phosphorylation	ANASRARSEQFINLR HCCHHHHCHHHCCHH	34.46	28450419
494	Phosphorylation	FRLPPGEYVVVPSTF CCCCCCCEEEECCCC	12.40	-
499	Phosphorylation	GEYVVVPSTFEPNKE CCEEEECCCCCCCCC	33.83	20071362
505	Ubiquitination	PSTFEPNKEGDFVLR CCCCCCCCCCCEEEE	74.02	21890473
539	Phosphorylation	LPDEQVLSEEEIDEN CCCHHCCCHHHHHHH	44.07	-
559	Sulfoxidation	RQLAGEDMEISVKEL HHHCCCCCCCCHHHH	4.25	21406390
564	Ubiquitination	EDMEISVKELRTILN CCCCCCHHHHHHHHH	44.21	2190698
575	Phosphorylation	TILNRIISKHKDLRT HHHHHHHHHCCCHHC	26.74	29978859
583	2-Hydroxyisobutyrylation	KHKDLRTKGFSLESC HCCCHHCCCCCHHHH	52.07	-
583	Malonylation	KHKDLRTKGFSLESC HCCCHHCCCCCHHHH	52.07	26320211
583	Ubiquitination	KHKDLRTKGFSLESC HCCCHHCCCCCHHHH	52.07	-
622	Phosphorylation	NRIRNYLSIFRKFDL HHHHHHHHHHHHCCC	14.88	28857561
634	Phosphorylation	FDLDKSGSMSAYEMR CCCCCCCCCCHHHHH	19.36	25332170
636	Phosphorylation	LDKSGSMSAYEMRMA CCCCCCCCHHHHHHH	29.42	-
638	Phosphorylation	KSGSMSAYEMRMAIE CCCCCCHHHHHHHHH	11.71	25332170
642	Sulfoxidation	MSAYEMRMAIESAGF CCHHHHHHHHHHCCC	4.20	30846556
646	Phosphorylation	EMRMAIESAGFKLNK HHHHHHHHCCCCCCH	27.81	25332170
656	Phosphorylation	FKLNKKLYELIITRY CCCCHHHHHHHHHCC	19.98	28152594
691	Phosphorylation	TMFRFFKTLDTDLDG HHHHHHHHCCCCCCC	25.39	28387310
701	Phosphorylation	TDLDGVVTFDLFKWL CCCCCEEEHHHHHHH	14.71	28387310

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
255	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
256	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
415	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
418	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
474	S	Phosphorylation	Kinase	PRKACA	P17612	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CAN1_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 CAN1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FANCA_HUMAN	FANCA	physical	20518497
FANCC_HUMAN	FANCC	physical	20518497
PALB2_HUMAN	PALB2	physical	20518497
FANCG_HUMAN	FANCG	physical	20518497
GAS2_HUMAN	GAS2	physical	20679491
ICAL_HUMAN	CAST	physical	20679491
RAD21_HUMAN	RAD21	physical	21876002
HIF1A_HUMAN	HIF1A	physical	19458911
ANM5_HUMAN	PRMT5	physical	12358155
SH3BG_HUMAN	SH3BGR	physical	12358155
FHL2_HUMAN	FHL2	physical	12358155
TINAL_HUMAN	TINAGL1	physical	12358155
CREG1_HUMAN	CREG1	physical	12358155
ECHM_HUMAN	ECHS1	physical	12358155
NDUB7_HUMAN	NDUFB7	physical	12358155
SLIT3_HUMAN	SLIT3	physical	12358155
ALAT1_HUMAN	GPT	physical	12358155
CATC_HUMAN	CTSC	physical	12358155
PTGDS_HUMAN	PTGDS	physical	12358155
AES_HUMAN	AES	physical	12358155
NF2L1_HUMAN	NFE2L1	physical	12358155
ACTC_HUMAN	ACTC1	physical	12358155
MYPC3_HUMAN	MYBPC3	physical	12358155
ACTN2_HUMAN	ACTN2	physical	12358155
DESM_HUMAN	DES	physical	12358155
CO1A1_HUMAN	COL1A1	physical	12358155
VIME_HUMAN	VIM	physical	12358155
SPTN1_HUMAN	SPTAN1	physical	8993318
STAT3_HUMAN	STAT3	physical	21988832
ASSY_HUMAN	ASS1	physical	22863883
BZW2_HUMAN	BZW2	physical	22863883
CASP7_HUMAN	CASP7	physical	22863883
ECHM_HUMAN	ECHS1	physical	22863883
EF2_HUMAN	EEF2	physical	22863883
GBP2_HUMAN	GBP2	physical	22863883
PSF2_HUMAN	GINS2	physical	22863883
PSF3_HUMAN	GINS3	physical	22863883
AGAL_HUMAN	GLA	physical	22863883
GLSK_HUMAN	GLS	physical	22863883
GRP75_HUMAN	HSPA9	physical	22863883
MVD1_HUMAN	MVD	physical	22863883
GDS1_HUMAN	RAP1GDS1	physical	22863883
KS6A1_HUMAN	RPS6KA1	physical	22863883
ATG5_HUMAN	ATG5	physical	16998475
VATA_HUMAN	ATP6V1A	physical	26344197
EIF2A_HUMAN	EIF2A	physical	26344197
HNRPR_HUMAN	HNRNPR	physical	26344197
NIT1_HUMAN	NIT1	physical	26344197
SK2L2_HUMAN	SKIV2L2	physical	26344197
HNRPQ_HUMAN	SYNCRIP	physical	26344197
CPNS1_HUMAN	CAPNS1	physical	26496610
ICAL_HUMAN	CAST	physical	26496610
COG1_HUMAN	COG1	physical	26496610
DPOA2_HUMAN	POLA2	physical	26496610
ANR17_HUMAN	ANKRD17	physical	26496610
SYCM_HUMAN	CARS2	physical	26496610
PAR1_HUMAN	F2R	physical	25241761
NMDE2_HUMAN	GRIN2B	physical	25241761
ICAL_HUMAN	CAST	physical	28514442
C99L2_HUMAN	CD99L2	physical	28514442
TRIPC_HUMAN	TRIP12	physical	28514442
CD109_HUMAN	CD109	physical	28514442
CPNS2_HUMAN	CAPNS2	physical	28514442
FNTB_HUMAN	FNTB	physical	28514442
CPNS1_HUMAN	CAPNS1	physical	28514442
CAN2_HUMAN	CAPN2	physical	28514442
NFM_HUMAN	NEFM	physical	28514442
RP9_HUMAN	RP9	physical	28514442
NEST_HUMAN	NES	physical	28514442
KTN1_HUMAN	KTN1	physical	28514442
FNTA_HUMAN	FNTA	physical	28514442
AINX_HUMAN	INA	physical	28514442
VIME_HUMAN	VIM	physical	28514442

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.

Regulatory Network of CAN1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84, AND MASS SPECTROMETRY.	19608861 [Abstract]