CPNS1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CPNS1_HUMAN
• UniProt AC: P04632
• Protein Name: Calpain small subunit 1
• Gene Name: CAPNS1
• Organism: Homo sapiens (Human).
• Sequence Length: 268
• Subcellular Localization: Cytoplasm. Cell membrane. Translocates to the plasma membrane upon calcium binding..
• Protein Description: Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction..
• Protein Sequence: MFLVNSFLKGGGGGGGGGGGLGGGLGNVLGGLISGAGGGGGGGGGGGGGGGGGGGGTAMRILGGVISAISEAAAQYNPEPPPPRTHYSNIEANESEEVRQFRRLFAQLAGDDMEVSATELMNILNKVVTRHPDLKTDGFGIDTCRSMVAVMDSDTTGKLGFEEFKYLWNNIKRWQAIYKQFDTDRSGTICSSELPGAFEAAGFHLNEHLYNMIIRRYSDESGNMDFDNFISCLVRLDAMFRAFKSLDKDGTGQIQVNIQEWLQLTMYS

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
1	Sulfoxidation	-------MFLVNSFL -------CCCCCCCC	5.45	28183972
1	Acetylation	-------MFLVNSFL -------CCCCCCCC	5.45	19413330
6	Phosphorylation	--MFLVNSFLKGGGG --CCCCCCCCCCCCC	25.20	28355574
9	Methylation	FLVNSFLKGGGGGGG CCCCCCCCCCCCCCC	54.20	-
9	Acetylation	FLVNSFLKGGGGGGG CCCCCCCCCCCCCCC	54.20	88577
9	Sumoylation	FLVNSFLKGGGGGGG CCCCCCCCCCCCCCC	54.20	-
34	Phosphorylation	NVLGGLISGAGGGGG HHHHHHHCCCCCCCC	27.86	20068231
34	O-linked_Glycosylation	NVLGGLISGAGGGGG HHHHHHHCCCCCCCC	27.86	23301498
57	Phosphorylation	GGGGGGGTAMRILGG CCCCCHHHHHHHHHH	22.13	28857561
57	O-linked_Glycosylation	GGGGGGGTAMRILGG CCCCCHHHHHHHHHH	22.13	23301498
59	Sulfoxidation	GGGGGTAMRILGGVI CCCHHHHHHHHHHHH	2.48	28465586
67	Acetylation	RILGGVISAISEAAA HHHHHHHHHHHHHHH	19.69	19608861
67	Ubiquitination	RILGGVISAISEAAA HHHHHHHHHHHHHHH	19.69	19608861
67	Phosphorylation	RILGGVISAISEAAA HHHHHHHHHHHHHHH	19.69	24719451
70	Phosphorylation	GGVISAISEAAAQYN HHHHHHHHHHHHHHC	22.39	27251275
85	Phosphorylation	PEPPPPRTHYSNIEA CCCCCCCCCCCCCCC	30.82	21945579
87	Phosphorylation	PPPPRTHYSNIEANE CCCCCCCCCCCCCCC	11.64	21945579
88	Phosphorylation	PPPRTHYSNIEANES CCCCCCCCCCCCCCC	24.59	21945579
99	Methylation	ANESEEVRQFRRLFA CCCCHHHHHHHHHHH	32.95	-
126	Ubiquitination	ELMNILNKVVTRHPD HHHHHHHHHHHHCCC	34.34	-
135	Ubiquitination	VTRHPDLKTDGFGID HHHCCCCCCCCCCHH	52.53	21906983
135	Acetylation	VTRHPDLKTDGFGID HHHCCCCCCCCCCHH	52.53	25953088
144	S-nitrosylation	DGFGIDTCRSMVAVM CCCCHHCCCCEEEHH	2.41	2212679
146	Phosphorylation	FGIDTCRSMVAVMDS CCHHCCCCEEEHHCC	21.54	-
147	Sulfoxidation	GIDTCRSMVAVMDSD CHHCCCCEEEHHCCC	0.86	21406390
151	Sulfoxidation	CRSMVAVMDSDTTGK CCCEEEHHCCCCCCC	2.69	30846556
153	Phosphorylation	SMVAVMDSDTTGKLG CEEEHHCCCCCCCCC	20.82	-
156	Phosphorylation	AVMDSDTTGKLGFEE EHHCCCCCCCCCHHH	36.99	-
158	Ubiquitination	MDSDTTGKLGFEEFK HCCCCCCCCCHHHHH	43.26	-
165	Ubiquitination	KLGFEEFKYLWNNIK CCCHHHHHHHHHHHH	42.59	-
172	Acetylation	KYLWNNIKRWQAIYK HHHHHHHHHHHHHHH	50.10	25953088
172	Ubiquitination	KYLWNNIKRWQAIYK HHHHHHHHHHHHHHH	50.10	21890473
172	2-Hydroxyisobutyrylation	KYLWNNIKRWQAIYK HHHHHHHHHHHHHHH	50.10	-
178	Phosphorylation	IKRWQAIYKQFDTDR HHHHHHHHHHHCCCC	11.18	25884760
179	Acetylation	KRWQAIYKQFDTDRS HHHHHHHHHHCCCCC	38.07	19608861
179	Malonylation	KRWQAIYKQFDTDRS HHHHHHHHHHCCCCC	38.07	26320211
179	2-Hydroxyisobutyrylation	KRWQAIYKQFDTDRS HHHHHHHHHHCCCCC	38.07	-
179	Ubiquitination	KRWQAIYKQFDTDRS HHHHHHHHHHCCCCC	38.07	21890473
218	Phosphorylation	NMIIRRYSDESGNMD HHHHHHHCCCCCCCC	32.84	21712546
224	Sulfoxidation	YSDESGNMDFDNFIS HCCCCCCCCHHHHHH	6.57	30846556
244	Acetylation	DAMFRAFKSLDKDGT HHHHHHHHCCCCCCC	49.47	27452117

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CPNS1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CPNS1_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 CPNS1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CSPG4_HUMAN	CSPG4	physical	22939629
TRAF5_HUMAN	TRAF5	physical	21988832
STAT3_HUMAN	STAT3	physical	21988832
PRGC1_HUMAN	PPARGC1A	physical	21988832
AL7A1_HUMAN	ALDH7A1	physical	22863883
APEX1_HUMAN	APEX1	physical	22863883
DCPS_HUMAN	DCPS	physical	22863883
ISOC1_HUMAN	ISOC1	physical	22863883
METK2_HUMAN	MAT2A	physical	22863883
MAT2B_HUMAN	MAT2B	physical	22863883
LIS1_HUMAN	PAFAH1B1	physical	22863883
PAK2_HUMAN	PAK2	physical	22863883
PDIA4_HUMAN	PDIA4	physical	22863883
PP1A_HUMAN	PPP1CA	physical	22863883
PLPHP_HUMAN	PROSC	physical	22863883
1433E_HUMAN	YWHAE	physical	22863883
1433G_HUMAN	YWHAG	physical	22863883
1433F_HUMAN	YWHAH	physical	22863883
1433T_HUMAN	YWHAQ	physical	22863883
1433Z_HUMAN	YWHAZ	physical	22863883
ATRAP_HUMAN	AGTRAP	physical	25416956
UBP1_HUMAN	USP1	physical	23589330

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.

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330

"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-179, AND MASS SPECTROMETRY.
PubMed: 19608861