PPIA_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PPIA_RAT
• UniProt AC: P10111
• Protein Name: Peptidyl-prolyl cis-trans isomerase A
• Gene Name: Ppia
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 164
• Subcellular Localization: Cytoplasm. Secreted. Secretion occurs in response to oxidative stress in vascular smooth muscle through a vesicular secretory pathway that involves actin remodeling and myosin II activation, and mediates ERK1/2 activation..
• Protein Description: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides..
• Protein Sequence: MVNPTVFFDITADGEPLGRVCFELFADKVPKTAENFRALSTGEKGFGYKGSSFHRIIPGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMSIVEAMERFGSRNGKTSKKITISDCGQL

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	Acetylation	-------MVNPTVFF -------CCCCEEEE	6.24	-
2	Acetylation	------MVNPTVFFD ------CCCCEEEEE	13.61	-
28	Acetylation	CFELFADKVPKTAEN HHHHHHCCCCCHHHH	57.94	25786129
28	Ubiquitination	CFELFADKVPKTAEN HHHHHHCCCCCHHHH	57.94	-
31	Ubiquitination	LFADKVPKTAENFRA HHHCCCCCHHHHHHH	64.45	-
31	Acetylation	LFADKVPKTAENFRA HHHCCCCCHHHHHHH	64.45	26302492
40	Phosphorylation	AENFRALSTGEKGFG HHHHHHCCCCCCCCC	33.12	23298284
44	Ubiquitination	RALSTGEKGFGYKGS HHCCCCCCCCCCCCC	61.97	-
44	Acetylation	RALSTGEKGFGYKGS HHCCCCCCCCCCCCC	61.97	25786129
49	Acetylation	GEKGFGYKGSSFHRI CCCCCCCCCCCCCEE	53.33	5806815
49	Ubiquitination	GEKGFGYKGSSFHRI CCCCCCCCCCCCCEE	53.33	-
51	Phosphorylation	KGFGYKGSSFHRIIP CCCCCCCCCCCEEEC	26.19	27097102
52	Phosphorylation	GFGYKGSSFHRIIPG CCCCCCCCCCEEECC	33.47	27097102
76	Acetylation	RHNGTGGKSIYGEKF EECCCCCCCCCCCEE	34.72	22902405
76	Ubiquitination	RHNGTGGKSIYGEKF EECCCCCCCCCCCEE	34.72	-
77	Phosphorylation	HNGTGGKSIYGEKFE ECCCCCCCCCCCEEC	25.07	23984901
79	Phosphorylation	GTGGKSIYGEKFEDE CCCCCCCCCCEECCC	26.73	23984901
82	Ubiquitination	GKSIYGEKFEDENFI CCCCCCCEECCCCEE	50.09	-
82	Acetylation	GKSIYGEKFEDENFI CCCCCCCEECCCCEE	50.09	22902405
91	Acetylation	EDENFILKHTGPGIL CCCCEEEEECCCCHH	34.01	26302492
93	Phosphorylation	ENFILKHTGPGILSM CCEEEEECCCCHHHC	43.41	-
108	N-linked_Glycosylation	ANAGPNTNGSQFFIC CCCCCCCCCCCEEEE	55.55	-
125	Acetylation	KTEWLDGKHVVFGKV ECEEECCCEEEEEEH	32.66	22902405
131	Acetylation	GKHVVFGKVKEGMSI CCEEEEEEHHHCCCH	38.37	25786129
133	Acetylation	HVVFGKVKEGMSIVE EEEEEEHHHCCCHHH	52.62	22902405
137	Phosphorylation	GKVKEGMSIVEAMER EEHHHCCCHHHHHHH	34.05	25403869
155	Succinylation	RNGKTSKKITISDCG CCCCCCCEEEECCCC	44.86	26843850
157	Phosphorylation	GKTSKKITISDCGQL CCCCCEEEECCCCCC	24.25	23984901
159	Phosphorylation	TSKKITISDCGQL-- CCCEEEECCCCCC--	20.42	23984901
161	S-nitrosocysteine	KKITISDCGQL---- CEEEECCCCCC----	2.74	-
161	S-nitrosylation	KKITISDCGQL---- CEEEECCCCCC----	2.74	22178444

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

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
125	K	Acetylation	Acetylation at Lys-125 favors the interaction with TARDBP (By similarity).	-
125	K	Acetylation	Acetylation at Lys-125 markedly inhibits catalysis of cis to trans isomerization (By similarity).	-

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of PPIA_RAT !!

Drug and Disease Associations

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