PPIA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PPIA_MOUSE
• UniProt AC: P17742
• Protein Name: Peptidyl-prolyl cis-trans isomerase A
• Gene Name: Ppia
• Organism: Mus musculus (Mouse).
• 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: MVNPTVFFDITADDEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSSFHRIIPGFMCQGGDFTRHNGTGGRSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITISDCGQL

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	-
5	Phosphorylation	---MVNPTVFFDITA ---CCCCEEEEECCC	25.41	26239621
11	Phosphorylation	PTVFFDITADDEPLG CEEEEECCCCCCCCC	26.36	26239621
21	Phosphorylation	DEPLGRVSFELFADK CCCCCEEEEEHHHHC	16.19	24899341
28	Malonylation	SFELFADKVPKTAEN EEEHHHHCCCCCHHH	57.94	26073543
28	Succinylation	SFELFADKVPKTAEN EEEHHHHCCCCCHHH	57.94	-
28	Acetylation	SFELFADKVPKTAEN EEEHHHHCCCCCHHH	57.94	23954790
28	Ubiquitination	SFELFADKVPKTAEN EEEHHHHCCCCCHHH	57.94	-
31	Acetylation	LFADKVPKTAENFRA HHHHCCCCCHHHHHH	64.45	30583327
31	Malonylation	LFADKVPKTAENFRA HHHHCCCCCHHHHHH	64.45	26320211
31	Ubiquitination	LFADKVPKTAENFRA HHHHCCCCCHHHHHH	64.45	-
44	Acetylation	RALSTGEKGFGYKGS HHCCCCCCCCCCCCC	61.97	22826441
44	Malonylation	RALSTGEKGFGYKGS HHCCCCCCCCCCCCC	61.97	26320211
44	Ubiquitination	RALSTGEKGFGYKGS HHCCCCCCCCCCCCC	61.97	-
48	Phosphorylation	TGEKGFGYKGSSFHR CCCCCCCCCCCCCCE	15.20	26643407
49	Acetylation	GEKGFGYKGSSFHRI CCCCCCCCCCCCCEE	53.33	23806337
49	Ubiquitination	GEKGFGYKGSSFHRI CCCCCCCCCCCCCEE	53.33	22790023
51	Phosphorylation	KGFGYKGSSFHRIIP CCCCCCCCCCCEEEC	26.19	25266776
52	Phosphorylation	GFGYKGSSFHRIIPG CCCCCCCCCCEEECC	33.47	26239621
62	S-nitrosocysteine	RIIPGFMCQGGDFTR EEECCCEEECCCCCE	2.96	-
62	Glutathionylation	RIIPGFMCQGGDFTR EEECCCEEECCCCCE	2.96	24333276
62	S-nitrosylation	RIIPGFMCQGGDFTR EEECCCEEECCCCCE	2.96	24926564
62	S-palmitoylation	RIIPGFMCQGGDFTR EEECCCEEECCCCCE	2.96	28526873
73	Phosphorylation	DFTRHNGTGGRSIYG CCCEECCCCCCCCCC	41.60	24719451
77	Phosphorylation	HNGTGGRSIYGEKFE ECCCCCCCCCCCEEC	24.36	19854140
79	Phosphorylation	GTGGRSIYGEKFEDE CCCCCCCCCCEECCC	22.07	24224561
82	Ubiquitination	GRSIYGEKFEDENFI CCCCCCCEECCCCEE	50.09	-
82	Acetylation	GRSIYGEKFEDENFI CCCCCCCEECCCCEE	50.09	22826441
82	Malonylation	GRSIYGEKFEDENFI CCCCCCCEECCCCEE	50.09	26073543
93	Phosphorylation	ENFILKHTGPGILSM CCEEEEECCCCHHHC	43.41	19060867
99	Phosphorylation	HTGPGILSMANAGPN ECCCCHHHCCCCCCC	17.58	21183079
108	N-linked_Glycosylation	ANAGPNTNGSQFFIC CCCCCCCCCCCEEEE	55.55	-
110	Phosphorylation	AGPNTNGSQFFICTA CCCCCCCCCEEEEEE	26.36	26239621
115	S-nitrosocysteine	NGSQFFICTAKTEWL CCCCEEEEEEECEEE	2.27	-
115	S-palmitoylation	NGSQFFICTAKTEWL CCCCEEEEEEECEEE	2.27	28526873
115	S-nitrosylation	NGSQFFICTAKTEWL CCCCEEEEEEECEEE	2.27	21278135
115	Glutathionylation	NGSQFFICTAKTEWL CCCCEEEEEEECEEE	2.27	24333276
116	Phosphorylation	GSQFFICTAKTEWLD CCCEEEEEEECEEEC	26.77	21183079
125	Acetylation	KTEWLDGKHVVFGKV ECEEECCCEEEEEEH	32.66	22826441
125	Malonylation	KTEWLDGKHVVFGKV ECEEECCCEEEEEEH	32.66	26320211
125	Ubiquitination	KTEWLDGKHVVFGKV ECEEECCCEEEEEEH	32.66	-
131	Ubiquitination	GKHVVFGKVKEGMNI CCEEEEEEHHCCCCH	38.37	-
131	Malonylation	GKHVVFGKVKEGMNI CCEEEEEEHHCCCCH	38.37	26320211
131	Acetylation	GKHVVFGKVKEGMNI CCEEEEEEHHCCCCH	38.37	22733758
133	Malonylation	HVVFGKVKEGMNIVE EEEEEEHHCCCCHHH	52.62	26320211
133	Ubiquitination	HVVFGKVKEGMNIVE EEEEEEHHCCCCHHH	52.62	-
133	Acetylation	HVVFGKVKEGMNIVE EEEEEEHHCCCCHHH	52.62	23806337
147	Phosphorylation	EAMERFGSRNGKTSK HHHHHHHCCCCCCCC	21.62	23375375
155	Acetylation	RNGKTSKKITISDCG CCCCCCCEEEECCCC	44.86	22826441
155	Ubiquitination	RNGKTSKKITISDCG CCCCCCCEEEECCCC	44.86	-
159	Phosphorylation	TSKKITISDCGQL-- CCCEEEECCCCCC--	20.42	26525534
161	S-nitrosocysteine	KKITISDCGQL---- CEEEECCCCCC----	2.74	-
161	Glutathionylation	KKITISDCGQL---- CEEEECCCCCC----	2.74	24333276
161	S-nitrosylation	KKITISDCGQL---- CEEEECCCCCC----	2.74	24895380
161	S-palmitoylation	KKITISDCGQL---- CEEEECCCCCC----	2.74	28526873

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

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

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HDAC1_MOUSE	Hdac1	physical	17071620
MBD2_MOUSE	Mbd2	physical	17071620

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative analysis of both protein expression and serine /threonine post-translational modifications through stable isotopelabeling with dithiothreitol.";
Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,Hart G.W., Burlingame A.L.;
Proteomics 5:388-398(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASSSPECTROMETRY.
PubMed: 15648052