dbPTM

PPIA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PPIA_HUMAN
UniProt AC	P62937
Protein Name	Peptidyl-prolyl cis-trans isomerase A
Gene Name	PPIA
Organism	Homo sapiens (Human).
Sequence Length	165
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	MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQLE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MVNPTVFF -------CCCCEEEE	6.24	19413330
1	Sulfoxidation	-------MVNPTVFF -------CCCCEEEE	6.24	28183972
2	Acetylation	------MVNPTVFFD ------CCCCEEEEE	13.61	25944712
5	Phosphorylation	---MVNPTVFFDIAV ---CCCCEEEEEEEE	25.41	30140170
16	Acetylation	DIAVDGEPLGRVSFE EEEECCEECCCEEEE	45.72	19608861
16	Ubiquitination	DIAVDGEPLGRVSFE EEEECCEECCCEEEE	45.72	19608861
16	Ubiquitination	DIAVDGEPLGRVSFE EEEECCEECCCEEEE	45.72	21890473
21	O-linked_Glycosylation	GEPLGRVSFELFADK CEECCCEEEEHHHHC	16.19	23301498
21	Phosphorylation	GEPLGRVSFELFADK CEECCCEEEEHHHHC	16.19	21815630
22	Acetylation	EPLGRVSFELFADKV EECCCEEEEHHHHCC	9.64	19608861
22	Ubiquitination	EPLGRVSFELFADKV EECCCEEEEHHHHCC	9.64	19608861
22	Ubiquitination	EPLGRVSFELFADKV EECCCEEEEHHHHCC	9.64	21890473
28	Ubiquitination	SFELFADKVPKTAEN EEEHHHHCCCCCHHH	57.94	21890473
28	Acetylation	SFELFADKVPKTAEN EEEHHHHCCCCCHHH	57.94	19608861
28	Sumoylation	SFELFADKVPKTAEN EEEHHHHCCCCCHHH	57.94	28112733
28	Ubiquitination	SFELFADKVPKTAEN EEEHHHHCCCCCHHH	57.94	19608861
31	Ubiquitination	LFADKVPKTAENFRA HHHHCCCCCHHHHHH	64.45	21890473
31	Sumoylation	LFADKVPKTAENFRA HHHHCCCCCHHHHHH	64.45	-
31	Acetylation	LFADKVPKTAENFRA HHHHCCCCCHHHHHH	64.45	23749302
31	Sumoylation	LFADKVPKTAENFRA HHHHCCCCCHHHHHH	64.45	-
31	Ubiquitination	LFADKVPKTAENFRA HHHHCCCCCHHHHHH	64.45	21890473
32	Phosphorylation	FADKVPKTAENFRAL HHHCCCCCHHHHHHC	32.89	25954137
40	Phosphorylation	AENFRALSTGEKGFG HHHHHHCCCCCCCCC	33.12	25954137
41	Phosphorylation	ENFRALSTGEKGFGY HHHHHCCCCCCCCCC	50.65	22210691
44	Ubiquitination	RALSTGEKGFGYKGS HHCCCCCCCCCCCCC	61.97	21890473
44	Sumoylation	RALSTGEKGFGYKGS HHCCCCCCCCCCCCC	61.97	-
44	Acetylation	RALSTGEKGFGYKGS HHCCCCCCCCCCCCC	61.97	19608861
44	Malonylation	RALSTGEKGFGYKGS HHCCCCCCCCCCCCC	61.97	26320211
44	Sumoylation	RALSTGEKGFGYKGS HHCCCCCCCCCCCCC	61.97	19608861
44	Ubiquitination	RALSTGEKGFGYKGS HHCCCCCCCCCCCCC	61.97	21890473
48	Phosphorylation	TGEKGFGYKGSCFHR CCCCCCCCCCCCCHH	15.20	20068231
49	Ubiquitination	GEKGFGYKGSCFHRI CCCCCCCCCCCCHHC	44.73	21890473
49	Sumoylation	GEKGFGYKGSCFHRI CCCCCCCCCCCCHHC	44.73	-
49	Acetylation	GEKGFGYKGSCFHRI CCCCCCCCCCCCHHC	44.73	23954790
49	Malonylation	GEKGFGYKGSCFHRI CCCCCCCCCCCCHHC	44.73	26320211
49	Methylation	GEKGFGYKGSCFHRI CCCCCCCCCCCCHHC	44.73	70199
49	Sumoylation	GEKGFGYKGSCFHRI CCCCCCCCCCCCHHC	44.73	19608861
49	Ubiquitination	GEKGFGYKGSCFHRI CCCCCCCCCCCCHHC	44.73	21890473
51	Phosphorylation	KGFGYKGSCFHRIIP CCCCCCCCCCHHCCC	14.95	30108239
52	Glutathionylation	GFGYKGSCFHRIIPG CCCCCCCCCHHCCCC	4.55	16372262
58	Acetylation	SCFHRIIPGFMCQGG CCCHHCCCCCEEECC	27.83	19608861
58	Ubiquitination	SCFHRIIPGFMCQGG CCCHHCCCCCEEECC	27.83	19608861
61	Sulfoxidation	HRIIPGFMCQGGDFT HHCCCCCEEECCCCC	1.75	21406390
62	Glutathionylation	RIIPGFMCQGGDFTR HCCCCCEEECCCCCE	2.96	16372262
62	S-palmitoylation	RIIPGFMCQGGDFTR HCCCCCEEECCCCCE	2.96	26865113
65	Acetylation	PGFMCQGGDFTRHNG CCCEEECCCCCEECC	10.86	19608861
65	Ubiquitination	PGFMCQGGDFTRHNG CCCEEECCCCCEECC	10.86	19608861
65	Ubiquitination	PGFMCQGGDFTRHNG CCCEEECCCCCEECC	10.86	21890473
68	Phosphorylation	MCQGGDFTRHNGTGG EEECCCCCEECCCCC	35.44	21712546
71	Acetylation	GGDFTRHNGTGGKSI CCCCCEECCCCCCCC	46.56	19608861
71	Ubiquitination	GGDFTRHNGTGGKSI CCCCCEECCCCCCCC	46.56	19608861
71	Ubiquitination	GGDFTRHNGTGGKSI CCCCCEECCCCCCCC	46.56	21890473
73	Phosphorylation	DFTRHNGTGGKSIYG CCCEECCCCCCCCCC	48.34	28857561
73	Ubiquitination	DFTRHNGTGGKSIYG CCCEECCCCCCCCCC	48.34	21890473
76	Ubiquitination	RHNGTGGKSIYGEKF EECCCCCCCCCCCEE	34.72	21890473
76	Acetylation	RHNGTGGKSIYGEKF EECCCCCCCCCCCEE	34.72	19608861
76	Malonylation	RHNGTGGKSIYGEKF EECCCCCCCCCCCEE	34.72	26320211
76	Sumoylation	RHNGTGGKSIYGEKF EECCCCCCCCCCCEE	34.72	19608861
76	Ubiquitination	RHNGTGGKSIYGEKF EECCCCCCCCCCCEE	34.72	21890473
77	Phosphorylation	HNGTGGKSIYGEKFE ECCCCCCCCCCCEEC	25.07	21712546
79	Phosphorylation	GTGGKSIYGEKFEDE CCCCCCCCCCEECCC	26.73	28796482
82	Ubiquitination	GKSIYGEKFEDENFI CCCCCCCEECCCCEE	50.09	21890473
82	Sumoylation	GKSIYGEKFEDENFI CCCCCCCEECCCCEE	50.09	-
82	Acetylation	GKSIYGEKFEDENFI CCCCCCCEECCCCEE	50.09	19608861
82	Succinylation	GKSIYGEKFEDENFI CCCCCCCEECCCCEE	50.09	23954790
82	Sumoylation	GKSIYGEKFEDENFI CCCCCCCEECCCCEE	50.09	19608861
82	Ubiquitination	GKSIYGEKFEDENFI CCCCCCCEECCCCEE	50.09	21890473
91	Acetylation	EDENFILKHTGPGIL CCCCEEEEECCCCHH	34.01	25953088
91	Methylation	EDENFILKHTGPGIL CCCCEEEEECCCCHH	34.01	7934193
91	Ubiquitination	EDENFILKHTGPGIL CCCCEEEEECCCCHH	34.01	-
93	Phosphorylation	ENFILKHTGPGILSM CCEEEEECCCCHHHC	43.41	22199227
99	Phosphorylation	HTGPGILSMANAGPN ECCCCHHHCCCCCCC	17.58	22199227
107	Phosphorylation	MANAGPNTNGSQFFI CCCCCCCCCCCCEEE	44.05	-
108	N-linked_Glycosylation	ANAGPNTNGSQFFIC CCCCCCCCCCCEEEE	55.55	UniProtKB CARBOHYD
110	Phosphorylation	AGPNTNGSQFFICTA CCCCCCCCCEEEEEE	26.36	17525332
116	Phosphorylation	GSQFFICTAKTEWLD CCCEEEEEEECEEEC	26.77	-
118	Acetylation	QFFICTAKTEWLDGK CEEEEEEECEEECCC	28.91	19608861
118	Sumoylation	QFFICTAKTEWLDGK CEEEEEEECEEECCC	28.91	19608861
118	Ubiquitination	QFFICTAKTEWLDGK CEEEEEEECEEECCC	28.91	21890473
125	Ubiquitination	KTEWLDGKHVVFGKV ECEEECCCEEEEEEH	32.66	21890473
125	Sumoylation	KTEWLDGKHVVFGKV ECEEECCCEEEEEEH	32.66	-
125	Acetylation	KTEWLDGKHVVFGKV ECEEECCCEEEEEEH	32.66	19608861
125	Malonylation	KTEWLDGKHVVFGKV ECEEECCCEEEEEEH	32.66	26320211
125	Methylation	KTEWLDGKHVVFGKV ECEEECCCEEEEEEH	32.66	19608861
125	Sumoylation	KTEWLDGKHVVFGKV ECEEECCCEEEEEEH	32.66	19608861
125	Ubiquitination	KTEWLDGKHVVFGKV ECEEECCCEEEEEEH	32.66	19608861
131	Ubiquitination	GKHVVFGKVKEGMNI CCEEEEEEHHCCCCH	38.37	21890473
131	Acetylation	GKHVVFGKVKEGMNI CCEEEEEEHHCCCCH	38.37	19608861
131	Succinylation	GKHVVFGKVKEGMNI CCEEEEEEHHCCCCH	38.37	27452117
131	Ubiquitination	GKHVVFGKVKEGMNI CCEEEEEEHHCCCCH	38.37	21890473
133	Ubiquitination	HVVFGKVKEGMNIVE EEEEEEHHCCCCHHH	52.62	21890473
133	Sumoylation	HVVFGKVKEGMNIVE EEEEEEHHCCCCHHH	52.62	-
133	Acetylation	HVVFGKVKEGMNIVE EEEEEEHHCCCCHHH	52.62	26051181
133	Sumoylation	HVVFGKVKEGMNIVE EEEEEEHHCCCCHHH	52.62	-
133	Ubiquitination	HVVFGKVKEGMNIVE EEEEEEHHCCCCHHH	52.62	21890473
136	Sulfoxidation	FGKVKEGMNIVEAME EEEHHCCCCHHHHHH	3.03	28465586
142	Sulfoxidation	GMNIVEAMERFGSRN CCCHHHHHHHHHCCC	2.10	30846556
147	Phosphorylation	EAMERFGSRNGKTSK HHHHHHHCCCCCCCC	21.62	25159151
151	Ubiquitination	RFGSRNGKTSKKITI HHHCCCCCCCCEEEE	53.85	-
152	Phosphorylation	FGSRNGKTSKKITIA HHCCCCCCCCEEEEE	47.37	23909892
153	Phosphorylation	GSRNGKTSKKITIAD HCCCCCCCCEEEEEE	35.12	27251275
155	Sumoylation	RNGKTSKKITIADCG CCCCCCCEEEEEECC	44.86	-
155	Acetylation	RNGKTSKKITIADCG CCCCCCCEEEEEECC	44.86	23749302
155	Malonylation	RNGKTSKKITIADCG CCCCCCCEEEEEECC	44.86	26320211
155	Sumoylation	RNGKTSKKITIADCG CCCCCCCEEEEEECC	44.86	-
155	Ubiquitination	RNGKTSKKITIADCG CCCCCCCEEEEEECC	44.86	-
157	Phosphorylation	GKTSKKITIADCGQL CCCCCEEEEEECCCC	20.99	16097034
161	Glutathionylation	KKITIADCGQLE--- CEEEEEECCCCC---	2.50	22555962
161	S-palmitoylation	KKITIADCGQLE--- CEEEEEECCCCC---	2.50	29575903

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
125	K	Acetylation	19608861
Acetylation at Lys-125 favors its interaction with TARDBP.
125	K	Acetylation	19608861
Acetylation at Lys-125 markedly inhibits catalysis of cis to trans isomerization and stabilizes cis rather than trans forms of the HIV-1 capsid.

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 PPIA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PRR13_HUMAN	PRR13	physical	16189514
JAK2_HUMAN	JAK2	physical	12668872
CANB1_HUMAN	PPP3R1	physical	12218175
PP2BA_HUMAN	PPP3CA	physical	12218175
ITK_HUMAN	ITK	physical	11830645
CHM4A_HUMAN	CHMP4A	physical	14505569
A4_HUMAN	APP	physical	21832049
TAGL2_HUMAN	TAGLN2	physical	22939629
RFA2_HUMAN	RPA2	physical	22939629
SNX3_HUMAN	SNX3	physical	22939629
RD23B_HUMAN	RAD23B	physical	22939629
SODC_HUMAN	SOD1	physical	22939629
PTMA_HUMAN	PTMA	physical	22939629
RB_HUMAN	RB1	physical	12210730
RL23A_HUMAN	RPL23A	physical	22863883
ITF2_HUMAN	TCF4	physical	25416956
LNX1_HUMAN	LNX1	physical	25416956
ANXA1_HUMAN	ANXA1	physical	26496610
ANXA7_HUMAN	ANXA7	physical	26496610
AL7A1_HUMAN	ALDH7A1	physical	26496610
LYST_HUMAN	LYST	physical	26496610
PUR2_HUMAN	GART	physical	26496610
RBM4_HUMAN	RBM4	physical	26496610
STX3_HUMAN	STX3	physical	26496610
UBE2N_HUMAN	UBE2N	physical	26496610
MKNK1_HUMAN	MKNK1	physical	26496610
BCL7B_HUMAN	BCL7B	physical	26496610
DNM1L_HUMAN	DNM1L	physical	26496610
ZER1_HUMAN	ZER1	physical	26496610
ATP5S_HUMAN	ATP5S	physical	26496610
PKN3_HUMAN	PKN3	physical	26496610
E41LB_HUMAN	EPB41L4B	physical	26496610
CSN7B_HUMAN	COPS7B	physical	26496610
DCA15_HUMAN	DCAF15	physical	26496610
TM189_HUMAN	TMEM189	physical	26496610
G3BP1_HUMAN	G3BP1	physical	28394340

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
DB00091	Cyclosporine
DB00172	L-Proline

Regulatory Network of PPIA_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-28; LYS-44; LYS-49; LYS-76;LYS-82; LYS-125 AND LYS-131, AND MASS SPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125, AND MASS SPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC."; Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.; Proteomics 5:3589-3599(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-157, AND MASSSPECTROMETRY.	16097034 [Abstract]
Ubiquitylation
Reference	PubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry."; Meierhofer D., Wang X., Huang L., Kaiser P.; J. Proteome Res. 7:4566-4576(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-28, AND MASSSPECTROMETRY.	18781797 [Abstract]

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