PDIA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PDIA1_HUMAN
• UniProt AC: P07237
• Protein Name: Protein disulfide-isomerase
• Gene Name: P4HB
• Organism: Homo sapiens (Human).
• Sequence Length: 508
• Subcellular Localization: Endoplasmic reticulum . Endoplasmic reticulum lumen . Melanosome . Cell membrane ; Peripheral membrane protein . Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant sheddi
• Protein Description: This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration. [PubMed: 21670307]
• Protein Sequence: MLRRALLCLAVAALVRADAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEDVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDMEEDDDQKAVKDEL

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
31	2-Hydroxyisobutyrylation	DHVLVLRKSNFAEAL CEEEEEECCCHHHHH	45.66	-
31	Ubiquitination	DHVLVLRKSNFAEAL CEEEEEECCCHHHHH	45.66	-
32	Phosphorylation	HVLVLRKSNFAEALA EEEEEECCCHHHHHH	30.65	25159151
53	S-nitrosocysteine	VEFYAPWCGHCKALA EEEECCCCCCHHHHH	2.31	-
53	S-nitrosylation	VEFYAPWCGHCKALA EEEECCCCCCHHHHH	2.31	22178444
56	S-nitrosocysteine	YAPWCGHCKALAPEY ECCCCCCHHHHHHHH	1.35	-
56	S-nitrosylation	YAPWCGHCKALAPEY ECCCCCCHHHHHHHH	1.35	22178444
63	Phosphorylation	CKALAPEYAKAAGKL HHHHHHHHHHHHCCC	16.61	29759185
65	2-Hydroxyisobutyrylation	ALAPEYAKAAGKLKA HHHHHHHHHHCCCCC	37.56	-
65	Acetylation	ALAPEYAKAAGKLKA HHHHHHHHHHCCCCC	37.56	22424773
65	Ubiquitination	ALAPEYAKAAGKLKA HHHHHHHHHHCCCCC	37.56	-
71	2-Hydroxyisobutyrylation	AKAAGKLKAEGSEIR HHHHCCCCCCCCEEE	48.13	-
78	Methylation	KAEGSEIRLAKVDAT CCCCCEEEEEECCCC	25.25	115486819
81	2-Hydroxyisobutyrylation	GSEIRLAKVDATEES CCEEEEEECCCCCHH	45.28	-
81	Acetylation	GSEIRLAKVDATEES CCEEEEEECCCCCHH	45.28	27178108
81	Ubiquitination	GSEIRLAKVDATEES CCEEEEEECCCCCHH	45.28	21890473
85	Phosphorylation	RLAKVDATEESDLAQ EEEECCCCCHHHHHH	35.50	30624053
88	Phosphorylation	KVDATEESDLAQQYG ECCCCCHHHHHHHHC	31.52	28152594
94	Phosphorylation	ESDLAQQYGVRGYPT HHHHHHHHCCCCCCE	12.90	28152594
97	Methylation	LAQQYGVRGYPTIKF HHHHHCCCCCCEEEE	34.27	115486843
99	Phosphorylation	QQYGVRGYPTIKFFR HHHCCCCCCEEEEEE	6.14	-
103	Ubiquitination	VRGYPTIKFFRNGDT CCCCCEEEEEECCCC	40.71	21890473
103	2-Hydroxyisobutyrylation	VRGYPTIKFFRNGDT CCCCCEEEEEECCCC	40.71	-
103	Acetylation	VRGYPTIKFFRNGDT CCCCCEEEEEECCCC	40.71	27452117
103	Ubiquitination	VRGYPTIKFFRNGDT CCCCCEEEEEECCCC	40.71	21890473
106	Methylation	YPTIKFFRNGDTASP CCEEEEEECCCCCCH	49.72	2380411
130	Ubiquitination	DDIVNWLKKRTGPAA HHHHHHHHHCCCCCC	31.65	21890473
130	2-Hydroxyisobutyrylation	DDIVNWLKKRTGPAA HHHHHHHHHCCCCCC	31.65	-
130	Acetylation	DDIVNWLKKRTGPAA HHHHHHHHHCCCCCC	31.65	27452117
130	Methylation	DDIVNWLKKRTGPAA HHHHHHHHHCCCCCC	31.65	66691099
130	Succinylation	DDIVNWLKKRTGPAA HHHHHHHHHCCCCCC	31.65	23954790
130	Ubiquitination	DDIVNWLKKRTGPAA HHHHHHHHHCCCCCC	31.65	21890473
139	Phosphorylation	RTGPAATTLPDGAAA CCCCCCCCCCCCHHH	31.41	28258704
148	Phosphorylation	PDGAAAESLVESSEV CCCHHHHHHHHHCCE	32.75	28258704
196	Phosphorylation	NSDVFSKYQLDKDGV CCCCHHHCEECCCCE	17.07	28152594
200	Ubiquitination	FSKYQLDKDGVVLFK HHHCEECCCCEEEEE	66.04	21890473
200	2-Hydroxyisobutyrylation	FSKYQLDKDGVVLFK HHHCEECCCCEEEEE	66.04	-
200	Acetylation	FSKYQLDKDGVVLFK HHHCEECCCCEEEEE	66.04	26051181
200	Ubiquitination	FSKYQLDKDGVVLFK HHHCEECCCCEEEEE	66.04	21890473
207	Acetylation	KDGVVLFKKFDEGRN CCCEEEEEECCCCCC	48.66	26051181
208	Acetylation	DGVVLFKKFDEGRNN CCEEEEEECCCCCCC	51.19	133417
221	Phosphorylation	NNFEGEVTKENLLDF CCCCCEECHHHHHHH	28.48	20068231
222	Ubiquitination	NFEGEVTKENLLDFI CCCCEECHHHHHHHH	50.18	21890473
222	Acetylation	NFEGEVTKENLLDFI CCCCEECHHHHHHHH	50.18	26822725
222	Succinylation	NFEGEVTKENLLDFI CCCCEECHHHHHHHH	50.18	-
222	Succinylation	NFEGEVTKENLLDFI CCCCEECHHHHHHHH	50.18	21890473
222	Ubiquitination	NFEGEVTKENLLDFI CCCCEECHHHHHHHH	50.18	21890473
241	O-linked_Glycosylation	LPLVIEFTEQTAPKI CCEEEEEEECCCCCC	17.88	OGP
244	Phosphorylation	VIEFTEQTAPKIFGG EEEEEECCCCCCCCC	38.40	21601212
247	Ubiquitination	FTEQTAPKIFGGEIK EEECCCCCCCCCEEE	48.48	21890473
247	2-Hydroxyisobutyrylation	FTEQTAPKIFGGEIK EEECCCCCCCCCEEE	48.48	-
247	Ubiquitination	FTEQTAPKIFGGEIK EEECCCCCCCCCEEE	48.48	21890473
254	2-Hydroxyisobutyrylation	KIFGGEIKTHILLFL CCCCCEEEEEEEEEC	29.73	-
255	Phosphorylation	IFGGEIKTHILLFLP CCCCEEEEEEEEECC	21.58	23882029
263	2-Hydroxyisobutyrylation	HILLFLPKSVSDYDG EEEEECCCCHHHCCC	66.68	-
263	Acetylation	HILLFLPKSVSDYDG EEEEECCCCHHHCCC	66.68	26051181
264	Phosphorylation	ILLFLPKSVSDYDGK EEEECCCCHHHCCCC	25.55	26437602
266	Phosphorylation	LFLPKSVSDYDGKLS EECCCCHHHCCCCCC	37.23	24719451
268	Phosphorylation	LPKSVSDYDGKLSNF CCCCHHHCCCCCCCH	21.06	-
271	Ubiquitination	SVSDYDGKLSNFKTA CHHHCCCCCCCHHHH	45.93	21890473
271	2-Hydroxyisobutyrylation	SVSDYDGKLSNFKTA CHHHCCCCCCCHHHH	45.93	-
271	Acetylation	SVSDYDGKLSNFKTA CHHHCCCCCCCHHHH	45.93	23236377
271	Malonylation	SVSDYDGKLSNFKTA CHHHCCCCCCCHHHH	45.93	26320211
271	Succinylation	SVSDYDGKLSNFKTA CHHHCCCCCCCHHHH	45.93	-
271	Succinylation	SVSDYDGKLSNFKTA CHHHCCCCCCCHHHH	45.93	-
271	Ubiquitination	SVSDYDGKLSNFKTA CHHHCCCCCCCHHHH	45.93	21890473
273	Phosphorylation	SDYDGKLSNFKTAAE HHCCCCCCCHHHHHH	43.64	24719451
276	2-Hydroxyisobutyrylation	DGKLSNFKTAAESFK CCCCCCHHHHHHHCC	41.32	-
276	Acetylation	DGKLSNFKTAAESFK CCCCCCHHHHHHHCC	41.32	25953088
277	Phosphorylation	GKLSNFKTAAESFKG CCCCCHHHHHHHCCC	27.28	26437602
281	Phosphorylation	NFKTAAESFKGKILF CHHHHHHHCCCCEEE	27.77	24719451
283	2-Hydroxyisobutyrylation	KTAAESFKGKILFIF HHHHHHCCCCEEEEE	69.45	-
283	Acetylation	KTAAESFKGKILFIF HHHHHHCCCCEEEEE	69.45	25953088
293	Phosphorylation	ILFIFIDSDHTDNQR EEEEEEECCCCCCHH	26.86	-
308	Acetylation	ILEFFGLKKEECPAV HHHHHCCCHHHCCCE	59.52	25953088
308	Ubiquitination	ILEFFGLKKEECPAV HHHHHCCCHHHCCCE	59.52	21890473
312	S-nitrosocysteine	FGLKKEECPAVRLIT HCCCHHHCCCEEEEE	2.48	-
312	S-nitrosylation	FGLKKEECPAVRLIT HCCCHHHCCCEEEEE	2.48	22178444
312	S-palmitoylation	FGLKKEECPAVRLIT HCCCHHHCCCEEEEE	2.48	21044946
324	Sulfoxidation	LITLEEEMTKYKPES EEECHHHHHHCCCCC	4.42	21406390
326	Acetylation	TLEEEMTKYKPESEE ECHHHHHHCCCCCHH	50.39	25038526
326	Ubiquitination	TLEEEMTKYKPESEE ECHHHHHHCCCCCHH	50.39	-
327	Phosphorylation	LEEEMTKYKPESEEL CHHHHHHCCCCCHHH	23.70	28152594
328	2-Hydroxyisobutyrylation	EEEMTKYKPESEELT HHHHHHCCCCCHHHC	43.81	-
328	Acetylation	EEEMTKYKPESEELT HHHHHHCCCCCHHHC	43.81	26822725
328	Succinylation	EEEMTKYKPESEELT HHHHHHCCCCCHHHC	43.81	27452117
328	Ubiquitination	EEEMTKYKPESEELT HHHHHHCCCCCHHHC	43.81	-
331	Phosphorylation	MTKYKPESEELTAER HHHCCCCCHHHCHHH	44.92	26657352
335	Phosphorylation	KPESEELTAERITEF CCCCHHHCHHHHHHH	29.74	-
338	Methylation	SEELTAERITEFCHR CHHHCHHHHHHHHHH	38.37	115486851
352	Acetylation	RFLEGKIKPHLMSQE HHHCCCCCHHHHCCC	29.85	26051181
357	Phosphorylation	KIKPHLMSQELPEDW CCCHHHHCCCCCCCC	27.19	8672469
366	2-Hydroxyisobutyrylation	ELPEDWDKQPVKVLV CCCCCCCCCCCEEEE	52.85	-
366	Acetylation	ELPEDWDKQPVKVLV CCCCCCCCCCCEEEE	52.85	26051181
370	2-Hydroxyisobutyrylation	DWDKQPVKVLVGKNF CCCCCCCEEEECCCH	36.21	-
375	Ubiquitination	PVKVLVGKNFEDVAF CCEEEECCCHHHCCC	51.49	21890473
375	2-Hydroxyisobutyrylation	PVKVLVGKNFEDVAF CCEEEECCCHHHCCC	51.49	-
375	Acetylation	PVKVLVGKNFEDVAF CCEEEECCCHHHCCC	51.49	25825284
375	Ubiquitination	PVKVLVGKNFEDVAF CCEEEECCCHHHCCC	51.49	21890473
385	2-Hydroxyisobutyrylation	EDVAFDEKKNVFVEF HHCCCCCCCCEEEEE	52.04	-
385	Acetylation	EDVAFDEKKNVFVEF HHCCCCCCCCEEEEE	52.04	26822725
385	Ubiquitination	EDVAFDEKKNVFVEF HHCCCCCCCCEEEEE	52.04	-
397	S-nitrosocysteine	VEFYAPWCGHCKQLA EEEECCCCCCHHHHH	2.31	-
397	S-nitrosylation	VEFYAPWCGHCKQLA EEEECCCCCCHHHHH	2.31	22178444
400	S-nitrosocysteine	YAPWCGHCKQLAPIW ECCCCCCHHHHHHHH	1.50	-
400	S-nitrosylation	YAPWCGHCKQLAPIW ECCCCCCHHHHHHHH	1.50	22178444
409	2-Hydroxyisobutyrylation	QLAPIWDKLGETYKD HHHHHHHHHCCCCCC	43.31	-
409	Acetylation	QLAPIWDKLGETYKD HHHHHHHHHCCCCCC	43.31	20167786
413	Phosphorylation	IWDKLGETYKDHENI HHHHHCCCCCCCCCE	33.79	28152594
414	Phosphorylation	WDKLGETYKDHENIV HHHHCCCCCCCCCEE	15.32	28152594
415	Acetylation	DKLGETYKDHENIVI HHHCCCCCCCCCEEE	61.09	26822725
415	Ubiquitination	DKLGETYKDHENIVI HHHCCCCCCCCCEEE	61.09	-
424	2-Hydroxyisobutyrylation	HENIVIAKMDSTANE CCCEEEEEECCCCCC	31.92	-
424	Acetylation	HENIVIAKMDSTANE CCCEEEEEECCCCCC	31.92	27452117
424	Ubiquitination	HENIVIAKMDSTANE CCCEEEEEECCCCCC	31.92	-
425	Sulfoxidation	ENIVIAKMDSTANEV CCEEEEEECCCCCCE	3.48	21406390
427	Phosphorylation	IVIAKMDSTANEVEA EEEEEECCCCCCEEE	26.39	23911959
428	Phosphorylation	VIAKMDSTANEVEAV EEEEECCCCCCEEEE	29.28	23911959
436	2-Hydroxyisobutyrylation	ANEVEAVKVHSFPTL CCCEEEEEEECCCCE	41.08	-
436	Acetylation	ANEVEAVKVHSFPTL CCCEEEEEEECCCCE	41.08	26051181
439	Phosphorylation	VEAVKVHSFPTLKFF EEEEEEECCCCEEEE	35.59	25159151
442	O-linked_Glycosylation	VKVHSFPTLKFFPAS EEEECCCCEEEECCC	40.34	29155159
442	Phosphorylation	VKVHSFPTLKFFPAS EEEECCCCEEEECCC	40.34	27251275
444	Ubiquitination	VHSFPTLKFFPASAD EECCCCEEEECCCCC	47.65	21890473
444	2-Hydroxyisobutyrylation	VHSFPTLKFFPASAD EECCCCEEEECCCCC	47.65	-
444	Acetylation	VHSFPTLKFFPASAD EECCCCEEEECCCCC	47.65	27178108
444	Ubiquitination	VHSFPTLKFFPASAD EECCCCEEEECCCCC	47.65	21890473
452	Methylation	FFPASADRTVIDYNG EECCCCCCEEEECCC	30.52	115486827
453	Phosphorylation	FPASADRTVIDYNGE ECCCCCCEEEECCCE	23.51	24719451
457	Phosphorylation	ADRTVIDYNGERTLD CCCEEEECCCEEEHH	17.59	28152594
462	Phosphorylation	IDYNGERTLDGFKKF EECCCEEEHHHHHHH	25.54	24719451
467	2-Hydroxyisobutyrylation	ERTLDGFKKFLESGG EEEHHHHHHHHHHCC	48.41	-
467	Acetylation	ERTLDGFKKFLESGG EEEHHHHHHHHHHCC	48.41	27452117
467	Methylation	ERTLDGFKKFLESGG EEEHHHHHHHHHHCC	48.41	2380271
467	Ubiquitination	ERTLDGFKKFLESGG EEEHHHHHHHHHHCC	48.41	-
472	Phosphorylation	GFKKFLESGGQDGAG HHHHHHHHCCCCCCC	50.82	29853039
495	Sulfoxidation	EEAEEPDMEEDDDQK HHHHCCCCCCCCHHH	9.94	30846556

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
357	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PDIA1_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 PDIA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FEZ1_HUMAN	FEZ1	physical	16169070
PTN_HUMAN	PTN	physical	16169070
THYG_HUMAN	TG	physical	10636893
PDIA6_HUMAN	PDIA6	physical	22939629
PPIB_HUMAN	PPIB	physical	22939629
PDIA4_HUMAN	PDIA4	physical	22939629
SURF4_HUMAN	SURF4	physical	22939629
TCPD_HUMAN	CCT4	physical	22939629
SERPH_HUMAN	SERPINH1	physical	22939629
TXNL1_HUMAN	TXNL1	physical	22939629
TMED9_HUMAN	TMED9	physical	22939629
TCPH_HUMAN	CCT7	physical	22939629
CALU_HUMAN	CALU	physical	22863883
PFD2_HUMAN	PFDN2	physical	22863883
PLIN3_HUMAN	PLIN3	physical	22863883
PSMD9_HUMAN	PSMD9	physical	22863883
TCAL4_HUMAN	TCEAL4	physical	22863883
PDIA1_HUMAN	P4HB	physical	25416956
SUCO_HUMAN	SUCO	physical	26186194
ZN292_HUMAN	ZNF292	physical	26186194
P4HA2_HUMAN	P4HA2	physical	26186194
ZBTB2_HUMAN	ZBTB2	physical	26186194
PDIA1_HUMAN	P4HB	physical	24549644
CALU_HUMAN	CALU	physical	26344197
DNJC3_HUMAN	DNAJC3	physical	26344197
ERO1A_HUMAN	ERO1L	physical	26344197
GSTO1_HUMAN	GSTO1	physical	26344197
HCD2_HUMAN	HSD17B10	physical	26344197
ENPL_HUMAN	HSP90B1	physical	26344197
CH60_HUMAN	HSPD1	physical	26344197
NACA2_HUMAN	NACA2	physical	26344197
P4HA1_HUMAN	P4HA1	physical	26344197
P4HA2_HUMAN	P4HA2	physical	26344197
PR40B_HUMAN	PRPF40B	physical	26344197
PSA7_HUMAN	PSMA7	physical	26344197
RCN1_HUMAN	RCN1	physical	26344197
UCHL3_HUMAN	UCHL3	physical	26344197
TERA_HUMAN	VCP	physical	26344197
MTP_HUMAN	MTTP	physical	23475612
SUCO_HUMAN	SUCO	physical	28514442
ZBTB2_HUMAN	ZBTB2	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 112240: Cole-Carpenter syndrome 1 (CLCRP1)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.