PDIA1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PDIA1_MOUSE
• UniProt AC: P09103
• Protein Name: Protein disulfide-isomerase
• Gene Name: P4hb
• Organism: Mus musculus (Mouse).
• Sequence Length: 509
• 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 (By similarity). 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: MLSRALLCLALAWAARVGADALEEEDNVLVLKKSNFEEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAAKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFKNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLSDTAAAESLVDSSEVTVIGFFKDVESDSAKQFLLAAEAIDDIPFGITSNSGVFSKYQLDKDGVVLFKKFDEGRNNFEGEITKEKLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSSFKRAAEGFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESDELTAEKITEFCHRFLEGKIKPHLMSQEVPEDWDKQPVKVLVGANFEEVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIIIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDEDLDLEEALEPDMEEDDDQKAVKDEL

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
33	Acetylation	DNVLVLKKSNFEEAL CCEEEEECCCHHHHH	46.61	22826441
33	Ubiquitination	DNVLVLKKSNFEEAL CCEEEEECCCHHHHH	46.61	22790023
34	Phosphorylation	NVLVLKKSNFEEALA CEEEEECCCHHHHHH	45.20	28464351
67	Malonylation	ALAPEYAKAAAKLKA HHCHHHHHHHHHHHH	37.34	26320211
67	Acetylation	ALAPEYAKAAAKLKA HHCHHHHHHHHHHHH	37.34	23806337
67	Ubiquitination	ALAPEYAKAAAKLKA HHCHHHHHHHHHHHH	37.34	27667366
67	Succinylation	ALAPEYAKAAAKLKA HHCHHHHHHHHHHHH	37.34	-
73	Succinylation	AKAAAKLKAEGSEIR HHHHHHHHHCCCEEE	43.62	23954790
83	Succinylation	GSEIRLAKVDATEES CCEEEEEECCCCCHH	45.28	23954790
83	Acetylation	GSEIRLAKVDATEES CCEEEEEECCCCCHH	45.28	23864654
83	Ubiquitination	GSEIRLAKVDATEES CCEEEEEECCCCCHH	45.28	-
90	Phosphorylation	KVDATEESDLAQQYG ECCCCCHHHHHHHHC	31.52	26525534
105	Acetylation	VRGYPTIKFFKNGDT CCCCCEEEEEECCCC	47.42	22826441
108	Succinylation	YPTIKFFKNGDTASP CCEEEEEECCCCCCH	64.25	23954790
108	Ubiquitination	YPTIKFFKNGDTASP CCEEEEEECCCCCCH	64.25	-
108	Acetylation	YPTIKFFKNGDTASP CCEEEEEECCCCCCH	64.25	22826441
114	Phosphorylation	FKNGDTASPKEYTAG EECCCCCCHHHHCCC	38.30	18779572
116	Acetylation	NGDTASPKEYTAGRE CCCCCCHHHHCCCCC	61.94	23954790
116	Succinylation	NGDTASPKEYTAGRE CCCCCCHHHHCCCCC	61.94	23954790
132	Ubiquitination	DDIVNWLKKRTGPAA HHHHHHHHHHCCCCC	31.65	-
132	Succinylation	DDIVNWLKKRTGPAA HHHHHHHHHHCCCCC	31.65	23806337
132	Acetylation	DDIVNWLKKRTGPAA HHHHHHHHHHCCCCC	31.65	23806337
135	Phosphorylation	VNWLKKRTGPAATTL HHHHHHHCCCCCCCH	57.29	23984901
140	Phosphorylation	KRTGPAATTLSDTAA HHCCCCCCCHHHHHH	30.31	23984901
141	Phosphorylation	RTGPAATTLSDTAAA HCCCCCCCHHHHHHH	21.38	23984901
143	Phosphorylation	GPAATTLSDTAAAES CCCCCCHHHHHHHHH	30.72	23984901
145	Phosphorylation	AATTLSDTAAAESLV CCCCHHHHHHHHHHC	18.15	23984901
150	Phosphorylation	SDTAAAESLVDSSEV HHHHHHHHHCCCCCE	29.03	23984901
168	Phosphorylation	GFFKDVESDSAKQFL EEEECCCCCCHHHHH	36.39	26239621
170	Phosphorylation	FKDVESDSAKQFLLA EECCCCCCHHHHHHH	46.79	26239621
192	Phosphorylation	PFGITSNSGVFSKYQ CCCEECCCCCCCEEE	35.78	23984901
196	Phosphorylation	TSNSGVFSKYQLDKD ECCCCCCCEEEECCC	28.22	23984901
202	Succinylation	FSKYQLDKDGVVLFK CCEEEECCCCEEEEE	66.04	23806337
202	Acetylation	FSKYQLDKDGVVLFK CCEEEECCCCEEEEE	66.04	23806337
202	Ubiquitination	FSKYQLDKDGVVLFK CCEEEECCCCEEEEE	66.04	-
209	Acetylation	KDGVVLFKKFDEGRN CCCEEEEEECCCCCC	48.66	23864654
210	Acetylation	DGVVLFKKFDEGRNN CCEEEEEECCCCCCC	51.19	133419
224	Acetylation	NFEGEITKEKLLDFI CCCCEECHHHHHHHH	59.52	23864654
224	Succinylation	NFEGEITKEKLLDFI CCCCEECHHHHHHHH	59.52	23806337
224	Succinylation	NFEGEITKEKLLDFI CCCCEECHHHHHHHH	59.52	-
226	Ubiquitination	EGEITKEKLLDFIKH CCEECHHHHHHHHHC	56.77	-
226	Succinylation	EGEITKEKLLDFIKH CCEECHHHHHHHHHC	56.77	23954790
232	Acetylation	EKLLDFIKHNQLPLV HHHHHHHHCCCCCEE	36.17	22826441
257	Phosphorylation	IFGGEIKTHILLFLP CCCCEEEEEEEEECC	21.58	22817900
265	Succinylation	HILLFLPKSVSDYDG EEEEECCCCHHCCCC	66.68	23954790
265	Acetylation	HILLFLPKSVSDYDG EEEEECCCCHHCCCC	66.68	23864654
266	Phosphorylation	ILLFLPKSVSDYDGK EEEECCCCHHCCCCC	25.55	28464351
273	Succinylation	SVSDYDGKLSSFKRA CHHCCCCCHHHHHHH	42.15	23806337
273	Succinylation	SVSDYDGKLSSFKRA CHHCCCCCHHHHHHH	42.15	-
273	Ubiquitination	SVSDYDGKLSSFKRA CHHCCCCCHHHHHHH	42.15	-
273	Acetylation	SVSDYDGKLSSFKRA CHHCCCCCHHHHHHH	42.15	23864654
275	Phosphorylation	SDYDGKLSSFKRAAE HCCCCCHHHHHHHHC	36.90	28464351
278	Acetylation	DGKLSSFKRAAEGFK CCCHHHHHHHHCCCC	42.97	22826441
285	Acetylation	KRAAEGFKGKILFIF HHHHCCCCCEEEEEE	70.88	2372715
310	Ubiquitination	ILEFFGLKKEECPAV HHHHHCCCHHHCCCE	59.52	-
310	Succinylation	ILEFFGLKKEECPAV HHHHHCCCHHHCCCE	59.52	23954790
310	Acetylation	ILEFFGLKKEECPAV HHHHHCCCHHHCCCE	59.52	23954790
311	Acetylation	LEFFGLKKEECPAVR HHHHCCCHHHCCCEE	64.88	22826441
314	S-palmitoylation	FGLKKEECPAVRLIT HCCCHHHCCCEEEEE	2.48	26165157
314	Glutathionylation	FGLKKEECPAVRLIT HCCCHHHCCCEEEEE	2.48	24333276
314	S-nitrosocysteine	FGLKKEECPAVRLIT HCCCHHHCCCEEEEE	2.48	-
328	Acetylation	TLEEEMTKYKPESDE ECCHHHHHCCCCCCC	50.39	23864654
328	Succinylation	TLEEEMTKYKPESDE ECCHHHHHCCCCCCC	50.39	23954790
330	Acetylation	EEEMTKYKPESDELT CHHHHHCCCCCCCCC	43.81	23864654
333	Phosphorylation	MTKYKPESDELTAEK HHHCCCCCCCCCHHH	44.93	28464351
340	Acetylation	SDELTAEKITEFCHR CCCCCHHHHHHHHHH	53.08	23864654
345	S-palmitoylation	AEKITEFCHRFLEGK HHHHHHHHHHHHCCC	1.51	26165157
354	Acetylation	RFLEGKIKPHLMSQE HHHCCCCCHHHHCCC	29.85	23201123
359	Phosphorylation	KIKPHLMSQEVPEDW CCCHHHHCCCCCCCC	29.55	-
368	Acetylation	EVPEDWDKQPVKVLV CCCCCCCCCCCEEEE	52.85	23806337
387	Acetylation	EEVAFDEKKNVFVEF EEEEECCCCCEEEEE	52.04	23806337
387	Ubiquitination	EEVAFDEKKNVFVEF EEEEECCCCCEEEEE	52.04	-
387	Succinylation	EEVAFDEKKNVFVEF EEEEECCCCCEEEEE	52.04	23954790
411	Succinylation	QLAPIWDKLGETYKD HHHHHHHHHCCCCCC	43.31	23954790
411	Acetylation	QLAPIWDKLGETYKD HHHHHHHHHCCCCCC	43.31	23864654
417	Succinylation	DKLGETYKDHENIII HHHCCCCCCCCCEEE	61.09	23954790
417	Acetylation	DKLGETYKDHENIII HHHCCCCCCCCCEEE	61.09	23864654
429	Phosphorylation	IIIAKMDSTANEVEA EEEEEECCCCCCEEE	26.39	29899451
438	Acetylation	ANEVEAVKVHSFPTL CCCEEEEEEECCCCE	41.08	22826441
441	Phosphorylation	VEAVKVHSFPTLKFF EEEEEEECCCCEEEE	35.59	-
444	Phosphorylation	VKVHSFPTLKFFPAS EEEECCCCEEEECCC	40.34	22817900
446	Ubiquitination	VHSFPTLKFFPASAD EECCCCEEEECCCCC	47.65	-
446	Succinylation	VHSFPTLKFFPASAD EECCCCEEEECCCCC	47.65	23806337
446	Acetylation	VHSFPTLKFFPASAD EECCCCEEEECCCCC	47.65	23806337
451	Phosphorylation	TLKFFPASADRTVID CEEEECCCCCCEEEE	30.82	28464351
464	Phosphorylation	IDYNGERTLDGFKKF EECCCEEEHHHHHHH	25.54	-
469	Acetylation	ERTLDGFKKFLESGG EEEHHHHHHHHHCCC	48.41	23864654
469	Succinylation	ERTLDGFKKFLESGG EEEHHHHHHHHHCCC	48.41	23954790
474	Phosphorylation	GFKKFLESGGQDGAG HHHHHHHCCCCCCCC	50.82	22942356

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

Oops, there are no upstream regulatory protein records of PDIA1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PDIA1_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of PDIA1_MOUSE !!

Drug and Disease Associations

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