PDIA1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PDIA1_RAT
• UniProt AC: P04785
• Protein Name: Protein disulfide-isomerase
• Gene Name: P4hb
• Organism: Rattus norvegicus (Rat).
• 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. 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..
• Protein Sequence: MLSRALLCLALAWAARVGADALEEEDNVLVLKKSNFAEALAAHNYLLVEFYAPWCGHCKALAPEYAKAAAKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFKNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLSDTAAAESLVDSSEVTVIGFFKDAGSDSAKQFLLAAEAVDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEITKEKLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKKAAEGFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESDELTAEKITQFCHHFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEEVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDNDDLDLEEALEPDMEEDDDQKAVKDEL

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
67	Acetylation	ALAPEYAKAAAKLKA HHCHHHHHHHHHHHH	37.34	22902405
73	Acetylation	AKAAAKLKAEGSEIR HHHHHHHHHCCCCEE	43.62	22902405
73	Succinylation	AKAAAKLKAEGSEIR HHHHHHHHHCCCCEE	43.62	26843850
83	Acetylation	GSEIRLAKVDATEES CCCEEEEECCCCCHH	45.28	22902405
87	Phosphorylation	RLAKVDATEESDLAQ EEEECCCCCHHHHHH	35.50	23984901
90	Phosphorylation	KVDATEESDLAQQYG ECCCCCHHHHHHHHC	31.52	23984901
105	Acetylation	VRGYPTIKFFKNGDT CCCCCEEEEEECCCC	47.42	22902405
108	Acetylation	YPTIKFFKNGDTASP CCEEEEEECCCCCCH	64.25	22902405
132	Acetylation	DDIVNWLKKRTGPAA HHHHHHHHHHCCCCC	31.65	22902405
202	Acetylation	FSKYQLDKDGVVLFK HHHCEECCCCEEEEE	66.04	22902405
202	Succinylation	FSKYQLDKDGVVLFK HHHCEECCCCEEEEE	66.04	26843850
210	Acetylation	DGVVLFKKFDEGRNN CCEEEEEECCCCCCC	51.19	22902405
224	Acetylation	NFEGEITKEKLLDFI CCCCEECHHHHHHHH	59.52	22902405
224	Succinylation	NFEGEITKEKLLDFI CCCCEECHHHHHHHH	59.52	-
224	Succinylation	NFEGEITKEKLLDFI CCCCEECHHHHHHHH	59.52	-
226	Acetylation	EGEITKEKLLDFIKH CCEECHHHHHHHHHC	56.77	22902405
273	Succinylation	SVSDYDGKLSNFKKA CHHHCCCCCHHHHHH	45.93	-
273	Acetylation	SVSDYDGKLSNFKKA CHHHCCCCCHHHHHH	45.93	22902405
273	Succinylation	SVSDYDGKLSNFKKA CHHHCCCCCHHHHHH	45.93	-
278	Acetylation	DGKLSNFKKAAEGFK CCCCHHHHHHHHCCC	45.83	22902405
310	Acetylation	ILEFFGLKKEECPAV HHHHHCCCHHHCCCE	59.52	22902405
311	Succinylation	LEFFGLKKEECPAVR HHHHCCCHHHCCCEE	64.88	26843850
328	Acetylation	TLEEEMTKYKPESDE ECCHHHHHCCCCCCC	50.39	22902405
330	Acetylation	EEEMTKYKPESDELT CHHHHHCCCCCCCCC	43.81	22902405
330	Succinylation	EEEMTKYKPESDELT CHHHHHCCCCCCCCC	43.81	26843850
333	Phosphorylation	MTKYKPESDELTAEK HHHCCCCCCCCCHHH	44.93	28432305
337	Phosphorylation	KPESDELTAEKITQF CCCCCCCCHHHHHHH	30.62	28432305
342	Phosphorylation	ELTAEKITQFCHHFL CCCHHHHHHHHHHHH	27.02	17089331
354	Acetylation	HFLEGKIKPHLMSQE HHHCCCCCHHHHCCC	29.85	22902405
354	Succinylation	HFLEGKIKPHLMSQE HHHCCCCCHHHHCCC	29.85	26843850
359	Phosphorylation	KIKPHLMSQELPEDW CCCHHHHCCCCCCCC	27.19	-
368	Acetylation	ELPEDWDKQPVKVLV CCCCCCCCCCCEEEE	52.85	22902405
368	Succinylation	ELPEDWDKQPVKVLV CCCCCCCCCCCEEEE	52.85	26843850
377	Acetylation	PVKVLVGKNFEEVAF CCEEEECCCHHHEEE	51.49	22902405
387	Acetylation	EEVAFDEKKNVFVEF HHEEECCCCCEEEEE	52.04	22902405
411	Acetylation	QLAPIWDKLGETYKD HHHHHHHHHCCCCCC	43.31	22902405
417	Succinylation	DKLGETYKDHENIVI HHHCCCCCCCCCEEE	61.09	26843850
429	Phosphorylation	IVIAKMDSTANEVEA EEEEEECCCCCCEEE	26.39	23984901
430	Phosphorylation	VIAKMDSTANEVEAV EEEEECCCCCCEEEE	29.28	23984901
438	Acetylation	ANEVEAVKVHSFPTL CCCEEEEEEECCCCE	41.08	22902405
441	Phosphorylation	VEAVKVHSFPTLKFF EEEEEEECCCCEEEE	35.59	29779826
451	Phosphorylation	TLKFFPASADRTVID CEEEECCCCCCEEEE	30.82	30181290
469	Acetylation	ERTLDGFKKFLESGG EEEHHHHHHHHHCCC	48.41	22902405

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

Oops, there are no upstream regulatory protein records of PDIA1_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PDIA1_RAT !!

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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SODC_RAT	Sod1	physical	23061969

Drug and Disease Associations

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