dbPTM

PDIA4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PDIA4_HUMAN
UniProt AC	P13667
Protein Name	Protein disulfide-isomerase A4
Gene Name	PDIA4
Organism	Homo sapiens (Human).
Sequence Length	645
Subcellular Localization	Endoplasmic reticulum lumen . Melanosome . Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065).
Protein Description
Protein Sequence	MRPRKAFLLLLLLGLVQLLAVAGAEGPDEDSSNRENAIEDEEEEEEEDDDEEEDDLEVKEENGVLVLNDANFDNFVADKDTVLLEFYAPWCGHCKQFAPEYEKIANILKDKDPPIPVAKIDATSASVLASRFDVSGYPTIKILKKGQAVDYEGSRTQEEIVAKVREVSQPDWTPPPEVTLVLTKENFDEVVNDADIILVEFYAPWCGHCKKLAPEYEKAAKELSKRSPPIPLAKVDATAETDLAKRFDVSGYPTLKIFRKGRPYDYNGPREKYGIVDYMIEQSGPPSKEILTLKQVQEFLKDGDDVIIIGVFKGESDPAYQQYQDAANNLREDYKFHHTFSTEIAKFLKVSQGQLVVMQPEKFQSKYEPRSHMMDVQGSTQDSAIKDFVLKYALPLVGHRKVSNDAKRYTRRPLVVVYYSVDFSFDYRAATQFWRSKVLEVAKDFPEYTFAIADEEDYAGEVKDLGLSESGEDVNAAILDESGKKFAMEPEEFDSDTLREFVTAFKKGKLKPVIKSQPVPKNNKGPVKVVVGKTFDSIVMDPKKDVLIEFYAPWCGHCKQLEPVYNSLAKKYKGQKGLVIAKMDATANDVPSDRYKVEGFPTIYFAPSGDKKNPVKFEGGDRDLEHLSKFIEEHATKLSRTKEEL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
101	Phosphorylation	CKQFAPEYEKIANIL HHHHHHHHHHHHHHH	22.82	-
103	Ubiquitination	QFAPEYEKIANILKD HHHHHHHHHHHHHCC	46.33	21890473
103	Ubiquitination	QFAPEYEKIANILKD HHHHHHHHHHHHHCC	46.33	21890473
103	Ubiquitination	QFAPEYEKIANILKD HHHHHHHHHHHHHCC	46.33	21890473
111	2-Hydroxyisobutyrylation	IANILKDKDPPIPVA HHHHHCCCCCCCCCE	71.23	-
119	2-Hydroxyisobutyrylation	DPPIPVAKIDATSAS CCCCCCEEEECCCHH	41.16	-
119	Ubiquitination	DPPIPVAKIDATSAS CCCCCCEEEECCCHH	41.16	-
123	O-linked_Glycosylation	PVAKIDATSASVLAS CCEEEECCCHHHHHH	22.52	OGP
124	Phosphorylation	VAKIDATSASVLASR CEEEECCCHHHHHHC	21.92	21712546
126	Phosphorylation	KIDATSASVLASRFD EEECCCHHHHHHCCC	19.89	23403867
130	Phosphorylation	TSASVLASRFDVSGY CCHHHHHHCCCCCCC	29.35	21712546
135	Phosphorylation	LASRFDVSGYPTIKI HHHCCCCCCCCEEEE	34.16	23403867
137	Phosphorylation	SRFDVSGYPTIKILK HCCCCCCCCEEEEEE	6.95	23403867
141	Ubiquitination	VSGYPTIKILKKGQA CCCCCEEEEEECCCC	44.45	21890473
141	2-Hydroxyisobutyrylation	VSGYPTIKILKKGQA CCCCCEEEEEECCCC	44.45	-
141	Ubiquitination	VSGYPTIKILKKGQA CCCCCEEEEEECCCC	44.45	21890473
141	Ubiquitination	VSGYPTIKILKKGQA CCCCCEEEEEECCCC	44.45	21890473
144	Ubiquitination	YPTIKILKKGQAVDY CCEEEEEECCCCCCC	59.33	-
151	Phosphorylation	KKGQAVDYEGSRTQE ECCCCCCCCCCCCHH	18.65	28152594
154	Phosphorylation	QAVDYEGSRTQEEIV CCCCCCCCCCHHHHH	21.88	28152594
156	Phosphorylation	VDYEGSRTQEEIVAK CCCCCCCCHHHHHHH	41.87	23312004
163	Ubiquitination	TQEEIVAKVREVSQP CHHHHHHHHHHCCCC	30.82	-
168	Phosphorylation	VAKVREVSQPDWTPP HHHHHHCCCCCCCCC	31.10	21712546
173	Phosphorylation	EVSQPDWTPPPEVTL HCCCCCCCCCCCEEE	33.04	-
216	Phosphorylation	CKKLAPEYEKAAKEL HHHHHHHHHHHHHHH	22.98	28152594
218	Ubiquitination	KLAPEYEKAAKELSK HHHHHHHHHHHHHHH	53.38	-
227	Phosphorylation	AKELSKRSPPIPLAK HHHHHHCCCCCCCCC	38.47	23911959
234	2-Hydroxyisobutyrylation	SPPIPLAKVDATAET CCCCCCCCCCCCCCC	48.61	-
234	Ubiquitination	SPPIPLAKVDATAET CCCCCCCCCCCCCCC	48.61	-
238	Phosphorylation	PLAKVDATAETDLAK CCCCCCCCCCCHHHH	22.14	-
241	Phosphorylation	KVDATAETDLAKRFD CCCCCCCCHHHHHCC	33.57	-
245	2-Hydroxyisobutyrylation	TAETDLAKRFDVSGY CCCCHHHHHCCCCCC	61.98	-
245	Succinylation	TAETDLAKRFDVSGY CCCCHHHHHCCCCCC	61.98	23954790
245	Ubiquitination	TAETDLAKRFDVSGY CCCCHHHHHCCCCCC	61.98	-
250	Phosphorylation	LAKRFDVSGYPTLKI HHHHCCCCCCCCEEE	34.16	28152594
252	Phosphorylation	KRFDVSGYPTLKIFR HHCCCCCCCCEEEEE	5.87	28152594
254	Phosphorylation	FDVSGYPTLKIFRKG CCCCCCCCEEEEECC	32.00	28152594
256	Ubiquitination	VSGYPTLKIFRKGRP CCCCCCEEEEECCCC	42.13	21890473
256	Acetylation	VSGYPTLKIFRKGRP CCCCCCEEEEECCCC	42.13	88011
256	Ubiquitination	VSGYPTLKIFRKGRP CCCCCCEEEEECCCC	42.13	21890473
256	Ubiquitination	VSGYPTLKIFRKGRP CCCCCCEEEEECCCC	42.13	21890473
264	Phosphorylation	IFRKGRPYDYNGPRE EEECCCCCCCCCCHH	29.69	28152594
266	Phosphorylation	RKGRPYDYNGPREKY ECCCCCCCCCCHHHC	19.04	28152594
270	Methylation	PYDYNGPREKYGIVD CCCCCCCHHHCCHHH	55.21	115486859
272	2-Hydroxyisobutyrylation	DYNGPREKYGIVDYM CCCCCHHHCCHHHHH	50.48	-
272	Acetylation	DYNGPREKYGIVDYM CCCCCHHHCCHHHHH	50.48	25038526
273	Phosphorylation	YNGPREKYGIVDYMI CCCCHHHCCHHHHHH	13.82	28348404
278	Phosphorylation	EKYGIVDYMIEQSGP HHCCHHHHHHHCCCC	6.79	-
279	Sulfoxidation	KYGIVDYMIEQSGPP HCCHHHHHHHCCCCC	2.05	30846556
287	Phosphorylation	IEQSGPPSKEILTLK HHCCCCCCHHEEEHH	46.16	-
294	Ubiquitination	SKEILTLKQVQEFLK CHHEEEHHHHHHHHH	43.09	21890473
294	2-Hydroxyisobutyrylation	SKEILTLKQVQEFLK CHHEEEHHHHHHHHH	43.09	-
294	Ubiquitination	SKEILTLKQVQEFLK CHHEEEHHHHHHHHH	43.09	21890473
294	Ubiquitination	SKEILTLKQVQEFLK CHHEEEHHHHHHHHH	43.09	21890473
320	Phosphorylation	KGESDPAYQQYQDAA CCCCCHHHHHHHHHH	11.09	27642862
323	Phosphorylation	SDPAYQQYQDAANNL CCHHHHHHHHHHHHH	7.88	-
334	Phosphorylation	ANNLREDYKFHHTFS HHHHHHHHHHCCCCH	15.71	28152594
335	2-Hydroxyisobutyrylation	NNLREDYKFHHTFST HHHHHHHHHCCCCHH	51.01	-
335	Acetylation	NNLREDYKFHHTFST HHHHHHHHHCCCCHH	51.01	27452117
339	Phosphorylation	EDYKFHHTFSTEIAK HHHHHCCCCHHHHHH	15.65	28152594
341	Phosphorylation	YKFHHTFSTEIAKFL HHHCCCCHHHHHHHH	26.70	28152594
342	Phosphorylation	KFHHTFSTEIAKFLK HHCCCCHHHHHHHHC	27.50	28152594
351	Phosphorylation	IAKFLKVSQGQLVVM HHHHHCCCCCCEEEE	27.31	23911959
358	Sulfoxidation	SQGQLVVMQPEKFQS CCCCEEEECCHHHHC	4.25	21406390
362	2-Hydroxyisobutyrylation	LVVMQPEKFQSKYEP EEEECCHHHHCCCCC	56.22	-
362	Acetylation	LVVMQPEKFQSKYEP EEEECCHHHHCCCCC	56.22	27452117
365	Phosphorylation	MQPEKFQSKYEPRSH ECCHHHHCCCCCCCC	40.10	29449344
366	2-Hydroxyisobutyrylation	QPEKFQSKYEPRSHM CCHHHHCCCCCCCCC	42.73	-
366	Acetylation	QPEKFQSKYEPRSHM CCHHHHCCCCCCCCC	42.73	19608861
367	Phosphorylation	PEKFQSKYEPRSHMM CHHHHCCCCCCCCCC	36.09	22817900
371	Phosphorylation	QSKYEPRSHMMDVQG HCCCCCCCCCCCCCC	26.84	28258704
373	Sulfoxidation	KYEPRSHMMDVQGST CCCCCCCCCCCCCCC	2.30	21406390
374	Sulfoxidation	YEPRSHMMDVQGSTQ CCCCCCCCCCCCCCC	3.70	30846556
379	Phosphorylation	HMMDVQGSTQDSAIK CCCCCCCCCCHHHHH	13.05	28258704
380	Phosphorylation	MMDVQGSTQDSAIKD CCCCCCCCCHHHHHH	43.13	20068231
383	Phosphorylation	VQGSTQDSAIKDFVL CCCCCCHHHHHHHHH	23.29	20068231
386	Acetylation	STQDSAIKDFVLKYA CCCHHHHHHHHHHHH	44.84	26822725
391	Ubiquitination	AIKDFVLKYALPLVG HHHHHHHHHHHHHCC	24.15	21890473
391	Acetylation	AIKDFVLKYALPLVG HHHHHHHHHHHHHCC	24.15	25038526
391	Ubiquitination	AIKDFVLKYALPLVG HHHHHHHHHHHHHCC	24.15	21890473
391	Ubiquitination	AIKDFVLKYALPLVG HHHHHHHHHHHHHCC	24.15	21890473
392	Phosphorylation	IKDFVLKYALPLVGH HHHHHHHHHHHHCCC	14.81	24927040
403	Phosphorylation	LVGHRKVSNDAKRYT HCCCCCCCCCHHHHC	31.84	24719451
409	Phosphorylation	VSNDAKRYTRRPLVV CCCCHHHHCCCCEEE	12.14	24719451
410	Phosphorylation	SNDAKRYTRRPLVVV CCCHHHHCCCCEEEE	25.00	24719451
437	2-Hydroxyisobutyrylation	ATQFWRSKVLEVAKD HHHHHHHHHHHHHHH	42.12	-
448	Phosphorylation	VAKDFPEYTFAIADE HHHHCCCCEEEEECC	13.85	-
449	Phosphorylation	AKDFPEYTFAIADEE HHHCCCCEEEEECCC	12.62	-
458	Phosphorylation	AIADEEDYAGEVKDL EEECCCCCCCCCCCC	21.56	-
468	Phosphorylation	EVKDLGLSESGEDVN CCCCCCCCCCCCCCC	28.11	25693802
470	Phosphorylation	KDLGLSESGEDVNAA CCCCCCCCCCCCCHH	44.07	26657352
482	Phosphorylation	NAAILDESGKKFAME CHHEECCCCCEECCC	56.43	25693802
484	Acetylation	AILDESGKKFAMEPE HEECCCCCEECCCHH	54.73	69971
484	Ubiquitination	AILDESGKKFAMEPE HEECCCCCEECCCHH	54.73	-
485	Acetylation	ILDESGKKFAMEPEE EECCCCCEECCCHHH	41.71	27452117
488	Sulfoxidation	ESGKKFAMEPEEFDS CCCCEECCCHHHCCH	11.26	30846556
495	Phosphorylation	MEPEEFDSDTLREFV CCHHHCCHHHHHHHH	37.50	-
503	O-linked_Glycosylation	DTLREFVTAFKKGKL HHHHHHHHHHHCCCC	31.53	55829001
506	2-Hydroxyisobutyrylation	REFVTAFKKGKLKPV HHHHHHHHCCCCCCC	59.14	-
506	Acetylation	REFVTAFKKGKLKPV HHHHHHHHCCCCCCC	59.14	7479711
509	Acetylation	VTAFKKGKLKPVIKS HHHHHCCCCCCCCCC	63.32	7350211
516	Phosphorylation	KLKPVIKSQPVPKNN CCCCCCCCCCCCCCC	28.70	-
528	2-Hydroxyisobutyrylation	KNNKGPVKVVVGKTF CCCCCCEEEEEECEE	32.23	-
528	Succinylation	KNNKGPVKVVVGKTF CCCCCCEEEEEECEE	32.23	27452117
533	2-Hydroxyisobutyrylation	PVKVVVGKTFDSIVM CEEEEEECEECEEEC	34.11	-
533	Acetylation	PVKVVVGKTFDSIVM CEEEEEECEECEEEC	34.11	26822725
540	Sulfoxidation	KTFDSIVMDPKKDVL CEECEEECCCCCCEE	7.52	21406390
543	2-Hydroxyisobutyrylation	DSIVMDPKKDVLIEF CEEECCCCCCEEEEE	58.29	-
543	Succinylation	DSIVMDPKKDVLIEF CEEECCCCCCEEEEE	58.29	23954790
551	Phosphorylation	KDVLIEFYAPWCGHC CCEEEEEECCCCCCC	10.04	24719451
565	Phosphorylation	CKQLEPVYNSLAKKY CHHHHHHHHHHHHHH	15.11	-
567	Phosphorylation	QLEPVYNSLAKKYKG HHHHHHHHHHHHHCC	16.41	24719451
570	Succinylation	PVYNSLAKKYKGQKG HHHHHHHHHHCCCCC	63.03	23954790
572	Phosphorylation	YNSLAKKYKGQKGLV HHHHHHHHCCCCCEE	21.46	20068231
576	2-Hydroxyisobutyrylation	AKKYKGQKGLVIAKM HHHHCCCCCEEEEEE	63.98	-
576	Ubiquitination	AKKYKGQKGLVIAKM HHHHCCCCCEEEEEE	63.98	-
583	Sulfoxidation	KGLVIAKMDATANDV CCEEEEEEECCCCCC	2.91	21406390
586	Phosphorylation	VIAKMDATANDVPSD EEEEEECCCCCCCCC	23.02	-
592	Phosphorylation	ATANDVPSDRYKVEG CCCCCCCCCCCEECC	34.27	21712546
594	Methylation	ANDVPSDRYKVEGFP CCCCCCCCCEECCCC	37.19	115486867
595	Phosphorylation	NDVPSDRYKVEGFPT CCCCCCCCEECCCCE	25.11	28152594
596	Acetylation	DVPSDRYKVEGFPTI CCCCCCCEECCCCEE	34.40	26051181
602	Phosphorylation	YKVEGFPTIYFAPSG CEECCCCEEEECCCC	26.50	28152594
604	Phosphorylation	VEGFPTIYFAPSGDK ECCCCEEEECCCCCC	9.00	-
608	Phosphorylation	PTIYFAPSGDKKNPV CEEEECCCCCCCCCC	57.08	-
616	Acetylation	GDKKNPVKFEGGDRD CCCCCCCCCCCCCCC	38.67	27452117
629	2-Hydroxyisobutyrylation	RDLEHLSKFIEEHAT CCHHHHHHHHHHHHH	57.64	-
629	Acetylation	RDLEHLSKFIEEHAT CCHHHHHHHHHHHHH	57.64	26051181
637	2-Hydroxyisobutyrylation	FIEEHATKLSRTKEE HHHHHHHHHHHCHHC	45.29	-
637	Acetylation	FIEEHATKLSRTKEE HHHHHHHHHHHCHHC	45.29	27452117
639	Phosphorylation	EEHATKLSRTKEEL- HHHHHHHHHCHHCC-	39.19	24719451

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 PDIA4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PDIA4_HUMAN !!

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 PDIA4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ASNS_HUMAN	ASNS	physical	22863883
CAN2_HUMAN	CAPN2	physical	22863883
MOES_HUMAN	MSN	physical	22863883
ULA1_HUMAN	NAE1	physical	22863883
LIS1_HUMAN	PAFAH1B1	physical	22863883
PA1B2_HUMAN	PAFAH1B2	physical	22863883
IPP2_HUMAN	PPP1R2	physical	22863883
PLPHP_HUMAN	PROSC	physical	22863883
GDS1_HUMAN	RAP1GDS1	physical	22863883
TATD1_HUMAN	TATDN1	physical	22863883
EFTU_HUMAN	TUFM	physical	22863883
1433E_HUMAN	YWHAE	physical	22863883
1433F_HUMAN	YWHAH	physical	22863883
PDIA1_HUMAN	P4HB	physical	26344197
EMC7_HUMAN	EMC7	physical	28514442

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
There are no disease associations of PTM sites.

Regulatory Network of PDIA4_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-366, AND MASS SPECTROMETRY.	19608861 [Abstract]