dbPTM

IDHP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IDHP_HUMAN
UniProt AC	P48735
Protein Name	Isocitrate dehydrogenase [NADP], mitochondrial
Gene Name	IDH2
Organism	Homo sapiens (Human).
Sequence Length	452
Subcellular Localization	Mitochondrion.
Protein Description	Plays a role in intermediary metabolism and energy production. It may tightly associate or interact with the pyruvate dehydrogenase complex..
Protein Sequence	MAGYLRVVRSLCRASGSRPAWAPAALTAPTSQEQPRRHYADKRIKVAKPVVEMDGDEMTRIIWQFIKEKLILPHVDIQLKYFDLGLPNRDQTDDQVTIDSALATQKYSVAVKCATITPDEARVEEFKLKKMWKSPNGTIRNILGGTVFREPIICKNIPRLVPGWTKPITIGRHAHGDQYKATDFVADRAGTFKMVFTPKDGSGVKEWEVYNFPAGGVGMGMYNTDESISGFAHSCFQYAIQKKWPLYMSTKNTILKAYDGRFKDIFQEIFDKHYKTDFDKNKIWYEHRLIDDMVAQVLKSSGGFVWACKNYDGDVQSDILAQGFGSLGLMTSVLVCPDGKTIEAEAAHGTVTRHYREHQKGRPTSTNPIASIFAWTRGLEHRGKLDGNQDLIRFAQMLEKVCVETVESGAMTKDLAGCIHGLSNVKLNEHFLNTTDFLDTIKSNLDRALGRQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Ubiquitination	VRSLCRASGSRPAWA HHHHHHHCCCCCCCC	20.25	-
15	Acetylation	VRSLCRASGSRPAWA HHHHHHHCCCCCCCC	20.25	19608861
17	Acetylation	SLCRASGSRPAWAPA HHHHHCCCCCCCCCC	32.37	-
28	Acetylation	WAPAALTAPTSQEQP CCCCEECCCCCCCCC	13.26	-
28	Acetylation	WAPAALTAPTSQEQP CCCCEECCCCCCCCC	13.26	19608861
45	Acetylation	HYADKRIKVAKPVVE HHHCCCEEECCCEEE	39.92	25953088
45	Malonylation	HYADKRIKVAKPVVE HHHCCCEEECCCEEE	39.92	26320211
48	Acetylation	DKRIKVAKPVVEMDG CCCEEECCCEEEECH	41.13	23749302
48	Malonylation	DKRIKVAKPVVEMDG CCCEEECCCEEEECH	41.13	26320211
53	Sulfoxidation	VAKPVVEMDGDEMTR ECCCEEEECHHHHHH	4.76	21406390
54	Acetylation	AKPVVEMDGDEMTRI CCCEEEECHHHHHHH	48.13	-
54	Acetylation	AKPVVEMDGDEMTRI CCCEEEECHHHHHHH	48.13	19608861
60	Ubiquitination	MDGDEMTRIIWQFIK ECHHHHHHHHHHHHH	19.65	-
67	Acetylation	RIIWQFIKEKLILPH HHHHHHHHHCCCCCC	50.51	19608861
67	Ubiquitination	RIIWQFIKEKLILPH HHHHHHHHHCCCCCC	50.51	-
69	Acetylation	IWQFIKEKLILPHVD HHHHHHHCCCCCCCE	35.51	23749302
69	Malonylation	IWQFIKEKLILPHVD HHHHHHHCCCCCCCE	35.51	26320211
69	Ubiquitination	IWQFIKEKLILPHVD HHHHHHHCCCCCCCE	35.51	-
75	Acetylation	EKLILPHVDIQLKYF HCCCCCCCEEEEEEE	7.01	-
75	Ubiquitination	EKLILPHVDIQLKYF HCCCCCCCEEEEEEE	7.01	-
77	Ubiquitination	LILPHVDIQLKYFDL CCCCCCEEEEEEEEC	5.13	-
80	Acetylation	PHVDIQLKYFDLGLP CCCEEEEEEEECCCC	27.74	23954790
80	Succinylation	PHVDIQLKYFDLGLP CCCEEEEEEEECCCC	27.74	-
80	Succinylation	PHVDIQLKYFDLGLP CCCEEEEEEEECCCC	27.74	-
80	Ubiquitination	PHVDIQLKYFDLGLP CCCEEEEEEEECCCC	27.74	19608861
81	Acetylation	HVDIQLKYFDLGLPN CCEEEEEEEECCCCC	15.77	19608861
92	Phosphorylation	GLPNRDQTDDQVTID CCCCCCCCCCCEEHH	45.92	29978859
97	Phosphorylation	DQTDDQVTIDSALAT CCCCCCEEHHHHHHC	17.27	29978859
100	Phosphorylation	DDQVTIDSALATQKY CCCEEHHHHHHCCCE	22.72	29978859
103	Acetylation	VTIDSALATQKYSVA EEHHHHHHCCCEEEE	14.01	-
103	Acetylation	VTIDSALATQKYSVA EEHHHHHHCCCEEEE	14.01	19608861
104	Phosphorylation	TIDSALATQKYSVAV EHHHHHHCCCEEEEE	26.83	29978859
106	Acetylation	DSALATQKYSVAVKC HHHHHCCCEEEEEEE	34.83	19608861
106	Malonylation	DSALATQKYSVAVKC HHHHHCCCEEEEEEE	34.83	26320211
106	Succinylation	DSALATQKYSVAVKC HHHHHCCCEEEEEEE	34.83	-
106	Succinylation	DSALATQKYSVAVKC HHHHHCCCEEEEEEE	34.83	-
106	Ubiquitination	DSALATQKYSVAVKC HHHHHCCCEEEEEEE	34.83	19608861
107	Phosphorylation	SALATQKYSVAVKCA HHHHCCCEEEEEEEE	9.88	29978859
108	Phosphorylation	ALATQKYSVAVKCAT HHHCCCEEEEEEEEE	15.61	29978859
112	Ubiquitination	QKYSVAVKCATITPD CCEEEEEEEEEECCC	14.39	-
114	Acetylation	YSVAVKCATITPDEA EEEEEEEEEECCCHH	9.05	-
114	Ubiquitination	YSVAVKCATITPDEA EEEEEEEEEECCCHH	9.05	-
114	Acetylation	YSVAVKCATITPDEA EEEEEEEEEECCCHH	9.05	19608861
114	Ubiquitination	YSVAVKCATITPDEA EEEEEEEEEECCCHH	9.05	19608861
115	Phosphorylation	SVAVKCATITPDEAR EEEEEEEEECCCHHH	34.55	20058876
117	Phosphorylation	AVKCATITPDEARVE EEEEEEECCCHHHHH	21.97	27251275
127	Acetylation	EARVEEFKLKKMWKS HHHHHHHCHHHHCCC	63.78	23749302
127	Ubiquitination	EARVEEFKLKKMWKS HHHHHHHCHHHHCCC	63.78	-
128	Acetylation	ARVEEFKLKKMWKSP HHHHHHCHHHHCCCC	8.60	-
128	Ubiquitination	ARVEEFKLKKMWKSP HHHHHHCHHHHCCCC	8.60	-
128	Acetylation	ARVEEFKLKKMWKSP HHHHHHCHHHHCCCC	8.60	19608861
133	Acetylation	FKLKKMWKSPNGTIR HCHHHHCCCCCCCCC	53.16	19608861
133	Malonylation	FKLKKMWKSPNGTIR HCHHHHCCCCCCCCC	53.16	32601280
134	Phosphorylation	KLKKMWKSPNGTIRN CHHHHCCCCCCCCCH	14.21	21406692
138	Phosphorylation	MWKSPNGTIRNILGG HCCCCCCCCCHHHCC	24.33	21406692
141	Ubiquitination	SPNGTIRNILGGTVF CCCCCCCHHHCCCCC	29.95	-
146	Phosphorylation	IRNILGGTVFREPII CCHHHCCCCCCCCEE	18.05	27080861
155	Acetylation	FREPIICKNIPRLVP CCCCEECCCCCCCCC	47.72	19608861
155	Malonylation	FREPIICKNIPRLVP CCCCEECCCCCCCCC	47.72	26320211
155	Ubiquitination	FREPIICKNIPRLVP CCCCEECCCCCCCCC	47.72	19608861
166	Ubiquitination	RLVPGWTKPITIGRH CCCCCCCCCEEEECC	28.10	21890473
166	Acetylation	RLVPGWTKPITIGRH CCCCCCCCCEEEECC	28.10	19608861
166	Malonylation	RLVPGWTKPITIGRH CCCCCCCCCEEEECC	28.10	26320211
166	Succinylation	RLVPGWTKPITIGRH CCCCCCCCCEEEECC	28.10	-
166	Succinylation	RLVPGWTKPITIGRH CCCCCCCCCEEEECC	28.10	-
166	Ubiquitination	RLVPGWTKPITIGRH CCCCCCCCCEEEECC	28.10	21890473
179	Phosphorylation	RHAHGDQYKATDFVA CCCCCCHHCCCCCEE	13.82	-
180	Acetylation	HAHGDQYKATDFVAD CCCCCHHCCCCCEEC	38.89	19608861
180	Malonylation	HAHGDQYKATDFVAD CCCCCHHCCCCCEEC	38.89	26320211
180	Succinylation	HAHGDQYKATDFVAD CCCCCHHCCCCCEEC	38.89	-
180	Succinylation	HAHGDQYKATDFVAD CCCCCHHCCCCCEEC	38.89	-
180	Ubiquitination	HAHGDQYKATDFVAD CCCCCHHCCCCCEEC	38.89	19608861
182	Phosphorylation	HGDQYKATDFVADRA CCCHHCCCCCEECCC	26.31	-
188	Methylation	ATDFVADRAGTFKMV CCCCEECCCCEEEEE	25.77	115480147
191	Phosphorylation	FVADRAGTFKMVFTP CEECCCCEEEEEECC	21.06	-
193	Acetylation	ADRAGTFKMVFTPKD ECCCCEEEEEECCCC	33.71	25953088
193	Succinylation	ADRAGTFKMVFTPKD ECCCCEEEEEECCCC	33.71	-
193	Succinylation	ADRAGTFKMVFTPKD ECCCCEEEEEECCCC	33.71	-
193	Ubiquitination	ADRAGTFKMVFTPKD ECCCCEEEEEECCCC	33.71	-
197	Phosphorylation	GTFKMVFTPKDGSGV CEEEEEECCCCCCCC	20.30	-
199	Acetylation	FKMVFTPKDGSGVKE EEEEECCCCCCCCCE	72.21	-
199	Malonylation	FKMVFTPKDGSGVKE EEEEECCCCCCCCCE	72.21	26320211
199	Ubiquitination	FKMVFTPKDGSGVKE EEEEECCCCCCCCCE	72.21	-
204	Ubiquitination	TPKDGSGVKEWEVYN CCCCCCCCCEEEEEE	5.63	-
204	Acetylation	TPKDGSGVKEWEVYN CCCCCCCCCEEEEEE	5.63	19608861
204	Ubiquitination	TPKDGSGVKEWEVYN CCCCCCCCCEEEEEE	5.63	19608861
211	Acetylation	VKEWEVYNFPAGGVG CCEEEEEEECCCCCC	41.42	-
211	Ubiquitination	VKEWEVYNFPAGGVG CCEEEEEEECCCCCC	41.42	-
211	Acetylation	VKEWEVYNFPAGGVG CCEEEEEEECCCCCC	41.42	19608861
211	Ubiquitination	VKEWEVYNFPAGGVG CCEEEEEEECCCCCC	41.42	19608861
220	Acetylation	PAGGVGMGMYNTDES CCCCCCCCCCCCCCC	14.97	-
220	Ubiquitination	PAGGVGMGMYNTDES CCCCCCCCCCCCCCC	14.97	-
220	Acetylation	PAGGVGMGMYNTDES CCCCCCCCCCCCCCC	14.97	19608861
223	Acetylation	GVGMGMYNTDESISG CCCCCCCCCCCCHHH	31.96	19608861
228	Acetylation	MYNTDESISGFAHSC CCCCCCCHHHHHHHH	4.37	-
228	Ubiquitination	MYNTDESISGFAHSC CCCCCCCHHHHHHHH	4.37	-
230	Acetylation	NTDESISGFAHSCFQ CCCCCHHHHHHHHHH	23.30	-
230	Acetylation	NTDESISGFAHSCFQ CCCCCHHHHHHHHHH	23.30	19608861
242	Acetylation	CFQYAIQKKWPLYMS HHHHHHHHCCCEEEC	51.17	30582909
247	Phosphorylation	IQKKWPLYMSTKNTI HHHCCCEEECCCCCH	5.73	-
251	Acetylation	WPLYMSTKNTILKAY CCEEECCCCCHHHHC	44.80	25953088
256	Acetylation	STKNTILKAYDGRFK CCCCCHHHHCCCCHH	40.84	19608861
256	Succinylation	STKNTILKAYDGRFK CCCCCHHHHCCCCHH	40.84	-
256	Succinylation	STKNTILKAYDGRFK CCCCCHHHHCCCCHH	40.84	19608861
256	Ubiquitination	STKNTILKAYDGRFK CCCCCHHHHCCCCHH	40.84	19608861
258	Phosphorylation	KNTILKAYDGRFKDI CCCHHHHCCCCHHHH	19.83	22817900
263	Ubiquitination	KAYDGRFKDIFQEIF HHCCCCHHHHHHHHH	48.86	21890473
263	2-Hydroxyisobutyrylation	KAYDGRFKDIFQEIF HHCCCCHHHHHHHHH	48.86	-
263	Acetylation	KAYDGRFKDIFQEIF HHCCCCHHHHHHHHH	48.86	19608861
263	Ubiquitination	KAYDGRFKDIFQEIF HHCCCCHHHHHHHHH	48.86	19608861
272	Ubiquitination	IFQEIFDKHYKTDFD HHHHHHHHHCCCCCC	37.78	21890473
272	Acetylation	IFQEIFDKHYKTDFD HHHHHHHHHCCCCCC	37.78	19608861
272	Ubiquitination	IFQEIFDKHYKTDFD HHHHHHHHHCCCCCC	37.78	21890473
275	2-Hydroxyisobutyrylation	EIFDKHYKTDFDKNK HHHHHHCCCCCCCCC	41.14	-
275	Acetylation	EIFDKHYKTDFDKNK HHHHHHCCCCCCCCC	41.14	19608861
275	Ubiquitination	EIFDKHYKTDFDKNK HHHHHHCCCCCCCCC	41.14	19608861
280	Acetylation	HYKTDFDKNKIWYEH HCCCCCCCCCCHHHH	61.20	23749302
280	Ubiquitination	HYKTDFDKNKIWYEH HCCCCCCCCCCHHHH	61.20	-
282	2-Hydroxyisobutyrylation	KTDFDKNKIWYEHRL CCCCCCCCCHHHHHH	40.12	-
282	Acetylation	KTDFDKNKIWYEHRL CCCCCCCCCHHHHHH	40.12	19608861
282	Malonylation	KTDFDKNKIWYEHRL CCCCCCCCCHHHHHH	40.12	26320211
282	Succinylation	KTDFDKNKIWYEHRL CCCCCCCCCHHHHHH	40.12	-
282	Succinylation	KTDFDKNKIWYEHRL CCCCCCCCCHHHHHH	40.12	-
282	Ubiquitination	KTDFDKNKIWYEHRL CCCCCCCCCHHHHHH	40.12	19608861
293	Sulfoxidation	EHRLIDDMVAQVLKS HHHHHHHHHHHHHHH	2.09	21406390
299	Acetylation	DMVAQVLKSSGGFVW HHHHHHHHHCCCEEE	43.66	25038526
300	Phosphorylation	MVAQVLKSSGGFVWA HHHHHHHHCCCEEEE	30.01	26437602
301	Phosphorylation	VAQVLKSSGGFVWAC HHHHHHHCCCEEEEE	41.15	28857561
332	Acetylation	GSLGLMTSVLVCPDG CCCCEEEEEEECCCC	10.25	-
332	Ubiquitination	GSLGLMTSVLVCPDG CCCCEEEEEEECCCC	10.25	-
341	Phosphorylation	LVCPDGKTIEAEAAH EECCCCCEEEHHHHC	29.58	20068231
350	Phosphorylation	EAEAAHGTVTRHYRE EHHHHCCCHHHHHHH	14.61	30108239
352	Phosphorylation	EAAHGTVTRHYREHQ HHHCCCHHHHHHHHH	16.15	30108239
361	Acetylation	HYREHQKGRPTSTNP HHHHHHCCCCCCCCC	33.94	-
361	Ubiquitination	HYREHQKGRPTSTNP HHHHHHCCCCCCCCC	33.94	-
361	Acetylation	HYREHQKGRPTSTNP HHHHHHCCCCCCCCC	33.94	19608861
364	Phosphorylation	EHQKGRPTSTNPIAS HHHCCCCCCCCCHHH	46.99	30108239
365	Phosphorylation	HQKGRPTSTNPIASI HHCCCCCCCCCHHHH	28.95	28857561
366	Phosphorylation	QKGRPTSTNPIASIF HCCCCCCCCCHHHHH	47.71	30108239
371	Phosphorylation	TSTNPIASIFAWTRG CCCCCHHHHHHHHCC	20.96	21210654
376	Phosphorylation	IASIFAWTRGLEHRG HHHHHHHHCCCCCCC	16.07	21210654
384	2-Hydroxyisobutyrylation	RGLEHRGKLDGNQDL CCCCCCCCCCCCHHH	43.28	-
384	Acetylation	RGLEHRGKLDGNQDL CCCCCCCCCCCCHHH	43.28	23954790
384	Malonylation	RGLEHRGKLDGNQDL CCCCCCCCCCCCHHH	43.28	26320211
384	Succinylation	RGLEHRGKLDGNQDL CCCCCCCCCCCCHHH	43.28	-
384	Succinylation	RGLEHRGKLDGNQDL CCCCCCCCCCCCHHH	43.28	-
384	Ubiquitination	RGLEHRGKLDGNQDL CCCCCCCCCCCCHHH	43.28	-
390	Acetylation	GKLDGNQDLIRFAQM CCCCCCHHHHHHHHH	48.33	-
390	Acetylation	GKLDGNQDLIRFAQM CCCCCCHHHHHHHHH	48.33	19608861
400	Acetylation	RFAQMLEKVCVETVE HHHHHHHHHHHHHHH	36.65	25953088
400	Ubiquitination	RFAQMLEKVCVETVE HHHHHHHHHHHHHHH	36.65	-
411	Sulfoxidation	ETVESGAMTKDLAGC HHHHCCCCCHHHHHH	5.66	21406390
413	Acetylation	VESGAMTKDLAGCIH HHCCCCCHHHHHHHH	37.35	19608861
413	Malonylation	VESGAMTKDLAGCIH HHCCCCCHHHHHHHH	37.35	26320211
413	Succinylation	VESGAMTKDLAGCIH HHCCCCCHHHHHHHH	37.35	27452117
413	Ubiquitination	VESGAMTKDLAGCIH HHCCCCCHHHHHHHH	37.35	19608861
418	Glutathionylation	MTKDLAGCIHGLSNV CCHHHHHHHHHHCCC	1.40	22555962
423	Phosphorylation	AGCIHGLSNVKLNEH HHHHHHHCCCCCCHH	44.14	28450419
426	Acetylation	IHGLSNVKLNEHFLN HHHHCCCCCCHHHCC	50.25	25953088
426	Ubiquitination	IHGLSNVKLNEHFLN HHHHCCCCCCHHHCC	50.25	-
440	Phosphorylation	NTTDFLDTIKSNLDR CCHHHHHHHHHHHHH	32.24	28122231
442	Acetylation	TDFLDTIKSNLDRAL HHHHHHHHHHHHHHH	35.07	19608861
442	Ubiquitination	TDFLDTIKSNLDRAL HHHHHHHHHHHHHHH	35.07	19608861
443	Phosphorylation	DFLDTIKSNLDRALG HHHHHHHHHHHHHHC	38.48	28122231

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 IDHP_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
413	K	Acetylation		22416140
Acetylation at Lys-413 dramatically reduces catalytic activity.

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 IDHP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PYGL_HUMAN	PYGL	physical	21988832
IDHC_HUMAN	IDH1	physical	26344197
IDH3A_HUMAN	IDH3A	physical	26344197
IDH3B_HUMAN	IDH3B	physical	26344197
IDH3G_HUMAN	IDH3G	physical	26344197
TRAP1_HUMAN	TRAP1	physical	27173435
SND1_HUMAN	SND1	physical	27173435
ANXA5_HUMAN	ANXA5	physical	27173435
IF2P_HUMAN	EIF5B	physical	27173435
G6PI_HUMAN	GPI	physical	27173435
PDIA3_HUMAN	PDIA3	physical	27173435
UBE2N_HUMAN	UBE2N	physical	27173435
CRNN_HUMAN	CRNN	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613657	D-2-hydroxyglutaric aciduria 2 (D2HGA2)
137800	Glioma (GLM)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of IDHP_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-67; LYS-80; LYS-106;LYS-133; LYS-155; LYS-166; LYS-180; LYS-256; LYS-263; LYS-272;LYS-275; LYS-282 AND LYS-442, AND MASS SPECTROMETRY.	19608861 [Abstract]

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