dbPTM

IDHC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IDHC_HUMAN
UniProt AC	O75874
Protein Name	Isocitrate dehydrogenase [NADP] cytoplasmic
Gene Name	IDH1
Organism	Homo sapiens (Human).
Sequence Length	414
Subcellular Localization	Cytoplasm . Peroxisome .
Protein Description
Protein Sequence	MSKKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSYDLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVSGWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGTQKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQKIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKGQETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEVSIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLGENLKIKLAQAKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSKKISGGS ------CCCCCCCCC	42.53	22814378
2	Phosphorylation	------MSKKISGGS ------CCCCCCCCC	42.53	29083192
6	Phosphorylation	--MSKKISGGSVVEM --CCCCCCCCCEEEE	46.08	28857561
9	Phosphorylation	SKKISGGSVVEMQGD CCCCCCCCEEEECHH	26.89	28857561
13	Sulfoxidation	SGGSVVEMQGDEMTR CCCCEEEECHHHHHH	3.49	30846556
18	Sulfoxidation	VEMQGDEMTRIIWEL EEECHHHHHHHHHHH	3.48	30846556
19	Phosphorylation	EMQGDEMTRIIWELI EECHHHHHHHHHHHH	19.37	20068231
29	Ubiquitination	IWELIKEKLIFPYVE HHHHHHHHCCCCEEE	41.71	-
34	Phosphorylation	KEKLIFPYVELDLHS HHHCCCCEEEEEEEE	8.87	-
41	Phosphorylation	YVELDLHSYDLGIEN EEEEEEEECCCCCCC	27.86	-
42	Phosphorylation	VELDLHSYDLGIENR EEEEEEECCCCCCCC	12.39	24927040
58	Acetylation	ATNDQVTKDAAEAIK CCCCCCCHHHHHHHH	46.65	23236377
58	Ubiquitination	ATNDQVTKDAAEAIK CCCCCCCHHHHHHHH	46.65	21906983
58	Ubiquitination	ATNDQVTKDAAEAIK CCCCCCCHHHHHHHH	46.65	21890473
65	Acetylation	KDAAEAIKKHNVGVK HHHHHHHHHCCCCCE	55.84	25953088
65	Ubiquitination	KDAAEAIKKHNVGVK HHHHHHHHHCCCCCE	55.84	-
72	Ubiquitination	KKHNVGVKCATITPD HHCCCCCEEEEECCC	16.54	-
73	S-nitrosylation	KHNVGVKCATITPDE HCCCCCEEEEECCCH	3.62	24105792
75	Phosphorylation	NVGVKCATITPDEKR CCCCEEEEECCCHHH	34.55	-
77	Phosphorylation	GVKCATITPDEKRVE CCEEEEECCCHHHHH	21.97	21815630
81	Acetylation	ATITPDEKRVEEFKL EEECCCHHHHHHHHH	69.95	23954790
81	Ubiquitination	ATITPDEKRVEEFKL EEECCCHHHHHHHHH	69.95	19608861
87	Acetylation	EKRVEEFKLKQMWKS HHHHHHHHHHHHHCC	59.04	27178108
87	Ubiquitination	EKRVEEFKLKQMWKS HHHHHHHHHHHHHCC	59.04	-
89	Ubiquitination	RVEEFKLKQMWKSPN HHHHHHHHHHHCCCC	38.40	-
93	Acetylation	FKLKQMWKSPNGTIR HHHHHHHCCCCCCCC	51.17	23954790
94	Phosphorylation	KLKQMWKSPNGTIRN HHHHHHCCCCCCCCH	14.21	28857561
98	Phosphorylation	MWKSPNGTIRNILGG HHCCCCCCCCHHHCC	24.33	21406692
106	Phosphorylation	IRNILGGTVFREAII CCHHHCCHHHHEHHH	18.05	23312004
114	S-nitrosylation	VFREAIICKNIPRLV HHHEHHHHCCCHHHH	1.95	24105792
115	Acetylation	FREAIICKNIPRLVS HHEHHHHCCCHHHHC	47.72	27178108
126	Acetylation	RLVSGWVKPIIIGRH HHHCCCCCCEEEECC	24.80	26051181
126	Succinylation	RLVSGWVKPIIIGRH HHHCCCCCCEEEECC	24.80	-
126	Succinylation	RLVSGWVKPIIIGRH HHHCCCCCCEEEECC	24.80	21890473
126	Ubiquitination	RLVSGWVKPIIIGRH HHHCCCCCCEEEECC	24.80	21890473
126	Ubiquitination	RLVSGWVKPIIIGRH HHHCCCCCCEEEECC	24.80	21890473
126	Ubiquitination	RLVSGWVKPIIIGRH HHHCCCCCCEEEECC	24.80	21890473
126	Ubiquitination	RLVSGWVKPIIIGRH HHHCCCCCCEEEECC	24.80	21890473
135	Phosphorylation	IIIGRHAYGDQYRAT EEEECCCCCCCCEEE	18.34	28152594
139	Phosphorylation	RHAYGDQYRATDFVV CCCCCCCCEEECEEE	13.62	28152594
151	Acetylation	FVVPGPGKVEITYTP EEECCCCEEEEEEEC	39.57	26051181
151	Ubiquitination	FVVPGPGKVEITYTP EEECCCCEEEEEEEC	39.57	21906983
155	Phosphorylation	GPGKVEITYTPSDGT CCCEEEEEEECCCCC	14.08	28152594
156	Phosphorylation	PGKVEITYTPSDGTQ CCEEEEEEECCCCCE	23.47	28152594
157	Phosphorylation	GKVEITYTPSDGTQK CEEEEEEECCCCCEE	13.99	28152594
159	Phosphorylation	VEITYTPSDGTQKVT EEEEEECCCCCEEEE	40.65	28152594
162	Phosphorylation	TYTPSDGTQKVTYLV EEECCCCCEEEEEEE	30.15	28152594
167	Phosphorylation	DGTQKVTYLVHNFEE CCCEEEEEEEEEECC	15.09	24275569
180	Sulfoxidation	EEGGGVAMGMYNQDK CCCCEEEEEEECCCC	2.70	30846556
182	Sulfoxidation	GGGVAMGMYNQDKSI CCEEEEEEECCCCCH	1.50	30846556
188	Phosphorylation	GMYNQDKSIEDFAHS EEECCCCCHHHHCHH	39.23	27251275
199	Sulfoxidation	FAHSSFQMALSKGWP HCHHHHHHHHHCCCC	3.69	30846556
208	Phosphorylation	LSKGWPLYLSTKNTI HHCCCCEEEEECCCH	8.43	28152594
210	Phosphorylation	KGWPLYLSTKNTILK CCCCEEEEECCCHHH	24.63	28152594
211	Phosphorylation	GWPLYLSTKNTILKK CCCEEEEECCCHHHH	26.22	28152594
212	Ubiquitination	WPLYLSTKNTILKKY CCEEEEECCCHHHHC	49.03	-
214	Phosphorylation	LYLSTKNTILKKYDG EEEEECCCHHHHCCC	29.28	28152594
219	Phosphorylation	KNTILKKYDGRFKDI CCCHHHHCCCCHHHH	23.26	20068231
224	Acetylation	KKYDGRFKDIFQEIY HHCCCCHHHHHHHHH	48.86	23954790
224	Ubiquitination	KKYDGRFKDIFQEIY HHCCCCHHHHHHHHH	48.86	21890473
224	Ubiquitination	KKYDGRFKDIFQEIY HHCCCCHHHHHHHHH	48.86	21890473
224	Ubiquitination	KKYDGRFKDIFQEIY HHCCCCHHHHHHHHH	48.86	21890473
224	Ubiquitination	KKYDGRFKDIFQEIY HHCCCCHHHHHHHHH	48.86	21890473
231	Phosphorylation	KDIFQEIYDKQYKSQ HHHHHHHHHHHHHHH	19.14	30108239
233	Acetylation	IFQEIYDKQYKSQFE HHHHHHHHHHHHHHH	38.26	27452117
233	Ubiquitination	IFQEIYDKQYKSQFE HHHHHHHHHHHHHHH	38.26	21890473
233	Ubiquitination	IFQEIYDKQYKSQFE HHHHHHHHHHHHHHH	38.26	21890473
233	Ubiquitination	IFQEIYDKQYKSQFE HHHHHHHHHHHHHHH	38.26	21890473
233	Ubiquitination	IFQEIYDKQYKSQFE HHHHHHHHHHHHHHH	38.26	21890473
236	Acetylation	EIYDKQYKSQFEAQK HHHHHHHHHHHHHHH	34.97	27452117
236	Ubiquitination	EIYDKQYKSQFEAQK HHHHHHHHHHHHHHH	34.97	-
237	Phosphorylation	IYDKQYKSQFEAQKI HHHHHHHHHHHHHHH	34.86	27251275
243	Acetylation	KSQFEAQKIWYEHRL HHHHHHHHHHHHHHH	42.10	23954790
243	Ubiquitination	KSQFEAQKIWYEHRL HHHHHHHHHHHHHHH	42.10	-
254	Sulfoxidation	EHRLIDDMVAQAMKS HHHHHHHHHHHHHHC	2.09	21406390
259	Sulfoxidation	DDMVAQAMKSEGGFI HHHHHHHHHCCCCEE	3.05	30846556
261	Phosphorylation	MVAQAMKSEGGFIWA HHHHHHHCCCCEEEE	28.52	21712546
269	Glutathionylation	EGGFIWACKNYDGDV CCCEEEEEECCCCCC	1.44	15653693
278	Phosphorylation	NYDGDVQSDSVAQGY CCCCCCCCCHHHCCC	31.53	22210691
280	Phosphorylation	DGDVQSDSVAQGYGS CCCCCCCHHHCCCCC	25.30	22210691
285	Phosphorylation	SDSVAQGYGSLGMMT CCHHHCCCCCCCCEE	7.46	22210691
287	Phosphorylation	SVAQGYGSLGMMTSV HHHCCCCCCCCEEEE	17.17	22210691
292	Phosphorylation	YGSLGMMTSVLVCPD CCCCCCEEEEEECCC	13.54	22210691
293	Phosphorylation	GSLGMMTSVLVCPDG CCCCCEEEEEECCCC	8.78	22210691
302	Phosphorylation	LVCPDGKTVEAEAAH EECCCCCEEEEHHHC	29.16	26437602
311	Phosphorylation	EAEAAHGTVTRHYRM EEHHHCCCCHHHHCC	14.61	26074081
313	Phosphorylation	EAAHGTVTRHYRMYQ HHHCCCCHHHHCCHH	16.15	26074081
316	Phosphorylation	HGTVTRHYRMYQKGQ CCCCHHHHCCHHCCC	8.19	26074081
319	Phosphorylation	VTRHYRMYQKGQETS CHHHHCCHHCCCCCC	9.70	26074081
321	Acetylation	RHYRMYQKGQETSTN HHHCCHHCCCCCCCC	45.11	19608861
321	Ubiquitination	RHYRMYQKGQETSTN HHHCCHHCCCCCCCC	45.11	21890473
321	Ubiquitination	RHYRMYQKGQETSTN HHHCCHHCCCCCCCC	45.11	21890473
321	Ubiquitination	RHYRMYQKGQETSTN HHHCCHHCCCCCCCC	45.11	21890473
321	Ubiquitination	RHYRMYQKGQETSTN HHHCCHHCCCCCCCC	45.11	21890473
325	Phosphorylation	MYQKGQETSTNPIAS CHHCCCCCCCCCHHH	32.72	-
350	Ubiquitination	RAKLDNNKELAFFAN HHCCCCCHHHHHHHH	61.43	-
372	Sulfoxidation	ETIEAGFMTKDLAAC HHHHCCCCCHHHHHH	4.44	30846556
379	S-nitrosylation	MTKDLAACIKGLPNV CCHHHHHHHCCCCCC	2.48	24105792
381	Acetylation	KDLAACIKGLPNVQR HHHHHHHCCCCCCCH	55.04	26051181
381	Ubiquitination	KDLAACIKGLPNVQR HHHHHHHCCCCCCCH	55.04	-
389	Phosphorylation	GLPNVQRSDYLNTFE CCCCCCHHHCCCHHH	17.32	28857561
391	Phosphorylation	PNVQRSDYLNTFEFM CCCCHHHCCCHHHHH	11.78	24927040
398	Sulfoxidation	YLNTFEFMDKLGENL CCCHHHHHHHHCHHH	3.32	30846556
400	Succinylation	NTFEFMDKLGENLKI CHHHHHHHHCHHHHH	46.75	-
400	Succinylation	NTFEFMDKLGENLKI CHHHHHHHHCHHHHH	46.75	-
400	Ubiquitination	NTFEFMDKLGENLKI CHHHHHHHHCHHHHH	46.75	-
406	Acetylation	DKLGENLKIKLAQAK HHHCHHHHHEEECCC	49.75	25953088
406	Ubiquitination	DKLGENLKIKLAQAK HHHCHHHHHEEECCC	49.75	-
408	Ubiquitination	LGENLKIKLAQAKL- HCHHHHHEEECCCC-	35.86	-

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 IDHC_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
374	K	Acetylation		-
Acetylation at Lys-374 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 IDHC_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZHX1_HUMAN	ZHX1	physical	16169070
KAD1_HUMAN	AK1	physical	22939629
MDHM_HUMAN	MDH2	physical	22939629
KAD2_HUMAN	AK2	physical	22939629
PURA2_HUMAN	ADSS	physical	22863883
GLRX3_HUMAN	GLRX3	physical	22863883
CH10_HUMAN	HSPE1	physical	22863883
PTMS_HUMAN	PTMS	physical	22863883
RBBP7_HUMAN	RBBP7	physical	22863883
RCN1_HUMAN	RCN1	physical	22863883
SGT1_HUMAN	SUGT1	physical	22863883
TALDO_HUMAN	TALDO1	physical	22863883
CAB39_HUMAN	CAB39	physical	26344197
DAZP1_HUMAN	DAZAP1	physical	26344197
FA49B_HUMAN	FAM49B	physical	26344197
DHB4_HUMAN	HSD17B4	physical	26344197
LKHA4_HUMAN	LTA4H	physical	26344197
PCBP1_HUMAN	PCBP1	physical	26344197
PHB2_HUMAN	PHB2	physical	26344197
IDHC_HUMAN	IDH1	physical	26280302
AGGF1_HUMAN	AGGF1	physical	27229929
DKK3_HUMAN	DKK3	physical	27229929
EFC4A_HUMAN	CRACR2B	physical	27229929
F131A_HUMAN	FAM131A	physical	27229929
FHL2_HUMAN	FHL2	physical	27229929
FIGL1_HUMAN	FIGNL1	physical	27229929
LAX1_HUMAN	LAX1	physical	27229929
NUP62_HUMAN	NUP62	physical	27229929
PRD14_HUMAN	PRDM14	physical	27229929
TMOD4_HUMAN	TMOD4	physical	27229929
UBL7_HUMAN	UBL7	physical	27229929

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
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 IDHC_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-81; LYS-224 AND LYS-321, ANDMASS SPECTROMETRY.	19608861 [Abstract]

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