dbPTM

IMDH2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IMDH2_HUMAN
UniProt AC	P12268
Protein Name	Inosine-5'-monophosphate dehydrogenase 2 {ECO:0000255\|HAMAP-Rule:MF_03156}
Gene Name	IMPDH2 {ECO:0000255\|HAMAP-Rule:MF_03156}
Organism	Homo sapiens (Human).
Sequence Length	514
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors..
Protein Sequence	MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
60	Phosphorylation	SALTKKITLKTPLVS HHHCCEEECCCCCCC	30.95	24719451
63	O-linked_Glycosylation	TKKITLKTPLVSSPM CCEEECCCCCCCCCC	25.60	23301498
108	Ubiquitination	ANEVRKVKKYEQGFI HHHHHHHHEECCCCC	53.31	-
109	Acetylation	NEVRKVKKYEQGFIT HHHHHHHEECCCCCC	57.94	26051181
109	Ubiquitination	NEVRKVKKYEQGFIT HHHHHHHEECCCCCC	57.94	-
110	Phosphorylation	EVRKVKKYEQGFITD HHHHHHEECCCCCCC	14.04	28152594
116	Phosphorylation	KYEQGFITDPVVLSP EECCCCCCCCEECCC	31.80	30266825
122	Phosphorylation	ITDPVVLSPKDRVRD CCCCEECCCHHHHHH	20.49	29255136
124	2-Hydroxyisobutyrylation	DPVVLSPKDRVRDVF CCEECCCHHHHHHHH	55.58	-
124	Acetylation	DPVVLSPKDRVRDVF CCEECCCHHHHHHHH	55.58	26051181
124	Ubiquitination	DPVVLSPKDRVRDVF CCEECCCHHHHHHHH	55.58	21906983
134	Acetylation	VRDVFEAKARHGFCG HHHHHHHHHHHCCCC	38.46	23749302
134	Ubiquitination	VRDVFEAKARHGFCG HHHHHHHHHHHCCCC	38.46	21890473
140	S-nitrosocysteine	AKARHGFCGIPITDT HHHHHCCCCCEECCC	5.98	-
140	Glutathionylation	AKARHGFCGIPITDT HHHHHCCCCCEECCC	5.98	22555962
140	S-nitrosylation	AKARHGFCGIPITDT HHHHHCCCCCEECCC	5.98	22178444
159	Phosphorylation	SRLVGIISSRDIDFL HHHEEEEECCCCCHH	19.87	29255136
160	Phosphorylation	RLVGIISSRDIDFLK HHEEEEECCCCCHHH	24.46	19664994
173	Glutathionylation	LKEEEHDCFLEEIMT HHHHHCCCHHHHHHH	4.53	22555962
173	S-nitrosylation	LKEEEHDCFLEEIMT HHHHHCCCHHHHHHH	4.53	22178444
179	Sulfoxidation	DCFLEEIMTKREDLV CCHHHHHHHHCHHEE	4.01	30846556
181	2-Hydroxyisobutyrylation	FLEEIMTKREDLVVA HHHHHHHHCHHEEEE	36.09	-
181	Ubiquitination	FLEEIMTKREDLVVA HHHHHHHHCHHEEEE	36.09	-
195	2-Hydroxyisobutyrylation	APAGITLKEANEILQ ECCCCCHHHHHHHHH	46.24	-
195	Acetylation	APAGITLKEANEILQ ECCCCCHHHHHHHHH	46.24	25953088
195	Sumoylation	APAGITLKEANEILQ ECCCCCHHHHHHHHH	46.24	28112733
195	Ubiquitination	APAGITLKEANEILQ ECCCCCHHHHHHHHH	46.24	21890473
203	Methylation	EANEILQRSKKGKLP HHHHHHHHHHCCCCC	47.18	-
205	Ubiquitination	NEILQRSKKGKLPIV HHHHHHHHCCCCCCC	68.67	-
206	Ubiquitination	EILQRSKKGKLPIVN HHHHHHHCCCCCCCC	63.63	-
208	Acetylation	LQRSKKGKLPIVNED HHHHHCCCCCCCCCC	61.03	23236377
208	Sumoylation	LQRSKKGKLPIVNED HHHHHCCCCCCCCCC	61.03	28112733
208	Ubiquitination	LQRSKKGKLPIVNED HHHHHCCCCCCCCCC	61.03	21890473
231	Methylation	RTDLKKNRDYPLASK ECCHHHCCCCCCCCH	54.44	-
233	Phosphorylation	DLKKNRDYPLASKDA CHHHCCCCCCCCHHH	9.26	21406692
237	Phosphorylation	NRDYPLASKDAKKQL CCCCCCCCHHHHHHH	38.46	21406692
238	2-Hydroxyisobutyrylation	RDYPLASKDAKKQLL CCCCCCCHHHHHHHH	56.98	-
238	Ubiquitination	RDYPLASKDAKKQLL CCCCCCCHHHHHHHH	56.98	21906983
242	2-Hydroxyisobutyrylation	LASKDAKKQLLCGAA CCCHHHHHHHHCCCC	48.15	-
242	Malonylation	LASKDAKKQLLCGAA CCCHHHHHHHHCCCC	48.15	26320211
242	Ubiquitination	LASKDAKKQLLCGAA CCCHHHHHHHHCCCC	48.15	-
246	Glutathionylation	DAKKQLLCGAAIGTH HHHHHHHCCCCCCCC	4.78	22555962
257	Acetylation	IGTHEDDKYRLDLLA CCCCCCHHHHHHHHH	44.59	26822725
257	Ubiquitination	IGTHEDDKYRLDLLA CCCCCCHHHHHHHHH	44.59	-
288	Ubiquitination	IFQINMIKYIKDKYP EEEEEEEHHHHHHCC	30.10	-
289	Phosphorylation	FQINMIKYIKDKYPN EEEEEEHHHHHHCCC	11.41	28152594
291	Acetylation	INMIKYIKDKYPNLQ EEEEHHHHHHCCCEE	45.11	26051181
291	Ubiquitination	INMIKYIKDKYPNLQ EEEEHHHHHHCCCEE	45.11	-
293	Acetylation	MIKYIKDKYPNLQVI EEHHHHHHCCCEEEE	58.57	23954790
293	Ubiquitination	MIKYIKDKYPNLQVI EEHHHHHHCCCEEEE	58.57	21890473
294	Phosphorylation	IKYIKDKYPNLQVIG EHHHHHHCCCEEEEC	13.90	28152594
306	Phosphorylation	VIGGNVVTAAQAKNL EECCCCCCHHHHHHH	16.40	-
311	Ubiquitination	VVTAAQAKNLIDAGV CCCHHHHHHHHHHCC	39.96	21906983
327	Phosphorylation	ALRVGMGSGSICITQ EEEECCCCCCEEEEH	22.07	28348404
329	Phosphorylation	RVGMGSGSICITQEV EECCCCCCEEEEHHH	18.91	28348404
345	Phosphorylation	ACGRPQATAVYKVSE HCCCCCCEEEEHHHH	16.06	20068231
348	Phosphorylation	RPQATAVYKVSEYAR CCCCEEEEHHHHHHH	11.83	20090780
349	Ubiquitination	PQATAVYKVSEYARR CCCEEEEHHHHHHHH	32.46	21906983
351	Phosphorylation	ATAVYKVSEYARRFG CEEEEHHHHHHHHHC	22.27	20068231
353	Phosphorylation	AVYKVSEYARRFGVP EEEHHHHHHHHHCCC	9.63	20068231
375	Ubiquitination	QNVGHIAKALALGAS CCHHHHHHHHHHCCH	43.24	-
400	Phosphorylation	TTEAPGEYFFSDGIR CCCCCCCEECCCCCE	18.81	22817900
411	Phosphorylation	DGIRLKKYRGMGSLD CCCEEEEECCCCCHH	15.71	30576142
412	Methylation	GIRLKKYRGMGSLDA CCEEEEECCCCCHHH	37.19	115480315
416	Phosphorylation	KKYRGMGSLDAMDKH EEECCCCCHHHHHHH	17.74	29255136
422	2-Hydroxyisobutyrylation	GSLDAMDKHLSSQNR CCHHHHHHHHHHCCC	33.10	-
422	Acetylation	GSLDAMDKHLSSQNR CCHHHHHHHHHHCCC	33.10	23954790
422	Malonylation	GSLDAMDKHLSSQNR CCHHHHHHHHHHCCC	33.10	26320211
422	Ubiquitination	GSLDAMDKHLSSQNR CCHHHHHHHHHHCCC	33.10	21890473
425	Phosphorylation	DAMDKHLSSQNRYFS HHHHHHHHHCCCCCC	29.60	23401153
426	Phosphorylation	AMDKHLSSQNRYFSE HHHHHHHHCCCCCCH	37.52	20068231
429	Methylation	KHLSSQNRYFSEADK HHHHHCCCCCCHHHH	26.66	115480299
430	Phosphorylation	HLSSQNRYFSEADKI HHHHCCCCCCHHHHH	21.00	28152594
432	Phosphorylation	SSQNRYFSEADKIKV HHCCCCCCHHHHHHE	23.96	30108239
436	Acetylation	RYFSEADKIKVAQGV CCCCHHHHHHEECCC	52.02	23954790
436	Malonylation	RYFSEADKIKVAQGV CCCCHHHHHHEECCC	52.02	26320211
436	Ubiquitination	RYFSEADKIKVAQGV CCCCHHHHHHEECCC	52.02	21906983
438	2-Hydroxyisobutyrylation	FSEADKIKVAQGVSG CCHHHHHHEECCCCC	36.94	-
438	Acetylation	FSEADKIKVAQGVSG CCHHHHHHEECCCCC	36.94	25953088
438	Malonylation	FSEADKIKVAQGVSG CCHHHHHHEECCCCC	36.94	26320211
438	Sumoylation	FSEADKIKVAQGVSG CCHHHHHHEECCCCC	36.94	28112733
438	Ubiquitination	FSEADKIKVAQGVSG CCHHHHHHEECCCCC	36.94	21906983
444	Phosphorylation	IKVAQGVSGAVQDKG HHEECCCCCCCCCCC	28.05	25159151
450	Acetylation	VSGAVQDKGSIHKFV CCCCCCCCCCHHHHH	37.15	25953088
450	Ubiquitination	VSGAVQDKGSIHKFV CCCCCCCCCCHHHHH	37.15	21906983
455	Acetylation	QDKGSIHKFVPYLIA CCCCCHHHHHHHHHH	46.52	25953088
455	Ubiquitination	QDKGSIHKFVPYLIA CCCCCHHHHHHHHHH	46.52	21906983
459	Phosphorylation	SIHKFVPYLIAGIQH CHHHHHHHHHHHHHH	12.87	24927040
468	S-palmitoylation	IAGIQHSCQDIGAKS HHHHHHHHHHCCCCC	3.85	29575903
474	Acetylation	SCQDIGAKSLTQVRA HHHHCCCCCHHHHHH	40.56	26051181
474	Ubiquitination	SCQDIGAKSLTQVRA HHHHCCCCCHHHHHH	40.56	21890473
489	Ubiquitination	MMYSGELKFEKRTSS HHHCCCCEEEECCCC	47.37	21906983
494	Phosphorylation	ELKFEKRTSSAQVEG CCEEEECCCCCEEEC	37.79	23186163
495	Phosphorylation	LKFEKRTSSAQVEGG CEEEECCCCCEEECC	27.92	25159151
496	Phosphorylation	KFEKRTSSAQVEGGV EEEECCCCCEEECCC	23.31	29214152
505	Phosphorylation	QVEGGVHSLHSYEKR EEECCCCCCCCHHHC	25.93	28152594
508	Phosphorylation	GGVHSLHSYEKRLF- CCCCCCCCHHHCCC-	40.04	28152594
509	Phosphorylation	GVHSLHSYEKRLF-- CCCCCCCHHHCCC--	18.09	28152594
511	2-Hydroxyisobutyrylation	HSLHSYEKRLF---- CCCCCHHHCCC----	46.28	-
511	Acetylation	HSLHSYEKRLF---- CCCCCHHHCCC----	46.28	19608861
511	Malonylation	HSLHSYEKRLF---- CCCCCHHHCCC----	46.28	30639696
511	Ubiquitination	HSLHSYEKRLF---- CCCCCHHHCCC----	46.28	19608861

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
122	S	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IMDH2_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 IMDH2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AKT1_HUMAN	AKT1	physical	10930578
PIAS4_HUMAN	PIAS4	physical	15383276
RL15_HUMAN	RPL15	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
IMDH2_HUMAN	IMPDH2	physical	25416956
MTNB_HUMAN	APIP	physical	25416956
RSG1_HUMAN	RSG1	physical	25416956
IMDH1_HUMAN	IMPDH1	physical	26186194
SKP2_HUMAN	SKP2	physical	26186194
SMCR8_HUMAN	SMCR8	physical	26186194
ANKR9_HUMAN	ANKRD9	physical	26186194
PUSL1_HUMAN	PUSL1	physical	26186194
INT13_HUMAN	ASUN	physical	26344197
CD2AP_HUMAN	CD2AP	physical	26344197
DDX3X_HUMAN	DDX3X	physical	26344197
NOP9_HUMAN	NOP9	physical	26344197
SH3K1_HUMAN	SH3KBP1	physical	26344197
SNX6_HUMAN	SNX6	physical	26344197
STKL1_HUMAN	STKLD1	physical	26344197
IMDH1_HUMAN	IMPDH1	physical	28514442
ANKR9_HUMAN	ANKRD9	physical	28514442
SMCR8_HUMAN	SMCR8	physical	28514442
PUSL1_HUMAN	PUSL1	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
DB01033	Mercaptopurine
DB00688	Mycophenolate mofetil
DB01024	Mycophenolic acid

Regulatory Network of IMDH2_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-511, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-416, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-400, AND MASSSPECTROMETRY.	15592455 [Abstract]