dbPTM

MDHM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MDHM_HUMAN
UniProt AC	P40926
Protein Name	Malate dehydrogenase, mitochondrial
Gene Name	MDH2
Organism	Homo sapiens (Human).
Sequence Length	338
Subcellular Localization	Mitochondrion matrix .
Protein Description
Protein Sequence	MLSALARPASAALRRSFSTSAQNNAKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYDIAHTPGVAADLSHIETKAAVKGYLGPEQLPDCLKGCDVVVIPAGVPRKPGMTRDDLFNTNATIVATLTAACAQHCPEAMICVIANPVNSTIPITAEVFKKHGVYNPNKIFGVTTLDIVRANTFVAELKGLDPARVNVPVIGGHAGKTIIPLISQCTPKVDFPQDQLTALTGRIQEAGTEVVKAKAGAGSATLSMAYAGARFVFSLVDAMNGKEGVVECSFVKSQETECTYFSTPLLLGKKGIEKNLGIGKVSSFEEKMISDAIPELKASIKKGEDFVKTLK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MLSALARPAS -----CCHHHHCHHH	21.67	24043423
10	Phosphorylation	SALARPASAALRRSF HHHHCHHHHHHHHHC	19.43	24043423
16	Phosphorylation	ASAALRRSFSTSAQN HHHHHHHHCCCCCCC	19.67	20068231
18	Phosphorylation	AALRRSFSTSAQNNA HHHHHHCCCCCCCCC	23.77	20068231
19	Phosphorylation	ALRRSFSTSAQNNAK HHHHHCCCCCCCCCE	26.52	20068231
26	Ubiquitination	TSAQNNAKVAVLGAS CCCCCCCEEEEEECC	32.61	-
26	Ubiquitination	TSAQNNAKVAVLGAS CCCCCCCEEEEEECC	32.61	-
33	O-linked_Glycosylation	KVAVLGASGGIGQPL EEEEEECCCCCCHHH	35.44	UniProtKB CARBOHYD
33	Phosphorylation	KVAVLGASGGIGQPL EEEEEECCCCCCHHH	35.44	21406692
41	Phosphorylation	GGIGQPLSLLLKNSP CCCCHHHHHHHHCCC	24.53	21406692
45	Ubiquitination	QPLSLLLKNSPLVSR HHHHHHHHCCCCCEE	56.18	-
45	Ubiquitination	QPLSLLLKNSPLVSR HHHHHHHHCCCCCEE	56.18	-
47	Phosphorylation	LSLLLKNSPLVSRLT HHHHHHCCCCCEEEE	20.30	22210691
51	Phosphorylation	LKNSPLVSRLTLYDI HHCCCCCEEEEHHHH	29.29	23911959
54	Phosphorylation	SPLVSRLTLYDIAHT CCCCEEEEHHHHHCC	23.35	28152594
56	Nitration	LVSRLTLYDIAHTPG CCEEEEHHHHHCCCC	10.48	-
56	Phosphorylation	LVSRLTLYDIAHTPG CCEEEEHHHHHCCCC	10.48	27155012
61	Phosphorylation	TLYDIAHTPGVAADL EHHHHHCCCCHHHCC	16.83	28152594
69	Phosphorylation	PGVAADLSHIETKAA CCHHHCCHHHHHHHH	23.98	27251275
74	Acetylation	DLSHIETKAAVKGYL CCHHHHHHHHHCCCC	22.89	-
74	Ubiquitination	DLSHIETKAAVKGYL CCHHHHHHHHHCCCC	22.89	-
74	2-Hydroxyisobutyrylation	DLSHIETKAAVKGYL CCHHHHHHHHHCCCC	22.89	-
74	Acetylation	DLSHIETKAAVKGYL CCHHHHHHHHHCCCC	22.89	23954790
74	Ubiquitination	DLSHIETKAAVKGYL CCHHHHHHHHHCCCC	22.89	21906983
78	Ubiquitination	IETKAAVKGYLGPEQ HHHHHHHCCCCCHHH	36.79	21890473
78	Ubiquitination	IETKAAVKGYLGPEQ HHHHHHHCCCCCHHH	36.79	-
78	2-Hydroxyisobutyrylation	IETKAAVKGYLGPEQ HHHHHHHCCCCCHHH	36.79	-
78	Acetylation	IETKAAVKGYLGPEQ HHHHHHHCCCCCHHH	36.79	23954790
78	Malonylation	IETKAAVKGYLGPEQ HHHHHHHCCCCCHHH	36.79	26320211
78	Succinylation	IETKAAVKGYLGPEQ HHHHHHHCCCCCHHH	36.79	-
78	Succinylation	IETKAAVKGYLGPEQ HHHHHHHCCCCCHHH	36.79	-
78	Ubiquitination	IETKAAVKGYLGPEQ HHHHHHHCCCCCHHH	36.79	21890473
80	Nitration	TKAAVKGYLGPEQLP HHHHHCCCCCHHHCC	11.63	-
80	Phosphorylation	TKAAVKGYLGPEQLP HHHHHCCCCCHHHCC	11.63	20090780
89	Glutathionylation	GPEQLPDCLKGCDVV CHHHCCHHHCCCCEE	3.90	22555962
91	Acetylation	EQLPDCLKGCDVVVI HHCCHHHCCCCEEEE	64.92	-
91	Ubiquitination	EQLPDCLKGCDVVVI HHCCHHHCCCCEEEE	64.92	-
91	Acetylation	EQLPDCLKGCDVVVI HHCCHHHCCCCEEEE	64.92	23954790
91	Succinylation	EQLPDCLKGCDVVVI HHCCHHHCCCCEEEE	64.92	-
91	Succinylation	EQLPDCLKGCDVVVI HHCCHHHCCCCEEEE	64.92	23954790
91	Ubiquitination	EQLPDCLKGCDVVVI HHCCHHHCCCCEEEE	64.92	-
93	Glutathionylation	LPDCLKGCDVVVIPA CCHHHCCCCEEEECC	3.25	22555962
93	S-palmitoylation	LPDCLKGCDVVVIPA CCHHHCCCCEEEECC	3.25	26865113
156	Acetylation	PITAEVFKKHGVYNP CEEHHHHHHCCCCCC	49.38	30582861
157	Acetylation	ITAEVFKKHGVYNPN EEHHHHHHCCCCCCC	33.84	26822725
157	Succinylation	ITAEVFKKHGVYNPN EEHHHHHHCCCCCCC	33.84	27452117
157	Ubiquitination	ITAEVFKKHGVYNPN EEHHHHHHCCCCCCC	33.84	-
161	Ubiquitination	VFKKHGVYNPNKIFG HHHHCCCCCCCCEEE	29.51	-
161	Nitration	VFKKHGVYNPNKIFG HHHHCCCCCCCCEEE	29.51	-
161	Phosphorylation	VFKKHGVYNPNKIFG HHHHCCCCCCCCEEE	29.51	28152594
165	Acetylation	HGVYNPNKIFGVTTL CCCCCCCCEEEEEHH	40.44	19608861
165	Ubiquitination	HGVYNPNKIFGVTTL CCCCCCCCEEEEEHH	40.44	-
170	Phosphorylation	PNKIFGVTTLDIVRA CCCEEEEEHHHHHHH	23.24	20068231
171	Phosphorylation	NKIFGVTTLDIVRAN CCEEEEEHHHHHHHC	21.74	20068231
173	Acetylation	IFGVTTLDIVRANTF EEEEEHHHHHHHCCH	34.93	-
185	2-Hydroxyisobutyrylation	NTFVAELKGLDPARV CCHHHHHCCCCHHHE	49.27	-
185	Acetylation	NTFVAELKGLDPARV CCHHHHHCCCCHHHE	49.27	19608861
185	Malonylation	NTFVAELKGLDPARV CCHHHHHCCCCHHHE	49.27	26320211
185	Succinylation	NTFVAELKGLDPARV CCHHHHHCCCCHHHE	49.27	-
185	Succinylation	NTFVAELKGLDPARV CCHHHHHCCCCHHHE	49.27	-
185	Ubiquitination	NTFVAELKGLDPARV CCHHHHHCCCCHHHE	49.27	20167786
197	Acetylation	ARVNVPVIGGHAGKT HHEECCEECCCCCCC	4.47	-
197	Ubiquitination	ARVNVPVIGGHAGKT HHEECCEECCCCCCC	4.47	-
199	Ubiquitination	VNVPVIGGHAGKTII EECCEECCCCCCCHH	9.06	-
203	Acetylation	VIGGHAGKTIIPLIS EECCCCCCCHHHHHH	37.02	23954790
203	Malonylation	VIGGHAGKTIIPLIS EECCCCCCCHHHHHH	37.02	26320211
203	Succinylation	VIGGHAGKTIIPLIS EECCCCCCCHHHHHH	37.02	-
203	Succinylation	VIGGHAGKTIIPLIS EECCCCCCCHHHHHH	37.02	27452117
203	Ubiquitination	VIGGHAGKTIIPLIS EECCCCCCCHHHHHH	37.02	-
204	Phosphorylation	IGGHAGKTIIPLISQ ECCCCCCCHHHHHHH	24.18	21712546
212	S-nitrosocysteine	IIPLISQCTPKVDFP HHHHHHHCCCCCCCC	5.85	-
212	Glutathionylation	IIPLISQCTPKVDFP HHHHHHHCCCCCCCC	5.85	22555962
212	S-nitrosylation	IIPLISQCTPKVDFP HHHHHHHCCCCCCCC	5.85	19483679
213	Phosphorylation	IPLISQCTPKVDFPQ HHHHHHCCCCCCCCH	20.64	25159151
215	Acetylation	LISQCTPKVDFPQDQ HHHHCCCCCCCCHHH	35.96	23954790
215	Succinylation	LISQCTPKVDFPQDQ HHHHCCCCCCCCHHH	35.96	-
215	Succinylation	LISQCTPKVDFPQDQ HHHHCCCCCCCCHHH	35.96	-
224	Phosphorylation	DFPQDQLTALTGRIQ CCCHHHHHHHHHHHH	17.62	-
227	Phosphorylation	QDQLTALTGRIQEAG HHHHHHHHHHHHHHC	23.19	-
235	Phosphorylation	GRIQEAGTEVVKAKA HHHHHHCCEEEHHHC	32.43	29255136
239	N6-malonyllysine	EAGTEVVKAKAGAGS HHCCEEEHHHCCCCC	49.71	-
239	2-Hydroxyisobutyrylation	EAGTEVVKAKAGAGS HHCCEEEHHHCCCCC	49.71	-
239	Acetylation	EAGTEVVKAKAGAGS HHCCEEEHHHCCCCC	49.71	23749302
239	Malonylation	EAGTEVVKAKAGAGS HHCCEEEHHHCCCCC	49.71	26320211
239	Succinylation	EAGTEVVKAKAGAGS HHCCEEEHHHCCCCC	49.71	-
239	Ubiquitination	EAGTEVVKAKAGAGS HHCCEEEHHHCCCCC	49.71	-
241	Ubiquitination	GTEVVKAKAGAGSAT CCEEEHHHCCCCCHH	41.45	21906983
246	Phosphorylation	KAKAGAGSATLSMAY HHHCCCCCHHHHHHH	19.97	27499020
248	Phosphorylation	KAGAGSATLSMAYAG HCCCCCHHHHHHHHH	22.51	28152594
250	Phosphorylation	GAGSATLSMAYAGAR CCCCHHHHHHHHHHH	9.30	28152594
251	Sulfoxidation	AGSATLSMAYAGARF CCCHHHHHHHHHHHH	3.58	30846556
253	Phosphorylation	SATLSMAYAGARFVF CHHHHHHHHHHHHHH	9.27	28152594
254	Acetylation	ATLSMAYAGARFVFS HHHHHHHHHHHHHHH	8.81	-
254	Ubiquitination	ATLSMAYAGARFVFS HHHHHHHHHHHHHHH	8.81	-
257	Methylation	SMAYAGARFVFSLVD HHHHHHHHHHHHHHH	27.61	115483069
259	Ubiquitination	AYAGARFVFSLVDAM HHHHHHHHHHHHHHH	2.38	21890473
259	Acetylation	AYAGARFVFSLVDAM HHHHHHHHHHHHHHH	2.38	-
259	Ubiquitination	AYAGARFVFSLVDAM HHHHHHHHHHHHHHH	2.38	-
261	Phosphorylation	AGARFVFSLVDAMNG HHHHHHHHHHHHHCC	23.37	21712546
265	Acetylation	FVFSLVDAMNGKEGV HHHHHHHHHCCCCCE	5.95	-
265	Ubiquitination	FVFSLVDAMNGKEGV HHHHHHHHHCCCCCE	5.95	-
266	Sulfoxidation	VFSLVDAMNGKEGVV HHHHHHHHCCCCCEE	6.17	28465586
269	Acetylation	LVDAMNGKEGVVECS HHHHHCCCCCEEEEE	46.41	25038526
269	Succinylation	LVDAMNGKEGVVECS HHHHHCCCCCEEEEE	46.41	-
269	Succinylation	LVDAMNGKEGVVECS HHHHHCCCCCEEEEE	46.41	-
272	Acetylation	AMNGKEGVVECSFVK HHCCCCCEEEEEEEE	3.25	-
272	Ubiquitination	AMNGKEGVVECSFVK HHCCCCCEEEEEEEE	3.25	-
275	Glutathionylation	GKEGVVECSFVKSQE CCCCEEEEEEEECCC	2.30	22555962
276	O-linked_Glycosylation	KEGVVECSFVKSQET CCCEEEEEEEECCCC	21.40	28510447
276	Phosphorylation	KEGVVECSFVKSQET CCCEEEEEEEECCCC	21.40	23911959
279	Acetylation	VVECSFVKSQETECT EEEEEEEECCCCEEE	44.40	27178108
280	Phosphorylation	VECSFVKSQETECTY EEEEEEECCCCEEEE	28.13	28152594
282	Ubiquitination	CSFVKSQETECTYFS EEEEECCCCEEEEEE	54.38	-
283	Phosphorylation	SFVKSQETECTYFST EEEECCCCEEEEEEC	28.82	28152594
285	S-nitrosocysteine	VKSQETECTYFSTPL EECCCCEEEEEECCC	4.95	-
285	Glutathionylation	VKSQETECTYFSTPL EECCCCEEEEEECCC	4.95	22555962
285	S-nitrosylation	VKSQETECTYFSTPL EECCCCEEEEEECCC	4.95	19483679
286	Phosphorylation	KSQETECTYFSTPLL ECCCCEEEEEECCCC	22.75	28152594
287	Acetylation	SQETECTYFSTPLLL CCCCEEEEEECCCCC	13.75	-
287	Phosphorylation	SQETECTYFSTPLLL CCCCEEEEEECCCCC	13.75	28152594
289	Phosphorylation	ETECTYFSTPLLLGK CCEEEEEECCCCCCC	20.78	28152594
290	Phosphorylation	TECTYFSTPLLLGKK CEEEEEECCCCCCCC	14.20	28152594
293	Acetylation	TYFSTPLLLGKKGIE EEEECCCCCCCCCHH	6.62	-
293	Ubiquitination	TYFSTPLLLGKKGIE EEEECCCCCCCCCHH	6.62	-
296	2-Hydroxyisobutyrylation	STPLLLGKKGIEKNL ECCCCCCCCCHHHCC	48.04	-
296	Acetylation	STPLLLGKKGIEKNL ECCCCCCCCCHHHCC	48.04	23236377
296	Malonylation	STPLLLGKKGIEKNL ECCCCCCCCCHHHCC	48.04	26320211
296	Succinylation	STPLLLGKKGIEKNL ECCCCCCCCCHHHCC	48.04	-
296	Succinylation	STPLLLGKKGIEKNL ECCCCCCCCCHHHCC	48.04	27452117
296	Ubiquitination	STPLLLGKKGIEKNL ECCCCCCCCCHHHCC	48.04	-
297	Acetylation	TPLLLGKKGIEKNLG CCCCCCCCCHHHCCC	64.42	88391
297	Ubiquitination	TPLLLGKKGIEKNLG CCCCCCCCCHHHCCC	64.42	-
301	2-Hydroxyisobutyrylation	LGKKGIEKNLGIGKV CCCCCHHHCCCCCCC	56.40	-
301	Acetylation	LGKKGIEKNLGIGKV CCCCCHHHCCCCCCC	56.40	19608861
301	Malonylation	LGKKGIEKNLGIGKV CCCCCHHHCCCCCCC	56.40	26320211
301	Succinylation	LGKKGIEKNLGIGKV CCCCCHHHCCCCCCC	56.40	-
301	Succinylation	LGKKGIEKNLGIGKV CCCCCHHHCCCCCCC	56.40	-
301	Ubiquitination	LGKKGIEKNLGIGKV CCCCCHHHCCCCCCC	56.40	19608861
307	N6-malonyllysine	EKNLGIGKVSSFEEK HHCCCCCCCCHHHHH	36.70	-
307	Acetylation	EKNLGIGKVSSFEEK HHCCCCCCCCHHHHH	36.70	20167786
307	Malonylation	EKNLGIGKVSSFEEK HHCCCCCCCCHHHHH	36.70	26320211
307	Succinylation	EKNLGIGKVSSFEEK HHCCCCCCCCHHHHH	36.70	-
307	Ubiquitination	EKNLGIGKVSSFEEK HHCCCCCCCCHHHHH	36.70	20167786
309	Phosphorylation	NLGIGKVSSFEEKMI CCCCCCCCHHHHHHH	32.56	25850435
310	Phosphorylation	LGIGKVSSFEEKMIS CCCCCCCHHHHHHHH	39.40	25850435
314	2-Hydroxyisobutyrylation	KVSSFEEKMISDAIP CCCHHHHHHHHHHHH	34.04	-
314	Acetylation	KVSSFEEKMISDAIP CCCHHHHHHHHHHHH	34.04	19608861
314	Malonylation	KVSSFEEKMISDAIP CCCHHHHHHHHHHHH	34.04	26320211
314	Succinylation	KVSSFEEKMISDAIP CCCHHHHHHHHHHHH	34.04	-
314	Succinylation	KVSSFEEKMISDAIP CCCHHHHHHHHHHHH	34.04	-
314	Ubiquitination	KVSSFEEKMISDAIP CCCHHHHHHHHHHHH	34.04	20167786
315	Sulfoxidation	VSSFEEKMISDAIPE CCHHHHHHHHHHHHH	3.92	21406390
317	Phosphorylation	SFEEKMISDAIPELK HHHHHHHHHHHHHHH	19.93	28857561
324	2-Hydroxyisobutyrylation	SDAIPELKASIKKGE HHHHHHHHHHHHCCH	38.12	-
324	Acetylation	SDAIPELKASIKKGE HHHHHHHHHHHHCCH	38.12	23954790
324	Malonylation	SDAIPELKASIKKGE HHHHHHHHHHHHCCH	38.12	26320211
324	Succinylation	SDAIPELKASIKKGE HHHHHHHHHHHHCCH	38.12	-
324	Succinylation	SDAIPELKASIKKGE HHHHHHHHHHHHCCH	38.12	27452117
324	Ubiquitination	SDAIPELKASIKKGE HHHHHHHHHHHHCCH	38.12	-
326	Phosphorylation	AIPELKASIKKGEDF HHHHHHHHHHCCHHH	33.10	23186163
328	Acetylation	PELKASIKKGEDFVK HHHHHHHHCCHHHHH	52.83	2401887
328	Malonylation	PELKASIKKGEDFVK HHHHHHHHCCHHHHH	52.83	26320211
328	Succinylation	PELKASIKKGEDFVK HHHHHHHHCCHHHHH	52.83	-
328	Succinylation	PELKASIKKGEDFVK HHHHHHHHCCHHHHH	52.83	-
329	N6-malonyllysine	ELKASIKKGEDFVKT HHHHHHHCCHHHHHH	66.90	-
329	2-Hydroxyisobutyrylation	ELKASIKKGEDFVKT HHHHHHHCCHHHHHH	66.90	-
329	Acetylation	ELKASIKKGEDFVKT HHHHHHHCCHHHHHH	66.90	19608861
329	Malonylation	ELKASIKKGEDFVKT HHHHHHHCCHHHHHH	66.90	26320211
329	Succinylation	ELKASIKKGEDFVKT HHHHHHHCCHHHHHH	66.90	27452117
335	2-Hydroxyisobutyrylation	KKGEDFVKTLK---- HCCHHHHHHCC----	48.40	-
335	Acetylation	KKGEDFVKTLK---- HCCHHHHHHCC----	48.40	19608861
335	Malonylation	KKGEDFVKTLK---- HCCHHHHHHCC----	48.40	26320211
335	Succinylation	KKGEDFVKTLK---- HCCHHHHHHCC----	48.40	-
335	Succinylation	KKGEDFVKTLK---- HCCHHHHHHCC----	48.40	27452117
335	Ubiquitination	KKGEDFVKTLK---- HCCHHHHHHCC----	48.40	19608861
336	Phosphorylation	KGEDFVKTLK----- CCHHHHHHCC-----	34.18	23312004

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 MDHM_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SYWC_HUMAN	WARS	physical	16169070
FUMH_HUMAN	FH	physical	2759092
MDHM_HUMAN	MDH2	physical	9792106
SERPH_HUMAN	SERPINH1	physical	22939629
RT28_HUMAN	MRPS28	physical	22939629
COR1C_HUMAN	CORO1C	physical	26344197
IDH3A_HUMAN	IDH3A	physical	26344197
NUDC_HUMAN	NUDC	physical	26344197
QSOX2_HUMAN	QSOX2	physical	26344197
RAB10_HUMAN	RAB10	physical	26344197
SDHB_HUMAN	SDHB	physical	26344197
SERPH_HUMAN	SERPINH1	physical	26344197
UB2L3_HUMAN	UBE2L3	physical	26344197
UFM1_HUMAN	UFM1	physical	26344197

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 MDHM_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Regulation of cellular metabolism by protein lysine acetylation."; Zhao S., Xu W., Jiang W., Yu W., Lin Y., Zhang T., Yao J., Zhou L.,Zeng Y., Li H., Li Y., Shi J., An W., Hancock S.M., He F., Qin L.,Chin J., Yang P., Chen X., Lei Q., Xiong Y., Guan K.L.; Science 327:1000-1004(2010). Cited for: ACETYLATION AT LYS-185; LYS-301; LYS-307 AND LYS-314, ENZYMEREGULATION, MASS SPECTROMETRY, AND MUTAGENESIS OF LYS-185; LYS-301;LYS-307 AND LYS-314.	20167786 [Abstract]
"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-165; LYS-185; LYS-301;LYS-314; LYS-329 AND LYS-335, AND MASS SPECTROMETRY.	19608861 [Abstract]
Malonylation
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-307.	21908771 [Abstract]
N6-malonyllysine
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-307.	21908771 [Abstract]
Phosphorylation
Reference	PubMed
"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-56, AND MASSSPECTROMETRY.	15592455 [Abstract]