ENOA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ENOA_HUMAN
• UniProt AC: P06733
• Protein Name: Alpha-enolase
• Gene Name: ENO1
• Organism: Homo sapiens (Human).
• Sequence Length: 434
• Subcellular Localization: Cytoplasm . Cell membrane . Cytoplasm, myofibril, sarcomere, M line . Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. ENO1 is localized to the M line.; Isoform MBP-1: Nucleus.
• Protein Description: Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production.; MBP1 binds to the myc promoter and acts as a transcriptional repressor. May be a tumor suppressor..
• Protein Sequence: MSILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGASTGIYEALELRDNDKTRYMGKGVSKAVEHINKTIAPALVSKKLNVTEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCKAGAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGNKLAMQEFMILPVGAANFREAMRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKVVIGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLTVTNPKRIAKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLLRIEEELGSKAKFAGRNFRNPLAK

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSILKIHAR ------CCCEEEEEH	36.31	25944712
2	Phosphorylation	------MSILKIHAR ------CCCEEEEEH	36.31	24719451
5	2-Hydroxyisobutyrylation	---MSILKIHAREIF ---CCCEEEEEHHHH	30.67	-
5	Acetylation	---MSILKIHAREIF ---CCCEEEEEHHHH	30.67	19608861
5	Malonylation	---MSILKIHAREIF ---CCCEEEEEHHHH	30.67	26320211
5	Succinylation	---MSILKIHAREIF ---CCCEEEEEHHHH	30.67	23954790
5	Ubiquitination	---MSILKIHAREIF ---CCCEEEEEHHHH	30.67	21890473
5	Ubiquitination	---MSILKIHAREIF ---CCCEEEEEHHHH	30.67	21890473
5	Ubiquitination	---MSILKIHAREIF ---CCCEEEEEHHHH	30.67	21890473
9	Methylation	SILKIHAREIFDSRG CCEEEEEHHHHHCCC	24.31	-
10 (in isoform 2)	Ubiquitination	-	49.11	-
14	Phosphorylation	HAREIFDSRGNPTVE EEHHHHHCCCCCEEE	31.19	21815630
15	Methylation	AREIFDSRGNPTVEV EHHHHHCCCCCEEEE	51.24	-
19	Phosphorylation	FDSRGNPTVEVDLFT HHCCCCCEEEEEEEC	33.04	30624053
26	Phosphorylation	TVEVDLFTSKGLFRA EEEEEEECCCCCHHE	36.50	30266825
27	Phosphorylation	VEVDLFTSKGLFRAA EEEEEECCCCCHHEE	19.86	30266825
27 (in isoform 2)	Ubiquitination	-	19.86	21890473
28	Acetylation	EVDLFTSKGLFRAAV EEEEECCCCCHHEEC	57.48	23954790
28	Ubiquitination	EVDLFTSKGLFRAAV EEEEECCCCCHHEEC	57.48	21890473
28 (in isoform 1)	Ubiquitination	-	57.48	21890473
28	Ubiquitination	EVDLFTSKGLFRAAV EEEEECCCCCHHEEC	57.48	21890473
28	Ubiquitination	EVDLFTSKGLFRAAV EEEEECCCCCHHEEC	57.48	21890473
33	Acetylation	TSKGLFRAAVPSGAS CCCCCHHEECCCCCC	12.89	19608861
33	Ubiquitination	TSKGLFRAAVPSGAS CCCCCHHEECCCCCC	12.89	19608861
33 (in isoform 2)	Ubiquitination	-	12.89	21890473
37	Phosphorylation	LFRAAVPSGASTGIY CHHEECCCCCCCCHH	40.15	21945579
40	Phosphorylation	AAVPSGASTGIYEAL EECCCCCCCCHHHHH	30.60	29255136
41	Phosphorylation	AVPSGASTGIYEALE ECCCCCCCCHHHHHH	27.37	21945579
44	Phosphorylation	SGASTGIYEALELRD CCCCCCHHHHHHCCC	9.11	29255136
50	Methylation	IYEALELRDNDKTRY HHHHHHCCCCCCCCC	31.17	-
54	Acetylation	LELRDNDKTRYMGKG HHCCCCCCCCCCCCC	40.95	23236377
54	Ubiquitination	LELRDNDKTRYMGKG HHCCCCCCCCCCCCC	40.95	21890473
54 (in isoform 1)	Ubiquitination	-	40.95	21890473
54	Ubiquitination	LELRDNDKTRYMGKG HHCCCCCCCCCCCCC	40.95	21890473
54	Ubiquitination	LELRDNDKTRYMGKG HHCCCCCCCCCCCCC	40.95	21890473
55	Phosphorylation	ELRDNDKTRYMGKGV HCCCCCCCCCCCCCH	29.87	28857561
57	Phosphorylation	RDNDKTRYMGKGVSK CCCCCCCCCCCCHHH	18.56	22817900
60	2-Hydroxyisobutyrylation	DKTRYMGKGVSKAVE CCCCCCCCCHHHHHH	39.34	-
60	Acetylation	DKTRYMGKGVSKAVE CCCCCCCCCHHHHHH	39.34	19608861
60	Succinylation	DKTRYMGKGVSKAVE CCCCCCCCCHHHHHH	39.34	-
60	Succinylation	DKTRYMGKGVSKAVE CCCCCCCCCHHHHHH	39.34	23954790
60	Ubiquitination	DKTRYMGKGVSKAVE CCCCCCCCCHHHHHH	39.34	19608861
60 (in isoform 1)	Ubiquitination	-	39.34	21890473
63	Phosphorylation	RYMGKGVSKAVEHIN CCCCCCHHHHHHHHH	24.46	28857561
64	Acetylation	YMGKGVSKAVEHINK CCCCCHHHHHHHHHH	54.79	19608861
64	Ubiquitination	YMGKGVSKAVEHINK CCCCCHHHHHHHHHH	54.79	19608861
64 (in isoform 1)	Ubiquitination	-	54.79	21890473
64	Ubiquitination	YMGKGVSKAVEHINK CCCCCHHHHHHHHHH	54.79	21890473
64	Ubiquitination	YMGKGVSKAVEHINK CCCCCHHHHHHHHHH	54.79	21890473
71	2-Hydroxyisobutyrylation	KAVEHINKTIAPALV HHHHHHHHCHHHHHH	40.48	-
71	Acetylation	KAVEHINKTIAPALV HHHHHHHHCHHHHHH	40.48	19608861
71	Malonylation	KAVEHINKTIAPALV HHHHHHHHCHHHHHH	40.48	26320211
71	Ubiquitination	KAVEHINKTIAPALV HHHHHHHHCHHHHHH	40.48	21890473
71 (in isoform 1)	Ubiquitination	-	40.48	21890473
71	Ubiquitination	KAVEHINKTIAPALV HHHHHHHHCHHHHHH	40.48	21890473
71	Ubiquitination	KAVEHINKTIAPALV HHHHHHHHCHHHHHH	40.48	21890473
72	Phosphorylation	AVEHINKTIAPALVS HHHHHHHCHHHHHHH	20.20	22617229
79	Phosphorylation	TIAPALVSKKLNVTE CHHHHHHHHCCCCCC	25.56	23401153
80	2-Hydroxyisobutyrylation	IAPALVSKKLNVTEQ HHHHHHHHCCCCCCH	54.52	-
80	Acetylation	IAPALVSKKLNVTEQ HHHHHHHHCCCCCCH	54.52	23954790
80	Malonylation	IAPALVSKKLNVTEQ HHHHHHHHCCCCCCH	54.52	26320211
80	Ubiquitination	IAPALVSKKLNVTEQ HHHHHHHHCCCCCCH	54.52	21906983
80 (in isoform 1)	Ubiquitination	-	54.52	21890473
80	Ubiquitination	IAPALVSKKLNVTEQ HHHHHHHHCCCCCCH	54.52	21890473
80	Ubiquitination	IAPALVSKKLNVTEQ HHHHHHHHCCCCCCH	54.52	21890473
81	2-Hydroxyisobutyrylation	APALVSKKLNVTEQE HHHHHHHCCCCCCHH	37.47	-
81	Acetylation	APALVSKKLNVTEQE HHHHHHHCCCCCCHH	37.47	20433201
81	Malonylation	APALVSKKLNVTEQE HHHHHHHCCCCCCHH	37.47	26320211
81	Ubiquitination	APALVSKKLNVTEQE HHHHHHHCCCCCCHH	37.47	-
81 (in isoform 1)	Ubiquitination	-	37.47	21890473
85	Phosphorylation	VSKKLNVTEQEKIDK HHHCCCCCCHHHHHH	30.77	26437602
89	Acetylation	LNVTEQEKIDKLMIE CCCCCHHHHHHHEEE	56.77	19608861
89	Succinylation	LNVTEQEKIDKLMIE CCCCCHHHHHHHEEE	56.77	-
89	Succinylation	LNVTEQEKIDKLMIE CCCCCHHHHHHHEEE	56.77	27452117
89	Ubiquitination	LNVTEQEKIDKLMIE CCCCCHHHHHHHEEE	56.77	19608861
89 (in isoform 1)	Ubiquitination	-	56.77	21890473
92	Acetylation	TEQEKIDKLMIEMDG CCHHHHHHHEEECCC	43.35	23954790
92	Ubiquitination	TEQEKIDKLMIEMDG CCHHHHHHHEEECCC	43.35	21906983
92 (in isoform 1)	Ubiquitination	-	43.35	21890473
94	Sulfoxidation	QEKIDKLMIEMDGTE HHHHHHHEEECCCCC	2.76	21406390
97	Sulfoxidation	IDKLMIEMDGTENKS HHHHEEECCCCCCCH	3.89	28465586
100	Acetylation	LMIEMDGTENKSKFG HEEECCCCCCCHHHC	31.92	19608861
100	Phosphorylation	LMIEMDGTENKSKFG HEEECCCCCCCHHHC	31.92	20068231
100	Ubiquitination	LMIEMDGTENKSKFG HEEECCCCCCCHHHC	31.92	19608861
100 (in isoform 2)	Ubiquitination	-	31.92	21890473
103	2-Hydroxyisobutyrylation	EMDGTENKSKFGANA ECCCCCCCHHHCHHH	49.11	-
103	Acetylation	EMDGTENKSKFGANA ECCCCCCCHHHCHHH	49.11	20433201
103	Ubiquitination	EMDGTENKSKFGANA ECCCCCCCHHHCHHH	49.11	21906983
103 (in isoform 1)	Ubiquitination	-	49.11	21890473
104	Phosphorylation	MDGTENKSKFGANAI CCCCCCCHHHCHHHH	44.81	28857561
105	Acetylation	DGTENKSKFGANAIL CCCCCCHHHCHHHHH	49.80	20433201
105	Ubiquitination	DGTENKSKFGANAIL CCCCCCHHHCHHHHH	49.80	-
106	Acetylation	GTENKSKFGANAILG CCCCCHHHCHHHHHH	16.82	19608861
109 (in isoform 2)	Ubiquitination	-	28.08	21890473
115	Phosphorylation	ANAILGVSLAVCKAG HHHHHHHHHHHHHHC	14.60	-
119	S-palmitoylation	LGVSLAVCKAGAVEK HHHHHHHHHHCHHHC	1.76	29575903
120	Ubiquitination	GVSLAVCKAGAVEKG HHHHHHHHHCHHHCC	43.17	21906983
120 (in isoform 1)	Ubiquitination	-	43.17	21890473
126	Acetylation	CKAGAVEKGVPLYRH HHHCHHHCCCCCHHH	59.62	19608861
126	Malonylation	CKAGAVEKGVPLYRH HHHCHHHCCCCCHHH	59.62	26320211
126	Ubiquitination	CKAGAVEKGVPLYRH HHHCHHHCCCCCHHH	59.62	21890473
126 (in isoform 1)	Ubiquitination	-	59.62	21890473
128	Acetylation	AGAVEKGVPLYRHIA HCHHHCCCCCHHHHH	4.35	19608861
128	Ubiquitination	AGAVEKGVPLYRHIA HCHHHCCCCCHHHHH	4.35	19608861
128 (in isoform 2)	Ubiquitination	-	4.35	21890473
131	Phosphorylation	VEKGVPLYRHIADLA HHCCCCCHHHHHHHC	8.28	26356563
135	Acetylation	VPLYRHIADLAGNSE CCCHHHHHHHCCCCE	10.31	19608861
135	Ubiquitination	VPLYRHIADLAGNSE CCCHHHHHHHCCCCE	10.31	19608861
135 (in isoform 2)	Ubiquitination	-	10.31	21890473
140	Acetylation	HIADLAGNSEVILPV HHHHHCCCCEEEEEE	29.41	19608861
140	Ubiquitination	HIADLAGNSEVILPV HHHHHCCCCEEEEEE	29.41	19608861
140 (in isoform 2)	Ubiquitination	-	29.41	21890473
141	Phosphorylation	IADLAGNSEVILPVP HHHHCCCCEEEEEEC	32.11	28450419
157	Phosphorylation	FNVINGGSHAGNKLA EEEECCCCCCCCHHH	16.15	28450419
163	Acetylation	GSHAGNKLAMQEFMI CCCCCCHHHHCEECE	5.79	19608861
163	Ubiquitination	GSHAGNKLAMQEFMI CCCCCCHHHHCEECE	5.79	19608861
163 (in isoform 2)	Ubiquitination	-	5.79	21890473
165	Sulfoxidation	HAGNKLAMQEFMILP CCCCHHHHCEECEEC	5.94	21406390
169	Sulfoxidation	KLAMQEFMILPVGAA HHHHCEECEECCCHH	2.79	30846556
169 (in isoform 2)	Ubiquitination	-	2.79	21890473
183	Methylation	ANFREAMRIGAEVYH HHHHHHHHHCHHHHH	31.10	-
188	Acetylation	AMRIGAEVYHNLKNV HHHHCHHHHHHHHHH	6.13	19608861
188	Ubiquitination	AMRIGAEVYHNLKNV HHHHCHHHHHHHHHH	6.13	19608861
188 (in isoform 2)	Ubiquitination	-	6.13	21890473
189	Phosphorylation	MRIGAEVYHNLKNVI HHHCHHHHHHHHHHH	4.05	21712546
192	Acetylation	GAEVYHNLKNVIKEK CHHHHHHHHHHHHHH	2.45	19608861
192	Ubiquitination	GAEVYHNLKNVIKEK CHHHHHHHHHHHHHH	2.45	19608861
192 (in isoform 2)	Ubiquitination	-	2.45	21890473
193	2-Hydroxyisobutyrylation	AEVYHNLKNVIKEKY HHHHHHHHHHHHHHH	55.26	-
193	Acetylation	AEVYHNLKNVIKEKY HHHHHHHHHHHHHHH	55.26	19608861
193	Malonylation	AEVYHNLKNVIKEKY HHHHHHHHHHHHHHH	55.26	26320211
193	Ubiquitination	AEVYHNLKNVIKEKY HHHHHHHHHHHHHHH	55.26	21890473
193 (in isoform 1)	Ubiquitination	-	55.26	21890473
193	Ubiquitination	AEVYHNLKNVIKEKY HHHHHHHHHHHHHHH	55.26	21890473
193	Ubiquitination	AEVYHNLKNVIKEKY HHHHHHHHHHHHHHH	55.26	21890473
197	Acetylation	HNLKNVIKEKYGKDA HHHHHHHHHHHCCCC	43.82	26051181
197	Ubiquitination	HNLKNVIKEKYGKDA HHHHHHHHHHHCCCC	43.82	22053931
199	Acetylation	LKNVIKEKYGKDATN HHHHHHHHHCCCCCC	55.06	19608861
199	Ubiquitination	LKNVIKEKYGKDATN HHHHHHHHHCCCCCC	55.06	19608861
200	Phosphorylation	KNVIKEKYGKDATNV HHHHHHHHCCCCCCC	30.42	28152594
202	Acetylation	VIKEKYGKDATNVGD HHHHHHCCCCCCCCC	40.89	23954790
202	Malonylation	VIKEKYGKDATNVGD HHHHHHCCCCCCCCC	40.89	26320211
202	Sumoylation	VIKEKYGKDATNVGD HHHHHHCCCCCCCCC	40.89	28112733
202	Ubiquitination	VIKEKYGKDATNVGD HHHHHHCCCCCCCCC	40.89	-
202 (in isoform 1)	Ubiquitination	-	40.89	21890473
205	Phosphorylation	EKYGKDATNVGDEGG HHHCCCCCCCCCCCC	40.34	28152594
221	2-Hydroxyisobutyrylation	APNILENKEGLELLK CCCHHCCHHHHHHHH	43.73	-
221	Acetylation	APNILENKEGLELLK CCCHHCCHHHHHHHH	43.73	23954790
221	Succinylation	APNILENKEGLELLK CCCHHCCHHHHHHHH	43.73	23954790
221	Sumoylation	APNILENKEGLELLK CCCHHCCHHHHHHHH	43.73	19608861
221	Ubiquitination	APNILENKEGLELLK CCCHHCCHHHHHHHH	43.73	21890473
221 (in isoform 1)	Ubiquitination	-	43.73	21890473
221	Ubiquitination	APNILENKEGLELLK CCCHHCCHHHHHHHH	43.73	21890473
221	Ubiquitination	APNILENKEGLELLK CCCHHCCHHHHHHHH	43.73	21890473
228	2-Hydroxyisobutyrylation	KEGLELLKTAIGKAG HHHHHHHHHHHHHCC	48.84	-
228	Acetylation	KEGLELLKTAIGKAG HHHHHHHHHHHHHCC	48.84	19608861
228	Other	KEGLELLKTAIGKAG HHHHHHHHHHHHHCC	48.84	29775581
228	Succinylation	KEGLELLKTAIGKAG HHHHHHHHHHHHHCC	48.84	-
228	Succinylation	KEGLELLKTAIGKAG HHHHHHHHHHHHHCC	48.84	23954790
228	Ubiquitination	KEGLELLKTAIGKAG HHHHHHHHHHHHHCC	48.84	19608861
228 (in isoform 1)	Ubiquitination	-	48.84	21890473
229	Phosphorylation	EGLELLKTAIGKAGY HHHHHHHHHHHHCCC	24.39	28857561
233	N6-malonyllysine	LLKTAIGKAGYTDKV HHHHHHHHCCCCCEE	32.31	-
233	2-Hydroxyisobutyrylation	LLKTAIGKAGYTDKV HHHHHHHHCCCCCEE	32.31	-
233	Acetylation	LLKTAIGKAGYTDKV HHHHHHHHCCCCCEE	32.31	19608861
233	Malonylation	LLKTAIGKAGYTDKV HHHHHHHHCCCCCEE	32.31	26320211
233	Ubiquitination	LLKTAIGKAGYTDKV HHHHHHHHCCCCCEE	32.31	21890473
233 (in isoform 1)	Ubiquitination	-	32.31	21890473
233 (in isoform 2)	Ubiquitination	-	32.31	21890473
233	Ubiquitination	LLKTAIGKAGYTDKV HHHHHHHHCCCCCEE	32.31	21890473
233	Ubiquitination	LLKTAIGKAGYTDKV HHHHHHHHCCCCCEE	32.31	21890473
236	Nitration	TAIGKAGYTDKVVIG HHHHHCCCCCEEEEC	19.34	-
236	Phosphorylation	TAIGKAGYTDKVVIG HHHHHCCCCCEEEEC	19.34	19835603
237	Phosphorylation	AIGKAGYTDKVVIGM HHHHCCCCCEEEECE	28.55	19835603
239	2-Hydroxyisobutyrylation	GKAGYTDKVVIGMDV HHCCCCCEEEECEEH	30.51	-
239	Acetylation	GKAGYTDKVVIGMDV HHCCCCCEEEECEEH	30.51	20433201
239	Ubiquitination	GKAGYTDKVVIGMDV HHCCCCCEEEECEEH	30.51	-
242 (in isoform 2)	Ubiquitination	-	4.18	21890473
244	Sulfoxidation	TDKVVIGMDVAASEF CCEEEECEEHHHHHH	2.29	21406390
249	Phosphorylation	IGMDVAASEFFRSGK ECEEHHHHHHHHCCC	25.79	29514088
250	Acetylation	GMDVAASEFFRSGKY CEEHHHHHHHHCCCC	44.04	19608861
250	Ubiquitination	GMDVAASEFFRSGKY CEEHHHHHHHHCCCC	44.04	19608861
250 (in isoform 2)	Ubiquitination	-	44.04	21890473
254	Phosphorylation	AASEFFRSGKYDLDF HHHHHHHCCCCCCCC	34.18	23401153
256	2-Hydroxyisobutyrylation	SEFFRSGKYDLDFKS HHHHHCCCCCCCCCC	36.52	-
256	Acetylation	SEFFRSGKYDLDFKS HHHHHCCCCCCCCCC	36.52	19608861
256	Malonylation	SEFFRSGKYDLDFKS HHHHHCCCCCCCCCC	36.52	26320211
256	Methylation	SEFFRSGKYDLDFKS HHHHHCCCCCCCCCC	36.52	19608861
256	Sumoylation	SEFFRSGKYDLDFKS HHHHHCCCCCCCCCC	36.52	19608861
256	Ubiquitination	SEFFRSGKYDLDFKS HHHHHCCCCCCCCCC	36.52	21890473
256 (in isoform 1)	Ubiquitination	-	36.52	21890473
256	Ubiquitination	SEFFRSGKYDLDFKS HHHHHCCCCCCCCCC	36.52	21890473
256	Ubiquitination	SEFFRSGKYDLDFKS HHHHHCCCCCCCCCC	36.52	21890473
257	Phosphorylation	EFFRSGKYDLDFKSP HHHHCCCCCCCCCCC	25.84	30266825
262	2-Hydroxyisobutyrylation	GKYDLDFKSPDDPSR CCCCCCCCCCCCHHH	61.82	-
262	Acetylation	GKYDLDFKSPDDPSR CCCCCCCCCCCCHHH	61.82	20433201
262	Succinylation	GKYDLDFKSPDDPSR CCCCCCCCCCCCHHH	61.82	23954790
262	Sumoylation	GKYDLDFKSPDDPSR CCCCCCCCCCCCHHH	61.82	-
262	Ubiquitination	GKYDLDFKSPDDPSR CCCCCCCCCCCCHHH	61.82	21890473
262 (in isoform 1)	Ubiquitination	-	61.82	21890473
262	Ubiquitination	GKYDLDFKSPDDPSR CCCCCCCCCCCCHHH	61.82	21890473
262	Ubiquitination	GKYDLDFKSPDDPSR CCCCCCCCCCCCHHH	61.82	21890473
263	Phosphorylation	KYDLDFKSPDDPSRY CCCCCCCCCCCHHHC	33.29	22167270
268	Phosphorylation	FKSPDDPSRYISPDQ CCCCCCHHHCCCHHH	44.72	21945579
270	Phosphorylation	SPDDPSRYISPDQLA CCCCHHHCCCHHHHH	15.30	21945579
272	Phosphorylation	DDPSRYISPDQLADL CCHHHCCCHHHHHHH	17.31	23927012
280	Phosphorylation	PDQLADLYKSFIKDY HHHHHHHHHHHHCCC	12.72	21945579
281	2-Hydroxyisobutyrylation	DQLADLYKSFIKDYP HHHHHHHHHHHCCCC	46.30	-
281	Acetylation	DQLADLYKSFIKDYP HHHHHHHHHHHCCCC	46.30	19608861
281	Other	DQLADLYKSFIKDYP HHHHHHHHHHHCCCC	46.30	29775581
281	Succinylation	DQLADLYKSFIKDYP HHHHHHHHHHHCCCC	46.30	23954790
281	Ubiquitination	DQLADLYKSFIKDYP HHHHHHHHHHHCCCC	46.30	21890473
281 (in isoform 1)	Ubiquitination	-	46.30	21890473
281	Ubiquitination	DQLADLYKSFIKDYP HHHHHHHHHHHCCCC	46.30	21890473
281	Ubiquitination	DQLADLYKSFIKDYP HHHHHHHHHHHCCCC	46.30	21890473
282	Phosphorylation	QLADLYKSFIKDYPV HHHHHHHHHHCCCCE	20.74	22617229
285	Acetylation	DLYKSFIKDYPVVSI HHHHHHHCCCCEEEE	49.55	19608861
285	Methylation	DLYKSFIKDYPVVSI HHHHHHHCCCCEEEE	49.55	19608861
285	Succinylation	DLYKSFIKDYPVVSI HHHHHHHCCCCEEEE	49.55	23954790
285	Ubiquitination	DLYKSFIKDYPVVSI HHHHHHHCCCCEEEE	49.55	19608861
285 (in isoform 1)	Ubiquitination	-	49.55	21890473
287	Phosphorylation	YKSFIKDYPVVSIED HHHHHCCCCEEEECC	7.91	22115753
291	Phosphorylation	IKDYPVVSIEDPFDQ HCCCCEEEECCCCCC	22.09	26356563
306	Acetylation	DDWGAWQKFTASAGI CCCCHHHHHHHCCCC	33.70	70179
308	O-linked_Glycosylation	WGAWQKFTASAGIQV CCHHHHHHHCCCCEE	27.09	OGP
308	Phosphorylation	WGAWQKFTASAGIQV CCHHHHHHHCCCCEE	27.09	27050516
310	Phosphorylation	AWQKFTASAGIQVVG HHHHHHHCCCCEEEC	24.78	25159151
313	Acetylation	KFTASAGIQVVGDDL HHHHCCCCEEECCCC	2.55	19608861
313	Ubiquitination	KFTASAGIQVVGDDL HHHHCCCCEEECCCC	2.55	19608861
313 (in isoform 2)	Ubiquitination	-	2.55	21890473
321	Phosphorylation	QVVGDDLTVTNPKRI EEECCCCEECCHHHH	32.07	27251275
323	Phosphorylation	VGDDLTVTNPKRIAK ECCCCEECCHHHHHH	40.34	27251275
326	2-Hydroxyisobutyrylation	DLTVTNPKRIAKAVN CCEECCHHHHHHHCC	59.51	-
326	Acetylation	DLTVTNPKRIAKAVN CCEECCHHHHHHHCC	59.51	26051181
326	Ubiquitination	DLTVTNPKRIAKAVN CCEECCHHHHHHHCC	59.51	21906983
326 (in isoform 1)	Ubiquitination	-	59.51	21890473
327	Acetylation	LTVTNPKRIAKAVNE CEECCHHHHHHHCCC	35.04	19608861
327	Ubiquitination	LTVTNPKRIAKAVNE CEECCHHHHHHHCCC	35.04	19608861
327 (in isoform 2)	Ubiquitination	-	35.04	21890473
330	2-Hydroxyisobutyrylation	TNPKRIAKAVNEKSC CCHHHHHHHCCCCCC	50.96	-
330	Acetylation	TNPKRIAKAVNEKSC CCHHHHHHHCCCCCC	50.96	20433201
330	Succinylation	TNPKRIAKAVNEKSC CCHHHHHHHCCCCCC	50.96	23954790
330	Ubiquitination	TNPKRIAKAVNEKSC CCHHHHHHHCCCCCC	50.96	-
335	Acetylation	IAKAVNEKSCNCLLL HHHHCCCCCCCEEEE	55.92	23954790
335	Phosphoglycerylation	IAKAVNEKSCNCLLL HHHHCCCCCCCEEEE	55.92	-
335	Ubiquitination	IAKAVNEKSCNCLLL HHHHCCCCCCCEEEE	55.92	21890473
335 (in isoform 1)	Ubiquitination	-	55.92	21890473
335	Ubiquitination	IAKAVNEKSCNCLLL HHHHCCCCCCCEEEE	55.92	21890473
335	Ubiquitination	IAKAVNEKSCNCLLL HHHHCCCCCCCEEEE	55.92	21890473
336	Phosphorylation	AKAVNEKSCNCLLLK HHHCCCCCCCEEEEE	12.37	24114839
337	S-nitrosylation	KAVNEKSCNCLLLKV HHCCCCCCCEEEEEH	6.54	2212679
337	S-palmitoylation	KAVNEKSCNCLLLKV HHCCCCCCCEEEEEH	6.54	29575903
339	S-palmitoylation	VNEKSCNCLLLKVNQ CCCCCCCEEEEEHHH	3.12	29575903
343	2-Hydroxyisobutyrylation	SCNCLLLKVNQIGSV CCCEEEEEHHHHCCH	38.82	-
343	Acetylation	SCNCLLLKVNQIGSV CCCEEEEEHHHHCCH	38.82	23954790
343	Phosphoglycerylation	SCNCLLLKVNQIGSV CCCEEEEEHHHHCCH	38.82	-
343	Ubiquitination	SCNCLLLKVNQIGSV CCCEEEEEHHHHCCH	38.82	21890473
343 (in isoform 1)	Ubiquitination	-	38.82	21890473
343	Ubiquitination	SCNCLLLKVNQIGSV CCCEEEEEHHHHCCH	38.82	21890473
343	Ubiquitination	SCNCLLLKVNQIGSV CCCEEEEEHHHHCCH	38.82	21890473
349	Phosphorylation	LKVNQIGSVTESLQA EEHHHHCCHHHHHHH	27.74	20068231
351	Phosphorylation	VNQIGSVTESLQACK HHHHCCHHHHHHHHH	22.89	20068231
353	Phosphorylation	QIGSVTESLQACKLA HHCCHHHHHHHHHHH	19.20	20068231
357	S-palmitoylation	VTESLQACKLAQANG HHHHHHHHHHHHHCC	2.09	29575903
358	Acetylation	TESLQACKLAQANGW HHHHHHHHHHHHCCC	50.28	23954790
358	Succinylation	TESLQACKLAQANGW HHHHHHHHHHHHCCC	50.28	23954790
358	Ubiquitination	TESLQACKLAQANGW HHHHHHHHHHHHCCC	50.28	-
368	Sulfoxidation	QANGWGVMVSHRSGE HHCCCEEEEECCCCC	1.95	30846556
370	Phosphorylation	NGWGVMVSHRSGETE CCCEEEEECCCCCCC	8.62	-
372	Methylation	WGVMVSHRSGETEDT CEEEEECCCCCCCCC	38.56	-
373	Phosphorylation	GVMVSHRSGETEDTF EEEEECCCCCCCCCH	35.24	30278072
376	Phosphorylation	VSHRSGETEDTFIAD EECCCCCCCCCHHHH	42.56	30278072
379	Phosphorylation	RSGETEDTFIADLVV CCCCCCCCHHHHHHH	15.65	30278072
389	S-palmitoylation	ADLVVGLCTGQIKTG HHHHHHHHCCCCCCC	3.10	26865113
390	Phosphorylation	DLVVGLCTGQIKTGA HHHHHHHCCCCCCCC	36.84	28060719
394	Ubiquitination	GLCTGQIKTGAPCRS HHHCCCCCCCCCCCH	32.78	-
395	Phosphorylation	LCTGQIKTGAPCRSE HHCCCCCCCCCCCHH	39.96	23882029
406	2-Hydroxyisobutyrylation	CRSERLAKYNQLLRI CCHHHHHHHHHHHHH	49.69	-
406	Acetylation	CRSERLAKYNQLLRI CCHHHHHHHHHHHHH	49.69	25825284
406	Ubiquitination	CRSERLAKYNQLLRI CCHHHHHHHHHHHHH	49.69	21890473
406 (in isoform 1)	Ubiquitination	-	49.69	21890473
406	Ubiquitination	CRSERLAKYNQLLRI CCHHHHHHHHHHHHH	49.69	21890473
406	Ubiquitination	CRSERLAKYNQLLRI CCHHHHHHHHHHHHH	49.69	21890473
412	Methylation	AKYNQLLRIEEELGS HHHHHHHHHHHHHHH	42.75	-
419	Phosphorylation	RIEEELGSKAKFAGR HHHHHHHHHHHHCCC	41.90	23401153
420	N6-malonyllysine	IEEELGSKAKFAGRN HHHHHHHHHHHCCCC	54.52	-
420	2-Hydroxyisobutyrylation	IEEELGSKAKFAGRN HHHHHHHHHHHCCCC	54.52	-
420	Acetylation	IEEELGSKAKFAGRN HHHHHHHHHHHCCCC	54.52	19608861
420	Malonylation	IEEELGSKAKFAGRN HHHHHHHHHHHCCCC	54.52	26320211
420	Succinylation	IEEELGSKAKFAGRN HHHHHHHHHHHCCCC	54.52	-
420	Ubiquitination	IEEELGSKAKFAGRN HHHHHHHHHHHCCCC	54.52	19608861
420 (in isoform 1)	Ubiquitination	-	54.52	21890473
422	Acetylation	EELGSKAKFAGRNFR HHHHHHHHHCCCCCC	39.21	72614587
422	Ubiquitination	EELGSKAKFAGRNFR HHHHHHHHHCCCCCC	39.21	-
434	Acetylation	NFRNPLAK------- CCCCCCCC-------	69.43	11923871

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
44	Y	Phosphorylation	Kinase	SRC	P12931	GPS
44	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
115	S	Phosphorylation	Kinase	ULK1	O75385	PSP
282	S	Phosphorylation	Kinase	ULK1	O75385	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ENOA_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ENOA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PLMN_HUMAN	PLG	physical	11169399
TPC2A_HUMAN	TRAPPC2	physical	11134351
TPC2B_HUMAN	TRAPPC2	physical	11134351
HDAC1_HUMAN	HDAC1	physical	10403782
NS1BP_HUMAN	IVNS1ABP	physical	17996313
PGK1_HUMAN	PGK1	physical	22939629
G3P_HUMAN	GAPDH	physical	22939629
TPIS_HUMAN	TPI1	physical	22939629
FLNC_HUMAN	FLNC	physical	22939629
PPIA_HUMAN	PPIA	physical	22939629
ITPA_HUMAN	ITPA	physical	22939629
ENOB_HUMAN	ENO3	physical	22939629
IC1_HUMAN	SERPING1	physical	21988832
SZRD1_HUMAN	SZRD1	physical	22658674
NUDC_HUMAN	NUDC	physical	22658674
RCC1_HUMAN	RCC1	physical	22658674
SYYC_HUMAN	YARS	physical	22658674
LRC42_HUMAN	LRRC42	physical	22658674
RM37_HUMAN	MRPL37	physical	22658674
DPH5_HUMAN	DPH5	physical	22658674
GSTM3_HUMAN	GSTM3	physical	22658674
STRP1_HUMAN	STRIP1	physical	22658674
H2A2B_HUMAN	HIST2H2AB	physical	22658674
C42S1_HUMAN	CDC42SE1	physical	22658674
POGZ_HUMAN	POGZ	physical	22658674
LMNA_HUMAN	LMNA	physical	22658674
HDGF_HUMAN	HDGF	physical	22658674
DEDD_HUMAN	DEDD	physical	22658674
TM40L_HUMAN	TOMM40L	physical	22658674
STX6_HUMAN	STX6	physical	22658674
SRSF7_HUMAN	SRSF7	physical	22658674
FBLN3_HUMAN	EFEMP1	physical	22658674
TCPH_HUMAN	CCT7	physical	22658674
RPA1_HUMAN	POLR1A	physical	22658674
BIN1_HUMAN	BIN1	physical	22658674
IWS1_HUMAN	IWS1	physical	22658674
NAB1_HUMAN	NAB1	physical	22658674
ABI2_HUMAN	ABI2	physical	22658674
EF1B_HUMAN	EEF1B2	physical	22658674
ARPC4_HUMAN	ARPC4	physical	22658674
DHX30_HUMAN	DHX30	physical	22658674
QRIC1_HUMAN	QRICH1	physical	22658674
IFRD2_HUMAN	IFRD2	physical	22658674
THOC7_HUMAN	THOC7	physical	22658674
DHX15_HUMAN	DHX15	physical	22658674
HNRPD_HUMAN	HNRNPD	physical	22658674
FAT4_HUMAN	FAT4	physical	22658674
DCLK2_HUMAN	DCLK2	physical	22658674
ERAP1_HUMAN	ERAP1	physical	22658674
RPGF6_HUMAN	RAPGEF6	physical	22658674
GRP75_HUMAN	HSPA9	physical	22658674
STK10_HUMAN	STK10	physical	22658674
SYFM_HUMAN	FARS2	physical	22658674
H4_HUMAN	HIST1H4I	physical	22658674
KLDC3_HUMAN	KLHDC3	physical	22658674
MYO6_HUMAN	MYO6	physical	22658674
ASCC3_HUMAN	ASCC3	physical	22658674
HDAC2_HUMAN	HDAC2	physical	22658674
FBX5_HUMAN	FBXO5	physical	22658674
SCAF8_HUMAN	SCAF8	physical	22658674
OSBL3_HUMAN	OSBPL3	physical	22658674
ODO1_HUMAN	OGDH	physical	22658674
TENS3_HUMAN	TNS3	physical	22658674
GATD1_HUMAN	GATAD1	physical	22658674
MPPB_HUMAN	PMPCB	physical	22658674
NU205_HUMAN	NUP205	physical	22658674
XPO7_HUMAN	XPO7	physical	22658674
SCAR3_HUMAN	SCARA3	physical	22658674
MTFR1_HUMAN	MTFR1	physical	22658674
1433Z_HUMAN	YWHAZ	physical	22658674
CH033_HUMAN	C8orf33	physical	22658674
KANK1_HUMAN	KANK1	physical	22658674
MPDZ_HUMAN	MPDZ	physical	22658674
ACOC_HUMAN	ACO1	physical	22658674
UBAP1_HUMAN	UBAP1	physical	22658674
ANXA1_HUMAN	ANXA1	physical	22658674
DPOE3_HUMAN	POLE3	physical	22658674
HNRH3_HUMAN	HNRNPH3	physical	22658674
FBW1A_HUMAN	BTRC	physical	22658674
NP1L4_HUMAN	NAP1L4	physical	22658674
COPB_HUMAN	COPB1	physical	22658674
CATA_HUMAN	CAT	physical	22658674
PRP19_HUMAN	PRPF19	physical	22658674
CPSF7_HUMAN	CPSF7	physical	22658674
SYT12_HUMAN	SYT12	physical	22658674
CPT1A_HUMAN	CPT1A	physical	22658674
NUMA1_HUMAN	NUMA1	physical	22658674
ENDD1_HUMAN	ENDOD1	physical	22658674
YAP1_HUMAN	YAP1	physical	22658674
DCPS_HUMAN	DCPS	physical	22658674
CNDD3_HUMAN	NCAPD3	physical	22658674
VP26B_HUMAN	VPS26B	physical	22658674
MPRD_HUMAN	M6PR	physical	22658674
LIPB1_HUMAN	PPFIBP1	physical	22658674
LTMD1_HUMAN	LETMD1	physical	22658674
RBMS2_HUMAN	RBMS2	physical	22658674
NET4_HUMAN	NTN4	physical	22658674
KIME_HUMAN	MVK	physical	22658674
RNF10_HUMAN	RNF10	physical	22658674
RHOF_HUMAN	RHOF	physical	22658674
STX2_HUMAN	STX2	physical	22658674
MPP8_HUMAN	MPHOSPH8	physical	22658674
DIAP3_HUMAN	DIAPH3	physical	22658674
MBNL2_HUMAN	MBNL2	physical	22658674
NNRD_HUMAN	CARKD	physical	22658674
PNPH_HUMAN	PNP	physical	22658674
IPO4_HUMAN	IPO4	physical	22658674
RBM25_HUMAN	RBM25	physical	22658674
ERG28_HUMAN	C14orf1	physical	22658674
SKAP_HUMAN	KNSTRN	physical	22658674
TP53B_HUMAN	TP53BP1	physical	22658674
MYO1E_HUMAN	MYO1E	physical	22658674
KIF23_HUMAN	KIF23	physical	22658674
PTN9_HUMAN	PTPN9	physical	22658674
SNR25_HUMAN	SNRNP25	physical	22658674
CHIP_HUMAN	STUB1	physical	22658674
TXD11_HUMAN	TXNDC11	physical	22658674
VPS35_HUMAN	VPS35	physical	22658674
E2F4_HUMAN	E2F4	physical	22658674
NFAC3_HUMAN	NFATC3	physical	22658674
CYB5B_HUMAN	CYB5B	physical	22658674
PDPR_HUMAN	PDPR	physical	22658674
SYAC_HUMAN	AARS	physical	22658674
WDR81_HUMAN	WDR81	physical	22658674
CHD3_HUMAN	CHD3	physical	22658674
RAB34_HUMAN	RAB34	physical	22658674
MY18A_HUMAN	MYO18A	physical	22658674
ACACA_HUMAN	ACACA	physical	22658674
THA_HUMAN	THRA	physical	22658674
SMCE1_HUMAN	SMARCE1	physical	22658674
DHX8_HUMAN	DHX8	physical	22658674
S2539_HUMAN	SLC25A39	physical	22658674
ANR40_HUMAN	ANKRD40	physical	22658674
LC7L3_HUMAN	LUC7L3	physical	22658674
NPL4_HUMAN	NPLOC4	physical	22658674
GIPC3_HUMAN	GIPC3	physical	22658674
HNRPM_HUMAN	HNRNPM	physical	22658674
CRLF1_HUMAN	CRLF1	physical	22658674
MED29_HUMAN	MED29	physical	22658674
SPT5H_HUMAN	SUPT5H	physical	22658674
FBRL_HUMAN	FBL	physical	22658674
PPP5_HUMAN	PPP5C	physical	22658674
ISOC2_HUMAN	ISOC2	physical	22658674
NOP56_HUMAN	NOP56	physical	22658674
XRN2_HUMAN	XRN2	physical	22658674
OFUT1_HUMAN	POFUT1	physical	22658674
CP250_HUMAN	CEP250	physical	22658674
ZNFX1_HUMAN	ZNFX1	physical	22658674
ATP5J_HUMAN	ATP5J	physical	22658674
SUMO3_HUMAN	SUMO3	physical	22658674
CLH2_HUMAN	CLTCL1	physical	22658674
PIPNB_HUMAN	PITPNB	physical	22658674
NIPS1_HUMAN	NIPSNAP1	physical	22658674
SF3A1_HUMAN	SF3A1	physical	22658674
XRCC6_HUMAN	XRCC6	physical	22658674
NB5R3_HUMAN	CYB5R3	physical	22658674
TXLNG_HUMAN	TXLNG	physical	22658674
SH3K1_HUMAN	SH3KBP1	physical	22658674
PRDX4_HUMAN	PRDX4	physical	22658674
DPOLA_HUMAN	POLA1	physical	22658674
EBP_HUMAN	EBP	physical	22658674
MORC4_HUMAN	MORC4	physical	22658674
BAP31_HUMAN	BCAP31	physical	22658674
ALDR_HUMAN	AKR1B1	physical	26344197
AK1BF_HUMAN	AKR1B15	physical	26344197
ATP5J_HUMAN	ATP5J	physical	26344197
CALR_HUMAN	CALR	physical	26344197
CATA_HUMAN	CAT	physical	26344197
DUT_HUMAN	DUT	physical	26344197
EF2_HUMAN	EEF2	physical	26344197
FABP5_HUMAN	FABP5	physical	26344197
FKB1A_HUMAN	FKBP1A	physical	26344197
FKB1B_HUMAN	FKBP1B	physical	26344197
FKBP7_HUMAN	FKBP7	physical	26344197
G6PI_HUMAN	GPI	physical	26344197
MIF_HUMAN	MIF	physical	26344197
NIT2_HUMAN	NIT2	physical	26344197
PDIA1_HUMAN	P4HB	physical	26344197
PEF1_HUMAN	PEF1	physical	26344197
PGAM1_HUMAN	PGAM1	physical	26344197
MYP2_HUMAN	PMP2	physical	26344197
PUS7_HUMAN	PUS7	physical	26344197
SORCN_HUMAN	SRI	physical	26344197
TALDO_HUMAN	TALDO1	physical	26344197
TPIS_HUMAN	TPI1	physical	26344197
THIO_HUMAN	TXN	physical	26344197
UCHL3_HUMAN	UCHL3	physical	26344197
FBXW7_HUMAN	FBXW7	physical	26097998

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.

Related Literatures of Post-Translational Modification

Acetylation

"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-5; LYS-60; LYS-64; LYS-71;LYS-89; LYS-126; LYS-193; LYS-199; LYS-228; LYS-233; LYS-256; LYS-281;LYS-285; LYS-406 AND LYS-420, AND MASS SPECTROMETRY.
PubMed: 19608861

"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-71, AND MASS SPECTROMETRY.
PubMed: 16916647

Malonylation

"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-233 AND LYS-420.
PubMed: 21908771

N6-malonyllysine

"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-233 AND LYS-420.
PubMed: 21908771

Phosphorylation

"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-37; TYR-44; SER-272 ANDTHR-390, AND MASS SPECTROMETRY.
PubMed: 19690332

"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-254 AND SER-263, ANDMASS SPECTROMETRY.
PubMed: 18669648

"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-57 AND SER-63, AND MASSSPECTROMETRY.
PubMed: 17287340

"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72, AND MASSSPECTROMETRY.
PubMed: 17924679

"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44 AND TYR-287, AND MASSSPECTROMETRY.
PubMed: 18083107

"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-44 AND TYR-287, AND MASSSPECTROMETRY.
PubMed: 15592455