KPYM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KPYM_HUMAN
• UniProt AC: P14618
• Protein Name: Pyruvate kinase PKM
• Gene Name: PKM
• Organism: Homo sapiens (Human).
• Sequence Length: 531
• Subcellular Localization: Cytoplasm . Nucleus. Translocates to the nucleus in response to different apoptotic stimuli. Nuclear translocation is sufficient to induce cell death that is caspase independent, isoform-specific and independent of its enzymatic activity.
• Protein Description: Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival..
• Protein Sequence: MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKEMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGLISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEASFKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP

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	------MSKPHSEAG ------CCCCCCCCC	55.69	19413330
2	Phosphorylation	------MSKPHSEAG ------CCCCCCCCC	55.69	28450419
2 (in isoform 3)	Phosphorylation	-	55.69	25159151
3	"N6,N6,N6-trimethyllysine"	-----MSKPHSEAGT -----CCCCCCCCCC	45.51	-
3	Acetylation	-----MSKPHSEAGT -----CCCCCCCCCC	45.51	25953088
3	Malonylation	-----MSKPHSEAGT -----CCCCCCCCCC	45.51	26320211
3	Methylation	-----MSKPHSEAGT -----CCCCCCCCCC	45.51	24129315
3	Ubiquitination	-----MSKPHSEAGT -----CCCCCCCCCC	45.51	-
6	Phosphorylation	--MSKPHSEAGTAFI --CCCCCCCCCCCHH	37.35	28450419
10	Phosphorylation	KPHSEAGTAFIQTQQ CCCCCCCCCHHHHHH	25.99	28450419
13	Phosphorylation	SEAGTAFIQTQQLHA CCCCCCHHHHHHHHH	3.93	27251275
15	Phosphorylation	AGTAFIQTQQLHAAM CCCCHHHHHHHHHHH	17.29	28450419
25	Phosphorylation	LHAAMADTFLEHMCR HHHHHHHHHHHHHHC	22.15	21406692
37	Phosphorylation	MCRLDIDSPPITARN HHCCCCCCCCEEECC	32.67	19664994
41	Phosphorylation	DIDSPPITARNTGII CCCCCCEEECCCEEE	25.91	25463755
45	Phosphorylation	PPITARNTGIICTIG CCEEECCCEEEEEEC	24.97	23911959
49	S-nitrosocysteine	ARNTGIICTIGPASR ECCCEEEEEECCCCC	1.83	-
49	Glutathionylation	ARNTGIICTIGPASR ECCCEEEEEECCCCC	1.83	22555962
49	S-nitrosylation	ARNTGIICTIGPASR ECCCEEEEEECCCCC	1.83	18335467
50	O-linked_Glycosylation	RNTGIICTIGPASRS CCCEEEEEECCCCCC	20.68	32830957
50	Phosphorylation	RNTGIICTIGPASRS CCCEEEEEECCCCCC	20.68	30266825
55	Phosphorylation	ICTIGPASRSVETLK EEEECCCCCCHHHHH	28.37	30266825
57	Phosphorylation	TIGPASRSVETLKEM EECCCCCCHHHHHHH	23.08	23927012
60	Phosphorylation	PASRSVETLKEMIKS CCCCCHHHHHHHHHC	40.76	30576142
62	2-Hydroxyisobutyrylation	SRSVETLKEMIKSGM CCCHHHHHHHHHCCC	53.29	-
62	Acetylation	SRSVETLKEMIKSGM CCCHHHHHHHHHCCC	53.29	19608861
62	Malonylation	SRSVETLKEMIKSGM CCCHHHHHHHHHCCC	53.29	26320211
62	Succinylation	SRSVETLKEMIKSGM CCCHHHHHHHHHCCC	53.29	27452117
62	Ubiquitination	SRSVETLKEMIKSGM CCCHHHHHHHHHCCC	53.29	21890473
62 (in isoform 1)	Ubiquitination	-	53.29	21890473
62 (in isoform 2)	Ubiquitination	-	53.29	21890473
63	Phosphorylation	RSVETLKEMIKSGMN CCHHHHHHHHHCCCC	49.61	24719451
64	Sulfoxidation	SVETLKEMIKSGMNV CHHHHHHHHHCCCCE	4.46	30846556
66	2-Hydroxyisobutyrylation	ETLKEMIKSGMNVAR HHHHHHHHCCCCEEE	39.38	-
66	Acetylation	ETLKEMIKSGMNVAR HHHHHHHHCCCCEEE	39.38	23954790
66	Malonylation	ETLKEMIKSGMNVAR HHHHHHHHCCCCEEE	39.38	26320211
66	Succinylation	ETLKEMIKSGMNVAR HHHHHHHHCCCCEEE	39.38	-
66	Succinylation	ETLKEMIKSGMNVAR HHHHHHHHCCCCEEE	39.38	21890473
66	Ubiquitination	ETLKEMIKSGMNVAR HHHHHHHHCCCCEEE	39.38	21890473
66 (in isoform 1)	Ubiquitination	-	39.38	21890473
66 (in isoform 2)	Ubiquitination	-	39.38	21890473
67	Acetylation	TLKEMIKSGMNVARL HHHHHHHCCCCEEEE	32.14	19608861
67	Phosphorylation	TLKEMIKSGMNVARL HHHHHHHCCCCEEEE	32.14	26437602
67	Ubiquitination	TLKEMIKSGMNVARL HHHHHHHCCCCEEEE	32.14	19608861
77	Phosphorylation	NVARLNFSHGTHEYH CEEEEECCCCCCCCC	21.67	29255136
78 (in isoform 3)	Phosphorylation	-	40.82	25159151
80	Phosphorylation	RLNFSHGTHEYHAET EEECCCCCCCCCHHH	13.20	29255136
83	Phosphorylation	FSHGTHEYHAETIKN CCCCCCCCCHHHHHH	9.95	27155012
87	Phosphorylation	THEYHAETIKNVRTA CCCCCHHHHHHHHHH	37.73	28152594
89	2-Hydroxyisobutyrylation	EYHAETIKNVRTATE CCCHHHHHHHHHHHH	57.73	-
89	Acetylation	EYHAETIKNVRTATE CCCHHHHHHHHHHHH	57.73	19608861
89	Malonylation	EYHAETIKNVRTATE CCCHHHHHHHHHHHH	57.73	26320211
89	Ubiquitination	EYHAETIKNVRTATE CCCHHHHHHHHHHHH	57.73	19608861
89 (in isoform 1)	Ubiquitination	-	57.73	21890473
89 (in isoform 2)	Ubiquitination	-	57.73	21890473
92	Methylation	AETIKNVRTATESFA HHHHHHHHHHHHHHC	28.21	115384321
93	Phosphorylation	ETIKNVRTATESFAS HHHHHHHHHHHHHCC	33.38	27273156
94	Acetylation	TIKNVRTATESFASD HHHHHHHHHHHHCCC	9.98	19608861
94	Ubiquitination	TIKNVRTATESFASD HHHHHHHHHHHHCCC	9.98	19608861
95	Phosphorylation	IKNVRTATESFASDP HHHHHHHHHHHCCCC	31.39	28102081
97	Acetylation	NVRTATESFASDPIL HHHHHHHHHCCCCCC	23.04	19608861
97	Phosphorylation	NVRTATESFASDPIL HHHHHHHHHCCCCCC	23.04	21712546
97	Ubiquitination	NVRTATESFASDPIL HHHHHHHHHCCCCCC	23.04	19608861
100	Phosphorylation	TATESFASDPILYRP HHHHHHCCCCCCCCC	41.74	22617229
105	Nitration	FASDPILYRPVAVAL HCCCCCCCCCEEEEE	17.37	-
105	Phosphorylation	FASDPILYRPVAVAL HCCCCCCCCCEEEEE	17.37	25159151
111	Phosphorylation	LYRPVAVALDTKGPE CCCCEEEEECCCCCC	7.03	27251275
114	Phosphorylation	PVAVALDTKGPEIRT CEEEEECCCCCCCCC	38.46	27259358
115	2-Hydroxyisobutyrylation	VAVALDTKGPEIRTG EEEEECCCCCCCCCE	72.62	-
115	Acetylation	VAVALDTKGPEIRTG EEEEECCCCCCCCCE	72.62	23954790
115	Malonylation	VAVALDTKGPEIRTG EEEEECCCCCCCCCE	72.62	26320211
115	Sumoylation	VAVALDTKGPEIRTG EEEEECCCCCCCCCE	72.62	28112733
115	Ubiquitination	VAVALDTKGPEIRTG EEEEECCCCCCCCCE	72.62	21906983
115 (in isoform 1)	Ubiquitination	-	72.62	21890473
115 (in isoform 2)	Ubiquitination	-	72.62	21890473
121	Phosphorylation	TKGPEIRTGLIKGSG CCCCCCCCEEECCCC	41.84	26437602
124	Acetylation	PEIRTGLIKGSGTAE CCCCCEEECCCCEEE	5.13	19608861
124	Ubiquitination	PEIRTGLIKGSGTAE CCCCCEEECCCCEEE	5.13	19608861
125	2-Hydroxyisobutyrylation	EIRTGLIKGSGTAEV CCCCEEECCCCEEEE	52.66	-
125	Acetylation	EIRTGLIKGSGTAEV CCCCEEECCCCEEEE	52.66	26051181
125	Ubiquitination	EIRTGLIKGSGTAEV CCCCEEECCCCEEEE	52.66	21906983
125 (in isoform 1)	Ubiquitination	-	52.66	21890473
125 (in isoform 2)	Ubiquitination	-	52.66	21890473
127	Phosphorylation	RTGLIKGSGTAEVEL CCEEECCCCEEEEEE	28.15	29255136
129	Phosphorylation	GLIKGSGTAEVELKK EEECCCCEEEEEECC	22.72	29255136
131	Phosphorylation	IKGSGTAEVELKKGA ECCCCEEEEEECCCC	36.04	27251275
135	2-Hydroxyisobutyrylation	GTAEVELKKGATLKI CEEEEEECCCCEEEE	35.34	-
135	Acetylation	GTAEVELKKGATLKI CEEEEEECCCCEEEE	35.34	23954790
135	Malonylation	GTAEVELKKGATLKI CEEEEEECCCCEEEE	35.34	26320211
135	Ubiquitination	GTAEVELKKGATLKI CEEEEEECCCCEEEE	35.34	21906983
135 (in isoform 1)	Ubiquitination	-	35.34	21890473
135 (in isoform 2)	Ubiquitination	-	35.34	21890473
136	Acetylation	TAEVELKKGATLKIT EEEEEECCCCEEEEE	67.42	25953088
136	Ubiquitination	TAEVELKKGATLKIT EEEEEECCCCEEEEE	67.42	19608861
136 (in isoform 2)	Ubiquitination	-	67.42	-
140	Acetylation	ELKKGATLKITLDNA EECCCCEEEEEECCH	3.61	19608861
140	Ubiquitination	ELKKGATLKITLDNA EECCCCEEEEEECCH	3.61	19608861
141	2-Hydroxyisobutyrylation	LKKGATLKITLDNAY ECCCCEEEEEECCHH	29.32	-
141	Acetylation	LKKGATLKITLDNAY ECCCCEEEEEECCHH	29.32	25953088
141	Ubiquitination	LKKGATLKITLDNAY ECCCCEEEEEECCHH	29.32	-
143	Phosphorylation	KGATLKITLDNAYME CCCEEEEEECCHHHH	26.86	21712546
148	Nitration	KITLDNAYMEKCDEN EEEECCHHHHHCCCC	16.44	-
148	Phosphorylation	KITLDNAYMEKCDEN EEEECCHHHHHCCCC	16.44	27273156
149	Sulfoxidation	ITLDNAYMEKCDENI EEECCHHHHHCCCCE	3.54	21406390
151	Acetylation	LDNAYMEKCDENILW ECCHHHHHCCCCEEE	30.38	26051181
151	Phosphorylation	LDNAYMEKCDENILW ECCHHHHHCCCCEEE	30.38	27251275
151	Ubiquitination	LDNAYMEKCDENILW ECCHHHHHCCCCEEE	30.38	19608861
151 (in isoform 1)	Ubiquitination	-	30.38	21890473
151 (in isoform 2)	Ubiquitination	-	30.38	21890473
152	S-nitrosocysteine	DNAYMEKCDENILWL CCHHHHHCCCCEEEE	5.17	-
152	Glutathionylation	DNAYMEKCDENILWL CCHHHHHCCCCEEEE	5.17	22555962
152	S-nitrosylation	DNAYMEKCDENILWL CCHHHHHCCCCEEEE	5.17	19483679
161	Phosphorylation	ENILWLDYKNICKVV CCEEEEEHHCCEEEE	12.08	25147952
162	Acetylation	NILWLDYKNICKVVE CEEEEEHHCCEEEEE	39.23	26822725
162	Ubiquitination	NILWLDYKNICKVVE CEEEEEHHCCEEEEE	39.23	21906983
162 (in isoform 1)	Ubiquitination	-	39.23	21890473
162 (in isoform 2)	Ubiquitination	-	39.23	21890473
163	Acetylation	ILWLDYKNICKVVEV EEEEEHHCCEEEEEE	38.37	19608861
163	Ubiquitination	ILWLDYKNICKVVEV EEEEEHHCCEEEEEE	38.37	19608861
166	2-Hydroxyisobutyrylation	LDYKNICKVVEVGSK EEHHCCEEEEEECCE	45.58	-
166	Acetylation	LDYKNICKVVEVGSK EEHHCCEEEEEECCE	45.58	19608861
166	Malonylation	LDYKNICKVVEVGSK EEHHCCEEEEEECCE	45.58	26320211
166	Succinylation	LDYKNICKVVEVGSK EEHHCCEEEEEECCE	45.58	-
166	Succinylation	LDYKNICKVVEVGSK EEHHCCEEEEEECCE	45.58	21906983
166	Sumoylation	LDYKNICKVVEVGSK EEHHCCEEEEEECCE	45.58	19608861
166	Ubiquitination	LDYKNICKVVEVGSK EEHHCCEEEEEECCE	45.58	19608861
166 (in isoform 1)	Ubiquitination	-	45.58	21890473
166 (in isoform 2)	Ubiquitination	-	45.58	21890473
170	Acetylation	NICKVVEVGSKIYVD CCEEEEEECCEEEEC	7.68	19608861
170	Ubiquitination	NICKVVEVGSKIYVD CCEEEEEECCEEEEC	7.68	19608861
171	Acetylation	ICKVVEVGSKIYVDD CEEEEEECCEEEECC	15.09	19608861
171	Phosphorylation	ICKVVEVGSKIYVDD CEEEEEECCEEEECC	15.09	27251275
171	Ubiquitination	ICKVVEVGSKIYVDD CEEEEEECCEEEECC	15.09	19608861
172	Phosphorylation	CKVVEVGSKIYVDDG EEEEEECCEEEECCC	22.51	28152594
174	Phosphorylation	VVEVGSKIYVDDGLI EEEECCEEEECCCEE	4.31	27251275
175	Nitration	VEVGSKIYVDDGLIS EEECCEEEECCCEEE	11.10	-
175	Phosphorylation	VEVGSKIYVDDGLIS EEECCEEEECCCEEE	11.10	21712546
182	Phosphorylation	YVDDGLISLQVKQKG EECCCEEEEEEEECC	20.14	22199227
186	2-Hydroxyisobutyrylation	GLISLQVKQKGADFL CEEEEEEEECCCCEE	33.07	-
186	Acetylation	GLISLQVKQKGADFL CEEEEEEEECCCCEE	33.07	25953088
186	Succinylation	GLISLQVKQKGADFL CEEEEEEEECCCCEE	33.07	23954790
186	Ubiquitination	GLISLQVKQKGADFL CEEEEEEEECCCCEE	33.07	-
186 (in isoform 1)	Ubiquitination	-	33.07	21890473
186 (in isoform 2)	Ubiquitination	-	33.07	21890473
188	2-Hydroxyisobutyrylation	ISLQVKQKGADFLVT EEEEEEECCCCEEEE	50.80	-
188	Acetylation	ISLQVKQKGADFLVT EEEEEEECCCCEEEE	50.80	23749302
188	Ubiquitination	ISLQVKQKGADFLVT EEEEEEECCCCEEEE	50.80	21906983
188 (in isoform 1)	Ubiquitination	-	50.80	21890473
188 (in isoform 2)	Ubiquitination	-	50.80	21890473
195	Phosphorylation	KGADFLVTEVENGGS CCCCEEEEEEECCCC	36.14	28450419
201	Acetylation	VTEVENGGSLGSKKG EEEEECCCCCCCCCC	31.14	19608861
201	Phosphorylation	VTEVENGGSLGSKKG EEEEECCCCCCCCCC	31.14	27251275
201	Ubiquitination	VTEVENGGSLGSKKG EEEEECCCCCCCCCC	31.14	19608861
202	Phosphorylation	TEVENGGSLGSKKGV EEEECCCCCCCCCCC	30.84	28450419
205	Phosphorylation	ENGGSLGSKKGVNLP ECCCCCCCCCCCCCC	36.17	28450419
206	2-Hydroxyisobutyrylation	NGGSLGSKKGVNLPG CCCCCCCCCCCCCCC	52.31	-
206	Acetylation	NGGSLGSKKGVNLPG CCCCCCCCCCCCCCC	52.31	23954790
206	Malonylation	NGGSLGSKKGVNLPG CCCCCCCCCCCCCCC	52.31	26320211
206	Ubiquitination	NGGSLGSKKGVNLPG CCCCCCCCCCCCCCC	52.31	21890473
206 (in isoform 1)	Ubiquitination	-	52.31	21890473
206 (in isoform 2)	Ubiquitination	-	52.31	21890473
207	2-Hydroxyisobutyrylation	GGSLGSKKGVNLPGA CCCCCCCCCCCCCCC	70.55	-
207	Acetylation	GGSLGSKKGVNLPGA CCCCCCCCCCCCCCC	70.55	26051181
207	Malonylation	GGSLGSKKGVNLPGA CCCCCCCCCCCCCCC	70.55	26320211
207	Ubiquitination	GGSLGSKKGVNLPGA CCCCCCCCCCCCCCC	70.55	20972266
207 (in isoform 1)	Ubiquitination	-	70.55	21890473
207 (in isoform 2)	Ubiquitination	-	70.55	21890473
209	Acetylation	SLGSKKGVNLPGAAV CCCCCCCCCCCCCCC	10.25	19608861
209	Ubiquitination	SLGSKKGVNLPGAAV CCCCCCCCCCCCCCC	10.25	19608861
222	Phosphorylation	AVDLPAVSEKDIQDL CCCCCCCCHHHHHHH	40.82	29255136
224	2-Hydroxyisobutyrylation	DLPAVSEKDIQDLKF CCCCCCHHHHHHHCC	53.26	-
224	Acetylation	DLPAVSEKDIQDLKF CCCCCCHHHHHHHCC	53.26	23954790
224	Succinylation	DLPAVSEKDIQDLKF CCCCCCHHHHHHHCC	53.26	23954790
224	Sumoylation	DLPAVSEKDIQDLKF CCCCCCHHHHHHHCC	53.26	-
224	Ubiquitination	DLPAVSEKDIQDLKF CCCCCCHHHHHHHCC	53.26	-
224 (in isoform 1)	Ubiquitination	-	53.26	21890473
224 (in isoform 2)	Ubiquitination	-	53.26	21890473
230	Acetylation	EKDIQDLKFGVEQDV HHHHHHHCCCCHHCH	48.65	70481
230	Ubiquitination	EKDIQDLKFGVEQDV HHHHHHHCCCCHHCH	48.65	-
239	Sulfoxidation	GVEQDVDMVFASFIR CCHHCHHHHHHHHHH	2.41	30846556
240	Acetylation	VEQDVDMVFASFIRK CHHCHHHHHHHHHHH	2.91	19608861
240	Ubiquitination	VEQDVDMVFASFIRK CHHCHHHHHHHHHHH	2.91	19608861
243	Phosphorylation	DVDMVFASFIRKASD CHHHHHHHHHHHHHC	15.11	28450419
247	2-Hydroxyisobutyrylation	VFASFIRKASDVHEV HHHHHHHHHHCHHHH	47.64	-
247	Ubiquitination	VFASFIRKASDVHEV HHHHHHHHHHCHHHH	47.64	-
249	Phosphorylation	ASFIRKASDVHEVRK HHHHHHHHCHHHHHH	43.11	28355574
251	Acetylation	FIRKASDVHEVRKVL HHHHHHCHHHHHHHH	3.72	19608861
251	Ubiquitination	FIRKASDVHEVRKVL HHHHHHCHHHHHHHH	3.72	19608861
255	Methylation	ASDVHEVRKVLGEKG HHCHHHHHHHHCCCC	22.00	115487671
256	Ubiquitination	SDVHEVRKVLGEKGK HCHHHHHHHHCCCCC	47.16	-
261	2-Hydroxyisobutyrylation	VRKVLGEKGKNIKII HHHHHCCCCCCCEEE	73.68	-
261	Acetylation	VRKVLGEKGKNIKII HHHHHCCCCCCCEEE	73.68	23749302
261	Succinylation	VRKVLGEKGKNIKII HHHHHCCCCCCCEEE	73.68	23954790
261	Ubiquitination	VRKVLGEKGKNIKII HHHHHCCCCCCCEEE	73.68	-
261 (in isoform 1)	Ubiquitination	-	73.68	21890473
261 (in isoform 2)	Ubiquitination	-	73.68	21890473
266	Acetylation	GEKGKNIKIISKIEN CCCCCCCEEEEEECC	43.30	19608861
266	Sumoylation	GEKGKNIKIISKIEN CCCCCCCEEEEEECC	43.30	28112733
266	Ubiquitination	GEKGKNIKIISKIEN CCCCCCCEEEEEECC	43.30	266
266 (in isoform 1)	Ubiquitination	-	43.30	21890473
266 (in isoform 2)	Ubiquitination	-	43.30	21890473
269	Phosphorylation	GKNIKIISKIENHEG CCCCEEEEEECCCHH	30.93	30183078
270	Sumoylation	KNIKIISKIENHEGV CCCEEEEEECCCHHH	43.56	-
270	2-Hydroxyisobutyrylation	KNIKIISKIENHEGV CCCEEEEEECCCHHH	43.56	-
270	Acetylation	KNIKIISKIENHEGV CCCEEEEEECCCHHH	43.56	23236377
270	Sumoylation	KNIKIISKIENHEGV CCCEEEEEECCCHHH	43.56	28112733
270	Ubiquitination	KNIKIISKIENHEGV CCCEEEEEECCCHHH	43.56	21890473
270 (in isoform 1)	Ubiquitination	-	43.56	21890473
270 (in isoform 2)	Ubiquitination	-	43.56	21890473
271	Acetylation	NIKIISKIENHEGVR CCEEEEEECCCHHHC	5.24	19608861
271	Ubiquitination	NIKIISKIENHEGVR CCEEEEEECCCHHHC	5.24	19608861
276	Phosphorylation	SKIENHEGVRRFDEI EEECCCHHHCCHHHH	15.64	27251275
278	Methylation	IENHEGVRRFDEILE ECCCHHHCCHHHHHH	44.39	115487687
287	Phosphorylation	FDEILEASDGIMVAR HHHHHHHCCCEEEEE	27.30	26846344
290	Ubiquitination	ILEASDGIMVARGDL HHHHCCCEEEEECCC	2.11	21890473
290	Acetylation	ILEASDGIMVARGDL HHHHCCCEEEEECCC	2.11	19608861
290	Ubiquitination	ILEASDGIMVARGDL HHHHCCCEEEEECCC	2.11	19608861
291	Sulfoxidation	LEASDGIMVARGDLG HHHCCCEEEEECCCC	2.06	30846556
296	Ubiquitination	GIMVARGDLGIEIPA CEEEEECCCCCCCCH	35.85	21890473
296	Phosphorylation	GIMVARGDLGIEIPA CEEEEECCCCCCCCH	35.85	27251275
301	Acetylation	RGDLGIEIPAEKVFL ECCCCCCCCHHHHHH	3.56	19608861
301	Ubiquitination	RGDLGIEIPAEKVFL ECCCCCCCCHHHHHH	3.56	19608861
305	2-Hydroxyisobutyrylation	GIEIPAEKVFLAQKM CCCCCHHHHHHHHHH	40.15	-
305	Acetylation	GIEIPAEKVFLAQKM CCCCCHHHHHHHHHH	40.15	19608861
305	Ubiquitination	GIEIPAEKVFLAQKM CCCCCHHHHHHHHHH	40.15	20639865
305 (in isoform 1)	Ubiquitination	-	40.15	21890473
305 (in isoform 2)	Ubiquitination	-	40.15	21890473
310	Acetylation	AEKVFLAQKMMIGRC HHHHHHHHHHHHCCC	36.00	19608861
310	Ubiquitination	AEKVFLAQKMMIGRC HHHHHHHHHHHHCCC	36.00	19608861
311	Acetylation	EKVFLAQKMMIGRCN HHHHHHHHHHHCCCC	25.48	25953088
311	Ubiquitination	EKVFLAQKMMIGRCN HHHHHHHHHHHCCCC	25.48	21890473
311 (in isoform 1)	Ubiquitination	-	25.48	21890473
311 (in isoform 2)	Ubiquitination	-	25.48	21890473
319	Methylation	MMIGRCNRAGKPVIC HHHCCCCCCCCCEEE	48.63	115487679
322	2-Hydroxyisobutyrylation	GRCNRAGKPVICATQ CCCCCCCCCEEEEHH	34.82	-
322	Acetylation	GRCNRAGKPVICATQ CCCCCCCCCEEEEHH	34.82	26051181
322	Succinylation	GRCNRAGKPVICATQ CCCCCCCCCEEEEHH	34.82	-
322	Succinylation	GRCNRAGKPVICATQ CCCCCCCCCEEEEHH	34.82	21906983
322	Ubiquitination	GRCNRAGKPVICATQ CCCCCCCCCEEEEHH	34.82	-
322 (in isoform 1)	Ubiquitination	-	34.82	21890473
322 (in isoform 2)	Ubiquitination	-	34.82	21890473
323	Phosphorylation	RCNRAGKPVICATQM CCCCCCCCEEEEHHH	21.56	27251275
326	Glutathionylation	RAGKPVICATQMLES CCCCCEEEEHHHHHH	3.23	22555962
326	S-nitrosylation	RAGKPVICATQMLES CCCCCEEEEHHHHHH	3.23	25040305
328	Phosphorylation	GKPVICATQMLESMI CCCEEEEHHHHHHHH	15.31	17525332
330	Sulfoxidation	PVICATQMLESMIKK CEEEEHHHHHHHHCC	3.78	30846556
333	Phosphorylation	CATQMLESMIKKPRP EEHHHHHHHHCCCCC	23.11	30108239
334	Sulfoxidation	ATQMLESMIKKPRPT EHHHHHHHHCCCCCC	3.67	30846556
336	2-Hydroxyisobutyrylation	QMLESMIKKPRPTRA HHHHHHHCCCCCCCC	48.35	-
336	Acetylation	QMLESMIKKPRPTRA HHHHHHHCCCCCCCC	48.35	25953088
336	Malonylation	QMLESMIKKPRPTRA HHHHHHHCCCCCCCC	48.35	26320211
336	Ubiquitination	QMLESMIKKPRPTRA HHHHHHHCCCCCCCC	48.35	-
337	Acetylation	MLESMIKKPRPTRAE HHHHHHCCCCCCCCC	35.02	26051181
337	Ubiquitination	MLESMIKKPRPTRAE HHHHHHCCCCCCCCC	35.02	-
340	Acetylation	SMIKKPRPTRAEGSD HHHCCCCCCCCCCCC	34.46	19608861
340	Ubiquitination	SMIKKPRPTRAEGSD HHHCCCCCCCCCCCC	34.46	19608861
346	Phosphorylation	RPTRAEGSDVANAVL CCCCCCCCCHHHHHH	22.03	26356563
358	Glutathionylation	AVLDGADCIMLSGET HHHCCCCEEEEECCC	1.63	22555962
360	Sulfoxidation	LDGADCIMLSGETAK HCCCCEEEEECCCCC	2.83	30846556
362	Phosphorylation	GADCIMLSGETAKGD CCCEEEEECCCCCCC	19.73	26356563
365	Phosphorylation	CIMLSGETAKGDYPL EEEEECCCCCCCCCH	36.88	26356563
367	2-Hydroxyisobutyrylation	MLSGETAKGDYPLEA EEECCCCCCCCCHHH	60.79	-
367	Acetylation	MLSGETAKGDYPLEA EEECCCCCCCCCHHH	60.79	23236377
367	Malonylation	MLSGETAKGDYPLEA EEECCCCCCCCCHHH	60.79	26320211
367	Ubiquitination	MLSGETAKGDYPLEA EEECCCCCCCCCHHH	60.79	-
367 (in isoform 2)	Ubiquitination	-	60.79	-
370	Phosphorylation	GETAKGDYPLEAVRM CCCCCCCCCHHHHHH	20.56	22115753
377	Sulfoxidation	YPLEAVRMQHLIARE CCHHHHHHHHHHHHH	2.06	30846556
379	Acetylation	LEAVRMQHLIAREAE HHHHHHHHHHHHHHH	15.17	19608861
379	Ubiquitination	LEAVRMQHLIAREAE HHHHHHHHHHHHHHH	15.17	19608861
390	Phosphorylation	REAEAAIYHLQLFEE HHHHHHHHHHHHHHH	7.55	27155012
402 (in isoform 2)	Phosphorylation	-	7.52	20071362
403	Hydroxylation	EELRRLAPITSDPTE HHHHHHCCCCCCCCH	34.67	21620138
403 (in isoform 2)	Phosphorylation	-	34.67	29116813
405	O-linked_Glycosylation	LRRLAPITSDPTEAT HHHHCCCCCCCCHHH	26.47	32830957
405	Phosphorylation	LRRLAPITSDPTEAT HHHHCCCCCCCCHHH	26.47	28450419
405 (in isoform 2)	Phosphorylation	-	26.47	26437602
406	O-linked_Glycosylation	RRLAPITSDPTEATA HHHCCCCCCCCHHHH	42.17	32830957
406	Phosphorylation	RRLAPITSDPTEATA HHHCCCCCCCCHHHH	42.17	21712546
406 (in isoform 2)	Phosphorylation	-	42.17	26437602
408	Hydroxylation	LAPITSDPTEATAVG HCCCCCCCCHHHHHH	31.72	21620138
409	Phosphorylation	APITSDPTEATAVGA CCCCCCCCHHHHHHH	43.15	28450419
412	Phosphorylation	TSDPTEATAVGAVEA CCCCCHHHHHHHHHH	18.68	28450419
418	Acetylation	ATAVGAVEASFKCCS HHHHHHHHHHHEECC	37.75	19608861
418	Ubiquitination	ATAVGAVEASFKCCS HHHHHHHHHHHEECC	37.75	19608861
420	Phosphorylation	AVGAVEASFKCCSGA HHHHHHHHHEECCEE	16.25	28450419
420 (in isoform 2)	Phosphorylation	-	16.25	22210691
421 (in isoform 2)	Phosphorylation	-	10.14	21214269
422	Acetylation	GAVEASFKCCSGAII HHHHHHHEECCEEEE	31.66	18527159
423	S-nitrosocysteine	AVEASFKCCSGAIIV HHHHHHEECCEEEEE	1.79	-
423	S-nitrosylation	AVEASFKCCSGAIIV HHHHHHEECCEEEEE	1.79	19483679
424	S-nitrosocysteine	VEASFKCCSGAIIVL HHHHHEECCEEEEEE	4.30	-
424	S-nitrosylation	VEASFKCCSGAIIVL HHHHHEECCEEEEEE	4.30	19483679
425	Phosphorylation	EASFKCCSGAIIVLT HHHHEECCEEEEEEE	40.50	21712546
432	Phosphorylation	SGAIIVLTKSGRSAH CEEEEEEECCCCCHH	16.57	22199227
432 (in isoform 2)	Phosphorylation	-	16.57	21214269
433	Acetylation	GAIIVLTKSGRSAHQ EEEEEEECCCCCHHH	46.91	19608861
433	Malonylation	GAIIVLTKSGRSAHQ EEEEEEECCCCCHHH	46.91	26320211
433	Ubiquitination	GAIIVLTKSGRSAHQ EEEEEEECCCCCHHH	46.91	-
433 (in isoform 1)	Ubiquitination	-	46.91	21890473
434	Phosphorylation	AIIVLTKSGRSAHQV EEEEEECCCCCHHHH	33.92	26699800
434 (in isoform 2)	Phosphorylation	-	33.92	21214269
436	Phosphorylation	IVLTKSGRSAHQVAR EEEECCCCCHHHHHH	37.45	27251275
437	Phosphorylation	VLTKSGRSAHQVARY EEECCCCCHHHHHHH	33.36	26657352
437 (in isoform 2)	Phosphorylation	-	33.36	29743597
444	Phosphorylation	SAHQVARYRPRAPII CHHHHHHHCCCCCEE	18.41	24719451
454	Phosphorylation	RAPIIAVTRNPQTAR CCCEEEEECCHHHHH	18.73	21712546
466	Phosphorylation	TARQAHLYRGIFPVL HHHHHHHHCCCHHHC	9.27	21722762
467	Methylation	ARQAHLYRGIFPVLC HHHHHHHCCCHHHCC	37.78	115487695
474	S-nitrosocysteine	RGIFPVLCKDPVQEA CCCHHHCCCCCCHHH	4.84	-
474	Glutathionylation	RGIFPVLCKDPVQEA CCCHHHCCCCCCHHH	4.84	22555962
474	S-nitrosylation	RGIFPVLCKDPVQEA CCCHHHCCCCCCHHH	4.84	19483679
474	S-palmitoylation	RGIFPVLCKDPVQEA CCCHHHCCCCCCHHH	4.84	29575903
475	2-Hydroxyisobutyrylation	GIFPVLCKDPVQEAW CCHHHCCCCCCHHHH	61.99	-
475	Acetylation	GIFPVLCKDPVQEAW CCHHHCCCCCCHHHH	61.99	25038526
475	Ubiquitination	GIFPVLCKDPVQEAW CCHHHCCCCCCHHHH	61.99	21906983
475 (in isoform 1)	Ubiquitination	-	61.99	21890473
475 (in isoform 2)	Ubiquitination	-	61.99	21890473
494	Sulfoxidation	DLRVNFAMNVGKARG CEEEEEEEECHHHCC	3.50	21406390
498	2-Hydroxyisobutyrylation	NFAMNVGKARGFFKK EEEEECHHHCCCEEC	30.54	-
498	Acetylation	NFAMNVGKARGFFKK EEEEECHHHCCCEEC	30.54	25953088
498	Malonylation	NFAMNVGKARGFFKK EEEEECHHHCCCEEC	30.54	26320211
498	Succinylation	NFAMNVGKARGFFKK EEEEECHHHCCCEEC	30.54	-
498	Succinylation	NFAMNVGKARGFFKK EEEEECHHHCCCEEC	30.54	23954790
498	Ubiquitination	NFAMNVGKARGFFKK EEEEECHHHCCCEEC	30.54	21890473
498 (in isoform 1)	Ubiquitination	-	30.54	21890473
498 (in isoform 2)	Ubiquitination	-	30.54	21890473
505	Acetylation	KARGFFKKGDVVIVL HHCCCEECCCEEEEE	56.01	25038526
505	Ubiquitination	KARGFFKKGDVVIVL HHCCCEECCCEEEEE	56.01	-
513	Phosphorylation	GDVVIVLTGWRPGSG CCEEEEECCCCCCCC	24.65	29514088
519	Phosphorylation	LTGWRPGSGFTNTMR ECCCCCCCCCCCCEE	33.16	27422710
522	Phosphorylation	WRPGSGFTNTMRVVP CCCCCCCCCCEEEEE	33.05	28450419
524	Phosphorylation	PGSGFTNTMRVVPVP CCCCCCCCEEEEECC	11.87	28450419
525	Sulfoxidation	GSGFTNTMRVVPVP- CCCCCCCEEEEECC-	3.12	30846556
587	Phosphorylation	--------------------------------------------------------------- ---------------------------------------------------------------		27251275
593	Phosphorylation	--------------------------------------------------------------------- ---------------------------------------------------------------------		27251275
598	Phosphorylation	-------------------------------------------------------------------------- --------------------------------------------------------------------------		27251275

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
37	S	Phosphorylation	Kinase	AKT1	P31749	PSP
37	S	Phosphorylation	Kinase	CDK6	Q00534	PSP
37	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
37	S	Phosphorylation	Kinase	ERK1	P27361	PSP
45	T	Phosphorylation	Kinase	AURB	Q96GD4	PSP
97	S	Phosphorylation	Kinase	AKT1	P31749	PSP
105	Y	Phosphorylation	Kinase	NPM-ALK	AAA58698	PSP
129	T	Phosphorylation	Kinase	EEF2K	O00418	PSP
148	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
202	S	Phosphorylation	Kinase	AKT1	P31749	PSP
328	T	Phosphorylation	Kinase	ATM	Q13315	PSP
328	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
365	T	Phosphorylation	Kinase	MAPK8	P45983	GPS
454	T	Phosphorylation	Kinase	PIM2	Q9P1W9	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
305	K	Acetylation	Acetylation at Lys-305 is stimulated by high glucose concentration, it decreases enzyme activity and promotes its lysosomal-dependent degradation via chaperone-mediated autophagy.	21700219

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HERC1_HUMAN	HERC1	physical	12650930
PML_HUMAN	PML	physical	18298799
A4_HUMAN	APP	physical	21832049
PCBP1_HUMAN	PCBP1	physical	22939629
TKT_HUMAN	TKT	physical	22939629
PRDX2_HUMAN	PRDX2	physical	22939629
PRDX6_HUMAN	PRDX6	physical	22939629
EGLN1_HUMAN	EGLN1	physical	21620138
EGLN3_HUMAN	EGLN3	physical	21620138
TF65_HUMAN	RELA	physical	21988832
THIC_HUMAN	ACAT2	physical	22863883
AN32A_HUMAN	ANP32A	physical	22863883
CBS_HUMAN	CBS	physical	22863883
IF4A3_HUMAN	EIF4A3	physical	22863883
NPL4_HUMAN	NPLOC4	physical	22863883
PDLI5_HUMAN	PDLIM5	physical	22863883
PLIN3_HUMAN	PLIN3	physical	22863883
RD23B_HUMAN	RAD23B	physical	22863883
SRP14_HUMAN	SRP14	physical	22863883
TWF2_HUMAN	TWF2	physical	22863883
SAE2_HUMAN	UBA2	physical	22863883
DPOE2_HUMAN	POLE2	physical	25416956
NXT2_HUMAN	NXT2	physical	25416956
LNX1_HUMAN	LNX1	physical	25416956
SUMO1_HUMAN	SUMO1	physical	12565818
GDE_HUMAN	AGL	physical	26344197
AK1A1_HUMAN	AKR1A1	physical	26344197
SSDH_HUMAN	ALDH5A1	physical	26344197
ALDOA_HUMAN	ALDOA	physical	26344197
NAGA_HUMAN	AMDHD2	physical	26344197
ASSY_HUMAN	ASS1	physical	26344197
BAX_HUMAN	BAX	physical	26344197
DAZP1_HUMAN	DAZAP1	physical	26344197
DNJA3_HUMAN	DNAJA3	physical	26344197
EF1D_HUMAN	EEF1D	physical	26344197
FA49B_HUMAN	FAM49B	physical	26344197
FUMH_HUMAN	FH	physical	26344197
GBG12_HUMAN	GNG12	physical	26344197
HNRPD_HUMAN	HNRNPD	physical	26344197
HNRPK_HUMAN	HNRNPK	physical	26344197
HSPB1_HUMAN	HSPB1	physical	26344197
LYPA2_HUMAN	LYPLA2	physical	26344197
MAOX_HUMAN	ME1	physical	26344197
SIAS_HUMAN	NANS	physical	26344197
PCBP1_HUMAN	PCBP1	physical	26344197
PFKAM_HUMAN	PFKM	physical	26344197
PGK1_HUMAN	PGK1	physical	26344197
RAB10_HUMAN	RAB10	physical	26344197
RAC1_HUMAN	RAC1	physical	26344197
RPN1_HUMAN	RPN1	physical	26344197
4F2_HUMAN	SLC3A2	physical	26344197
TRAP1_HUMAN	TRAP1	physical	26344197
TBA4A_HUMAN	TUBA4A	physical	26344197
TBB5_HUMAN	TUBB	physical	26344197
UFM1_HUMAN	UFM1	physical	26344197
ARAF_HUMAN	ARAF	physical	25241761
TRI35_HUMAN	TRIM35	physical	25263439
FGFR1_HUMAN	FGFR1	physical	25263439
UBP7_HUMAN	USP7	physical	25695607
DDB2_HUMAN	DDB2	physical	26410533
EPM2A_HUMAN	EPM2A	physical	26493215
CTNB1_HUMAN	CTNNB1	physical	27485204
MLRV_HUMAN	MYL2	physical	25412762
MK01_HUMAN	MAPK1	physical	23178880
PIN1_HUMAN	PIN1	physical	23178880
MDM2_HUMAN	MDM2	physical	27264869

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
• DB00119: Pyruvic acid

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-62; LYS-89; LYS-166; LYS-266AND LYS-433, AND MASS SPECTROMETRY.
PubMed: 19608861

Hydroxylation

"Pyruvate kinase M2 is a PHD3-stimulated coactivator for hypoxia-inducible factor 1.";
Luo W., Hu H., Chang R., Zhong J., Knabel M., O'Meally R., Cole R.N.,Pandey A., Semenza G.L.;
Cell 145:732-744(2011).
Cited for: INTERACTION WITH EGLN3 AND HIF1A, SUBCELLULAR LOCATION, INDUCTION,FUNCTION, MASS SPECTROMETRY, HYDROXYLATION AT PRO-403 AND PRO-408, ANDMUTAGENESIS OF PRO-403 AND PRO-408.
PubMed: 21620138

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-148; TYR-175 ANDTHR-195, AND MASS SPECTROMETRY.
PubMed: 19690332

"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-37, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-37, AND MASSSPECTROMETRY.
PubMed: 18669648

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND MASSSPECTROMETRY.
PubMed: 18691976

"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND MASSSPECTROMETRY.
PubMed: 18088087

"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND MASSSPECTROMETRY.
PubMed: 18187866

"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 SER-37 AND THR-45, AND MASSSPECTROMETRY.
PubMed: 17287340

"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND MASSSPECTROMETRY.
PubMed: 16964243

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND MASSSPECTROMETRY.
PubMed: 17081983

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-328, AND MASSSPECTROMETRY.
PubMed: 17525332

"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, AND MASSSPECTROMETRY.
PubMed: 19534553

"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-83; TYR-105 AND TYR-390,AND MASS SPECTROMETRY.
PubMed: 15592455