dbPTM

DHE3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DHE3_HUMAN
UniProt AC	P00367
Protein Name	Glutamate dehydrogenase 1, mitochondrial
Gene Name	GLUD1
Organism	Homo sapiens (Human).
Sequence Length	558
Subcellular Localization	Mitochondrion matrix.
Protein Description	Mitochondrial glutamate dehydrogenase that converts L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity)..
Protein Sequence	MYRYLGEALLLSRAGPAALGSASADSAALLGWARGQPAAAPQPGLALAARRHYSEAVADREDDPNFFKMVEGFFDRGASIVEDKLVEDLRTRESEEQKRNRVRGILRIIKPCNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGIDVPAPDMSTGEREMSWIADTYASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFGDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILGFPKAKPYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLMSVQESLERKFGKHGGTIPIVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLDLRTAAYVNAIEKVFKVYNEAGVTFT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MYRYLGEAL ------CCCCHHHHH	14.15	30206219
4	Phosphorylation	----MYRYLGEALLL ----CCCCHHHHHHH	11.11	30206219
12	Phosphorylation	LGEALLLSRAGPAAL HHHHHHHHCCCCCHH	21.76	30206219
16	Ubiquitination	LLLSRAGPAALGSAS HHHHCCCCCHHCCCC	17.24	-
20	Ubiquitination	RAGPAALGSASADSA CCCCCHHCCCCHHHH	19.21	-
21	Phosphorylation	AGPAALGSASADSAA CCCCHHCCCCHHHHH	21.65	22210691
24	Ubiquitination	AALGSASADSAALLG CHHCCCCHHHHHHHH	17.94	21890473
29	Ubiquitination	ASADSAALLGWARGQ CCHHHHHHHHHHCCC	4.55	21890473
33	Ubiquitination	SAALLGWARGQPAAA HHHHHHHHCCCCCCC	12.15	21890473
44	Ubiquitination	PAAAPQPGLALAARR CCCCCCCCHHHHHHH	20.52	21890473
45	Ubiquitination	AAAPQPGLALAARRH CCCCCCCHHHHHHHH	4.49	21890473
58	Ubiquitination	RHYSEAVADREDDPN HHHHHHHCCCCCCCC	19.72	21890473
67	Ubiquitination	REDDPNFFKMVEGFF CCCCCCHHHHHHCHH	6.75	21890473
68	Acetylation	EDDPNFFKMVEGFFD CCCCCHHHHHHCHHH	37.59	30582663
68	Succinylation	EDDPNFFKMVEGFFD CCCCCHHHHHHCHHH	37.59	-
68	Succinylation	EDDPNFFKMVEGFFD CCCCCHHHHHHCHHH	37.59	-
69	Sulfoxidation	DDPNFFKMVEGFFDR CCCCHHHHHHCHHHC	2.54	21406390
76	Methylation	MVEGFFDRGASIVED HHHCHHHCCCHHHHH	37.10	-
78	Ubiquitination	EGFFDRGASIVEDKL HCHHHCCCHHHHHHH	9.29	21890473
79	Ubiquitination	GFFDRGASIVEDKLV CHHHCCCHHHHHHHH	29.95	21890473
79	Phosphorylation	GFFDRGASIVEDKLV CHHHCCCHHHHHHHH	29.95	25072903
84	2-Hydroxyisobutyrylation	GASIVEDKLVEDLRT CCHHHHHHHHHHHHC	40.71	-
84	Acetylation	GASIVEDKLVEDLRT CCHHHHHHHHHHHHC	40.71	19608861
84	Succinylation	GASIVEDKLVEDLRT CCHHHHHHHHHHHHC	40.71	-
84	Succinylation	GASIVEDKLVEDLRT CCHHHHHHHHHHHHC	40.71	21890473
84	Ubiquitination	GASIVEDKLVEDLRT CCHHHHHHHHHHHHC	40.71	21890473
98	Acetylation	TRESEEQKRNRVRGI CCCCHHHHHHHHHHH	55.72	6570497
110	Acetylation	RGILRIIKPCNHVLS HHHHHHHHCCCEEEE	40.94	-
110	Succinylation	RGILRIIKPCNHVLS HHHHHHHHCCCEEEE	40.94	-
110	Succinylation	RGILRIIKPCNHVLS HHHHHHHHCCCEEEE	40.94	-
112	S-nitrosylation	ILRIIKPCNHVLSLS HHHHHHCCCEEEEEE	4.70	24105792
128	Phosphorylation	PIRRDDGSWEVIEGY EEECCCCCEEEEEEE	27.36	23927012
135	Phosphorylation	SWEVIEGYRAQHSQH CEEEEEEEECCCCCC	7.03	23927012
147	2-Hydroxyisobutyrylation	SQHRTPCKGGIRYST CCCCCCCCCCCCCCC	62.47	-
152	Phosphorylation	PCKGGIRYSTDVSVD CCCCCCCCCCCCCHH	17.63	28152594
153	Phosphorylation	CKGGIRYSTDVSVDE CCCCCCCCCCCCHHH	14.32	28152594
154	Phosphorylation	KGGIRYSTDVSVDEV CCCCCCCCCCCHHHH	31.33	23927012
157	Phosphorylation	IRYSTDVSVDEVKAL CCCCCCCCHHHHHHH	27.02	23927012
159	Ubiquitination	YSTDVSVDEVKALAS CCCCCCHHHHHHHHH	47.68	-
162	Acetylation	DVSVDEVKALASLMT CCCHHHHHHHHHHHH	35.32	20167786
162	Succinylation	DVSVDEVKALASLMT CCCHHHHHHHHHHHH	35.32	-
162	Succinylation	DVSVDEVKALASLMT CCCHHHHHHHHHHHH	35.32	27452117
162	Ubiquitination	DVSVDEVKALASLMT CCCHHHHHHHHHHHH	35.32	21890473
170	Phosphorylation	ALASLMTYKCAVVDV HHHHHHHCEEEEEEC	7.07	-
171	Acetylation	LASLMTYKCAVVDVP HHHHHHCEEEEEECC	13.42	-
171	Methylation	LASLMTYKCAVVDVP HHHHHHCEEEEEECC	13.42	-
172	ADP-ribosylation	ASLMTYKCAVVDVPF HHHHHCEEEEEECCC	2.15	-
172	ADP-ribosylation	ASLMTYKCAVVDVPF HHHHHCEEEEEECCC	2.15	16023112
179	Acetylation	CAVVDVPFGGAKAGV EEEEECCCCCCCCCC	16.51	-
183	Acetylation	DVPFGGAKAGVKINP ECCCCCCCCCCCCCC	49.28	-
183	Succinylation	DVPFGGAKAGVKINP ECCCCCCCCCCCCCC	49.28	-
183	Succinylation	DVPFGGAKAGVKINP ECCCCCCCCCCCCCC	49.28	-
183	Sumoylation	DVPFGGAKAGVKINP ECCCCCCCCCCCCCC	49.28	-
183	Ubiquitination	DVPFGGAKAGVKINP ECCCCCCCCCCCCCC	49.28	-
185	Ubiquitination	PFGGAKAGVKINPKN CCCCCCCCCCCCCCC	22.12	21890473
187	Acetylation	GGAKAGVKINPKNYT CCCCCCCCCCCCCCC	35.53	25953088
187	Ubiquitination	GGAKAGVKINPKNYT CCCCCCCCCCCCCCC	35.53	-
191	Acetylation	AGVKINPKNYTDNEL CCCCCCCCCCCHHHH	59.09	25953088
191	Succinylation	AGVKINPKNYTDNEL CCCCCCCCCCCHHHH	59.09	-
191	Succinylation	AGVKINPKNYTDNEL CCCCCCCCCCCHHHH	59.09	27452117
191	Ubiquitination	AGVKINPKNYTDNEL CCCCCCCCCCCHHHH	59.09	-
193	Phosphorylation	VKINPKNYTDNELEK CCCCCCCCCHHHHHH	22.92	28152594
194	Phosphorylation	KINPKNYTDNELEKI CCCCCCCCHHHHHHH	41.56	-
198	Ubiquitination	KNYTDNELEKITRRF CCCCHHHHHHHHHHH	11.57	-
200	2-Hydroxyisobutyrylation	YTDNELEKITRRFTM CCHHHHHHHHHHHHH	63.10	-
200	Succinylation	YTDNELEKITRRFTM CCHHHHHHHHHHHHH	63.10	-
200	Succinylation	YTDNELEKITRRFTM CCHHHHHHHHHHHHH	63.10	21890473
200	Ubiquitination	YTDNELEKITRRFTM CCHHHHHHHHHHHHH	63.10	-
206	Phosphorylation	EKITRRFTMELAKKG HHHHHHHHHHHHHCC	14.13	-
211	2-Hydroxyisobutyrylation	RFTMELAKKGFIGPG HHHHHHHHCCCCCCC	67.08	-
211	Acetylation	RFTMELAKKGFIGPG HHHHHHHHCCCCCCC	67.08	7623875
211	Ubiquitination	RFTMELAKKGFIGPG HHHHHHHHCCCCCCC	67.08	21890473
212	Ubiquitination	FTMELAKKGFIGPGI HHHHHHHCCCCCCCC	54.14	21890473
219	Ubiquitination	KGFIGPGIDVPAPDM CCCCCCCCCCCCCCC	5.63	21890473
226	Sulfoxidation	IDVPAPDMSTGEREM CCCCCCCCCCCHHHH	3.63	21406390
227	Phosphorylation	DVPAPDMSTGEREMS CCCCCCCCCCHHHHH	40.41	28857561
228	Phosphorylation	VPAPDMSTGEREMSW CCCCCCCCCHHHHHH	36.10	28857561
232	Ubiquitination	DMSTGEREMSWIADT CCCCCHHHHHHHHHH	33.01	21890473
248	Acetylation	ASTIGHYDINAHACV HHHCCCCEECCCEEE	23.22	-
248	Ubiquitination	ASTIGHYDINAHACV HHHCCCCEECCCEEE	23.22	21890473
290	Acetylation	FINEASYMSILGMTP HHCHHHHHHHHCCCC	1.54	-
290	Ubiquitination	FINEASYMSILGMTP HHCHHHHHHHHCCCC	1.54	-
302	Methylation	MTPGFGDKTFVVQGF CCCCCCCCEEEEECC	44.21	-
313	Acetylation	VQGFGNVGLHSMRYL EECCCCCCHHHHHHH	22.98	-
313	Ubiquitination	VQGFGNVGLHSMRYL EECCCCCCHHHHHHH	22.98	-
316	Phosphorylation	FGNVGLHSMRYLHRF CCCCCHHHHHHHHHC	15.25	27251275
326	Acetylation	YLHRFGAKCIAVGES HHHHCCCEEEEECCC	26.93	-
326	Ubiquitination	YLHRFGAKCIAVGES HHHHCCCEEEEECCC	26.93	-
333	Phosphorylation	KCIAVGESDGSIWNP EEEEECCCCCCCCCC	41.15	25072903
336	Acetylation	AVGESDGSIWNPDGI EECCCCCCCCCCCCC	29.44	-
336	Ubiquitination	AVGESDGSIWNPDGI EECCCCCCCCCCCCC	29.44	21890473
336	Phosphorylation	AVGESDGSIWNPDGI EECCCCCCCCCCCCC	29.44	25072903
346	Acetylation	NPDGIDPKELEDFKL CCCCCCHHHHHHHCC	71.79	23236377
346	Succinylation	NPDGIDPKELEDFKL CCCCCCHHHHHHHCC	71.79	-
346	Succinylation	NPDGIDPKELEDFKL CCCCCCHHHHHHHCC	71.79	-
352	2-Hydroxyisobutyrylation	PKELEDFKLQHGSIL HHHHHHHCCCCCCCC	60.61	-
352	Acetylation	PKELEDFKLQHGSIL HHHHHHHCCCCCCCC	60.61	26822725
352	Succinylation	PKELEDFKLQHGSIL HHHHHHHCCCCCCCC	60.61	-
352	Succinylation	PKELEDFKLQHGSIL HHHHHHHCCCCCCCC	60.61	21890473
352	Ubiquitination	PKELEDFKLQHGSIL HHHHHHHCCCCCCCC	60.61	-
357	Phosphorylation	DFKLQHGSILGFPKA HHCCCCCCCCCCCCC	16.71	23312004
360	Acetylation	LQHGSILGFPKAKPY CCCCCCCCCCCCCCC	34.83	-
360	Ubiquitination	LQHGSILGFPKAKPY CCCCCCCCCCCCCCC	34.83	-
363	Acetylation	GSILGFPKAKPYEGS CCCCCCCCCCCCCCC	67.77	-
363	Succinylation	GSILGFPKAKPYEGS CCCCCCCCCCCCCCC	67.77	-
363	Succinylation	GSILGFPKAKPYEGS CCCCCCCCCCCCCCC	67.77	-
363	Ubiquitination	GSILGFPKAKPYEGS CCCCCCCCCCCCCCC	67.77	-
365	Acetylation	ILGFPKAKPYEGSIL CCCCCCCCCCCCCCE	55.01	-
365	Succinylation	ILGFPKAKPYEGSIL CCCCCCCCCCCCCCE	55.01	-
365	Succinylation	ILGFPKAKPYEGSIL CCCCCCCCCCCCCCE	55.01	21890473
365	Ubiquitination	ILGFPKAKPYEGSIL CCCCCCCCCCCCCCE	55.01	21890473
367	Phosphorylation	GFPKAKPYEGSILEA CCCCCCCCCCCCEEE	32.01	25850435
370	Phosphorylation	KAKPYEGSILEADCD CCCCCCCCCEEECCC	16.44	25850435
376	Glutathionylation	GSILEADCDILIPAA CCCEEECCCEEEECC	4.52	22555962
378	Ubiquitination	ILEADCDILIPAASE CEEECCCEEEECCCH	4.77	21890473
384	Phosphorylation	DILIPAASEKQLTKS CEEEECCCHHHCCCC	47.64	25850435
386	Acetylation	LIPAASEKQLTKSNA EEECCCHHHCCCCCC	48.38	-
386	Ubiquitination	LIPAASEKQLTKSNA EEECCCHHHCCCCCC	48.38	-
390	Acetylation	ASEKQLTKSNAPRVK CCHHHCCCCCCCHHE	50.75	25953088
390	Succinylation	ASEKQLTKSNAPRVK CCHHHCCCCCCCHHE	50.75	-
390	Succinylation	ASEKQLTKSNAPRVK CCHHHCCCCCCCHHE	50.75	27452117
390	Ubiquitination	ASEKQLTKSNAPRVK CCHHHCCCCCCCHHE	50.75	-
391	Phosphorylation	SEKQLTKSNAPRVKA CHHHCCCCCCCHHEE	32.75	29116813
399	Acetylation	NAPRVKAKIIAEGAN CCCHHEEEEEECCCC	29.00	-
399	Ubiquitination	NAPRVKAKIIAEGAN CCCHHEEEEEECCCC	29.00	21890473
409	Phosphorylation	AEGANGPTTPEADKI ECCCCCCCCHHHHHH	57.28	30266825
410	Phosphorylation	EGANGPTTPEADKIF CCCCCCCCHHHHHHH	23.43	30266825
415	Ubiquitination	PTTPEADKIFLERNI CCCHHHHHHHHHCCE	42.26	21890473
415	2-Hydroxyisobutyrylation	PTTPEADKIFLERNI CCCHHHHHHHHHCCE	42.26	-
415	Acetylation	PTTPEADKIFLERNI CCCHHHHHHHHHCCE	42.26	23236377
415	Succinylation	PTTPEADKIFLERNI CCCHHHHHHHHHCCE	42.26	-
415	Succinylation	PTTPEADKIFLERNI CCCHHHHHHHHHCCE	42.26	21890473
415	Ubiquitination	PTTPEADKIFLERNI CCCHHHHHHHHHCCE	42.26	21890473
438	Phosphorylation	NAGGVTVSYFEWLKN CCCCEEEEHHHHHHC	18.10	-
439	Phosphorylation	AGGVTVSYFEWLKNL CCCEEEEHHHHHHCC	10.94	-
450	Phosphorylation	LKNLNHVSYGRLTFK HHCCCCCEEEEEEEE	17.83	23401153
451	Phosphorylation	KNLNHVSYGRLTFKY HCCCCCEEEEEEEEE	12.74	28450419
457	N6-malonyllysine	SYGRLTFKYERDSNY EEEEEEEEEECCCCC	40.75	-
457	2-Hydroxyisobutyrylation	SYGRLTFKYERDSNY EEEEEEEEEECCCCC	40.75	-
457	Acetylation	SYGRLTFKYERDSNY EEEEEEEEEECCCCC	40.75	25825284
457	Malonylation	SYGRLTFKYERDSNY EEEEEEEEEECCCCC	40.75	26320211
457	Succinylation	SYGRLTFKYERDSNY EEEEEEEEEECCCCC	40.75	27452117
457	Ubiquitination	SYGRLTFKYERDSNY EEEEEEEEEECCCCC	40.75	-
458	Phosphorylation	YGRLTFKYERDSNYH EEEEEEEEECCCCCE	16.41	28152594
462	Phosphorylation	TFKYERDSNYHLLMS EEEEECCCCCEEEEE	45.57	28857561
464	Phosphorylation	KYERDSNYHLLMSVQ EEECCCCCEEEEEHH	9.59	28857561
477	Acetylation	VQESLERKFGKHGGT HHHHHHHHHHCCCCC	49.44	25953088
477	Succinylation	VQESLERKFGKHGGT HHHHHHHHHHCCCCC	49.44	-
477	Succinylation	VQESLERKFGKHGGT HHHHHHHHHHCCCCC	49.44	-
480	Acetylation	SLERKFGKHGGTIPI HHHHHHHCCCCCCCC	42.06	19608861
480	Malonylation	SLERKFGKHGGTIPI HHHHHHHCCCCCCCC	42.06	26320211
480	Succinylation	SLERKFGKHGGTIPI HHHHHHHCCCCCCCC	42.06	-
480	Succinylation	SLERKFGKHGGTIPI HHHHHHHCCCCCCCC	42.06	-
480	Ubiquitination	SLERKFGKHGGTIPI HHHHHHHCCCCCCCC	42.06	19608861
496	Methylation	PTAEFQDRISGASEK CCHHHHHHCCCCCHH	17.75	-
498	Phosphorylation	AEFQDRISGASEKDI HHHHHHCCCCCHHHH	29.24	27251275
501	Phosphorylation	QDRISGASEKDIVHS HHHCCCCCHHHHCHH	49.02	28857561
503	N6-malonyllysine	RISGASEKDIVHSGL HCCCCCHHHHCHHHH	50.70	-
503	2-Hydroxyisobutyrylation	RISGASEKDIVHSGL HCCCCCHHHHCHHHH	50.70	-
503	Acetylation	RISGASEKDIVHSGL HCCCCCHHHHCHHHH	50.70	19608861
503	Malonylation	RISGASEKDIVHSGL HCCCCCHHHHCHHHH	50.70	26320211
503	Succinylation	RISGASEKDIVHSGL HCCCCCHHHHCHHHH	50.70	-
503	Ubiquitination	RISGASEKDIVHSGL HCCCCCHHHHCHHHH	50.70	19608861
508	Phosphorylation	SEKDIVHSGLAYTME CHHHHCHHHHHHHHH	25.30	20068231
512	Phosphorylation	IVHSGLAYTMERSAR HCHHHHHHHHHHHHH	16.21	27259358
513	Phosphorylation	VHSGLAYTMERSARQ CHHHHHHHHHHHHHH	13.62	26356563
527	N6-malonyllysine	QIMRTAMKYNLGLDL HHHHHHHHHCCCCCH	28.64	-
527	Acetylation	QIMRTAMKYNLGLDL HHHHHHHHHCCCCCH	28.64	23954790
527	Malonylation	QIMRTAMKYNLGLDL HHHHHHHHHCCCCCH	28.64	26320211
527	Succinylation	QIMRTAMKYNLGLDL HHHHHHHHHCCCCCH	28.64	-
527	Ubiquitination	QIMRTAMKYNLGLDL HHHHHHHHHCCCCCH	28.64	21890473
528	Phosphorylation	IMRTAMKYNLGLDLR HHHHHHHHCCCCCHH	11.52	-
539	Phosphorylation	LDLRTAAYVNAIEKV CCHHHHHHHHHHHHH	7.56	28152594
545	2-Hydroxyisobutyrylation	AYVNAIEKVFKVYNE HHHHHHHHHHHHHHH	47.02	-
545	Acetylation	AYVNAIEKVFKVYNE HHHHHHHHHHHHHHH	47.02	19608861
545	Succinylation	AYVNAIEKVFKVYNE HHHHHHHHHHHHHHH	47.02	-
545	Succinylation	AYVNAIEKVFKVYNE HHHHHHHHHHHHHHH	47.02	21890473
545	Ubiquitination	AYVNAIEKVFKVYNE HHHHHHHHHHHHHHH	47.02	21890473
548	Acetylation	NAIEKVFKVYNEAGV HHHHHHHHHHHHCCC	46.96	25038526
550	Phosphorylation	IEKVFKVYNEAGVTF HHHHHHHHHHCCCCC	14.10	-

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 DHE3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DHE3_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 DHE3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A1AG1_HUMAN	ORM1	physical	21988832
NR4A1_HUMAN	NR4A1	physical	21988832
HEMO_HUMAN	HPX	physical	21988832
STA5A_HUMAN	STAT5A	physical	21988832
SEC62_HUMAN	SEC62	physical	21988832
VTNC_HUMAN	VTN	physical	21988832

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
606762	Familial hyperinsulinemic hypoglycemia 6 (HHF6)
256450], also referred to as congenital hyperinsulinism, nesidioblastosis, or persistent hyperinsulinemic hypoglycemia of infancy (PPHI), is the most common cause of persistent hypoglycemia in infancy and is due to defective negative feedback regulation of insulin secretion by low glucose levels. In HHF6 elevated oxidation rate of glutamate to alpha-ketoglutarate stimulates insulin secretion in the pancreatic beta cells, while they impair detoxification of ammonium in the liver. {ECO
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00756	Hexachlorophene

Regulatory Network of DHE3_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-84; LYS-480 AND LYS-503, ANDMASS 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-128, 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 THR-410, AND MASSSPECTROMETRY.	19413330 [Abstract]