dbPTM

AATM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AATM_HUMAN
UniProt AC	P00505
Protein Name	Aspartate aminotransferase, mitochondrial
Gene Name	GOT2
Organism	Homo sapiens (Human).
Sequence Length	430
Subcellular Localization	Mitochondrion matrix . Cell membrane . Exposure to alcohol promotes translocation to the cell membrane.
Protein Description	Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids..
Protein Sequence	MALLHSGRVLPGIAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENSEVLKSGRFVTVQTISGTGALRIGASFLQRFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFTGAVEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTMVCKDADEAKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKVMADRIIGMRTQLVSNLKKEGSTHNWQHITDQIGMFCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGYLAHAIHQVTK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
48	Phosphorylation	PDPILGVTEAFKRDT CCCCCCHHHHHHCCC	21.57	24275569
52	Acetylation	LGVTEAFKRDTNSKK CCHHHHHHCCCCCCC	57.31	30582669
59	2-Hydroxyisobutyrylation	KRDTNSKKMNLGVGA HCCCCCCCCEEEEEE	32.61	-
59	Acetylation	KRDTNSKKMNLGVGA HCCCCCCCCEEEEEE	32.61	-
59	Malonylation	KRDTNSKKMNLGVGA HCCCCCCCCEEEEEE	32.61	26320211
59	Succinylation	KRDTNSKKMNLGVGA HCCCCCCCCEEEEEE	32.61	27452117
59	Ubiquitination	KRDTNSKKMNLGVGA HCCCCCCCCEEEEEE	32.61	24816145
67	Phosphorylation	MNLGVGAYRDDNGKP CEEEEEEEECCCCCC	14.51	-
73	Acetylation	AYRDDNGKPYVLPSV EEECCCCCCCCCCCH	39.16	-
73	Acetylation	AYRDDNGKPYVLPSV EEECCCCCCCCCCCH	39.16	19608861
73	Malonylation	AYRDDNGKPYVLPSV EEECCCCCCCCCCCH	39.16	26320211
73	Succinylation	AYRDDNGKPYVLPSV EEECCCCCCCCCCCH	39.16	-
73	Succinylation	AYRDDNGKPYVLPSV EEECCCCCCCCCCCH	39.16	27452117
73	Ubiquitination	AYRDDNGKPYVLPSV EEECCCCCCCCCCCH	39.16	24816145
75	Phosphorylation	RDDNGKPYVLPSVRK ECCCCCCCCCCCHHH	20.36	28152594
79	Phosphorylation	GKPYVLPSVRKAEAQ CCCCCCCCHHHHHHH	30.32	28152594
82	2-Hydroxyisobutyrylation	YVLPSVRKAEAQIAA CCCCCHHHHHHHHHH	48.71	-
82	Acetylation	YVLPSVRKAEAQIAA CCCCCHHHHHHHHHH	48.71	-
82	Malonylation	YVLPSVRKAEAQIAA CCCCCHHHHHHHHHH	48.71	26320211
82	Succinylation	YVLPSVRKAEAQIAA CCCCCHHHHHHHHHH	48.71	27452117
82	Ubiquitination	YVLPSVRKAEAQIAA CCCCCHHHHHHHHHH	48.71	29967540
90	2-Hydroxyisobutyrylation	AEAQIAAKNLDKEYL HHHHHHHHCCCCCCC	49.36	-
90	Acetylation	AEAQIAAKNLDKEYL HHHHHHHHCCCCCCC	49.36	19608861
90	Malonylation	AEAQIAAKNLDKEYL HHHHHHHHCCCCCCC	49.36	26320211
90	Succinylation	AEAQIAAKNLDKEYL HHHHHHHHCCCCCCC	49.36	-
90	Succinylation	AEAQIAAKNLDKEYL HHHHHHHHCCCCCCC	49.36	-
90	Ubiquitination	AEAQIAAKNLDKEYL HHHHHHHHCCCCCCC	49.36	27667366
94	2-Hydroxyisobutyrylation	IAAKNLDKEYLPIGG HHHHCCCCCCCCCCH	51.96	-
94	Acetylation	IAAKNLDKEYLPIGG HHHHCCCCCCCCCCH	51.96	25825284
94	Ubiquitination	IAAKNLDKEYLPIGG HHHHCCCCCCCCCCH	51.96	22817900
96	Nitrated tyrosine	AKNLDKEYLPIGGLA HHCCCCCCCCCCHHH	24.42	-
96	Nitration	AKNLDKEYLPIGGLA HHCCCCCCCCCCHHH	24.42	-
96	Phosphorylation	AKNLDKEYLPIGGLA HHCCCCCCCCCCHHH	24.42	27155012
106	Glutathionylation	IGGLAEFCKASAELA CCHHHHHHHHHHHHH	2.44	22555962
107	Acetylation	GGLAEFCKASAELAL CHHHHHHHHHHHHHH	51.18	25038526
107	Succinylation	GGLAEFCKASAELAL CHHHHHHHHHHHHHH	51.18	-
107	Succinylation	GGLAEFCKASAELAL CHHHHHHHHHHHHHH	51.18	-
107	Ubiquitination	GGLAEFCKASAELAL CHHHHHHHHHHHHHH	51.18	21963094
109	Phosphorylation	LAEFCKASAELALGE HHHHHHHHHHHHHCC	14.05	25072903
116	Acetylation	SAELALGENSEVLKS HHHHHHCCCCHHHHC	59.44	-
116	Acetylation	SAELALGENSEVLKS HHHHHHCCCCHHHHC	59.44	19608861
118	Phosphorylation	ELALGENSEVLKSGR HHHHCCCCHHHHCCC	25.44	23911959
122	2-Hydroxyisobutyrylation	GENSEVLKSGRFVTV CCCCHHHHCCCEEEE	56.91	-
122	Acetylation	GENSEVLKSGRFVTV CCCCHHHHCCCEEEE	56.91	23954790
122	Malonylation	GENSEVLKSGRFVTV CCCCHHHHCCCEEEE	56.91	26320211
122	Succinylation	GENSEVLKSGRFVTV CCCCHHHHCCCEEEE	56.91	-
122	Succinylation	GENSEVLKSGRFVTV CCCCHHHHCCCEEEE	56.91	-
122	Ubiquitination	GENSEVLKSGRFVTV CCCCHHHHCCCEEEE	56.91	22817900
128	Phosphorylation	LKSGRFVTVQTISGT HHCCCEEEEEEECCC	12.27	18491316
131	Phosphorylation	GRFVTVQTISGTGAL CCEEEEEEECCCCHH	16.87	25867546
133	Phosphorylation	FVTVQTISGTGALRI EEEEEEECCCCHHHH	33.42	28857561
135	Phosphorylation	TVQTISGTGALRIGA EEEEECCCCHHHHCH	16.70	18491316
142	Acetylation	TGALRIGASFLQRFF CCHHHHCHHHHHHHH	8.50	-
142	Ubiquitination	TGALRIGASFLQRFF CCHHHHCHHHHHHHH	8.50	29967540
143	Phosphorylation	GALRIGASFLQRFFK CHHHHCHHHHHHHHH	22.67	30266825
150	Acetylation	SFLQRFFKFSRDVFL HHHHHHHHHCCCCCC	39.45	25825284
150	Methylation	SFLQRFFKFSRDVFL HHHHHHHHHCCCCCC	39.45	19608861
159	Acetylation	SRDVFLPKPTWGNHT CCCCCCCCCCCCCCC	58.17	19608861
159	Malonylation	SRDVFLPKPTWGNHT CCCCCCCCCCCCCCC	58.17	26320211
159	Succinylation	SRDVFLPKPTWGNHT CCCCCCCCCCCCCCC	58.17	-
159	Succinylation	SRDVFLPKPTWGNHT CCCCCCCCCCCCCCC	58.17	27452117
161	Phosphorylation	DVFLPKPTWGNHTPI CCCCCCCCCCCCCCC	52.72	28857561
166	Phosphorylation	KPTWGNHTPIFRDAG CCCCCCCCCCCCCCC	23.29	28655764
184	Acetylation	QGYRYYDPKTCGFDF CCEEECCCCCCCCCC	20.10	-
185	2-Hydroxyisobutyrylation	GYRYYDPKTCGFDFT CEEECCCCCCCCCCC	54.25	-
185	Acetylation	GYRYYDPKTCGFDFT CEEECCCCCCCCCCC	54.25	23236377
185	Succinylation	GYRYYDPKTCGFDFT CEEECCCCCCCCCCC	54.25	-
185	Succinylation	GYRYYDPKTCGFDFT CEEECCCCCCCCCCC	54.25	27452117
185	Ubiquitination	GYRYYDPKTCGFDFT CEEECCCCCCCCCCC	54.25	29967540
187	S-nitrosocysteine	RYYDPKTCGFDFTGA EECCCCCCCCCCCCC	6.80	-
187	S-nitrosylation	RYYDPKTCGFDFTGA EECCCCCCCCCCCCC	6.80	19483679
191	Acetylation	PKTCGFDFTGAVEDI CCCCCCCCCCCHHHH	6.74	-
191	Acetylation	PKTCGFDFTGAVEDI CCCCCCCCCCCHHHH	6.74	19608861
191	Ubiquitination	PKTCGFDFTGAVEDI CCCCCCCCCCCHHHH	6.74	27667366
199	Phosphorylation	TGAVEDISKIPEQSV CCCHHHHHHCCHHHH	36.53	21712546
227	Acetylation	DPRPEQWKEIATVVK CCCHHHHHHHHHHHH	38.65	23954790
227	Malonylation	DPRPEQWKEIATVVK CCCHHHHHHHHHHHH	38.65	26320211
227	Succinylation	DPRPEQWKEIATVVK CCCHHHHHHHHHHHH	38.65	-
227	Succinylation	DPRPEQWKEIATVVK CCCHHHHHHHHHHHH	38.65	27452117
231	Phosphorylation	EQWKEIATVVKKRNL HHHHHHHHHHHHCCH	31.34	23312004
234	2-Hydroxyisobutyrylation	KEIATVVKKRNLFAF HHHHHHHHHCCHHHH	41.50	-
234	Acetylation	KEIATVVKKRNLFAF HHHHHHHHHCCHHHH	41.50	19608861
234	Succinylation	KEIATVVKKRNLFAF HHHHHHHHHCCHHHH	41.50	27452117
234	Ubiquitination	KEIATVVKKRNLFAF HHHHHHHHHCCHHHH	41.50	19608861
235	Acetylation	EIATVVKKRNLFAFF HHHHHHHHCCHHHHH	34.60	2402897
253	Acetylation	YQGFASGDGDKDAWA HCCCCCCCCCHHHHH	60.67	-
253	Ubiquitination	YQGFASGDGDKDAWA HCCCCCCCCCHHHHH	60.67	-
253	Acetylation	YQGFASGDGDKDAWA HCCCCCCCCCHHHHH	60.67	19608861
256	Acetylation	FASGDGDKDAWAVRH CCCCCCCHHHHHHHH	55.67	30582681
259	Ubiquitination	GDGDKDAWAVRHFIE CCCCHHHHHHHHHHH	12.86	24816145
276	Phosphorylation	INVCLCQSYAKNMGL CCEEEEHHHHHHCCC	26.51	28152594
277	Phosphorylation	NVCLCQSYAKNMGLY CEEEEHHHHHHCCCC	8.84	28152594
279	N6-(pyridoxal phosphate)lysine	CLCQSYAKNMGLYGE EEEHHHHHHCCCCCC	38.95	-
279	Acetylation	CLCQSYAKNMGLYGE EEEHHHHHHCCCCCC	38.95	-
279	Other	CLCQSYAKNMGLYGE EEEHHHHHHCCCCCC	38.95	-
284	Phosphorylation	YAKNMGLYGERVGAF HHHHCCCCCCEECEE	15.94	27155012
295	Ubiquitination	VGAFTMVCKDADEAK ECEEEEEECCHHHHH	1.99	-
296	2-Hydroxyisobutyrylation	GAFTMVCKDADEAKR CEEEEEECCHHHHHH	44.53	-
296	Acetylation	GAFTMVCKDADEAKR CEEEEEECCHHHHHH	44.53	19608861
296	Malonylation	GAFTMVCKDADEAKR CEEEEEECCHHHHHH	44.53	26320211
296	Succinylation	GAFTMVCKDADEAKR CEEEEEECCHHHHHH	44.53	-
296	Succinylation	GAFTMVCKDADEAKR CEEEEEECCHHHHHH	44.53	27452117
296	Ubiquitination	GAFTMVCKDADEAKR CEEEEEECCHHHHHH	44.53	19608861
302	Acetylation	CKDADEAKRVESQLK ECCHHHHHHHHHHHH	55.73	25038526
302	Malonylation	CKDADEAKRVESQLK ECCHHHHHHHHHHHH	55.73	26320211
302	Ubiquitination	CKDADEAKRVESQLK ECCHHHHHHHHHHHH	55.73	24816145
306	Phosphorylation	DEAKRVESQLKILIR HHHHHHHHHHHHHHC	37.65	26437602
309	2-Hydroxyisobutyrylation	KRVESQLKILIRPMY HHHHHHHHHHHCCCC	28.03	-
309	Acetylation	KRVESQLKILIRPMY HHHHHHHHHHHCCCC	28.03	20167786
309	Malonylation	KRVESQLKILIRPMY HHHHHHHHHHHCCCC	28.03	26320211
309	Succinylation	KRVESQLKILIRPMY HHHHHHHHHHHCCCC	28.03	-
309	Succinylation	KRVESQLKILIRPMY HHHHHHHHHHHCCCC	28.03	27452117
313	Asymmetric dimethylarginine	SQLKILIRPMYSNPP HHHHHHHCCCCCCCC	13.39	-
313	Methylation	SQLKILIRPMYSNPP HHHHHHHCCCCCCCC	13.39	-
315	Sulfoxidation	LKILIRPMYSNPPLN HHHHHCCCCCCCCCC	4.04	28183972
316	Phosphorylation	KILIRPMYSNPPLNG HHHHCCCCCCCCCCH	14.15	22673903
317	Phosphorylation	ILIRPMYSNPPLNGA HHHCCCCCCCCCCHH	36.29	22673903
320	Acetylation	RPMYSNPPLNGARIA CCCCCCCCCCHHHHH	42.58	-
320	Ubiquitination	RPMYSNPPLNGARIA CCCCCCCCCCHHHHH	42.58	-
320	Ubiquitination	RPMYSNPPLNGARIA CCCCCCCCCCHHHHH	42.58	29967540
333	Phosphorylation	IAAAILNTPDLRKQW HHHHHHCCHHHHHHH	18.09	30266825
338	2-Hydroxyisobutyrylation	LNTPDLRKQWLQEVK HCCHHHHHHHHHHHH	53.79	-
338	Acetylation	LNTPDLRKQWLQEVK HCCHHHHHHHHHHHH	53.79	25825284
338	Malonylation	LNTPDLRKQWLQEVK HCCHHHHHHHHHHHH	53.79	26320211
338	Succinylation	LNTPDLRKQWLQEVK HCCHHHHHHHHHHHH	53.79	-
338	Succinylation	LNTPDLRKQWLQEVK HCCHHHHHHHHHHHH	53.79	27452117
338	Ubiquitination	LNTPDLRKQWLQEVK HCCHHHHHHHHHHHH	53.79	-
345	Acetylation	KQWLQEVKVMADRII HHHHHHHHHHHHHHH	26.07	25038526
353	Ubiquitination	VMADRIIGMRTQLVS HHHHHHHHHHHHHHH	9.35	21890473
353	Acetylation	VMADRIIGMRTQLVS HHHHHHHHHHHHHHH	9.35	-
353	Ubiquitination	VMADRIIGMRTQLVS HHHHHHHHHHHHHHH	9.35	-
353	Acetylation	VMADRIIGMRTQLVS HHHHHHHHHHHHHHH	9.35	19608861
353	Ubiquitination	VMADRIIGMRTQLVS HHHHHHHHHHHHHHH	9.35	21890473
356	Phosphorylation	DRIIGMRTQLVSNLK HHHHHHHHHHHHHHH	19.84	26437602
360	Phosphorylation	GMRTQLVSNLKKEGS HHHHHHHHHHHHCCC	45.07	23312004
361	Acetylation	MRTQLVSNLKKEGST HHHHHHHHHHHCCCC	48.69	-
361	Acetylation	MRTQLVSNLKKEGST HHHHHHHHHHHCCCC	48.69	19608861
361	Ubiquitination	MRTQLVSNLKKEGST HHHHHHHHHHHCCCC	48.69	23000965
363	2-Hydroxyisobutyrylation	TQLVSNLKKEGSTHN HHHHHHHHHCCCCCC	53.69	-
363	Acetylation	TQLVSNLKKEGSTHN HHHHHHHHHCCCCCC	53.69	23236377
363	Succinylation	TQLVSNLKKEGSTHN HHHHHHHHHCCCCCC	53.69	-
363	Succinylation	TQLVSNLKKEGSTHN HHHHHHHHHCCCCCC	53.69	27452117
363	Ubiquitination	TQLVSNLKKEGSTHN HHHHHHHHHCCCCCC	53.69	29967540
364	Acetylation	QLVSNLKKEGSTHNW HHHHHHHHCCCCCCH	71.16	25038526
387	Acetylation	MFCFTGLKPEQVERL CHHCCCCCHHHHHHH	48.10	25038526
396	2-Hydroxyisobutyrylation	EQVERLIKEFSIYMT HHHHHHHHHCEEEEE	58.25	-
396	Acetylation	EQVERLIKEFSIYMT HHHHHHHHHCEEEEE	58.25	19608861
396	Succinylation	EQVERLIKEFSIYMT HHHHHHHHHCEEEEE	58.25	-
396	Succinylation	EQVERLIKEFSIYMT HHHHHHHHHCEEEEE	58.25	19608861
396	Ubiquitination	EQVERLIKEFSIYMT HHHHHHHHHCEEEEE	58.25	22817900
399	Phosphorylation	ERLIKEFSIYMTKDG HHHHHHCEEEEECCC	17.57	27251275
401	Phosphorylation	LIKEFSIYMTKDGRI HHHHCEEEEECCCCE	9.49	22817900
404	2-Hydroxyisobutyrylation	EFSIYMTKDGRISVA HCEEEEECCCCEEEE	41.47	-
404	Acetylation	EFSIYMTKDGRISVA HCEEEEECCCCEEEE	41.47	19608861
404	Malonylation	EFSIYMTKDGRISVA HCEEEEECCCCEEEE	41.47	26320211
404	Succinylation	EFSIYMTKDGRISVA HCEEEEECCCCEEEE	41.47	-
404	Succinylation	EFSIYMTKDGRISVA HCEEEEECCCCEEEE	41.47	27452117
404	Ubiquitination	EFSIYMTKDGRISVA HCEEEEECCCCEEEE	41.47	23000965
409	Phosphorylation	MTKDGRISVAGVTSS EECCCCEEEEEECHH	12.45	25072903
414	Phosphorylation	RISVAGVTSSNVGYL CEEEEEECHHHHHHH	26.06	20068231
415	Phosphorylation	ISVAGVTSSNVGYLA EEEEEECHHHHHHHH	19.94	28152594
416	Phosphorylation	SVAGVTSSNVGYLAH EEEEECHHHHHHHHH	26.60	28152594
420	Phosphorylation	VTSSNVGYLAHAIHQ ECHHHHHHHHHHHHH	9.09	28152594
429	Phosphorylation	AHAIHQVTK------ HHHHHHHCC------	25.19	28152594
430	Acetylation	HAIHQVTK------- HHHHHHCC-------	60.53	155819

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 AATM_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
THOC7_HUMAN	THOC7	physical	16169070
HSP7C_HUMAN	HSPA8	physical	7559589
KAT3_HUMAN	CCBL2	physical	26344197
FAAA_HUMAN	FAH	physical	26344197
G6PI_HUMAN	GPI	physical	26344197
GLYG_HUMAN	GYG1	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
DB00128	L-Aspartic Acid

Regulatory Network of AATM_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-73; LYS-90; LYS-150;LYS-159; LYS-234; LYS-296; LYS-396 AND LYS-404, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-96, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Phosphoproteome analysis of HeLa cells using stable isotope labelingwith amino acids in cell culture (SILAC)."; Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A.; J. Proteome Res. 4:1661-1671(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-401, AND MASSSPECTROMETRY.	16212419 [Abstract]