dbPTM

ADT3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ADT3_HUMAN
UniProt AC	P12236
Protein Name	ADP/ATP translocase 3
Gene Name	SLC25A6
Organism	Homo sapiens (Human).
Sequence Length	298
Subcellular Localization	Mitochondrion inner membrane Multi-pass membrane protein. The complex formed with ARL2BP, ARL2 and SLC25A6 is expressed in mitochondria..
Protein Description	Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis..
Protein Sequence	MTEQAISFAKDFLAGGIAAAISKTAVAPIERVKLLLQVQHASKQIAADKQYKGIVDCIVRIPKEQGVLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDKHTQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKSGTEREFRGLGDCLVKITKSDGIRGLYQGFSVSVQGIIIYRAAYFGVYDTAKGMLPDPKNTHIVVSWMIAQTVTAVAGVVSYPFDTVRRRMMMQSGRKGADIMYTGTVDCWRKIFRDEGGKAFFKGAWSNVLRGMGGAFVLVLYDELKKVI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MTEQAISF -------CCHHHHHH	9.32	22223895
1	Sulfoxidation	-------MTEQAISF -------CCHHHHHH	9.32	28465586
2	Acetylation	------MTEQAISFA ------CCHHHHHHH	36.48	19413330
2	Phosphorylation	------MTEQAISFA ------CCHHHHHHH	36.48	27486199
7	Phosphorylation	-MTEQAISFAKDFLA -CCHHHHHHHHHHHH	23.36	28348404
10	Methylation	EQAISFAKDFLAGGI HHHHHHHHHHHHHHH	47.18	19820867
10	Ubiquitination	EQAISFAKDFLAGGI HHHHHHHHHHHHHHH	47.18	21906983
10	Acetylation	EQAISFAKDFLAGGI HHHHHHHHHHHHHHH	47.18	19820867
22	Phosphorylation	GGIAAAISKTAVAPI HHHHHHHHCCCCCCH	21.16	21712546
23	Ubiquitination	GIAAAISKTAVAPIE HHHHHHHCCCCCCHH	34.10	21890473
23	Acetylation	GIAAAISKTAVAPIE HHHHHHHCCCCCCHH	34.10	23954790
23	Malonylation	GIAAAISKTAVAPIE HHHHHHHCCCCCCHH	34.10	26320211
24	Phosphorylation	IAAAISKTAVAPIER HHHHHHCCCCCCHHH	21.41	20860994
33	Ubiquitination	VAPIERVKLLLQVQH CCCHHHHHHHHHHHH	39.37	21890473
33	Malonylation	VAPIERVKLLLQVQH CCCHHHHHHHHHHHH	39.37	26320211
33	Acetylation	VAPIERVKLLLQVQH CCCHHHHHHHHHHHH	39.37	-
42	Phosphorylation	LLQVQHASKQIAADK HHHHHHHHHHHHHCH	23.98	30266825
43	Ubiquitination	LQVQHASKQIAADKQ HHHHHHHHHHHHCHH	46.65	21890473
43	Acetylation	LQVQHASKQIAADKQ HHHHHHHHHHHHCHH	46.65	26051181
43	Succinylation	LQVQHASKQIAADKQ HHHHHHHHHHHHCHH	46.65	21890473
49	Methylation	SKQIAADKQYKGIVD HHHHHHCHHCCCEEE	51.29	-
49	Trimethylation	SKQIAADKQYKGIVD HHHHHHCHHCCCEEE	51.29	-
49	Ubiquitination	SKQIAADKQYKGIVD HHHHHHCHHCCCEEE	51.29	-
51	Phosphorylation	QIAADKQYKGIVDCI HHHHCHHCCCEEEEE	19.54	-
52	Methylation	IAADKQYKGIVDCIV HHHCHHCCCEEEEEE	39.40	24129315
52	"N6,N6,N6-trimethyllysine"	IAADKQYKGIVDCIV HHHCHHCCCEEEEEE	39.40	-
63	Ubiquitination	DCIVRIPKEQGVLSF EEEEEECHHHCCEEE	61.37	21890473
63	Acetylation	DCIVRIPKEQGVLSF EEEEEECHHHCCEEE	61.37	23954790
69	Phosphorylation	PKEQGVLSFWRGNLA CHHHCCEEEECCCHH	21.98	30108239
81	Phosphorylation	NLANVIRYFPTQALN CHHHHHHHCHHHHHH	11.64	21712546
84	Phosphorylation	NVIRYFPTQALNFAF HHHHHCHHHHHHHHC	19.30	21712546
92	Malonylation	QALNFAFKDKYKQIF HHHHHHCHHHCCEEE	50.29	26320211
92	Acetylation	QALNFAFKDKYKQIF HHHHHHCHHHCCEEE	50.29	133733
92	Ubiquitination	QALNFAFKDKYKQIF HHHHHHCHHHCCEEE	50.29	21890473
94	Acetylation	LNFAFKDKYKQIFLG HHHHCHHHCCEEEEC	55.74	24885209
96	Malonylation	FAFKDKYKQIFLGGV HHCHHHCCEEEECCC	42.53	26320211
96	Acetylation	FAFKDKYKQIFLGGV HHCHHHCCEEEECCC	42.53	130859
96	Ubiquitination	FAFKDKYKQIFLGGV HHCHHHCCEEEECCC	42.53	21890473
105	Acetylation	IFLGGVDKHTQFWRY EEECCCCCCHHHHHH	46.26	19608861
105	Malonylation	IFLGGVDKHTQFWRY EEECCCCCCHHHHHH	46.26	26320211
105	Ubiquitination	IFLGGVDKHTQFWRY EEECCCCCCHHHHHH	46.26	21890473
112	Phosphorylation	KHTQFWRYFAGNLAS CCHHHHHHHHCCCCC	6.59	28857561
119	Phosphorylation	YFAGNLASGGAAGAT HHHCCCCCCCCCCCC	40.71	20833797
126	Phosphorylation	SGGAAGATSLCFVYP CCCCCCCCEEEEEEE	22.70	20860994
127	Phosphorylation	GGAAGATSLCFVYPL CCCCCCCEEEEEEEC	23.70	28857561
139	Phosphorylation	YPLDFARTRLAADVG EECCCHHHHHHHHHC	26.97	20860994
140	Methylation	PLDFARTRLAADVGK ECCCHHHHHHHHHCC	19.44	-
147	Acetylation	RLAADVGKSGTEREF HHHHHHCCCCCHHHH	45.63	25825284
147	Methylation	RLAADVGKSGTEREF HHHHHHCCCCCHHHH	45.63	100189263
147	Succinylation	RLAADVGKSGTEREF HHHHHHCCCCCHHHH	45.63	21890473
147	Ubiquitination	RLAADVGKSGTEREF HHHHHHCCCCCHHHH	45.63	21890473
148	Phosphorylation	LAADVGKSGTEREFR HHHHHCCCCCHHHHC	45.05	23911959
150	Phosphorylation	ADVGKSGTEREFRGL HHHCCCCCHHHHCCC	38.67	30108239
155	Methylation	SGTEREFRGLGDCLV CCCHHHHCCCCCEEE	34.37	-
160	S-nitrosylation	EFRGLGDCLVKITKS HHCCCCCEEEEEECC	4.46	24105792
160	S-palmitoylation	EFRGLGDCLVKITKS HHCCCCCEEEEEECC	4.46	29575903
163	Ubiquitination	GLGDCLVKITKSDGI CCCCEEEEEECCCCC	31.54	21890473
163	Acetylation	GLGDCLVKITKSDGI CCCCEEEEEECCCCC	31.54	25825284
163	Malonylation	GLGDCLVKITKSDGI CCCCEEEEEECCCCC	31.54	26320211
166	Ubiquitination	DCLVKITKSDGIRGL CEEEEEECCCCCCCC	50.45	21890473
166	Acetylation	DCLVKITKSDGIRGL CEEEEEECCCCCCCC	50.45	26210075
166	Succinylation	DCLVKITKSDGIRGL CEEEEEECCCCCCCC	50.45	23954790
187	Phosphorylation	SVQGIIIYRAAYFGV EEEEEEEEEEHHHCC	5.47	-
191	Phosphorylation	IIIYRAAYFGVYDTA EEEEEEHHHCCHHCC	10.40	21082442
195	Phosphorylation	RAAYFGVYDTAKGML EEHHHCCHHCCCCCC	14.14	27259358
197	Phosphorylation	AYFGVYDTAKGMLPD HHHCCHHCCCCCCCC	16.75	26356563
199	Sumoylation	FGVYDTAKGMLPDPK HCCHHCCCCCCCCCC	47.12	-
199	Ubiquitination	FGVYDTAKGMLPDPK HCCHHCCCCCCCCCC	47.12	21890473
199	Malonylation	FGVYDTAKGMLPDPK HCCHHCCCCCCCCCC	47.12	26320211
206	Sumoylation	KGMLPDPKNTHIVVS CCCCCCCCCCEEEEE	80.16	-
215	Sulfoxidation	THIVVSWMIAQTVTA CEEEEEHHHHHHHHH	1.10	28183972
229	Phosphorylation	AVAGVVSYPFDTVRR HHHCCCCCCHHHHHH	9.05	-
242	Phosphorylation	RRRMMMQSGRKGADI HHHHHHHCCCCCCCE	23.75	24719451
245	Ubiquitination	MMMQSGRKGADIMYT HHHHCCCCCCCEEEE	63.07	21890473
260	Ubiquitination	GTVDCWRKIFRDEGG CCHHHHHHHHCCCCC	23.00	-
268	Acetylation	IFRDEGGKAFFKGAW HHCCCCCCEEHHHHH	53.53	19608861
268	Malonylation	IFRDEGGKAFFKGAW HHCCCCCCEEHHHHH	53.53	26320211
268	Ubiquitination	IFRDEGGKAFFKGAW HHCCCCCCEEHHHHH	53.53	21890473
272	Acetylation	EGGKAFFKGAWSNVL CCCCEEHHHHHHHHH	41.06	130857
272	Methylation	EGGKAFFKGAWSNVL CCCCEEHHHHHHHHH	41.06	130857
272	Ubiquitination	EGGKAFFKGAWSNVL CCCCEEHHHHHHHHH	41.06	21890473
272	Malonylation	EGGKAFFKGAWSNVL CCCCEEHHHHHHHHH	41.06	26320211
276	Phosphorylation	AFFKGAWSNVLRGMG EEHHHHHHHHHHHCC	19.27	28857561
282	Sulfoxidation	WSNVLRGMGGAFVLV HHHHHHHCCCEEEEE	3.46	28183972

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 ADT3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
52	K	Methylation		24129315
Trimethylated by ANTKMT at Lys-52.

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 ADT3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PLS1_HUMAN	PLSCR1	physical	16189514
KR412_HUMAN	KRTAP4-12	physical	16189514
SCG1_HUMAN	CHGB	physical	16169070
VIME_HUMAN	VIM	physical	16169070
TIM13_HUMAN	TIMM13	physical	22939629
TIM10_HUMAN	TIMM10	physical	22939629
TIM50_HUMAN	TIMM50	physical	22939629
TIM9_HUMAN	TIMM9	physical	22939629
RL10L_HUMAN	RPL10L	physical	22939629
LMNA_HUMAN	LMNA	physical	22939629
VAMP2_HUMAN	VAMP2	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RL10_HUMAN	RPL10	physical	22939629
RL10A_HUMAN	RPL10A	physical	22939629
NNTM_HUMAN	NNT	physical	22939629
NDUB8_HUMAN	NDUFB8	physical	22939629
QCR1_HUMAN	UQCRC1	physical	22939629
NDUV3_HUMAN	NDUFV3	physical	22939629
TRI23_HUMAN	TRIM23	physical	25416956
K1H1_HUMAN	KRT31	physical	25416956
TRAF1_HUMAN	TRAF1	physical	25416956
TRIP6_HUMAN	TRIP6	physical	25416956
TRIM1_HUMAN	MID2	physical	25416956
MTUS2_HUMAN	MTUS2	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
TEKT4_HUMAN	TEKT4	physical	25416956
NT2NL_HUMAN	NOTCH2NL	physical	25416956
VA0D1_HUMAN	ATP6V0D1	physical	26344197
PMM2_HUMAN	PMM2	physical	26344197
MCAT_HUMAN	SLC25A20	physical	26344197
SCMC1_HUMAN	SLC25A24	physical	26344197
LYAG_HUMAN	GAA	physical	28514442

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
DB00720	Clodronate

Regulatory Network of ADT3_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-23; LYS-96; LYS-105; LYS-268AND LYS-272, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-148, AND MASSSPECTROMETRY.	18691976 [Abstract]
"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-191, AND MASSSPECTROMETRY.	18083107 [Abstract]

show